HCFC1_HUMAN
ID HCFC1_HUMAN Reviewed; 2035 AA.
AC P51610; Q6P4G5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Host cell factor 1 {ECO:0000303|PubMed:10629049};
DE Short=HCF {ECO:0000303|PubMed:8392914};
DE Short=HCF-1 {ECO:0000303|PubMed:10629049};
DE AltName: Full=C1 factor {ECO:0000303|PubMed:7876203};
DE AltName: Full=CFF {ECO:0000305};
DE AltName: Full=VCAF {ECO:0000305};
DE AltName: Full=VP16 accessory protein {ECO:0000303|PubMed:7829097};
DE Contains:
DE RecName: Full=HCF N-terminal chain 1 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF N-terminal chain 2 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF N-terminal chain 3 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF N-terminal chain 4 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF N-terminal chain 5 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF N-terminal chain 6 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF C-terminal chain 1 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF C-terminal chain 2 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF C-terminal chain 3 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF C-terminal chain 4 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF C-terminal chain 5 {ECO:0000303|PubMed:7590226};
DE Contains:
DE RecName: Full=HCF C-terminal chain 6 {ECO:0000303|PubMed:7590226};
GN Name=HCFC1 {ECO:0000303|PubMed:7829097, ECO:0000312|HGNC:HGNC:4839};
GN Synonyms=HCF1, HFC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Hepatoma;
RX PubMed=8392914; DOI=10.1016/0092-8674(93)90299-6;
RA Wilson A.C., Lamarco K., Peterson M.G., Herr W.;
RT "The VP16 accessory protein HCF is a family of polypeptides processed from
RT a large precursor protein.";
RL Cell 74:115-125(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7876203; DOI=10.1074/jbc.270.9.4387;
RA Kristie T.M., Pomerantz J.L., Twomey T.C., Parent S.A., Sharp P.A.;
RT "The cellular C1 factor of the herpes simplex virus enhancer complex is a
RT family of polypeptides.";
RL J. Biol. Chem. 270:4387-4394(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-2035, AND VARIANT PRO-1164.
RC TISSUE=Fetal brain;
RX PubMed=7829097; DOI=10.1006/geno.1994.1455;
RA Frattini A., Faranda S., Redolfi E., Zucchi I., Villa A., Patrosso M.C.,
RA Strina D., Susani L., Vezzoni P.;
RT "Genomic organization of the human VP16 accessory protein, a housekeeping
RT gene (HCFC1) mapping to Xq28.";
RL Genomics 23:30-35(1994).
RN [6]
RP PROTEIN SEQUENCE OF 1324-1336; 1424-1436 AND 1446-1457, SUBUNIT, AND
RP AUTOCATALYTIC CLEAVAGE.
RX PubMed=10920196; DOI=10.1073/pnas.160266697;
RA Vogel J.L., Kristie T.M.;
RT "Autocatalytic proteolysis of the transcription factor-coactivator C1
RT (HCF): a potential role for proteolytic regulation of coactivator
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9425-9430(2000).
RN [7]
RP AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF 1017-PRO--HIS-1021 AND
RP 1072-VAL--ASN-1097.
RX PubMed=7590226; DOI=10.1101/gad.9.20.2445;
RA Wilson A.C., Peterson M.G., Herr W.;
RT "The HCF repeat is an unusual proteolytic cleavage signal.";
RL Genes Dev. 9:2445-2458(1995).
RN [8]
RP INTERACTION WITH CREB3 AND VP16, AND MUTAGENESIS OF PRO-134.
RX PubMed=9271389; DOI=10.1128/mcb.17.9.5117;
RA Lu R., Yang P., O'Hare P., Misra V.;
RT "Luman, a new member of the CREB/ATF family, binds to herpes simplex virus
RT VP16-associated host cellular factor.";
RL Mol. Cell. Biol. 17:5117-5126(1997).
RN [9]
RP INTERACTION WITH CREB3 AND VP16, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=9389645; DOI=10.1101/gad.11.23.3122;
RA Freiman R.N., Herr W.;
RT "Viral mimicry: common mode of association with HCF by VP16 and the
RT cellular protein LZIP.";
RL Genes Dev. 11:3122-3127(1997).
RN [10]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=9990006; DOI=10.1073/pnas.96.4.1229;
RA Kristie T.M., Vogel J.L., Sears A.E.;
RT "Nuclear localization of the C1 factor (host cell factor) in sensory
RT neurons correlates with reactivation of herpes simplex virus from
RT latency.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1229-1233(1999).
RN [11]
RP FUNCTION, AND INTERACTION WITH GABP2.
RX PubMed=10675337; DOI=10.1093/emboj/19.4.683;
RA Vogel J.L., Kristie T.M.;
RT "The novel coactivator C1 (HCF) coordinates multiprotein enhancer formation
RT and mediates transcription activation by GABP.";
RL EMBO J. 19:683-690(2000).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=10623756; DOI=10.1128/jvi.74.2.934-943.2000;
RA Lu R., Misra V.;
RT "Potential role for luman, the cellular homologue of herpes simplex virus
RT VP16 (alpha gene trans-inducing factor), in herpesvirus latency.";
RL J. Virol. 74:934-943(2000).
RN [13]
RP INTERACTION WITH SP1.
RX PubMed=10976766; DOI=10.1023/a:1007177623283;
RA Gunther M., Laithier M., Brison O.;
RT "A set of proteins interacting with transcription factor Sp1 identified in
RT a two-hybrid screening.";
RL Mol. Cell. Biochem. 210:131-142(2000).
RN [14]
RP FUNCTION, INTERACTION WITH POU2F1; VP16 AND CREB3, AND MUTAGENESIS OF
RP PRO-30; PRO-79; CYS-82; LYS-105; PRO-134; ARG-137; PRO-197; ARG-200;
RP ARG-228; PRO-252; ARG-255; 289-GLU--LYS-291; PRO-319; ARG-322; SER-338 AND
RP 344-ARG-LYS-345.
RX PubMed=10629049; DOI=10.1128/mcb.20.3.919-928.2000;
RA Mahajan S.S., Wilson A.C.;
RT "Mutations in host cell factor 1 separate its role in cell proliferation
RT from recruitment of VP16 and LZIP.";
RL Mol. Cell. Biol. 20:919-928(2000).
RN [15]
RP FUNCTION.
RX PubMed=10779346; DOI=10.1128/mcb.20.10.3568-3575.2000;
RA Scarr R.B., Smith M.R., Beddall M., Sharp P.A.;
RT "A novel 50-kilodalton fragment of host cell factor 1 (C1) in G(0) cells.";
RL Mol. Cell. Biol. 20:3568-3575(2000).
RN [16]
RP INTERACTION WITH CREBZF.
RX PubMed=10871379; DOI=10.1093/nar/28.12.2446;
RA Lu R., Misra V.;
RT "Zhangfei: a second cellular protein interacts with herpes simplex virus
RT accessory factor HCF in a manner similar to Luman and VP16.";
RL Nucleic Acids Res. 28:2446-2454(2000).
RN [17]
RP INTERACTION WITH CREB3.
RX PubMed=10984507; DOI=10.1073/pnas.190062797;
RA Luciano R.L., Wilson A.C.;
RT "N-terminal transcriptional activation domain of LZIP comprises two LxxLL
RT motifs and the host cell factor-1 binding motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10757-10762(2000).
RN [18]
RP SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH HCFC1R1.
RC TISSUE=Brain;
RX PubMed=12235138; DOI=10.1074/jbc.m205440200;
RA Mahajan S.S., Little M.M., Vazquez R., Wilson A.C.;
RT "Interaction of HCF-1 with a cellular nuclear export factor.";
RL J. Biol. Chem. 277:44292-44299(2002).
RN [19]
RP FUNCTION, AND INTERACTION WITH ZBTB17.
RX PubMed=12244100; DOI=10.1074/jbc.m206226200;
RA Piluso D., Bilan P., Capone J.P.;
RT "Host cell factor-1 interacts with and antagonizes transactivation by the
RT cell cycle regulatory factor Miz-1.";
RL J. Biol. Chem. 277:46799-46808(2002).
RN [20]
RP FUNCTION, AND INTERACTION WITH EGR2 AND E2F4.
RX PubMed=14532282; DOI=10.1074/jbc.m303470200;
RA Luciano R.L., Wilson A.C.;
RT "HCF-1 functions as a coactivator for the zinc finger protein Krox20.";
RL J. Biol. Chem. 278:51116-51124(2003).
RN [21]
RP FUNCTION, AND INTERACTION WITH SIN3A; HDAC1; HDAC2; SUDS3; SAP30; SIN3B;
RP OGT; SET1; ASH2L AND WDR5.
RX PubMed=12670868; DOI=10.1101/gad.252103;
RA Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
RT "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
RT methyltransferase are tethered together selectively by the cell-
RT proliferation factor HCF-1.";
RL Genes Dev. 17:896-911(2003).
RN [22]
RP FUNCTION.
RX PubMed=15190068; DOI=10.1074/jbc.m401255200;
RA Khurana B., Kristie T.M.;
RT "A protein sequestering system reveals control of cellular programs by the
RT transcriptional coactivator HCF-1.";
RL J. Biol. Chem. 279:33673-33683(2004).
RN [23]
RP IDENTIFICATION IN THE MLL1 COMPLEX.
RX PubMed=15199122; DOI=10.1128/mcb.24.13.5639-5649.2004;
RA Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I.,
RA Herr W., Cleary M.L.;
RT "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase
RT complex with menin to regulate Hox gene expression.";
RL Mol. Cell. Biol. 24:5639-5649(2004).
RN [24]
RP IDENTIFICATION IN THE MLL1 COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [25]
RP INTERACTION WITH CREBZF AND CREB3.
RX PubMed=15705566; DOI=10.1074/jbc.m500728200;
RA Misra V., Rapin N., Akhova O., Bainbridge M., Korchinski P.;
RT "Zhangfei is a potent and specific inhibitor of the host cell factor-
RT binding transcription factor Luman.";
RL J. Biol. Chem. 280:15257-15266(2005).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; THR-1491 AND SER-1507,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [27]
RP FUNCTION, AUTOCATALYTIC CLEAVAGE, AND INTERACTION WITH FHL2.
RX PubMed=16624878; DOI=10.1073/pnas.0602109103;
RA Vogel J.L., Kristie T.M.;
RT "Site-specific proteolysis of the transcriptional coactivator HCF-1 can
RT regulate its interaction with protein cofactors.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6817-6822(2006).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [29]
RP FUNCTION.
RX PubMed=17578910; DOI=10.1073/pnas.0704351104;
RA Narayanan A., Ruyechan W.T., Kristie T.M.;
RT "The coactivator host cell factor-1 mediates Set1 and MLL1 H3K4
RT trimethylation at herpesvirus immediate early promoters for initiation of
RT infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10835-10840(2007).
RN [30]
RP IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH SETD1A.
RX PubMed=17998332; DOI=10.1128/mcb.01356-07;
RA Lee J.H., Skalnik D.G.;
RT "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
RT Histone H3-Lys4 methyltransferase complex to transcription start sites of
RT transcribed human genes.";
RL Mol. Cell. Biol. 28:609-618(2008).
RN [31]
RP IDENTIFICATION IN SET1 COMPLEX.
RX PubMed=18838538; DOI=10.1128/mcb.00976-08;
RA Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
RA Shilatifard A.;
RT "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human
RT Set1/COMPASS.";
RL Mol. Cell. Biol. 28:7337-7344(2008).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-1205 AND SER-1507,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [34]
RP IDENTIFICATION IN A COMPLEX WITH ZNF335; HCFC1; CCAR2; EMSY; MKI67; RBBP5;
RP ASH2L AND WDR5.
RX PubMed=19131338; DOI=10.1074/jbc.m805872200;
RA Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.;
RT "Identification and characterization of a novel nuclear protein complex
RT involved in nuclear hormone receptor-mediated gene regulation.";
RL J. Biol. Chem. 284:7542-7552(2009).
RN [35]
RP UBIQUITINATION AT LYS-105; LYS-163; LYS-244 AND LYS-363, DEUBIQUITINATION
RP BY BAP1, AND MUTAGENESIS OF PRO-134.
RX PubMed=19815555; DOI=10.1074/jbc.m109.046755;
RA Machida Y.J., Machida Y., Vashisht A.A., Wohlschlegel J.A., Dutta A.;
RT "The deubiquitinating enzyme BAP1 regulates cell growth via interaction
RT with HCF-1.";
RL J. Biol. Chem. 284:34179-34188(2009).
RN [36]
RP UBIQUITINATION AT LYS-1807 AND LYS-1808, DEUBIQUITINATION BY BAP1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19188440; DOI=10.1128/mcb.01517-08;
RA Misaghi S., Ottosen S., Izrael-Tomasevic A., Arnott D., Lamkanfi M.,
RA Lee J., Liu J., O'Rourke K., Dixit V.M., Wilson A.C.;
RT "Association of C-terminal ubiquitin hydrolase BRCA1-associated protein 1
RT with cell cycle regulator host cell factor 1.";
RL Mol. Cell. Biol. 29:2181-2192(2009).
RN [37]
RP CAUTION.
RX PubMed=19377461; DOI=10.1038/nature07954;
RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
RA Kitagawa H., Kato S.;
RT "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
RT granulopoiesis.";
RL Nature 459:455-459(2009).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-1507, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [39]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-813 AND LYS-2005, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [40]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6; SER-666; SER-669 AND SER-1507, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [41]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [42]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6; SER-666 AND SER-1507, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [43]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [44]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [45]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-598; SER-666; SER-1205
RP AND SER-1224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [46]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1497; SER-1507 AND SER-1771,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [47]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-504; ARG-524 AND ARG-1219, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [48]
RP CAUTION, AND RETRACTION NOTICE OF PUBMED:24129315.
RX PubMed=24336203; DOI=10.1038/nature12896;
RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
RA Kitagawa H., Kato S.;
RT "Retraction: GlcNAcylation of a histone methyltransferase in retinoic-acid-
RT induced granulopoiesis.";
RL Nature 505:574-574(2014).
RN [49]
RP FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20018852; DOI=10.1074/jbc.c109.087981;
RA Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L.,
RA Washburn M.P., Conaway J.W., Conaway R.C.;
RT "Subunit composition and substrate specificity of a MOF-containing histone
RT acetyltransferase distinct from the male-specific lethal (MSL) complex.";
RL J. Biol. Chem. 285:4268-4272(2010).
RN [50]
RP IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT COMPLEX,
RP INTERACTION WITH OGT; THAP1 AND THAP3, GLYCOSYLATION, AND FUNCTION.
RX PubMed=20200153; DOI=10.1074/jbc.m109.072579;
RA Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L.,
RA Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B.,
RA Kristie T.M., Girard J.P.;
RT "The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and
RT O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias.";
RL J. Biol. Chem. 285:13364-13371(2010).
RN [51]
RP GLYCOSYLATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND
RP INTERACTION WITH OGT.
RX PubMed=21285374; DOI=10.1073/pnas.1013822108;
RA Daou S., Mashtalir N., Hammond-Martel I., Pak H., Yu H., Sui G.,
RA Vogel J.L., Kristie T.M., Affar E.B.;
RT "Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the
RT host cell factor-1 maturation pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2747-2752(2011).
RN [52]
RP GLYCOSYLATION, AND INTERACTION WITH OGT; TET2 AND TET3.
RX PubMed=23353889; DOI=10.1038/emboj.2012.357;
RA Deplus R., Delatte B., Schwinn M.K., Defrance M., Mendez J., Murphy N.,
RA Dawson M.A., Volkmar M., Putmans P., Calonne E., Shih A.H., Levine R.L.,
RA Bernard O., Mercher T., Solary E., Urh M., Daniels D.L., Fuks F.;
RT "TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and
RT SET1/COMPASS.";
RL EMBO J. 32:645-655(2013).
RN [53]
RP FUNCTION, INTERACTION WITH KMT2E AND E2F1, AND SUBCELLULAR LOCATION.
RX PubMed=23629655; DOI=10.1074/jbc.m112.439729;
RA Zhou P., Wang Z., Yuan X., Zhou C., Liu L., Wan X., Zhang F., Ding X.,
RA Wang C., Xiong S., Wang Z., Yuan J., Li Q., Zhang Y.;
RT "Mixed lineage leukemia 5 (MLL5) protein regulates cell cycle progression
RT and E2F1-responsive gene expression via association with host cell factor-1
RT (HCF-1).";
RL J. Biol. Chem. 288:17532-17543(2013).
RN [54]
RP GLYCOSYLATION, AND PROTEOLYTIC PROCESSING.
RX PubMed=28302723; DOI=10.1074/jbc.m116.771030;
RA Vaidyanathan K., Niranjan T., Selvan N., Teo C.F., May M., Patel S.,
RA Weatherly B., Skinner C., Opitz J., Carey J., Viskochil D., Gecz J.,
RA Shaw M., Peng Y., Alexov E., Wang T., Schwartz C., Wells L.;
RT "Identification and characterization of a missense mutation in the O-linked
RT beta-N-acetylglucosamine (O-GlcNAc) transferase gene that segregates with
RT X-linked intellectual disability.";
RL J. Biol. Chem. 292:8948-8963(2017).
RN [55]
RP GLYCOSYLATION, AND PROTEOLYTIC PROCESSING.
RX PubMed=28584052; DOI=10.1074/jbc.m117.790097;
RA Willems A.P., Gundogdu M., Kempers M.J.E., Giltay J.C., Pfundt R.,
RA Elferink M., Loza B.F., Fuijkschot J., Ferenbach A.T., van Gassen K.L.I.,
RA van Aalten D.M.F., Lefeber D.J.;
RT "Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with
RT X-linked intellectual disability.";
RL J. Biol. Chem. 292:12621-12631(2017).
RN [56]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-282 AND LYS-2024, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [57]
RP VARIANT MAHCX ASN-225.
RX PubMed=23000143; DOI=10.1016/j.ajhg.2012.08.011;
RA Huang L., Jolly L.A., Willis-Owen S., Gardner A., Kumar R., Douglas E.,
RA Shoubridge C., Wieczorek D., Tzschach A., Cohen M., Hackett A., Field M.,
RA Froyen G., Hu H., Haas S.A., Ropers H.H., Kalscheuer V.M., Corbett M.A.,
RA Gecz J.;
RT "A noncoding, regulatory mutation implicates HCFC1 in nonsyndromic
RT intellectual disability.";
RL Am. J. Hum. Genet. 91:694-702(2012).
CC -!- FUNCTION: Transcriptional coregulator (By similarity). Involved in
CC control of the cell cycle (PubMed:10629049, PubMed:10779346,
CC PubMed:15190068, PubMed:16624878, PubMed:23629655). Also antagonizes
CC transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the
CC p15(INK4b) promoter and inhibits its ability to recruit p300
CC (PubMed:10675337, PubMed:12244100). Coactivator for EGR2 and GABP2
CC (PubMed:12244100, PubMed:14532282). Tethers the chromatin modifying
CC Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3
CC histone deacetylase (HDAC) complexes (involved in the activation and
CC repression of transcription, respectively) together (PubMed:12670868).
CC Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the
CC regulation of the transcriptional activity of RRM1 (PubMed:20200153).
CC As part of the NSL complex it may be involved in acetylation of
CC nucleosomal histone H4 on several lysine residues (PubMed:20018852).
CC Recruits KMT2E/MLL5 to E2F1 responsive promoters promoting
CC transcriptional activation and thereby facilitates G1 to S phase
CC transition (PubMed:23629655). Modulates expression of homeobox protein
CC PDX1, perhaps acting in concert with transcription factor E2F1, thereby
CC regulating pancreatic beta-cell growth and glucose-stimulated insulin
CC secretion (By similarity). May negatively modulate transcriptional
CC activity of FOXO3 (By similarity). {ECO:0000250|UniProtKB:D3ZN95,
CC ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:10675337,
CC ECO:0000269|PubMed:10779346, ECO:0000269|PubMed:12244100,
CC ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:14532282,
CC ECO:0000269|PubMed:15190068, ECO:0000269|PubMed:16624878,
CC ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20200153,
CC ECO:0000269|PubMed:23629655}.
CC -!- FUNCTION: (Microbial infection) In case of human herpes simplex virus
CC (HSV) infection, HCFC1 forms a multiprotein-DNA complex with the viral
CC transactivator protein VP16 and POU2F1 thereby enabling the
CC transcription of the viral immediate early genes.
CC {ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:17578910}.
CC -!- SUBUNIT: Composed predominantly of six polypeptides ranging from 110 to
CC 150 kDa and a minor 300 kDa polypeptide (PubMed:10920196). The majority
CC of N- and C-terminal cleavage products remain tightly, albeit non-
CC covalently, associated (PubMed:10920196). Interacts with POU2F1, CREB3,
CC ZBTB17, EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A,
CC HDAC1, HDAC2, SUDS3), SAP30, SIN3B and FHL2 (PubMed:9271389,
CC PubMed:9389645, PubMed:10675337, PubMed:10976766, PubMed:10629049,
CC PubMed:10871379, PubMed:10984507, PubMed:12244100, PubMed:14532282,
CC PubMed:12670868, PubMed:15705566, PubMed:16624878). Component of a MLL1
CC complex, composed of at least the core components KMT2A/MLL1, ASH2L,
CC HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18,
CC CHD8, DPY30, E2F6, HCFC2, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
CC MEN1, MGA, KAT8, PELP1, PHF20, PRP31, RING2, RUVBL1, RUVBL2, SENP3,
CC TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15199122,
CC PubMed:15960975). Component of a THAP1/THAP3-HCFC1-OGT complex that is
CC required for the regulation of the transcriptional activity of RRM1
CC (PubMed:20200153). Interacts directly with THAP3 (via its HBM)
CC (PubMed:20200153). Interacts (via the Kelch-repeat domain) with THAP1
CC (via the HBM); the interaction recruits HCHC1 to the RRM1
CC (PubMed:20200153). Interacts directly with OGT; the interaction, which
CC requires the HCFC1 cleavage site domain, glycosylates and promotes the
CC proteolytic processing of HCFC1, retains OGT in the nucleus and impacts
CC the expression of herpes simplex virus immediate early viral genes
CC (PubMed:12670868, PubMed:21285374, PubMed:23353889). Component of the
CC SET1 complex, at least composed of the catalytic subunit (SETD1A or
CC SETD1B), WDR5, WDR82, RBBP5, ASH2L, CXXC1, HCFC1 and DPY30
CC (PubMed:17998332, PubMed:18838538). Component of the NSL complex at
CC least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20,
CC OGT1/OGT, WDR5 and HCFC1 (PubMed:20018852). Component of a complex at
CC least composed of ZNF335, HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and
CC WDR5; the complex is formed as a result of interactions between
CC components of a nuclear receptor-mediated transcription complex and a
CC histone methylation complex (PubMed:19131338). Within the complex
CC interacts with ZNF335 (PubMed:19131338). Interacts with TET2 and TET3
CC (PubMed:23353889). Interacts with HCFC1R1 (PubMed:12235138). Interacts
CC with THAP11 (By similarity). Interacts (via Kelch domain) with
CC KMT2E/MLL5 isoform 3 (via HBM motif) (PubMed:23629655). Interacts with
CC E2F1 (PubMed:23629655). {ECO:0000250|UniProtKB:Q61191,
CC ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:10675337,
CC ECO:0000269|PubMed:10871379, ECO:0000269|PubMed:10920196,
CC ECO:0000269|PubMed:10976766, ECO:0000269|PubMed:10984507,
CC ECO:0000269|PubMed:12235138, ECO:0000269|PubMed:12244100,
CC ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:14532282,
CC ECO:0000269|PubMed:15199122, ECO:0000269|PubMed:15705566,
CC ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16624878,
CC ECO:0000269|PubMed:17998332, ECO:0000269|PubMed:18838538,
CC ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:20018852,
CC ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:21285374,
CC ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:23629655,
CC ECO:0000269|PubMed:9271389, ECO:0000269|PubMed:9389645}.
CC -!- SUBUNIT: (Microbial infection) Associates with the VP16-induced
CC complex; binding to HCFC1 activates the viral transcriptional activator
CC VP16 for association with POU2F1, to form a multiprotein-DNA complex
CC responsible for activating transcription of the viral immediate early
CC genes (PubMed:10629049). Interacts with the viral transactivator
CC protein VP16 (PubMed:9271389, PubMed:9389645, PubMed:10629049).
CC {ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:9271389,
CC ECO:0000269|PubMed:9389645}.
CC -!- INTERACTION:
CC P51610; Q9UBL3: ASH2L; NbExp=6; IntAct=EBI-396176, EBI-540797;
CC P51610; Q92560: BAP1; NbExp=4; IntAct=EBI-396176, EBI-1791447;
CC P51610; O43889: CREB3; NbExp=5; IntAct=EBI-396176, EBI-625002;
CC P51610; O43889-2: CREB3; NbExp=4; IntAct=EBI-396176, EBI-625022;
CC P51610; Q9NS37: CREBZF; NbExp=8; IntAct=EBI-396176, EBI-632965;
CC P51610; O43524: FOXO3; NbExp=2; IntAct=EBI-396176, EBI-1644164;
CC P51610; Q06546: GABPA; NbExp=2; IntAct=EBI-396176, EBI-638925;
CC P51610; Q06547: GABPB1; NbExp=3; IntAct=EBI-396176, EBI-618165;
CC P51610; Q06547-2: GABPB1; NbExp=6; IntAct=EBI-396176, EBI-618189;
CC P51610; P51610: HCFC1; NbExp=2; IntAct=EBI-396176, EBI-396176;
CC P51610; Q13547: HDAC1; NbExp=2; IntAct=EBI-396176, EBI-301834;
CC P51610; Q92769: HDAC2; NbExp=2; IntAct=EBI-396176, EBI-301821;
CC P51610; O15294: OGT; NbExp=10; IntAct=EBI-396176, EBI-539828;
CC P51610; O15047: SETD1A; NbExp=2; IntAct=EBI-396176, EBI-540779;
CC P51610; Q96ST3: SIN3A; NbExp=6; IntAct=EBI-396176, EBI-347218;
CC P51610; Q96EB6: SIRT1; NbExp=2; IntAct=EBI-396176, EBI-1802965;
CC P51610; P08047: SP1; NbExp=4; IntAct=EBI-396176, EBI-298336;
CC P51610; Q9H7L9: SUDS3; NbExp=2; IntAct=EBI-396176, EBI-540496;
CC P51610; Q9NVV9: THAP1; NbExp=6; IntAct=EBI-396176, EBI-741515;
CC P51610; Q96EK4: THAP11; NbExp=2; IntAct=EBI-396176, EBI-1790529;
CC P51610; P61964: WDR5; NbExp=6; IntAct=EBI-396176, EBI-540834;
CC P51610; Q13105: ZBTB17; NbExp=9; IntAct=EBI-396176, EBI-372156;
CC P51610-1; Q14192: FHL2; NbExp=5; IntAct=EBI-396188, EBI-701903;
CC P51610-1; Q9UPP1-2: PHF8; NbExp=2; IntAct=EBI-396188, EBI-6601215;
CC P51610-4; Q9NS37: CREBZF; NbExp=3; IntAct=EBI-18150048, EBI-632965;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12235138}. Nucleus
CC {ECO:0000269|PubMed:10623756, ECO:0000269|PubMed:12235138,
CC ECO:0000269|PubMed:19188440, ECO:0000269|PubMed:20018852,
CC ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:23629655}. Note=HCFC1R1
CC modulates its subcellular localization and overexpression of HCFC1R1
CC leads to accumulation of HCFC1 in the cytoplasm (PubMed:12235138). Non-
CC processed HCFC1 associates with chromatin. Colocalizes with CREB3 and
CC CANX in the ER. {ECO:0000269|PubMed:12235138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P51610-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51610-2; Sequence=VSP_002815;
CC Name=3;
CC IsoId=P51610-3; Sequence=VSP_012984, VSP_012985;
CC Name=4;
CC IsoId=P51610-4; Sequence=VSP_047138;
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal tissues and the adult
CC kidney. Present in all tissues tested. {ECO:0000269|PubMed:9389645}.
CC -!- DOMAIN: The HCF repeat is a highly specific proteolytic cleavage
CC signal. {ECO:0000269|PubMed:10920196, ECO:0000269|PubMed:7590226}.
CC -!- DOMAIN: The kelch repeats fold into a 6-bladed kelch beta-propeller
CC called the beta-propeller domain which mediates interaction with
CC HCFC1R1. {ECO:0000269|PubMed:12235138}.
CC -!- PTM: Proteolytically cleaved at one or several PPCE--THET sites within
CC the HCF repeats (PubMed:7590226, PubMed:10920196, PubMed:21285374).
CC Further cleavage of the primary N- and C-terminal chains results in a
CC 'trimming' and accumulation of the smaller chains. Cleavage is promoted
CC by O-glycosylation (PubMed:21285374, PubMed:28302723, PubMed:28584052).
CC {ECO:0000269|PubMed:10920196, ECO:0000269|PubMed:21285374,
CC ECO:0000269|PubMed:28302723, ECO:0000269|PubMed:28584052,
CC ECO:0000269|PubMed:7590226}.
CC -!- PTM: O-glycosylated. GlcNAcylation by OGT promotes proteolytic
CC processing. {ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:28302723,
CC ECO:0000269|PubMed:28584052}.
CC -!- PTM: Ubiquitinated. Lys-1807 and Lys-1808 are ubiquitinated both via
CC 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. BAP1 mediated
CC deubiquitination of 'Lys-48'-linked polyubiquitin chains;
CC deubiquitination by BAP1 does not seem to stabilize the protein.
CC {ECO:0000269|PubMed:19188440, ECO:0000269|PubMed:19815555}.
CC -!- DISEASE: Methylmalonic aciduria and homocystinuria, cblX type (MAHCX)
CC [MIM:309541]: An X-linked recessive metabolic disorder characterized by
CC severely delayed psychomotor development apparent in infancy, failure
CC to thrive, impaired intellectual development, and intractable epilepsy.
CC Additional features may include microcephaly and choreoathetosis.
CC {ECO:0000269|PubMed:23000143}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: The N- and the C-terminal fragments fail to
CC associate. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be part of the MLL5-L complex, at
CC least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and
CC OGT (PubMed:19377461). However, the corresponding article has been
CC retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461,
CC ECO:0000269|PubMed:24336203}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55790.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L20010; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063435; AAH63435.1; -; mRNA.
DR EMBL; X79198; CAA55790.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS44020.1; -. [P51610-1]
DR PIR; A40718; A40718.
DR RefSeq; NP_005325.2; NM_005334.2. [P51610-1]
DR RefSeq; XP_006724879.1; XM_006724816.2. [P51610-4]
DR PDB; 4GO6; X-ray; 2.70 A; A/C=360-402, B/D=1806-2035.
DR PDB; 4N39; X-ray; 1.76 A; B=1082-1097.
DR PDB; 4N3A; X-ray; 1.88 A; B=1072-1097.
DR PDB; 4N3B; X-ray; 2.17 A; B=1072-1097.
DR PDB; 4N3C; X-ray; 2.55 A; B=1072-1097.
DR PDB; 5LWV; X-ray; 1.90 A; A=1078-1095.
DR PDB; 6MA1; X-ray; 2.75 A; B=1082-1097.
DR PDB; 6MA2; X-ray; 2.10 A; B=1082-1097.
DR PDB; 6MA3; X-ray; 2.00 A; B=1082-1097.
DR PDB; 6MA4; X-ray; 2.00 A; B=1082-1097.
DR PDB; 6MA5; X-ray; 2.00 A; B=1082-1097.
DR PDBsum; 4GO6; -.
DR PDBsum; 4N39; -.
DR PDBsum; 4N3A; -.
DR PDBsum; 4N3B; -.
DR PDBsum; 4N3C; -.
DR PDBsum; 5LWV; -.
DR PDBsum; 6MA1; -.
DR PDBsum; 6MA2; -.
DR PDBsum; 6MA3; -.
DR PDBsum; 6MA4; -.
DR PDBsum; 6MA5; -.
DR AlphaFoldDB; P51610; -.
DR BMRB; P51610; -.
DR SMR; P51610; -.
DR BioGRID; 109304; 189.
DR ComplexPortal; CPX-5850; Histone-lysine N-methyltransferase complex, KMT2A variant.
DR ComplexPortal; CPX-7062; Histone-lysine N-methyltransferase complex, KMT2B variant.
DR ComplexPortal; CPX-7110; Histone-lysine N-methyltransferase complex, SET1A variant.
DR ComplexPortal; CPX-7111; Histone-lysine N-methyltransferase complex, SET1B variant.
DR ComplexPortal; CPX-809; NSL histone acetyltransferase complex.
DR CORUM; P51610; -.
DR DIP; DIP-32955N; -.
DR ELM; P51610; -.
DR IntAct; P51610; 88.
DR MINT; P51610; -.
DR STRING; 9606.ENSP00000309555; -.
DR GlyConnect; 2879; 1 O-Linked glycan (30 sites).
DR GlyGen; P51610; 170 sites, 2 O-linked glycans (170 sites).
DR iPTMnet; P51610; -.
DR MetOSite; P51610; -.
DR PhosphoSitePlus; P51610; -.
DR BioMuta; HCFC1; -.
DR DMDM; 160332311; -.
DR EPD; P51610; -.
DR jPOST; P51610; -.
DR MassIVE; P51610; -.
DR MaxQB; P51610; -.
DR PaxDb; P51610; -.
DR PeptideAtlas; P51610; -.
DR PRIDE; P51610; -.
DR ProteomicsDB; 56346; -. [P51610-1]
DR ProteomicsDB; 56347; -. [P51610-2]
DR ProteomicsDB; 56348; -. [P51610-3]
DR TopDownProteomics; P51610-2; -. [P51610-2]
DR Antibodypedia; 7165; 260 antibodies from 33 providers.
DR DNASU; 3054; -.
DR Ensembl; ENST00000310441.12; ENSP00000309555.7; ENSG00000172534.14. [P51610-1]
DR GeneID; 3054; -.
DR KEGG; hsa:3054; -.
DR MANE-Select; ENST00000310441.12; ENSP00000309555.7; NM_005334.3; NP_005325.2.
DR UCSC; uc004fjp.4; human. [P51610-1]
DR CTD; 3054; -.
DR DisGeNET; 3054; -.
DR GeneCards; HCFC1; -.
DR GeneReviews; HCFC1; -.
DR HGNC; HGNC:4839; HCFC1.
DR HPA; ENSG00000172534; Low tissue specificity.
DR MalaCards; HCFC1; -.
DR MIM; 300019; gene.
DR MIM; 309541; phenotype.
DR neXtProt; NX_P51610; -.
DR OpenTargets; ENSG00000172534; -.
DR Orphanet; 369962; Methylmalonic acidemia with homocystinuria, type cblX.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA29215; -.
DR VEuPathDB; HostDB:ENSG00000172534; -.
DR eggNOG; KOG4152; Eukaryota.
DR GeneTree; ENSGT00940000161383; -.
DR HOGENOM; CLU_002603_0_0_1; -.
DR InParanoid; P51610; -.
DR OMA; GPCGTIH; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; P51610; -.
DR TreeFam; TF314757; -.
DR PathwayCommons; P51610; -.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR SignaLink; P51610; -.
DR SIGNOR; P51610; -.
DR BioGRID-ORCS; 3054; 420 hits in 716 CRISPR screens.
DR ChiTaRS; HCFC1; human.
DR GeneWiki; Host_cell_factor_C1; -.
DR GenomeRNAi; 3054; -.
DR Pharos; P51610; Tbio.
DR PRO; PR:P51610; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51610; protein.
DR Bgee; ENSG00000172534; Expressed in tendon of biceps brachii and 196 other tissues.
DR ExpressionAtlas; P51610; baseline and differential.
DR Genevisible; P51610; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0044665; C:MLL1/2 complex; IPI:ComplexPortal.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0044545; C:NSL complex; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0051568; P:histone H3-K4 methylation; IC:ComplexPortal.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; TAS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0019046; P:release from viral latency; NAS:UniProtKB.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR037854; HCF1.
DR InterPro; IPR043536; HCF1/2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR PANTHER; PTHR46003; PTHR46003; 2.
DR PANTHER; PTHR46003:SF3; PTHR46003:SF3; 2.
DR Pfam; PF01344; Kelch_1; 1.
DR SMART; SM00060; FN3; 3.
DR SUPFAM; SSF117281; SSF117281; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Autocatalytic cleavage;
KW Cell cycle; Chromatin regulator; Cytoplasm; Direct protein sequencing;
KW Disease variant; Glycoprotein; Host-virus interaction;
KW Intellectual disability; Isopeptide bond; Kelch repeat; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..1423
FT /note="HCF N-terminal chain 6"
FT /evidence="ECO:0000305|PubMed:7590226"
FT /id="PRO_0000016611"
FT CHAIN 2..1323
FT /note="HCF N-terminal chain 5"
FT /evidence="ECO:0000305|PubMed:7590226"
FT /id="PRO_0000016612"
FT CHAIN 2..1295
FT /note="HCF N-terminal chain 4"
FT /evidence="ECO:0000305|PubMed:7590226"
FT /id="PRO_0000016613"
FT CHAIN 2..1110
FT /note="HCF N-terminal chain 3"
FT /evidence="ECO:0000305|PubMed:7590226"
FT /id="PRO_0000016614"
FT CHAIN 2..1081
FT /note="HCF N-terminal chain 2"
FT /evidence="ECO:0000269|PubMed:7590226"
FT /id="PRO_0000016615"
FT CHAIN 2..1019
FT /note="HCF N-terminal chain 1"
FT /evidence="ECO:0000269|PubMed:7590226"
FT /id="PRO_0000016616"
FT CHAIN 1020..2035
FT /note="HCF C-terminal chain 1"
FT /evidence="ECO:0000269|PubMed:7590226"
FT /id="PRO_0000016617"
FT CHAIN 1082..2035
FT /note="HCF C-terminal chain 2"
FT /evidence="ECO:0000269|PubMed:7590226"
FT /id="PRO_0000016618"
FT CHAIN 1111..2035
FT /note="HCF C-terminal chain 3"
FT /evidence="ECO:0000305|PubMed:7590226"
FT /id="PRO_0000016619"
FT CHAIN 1296..2035
FT /note="HCF C-terminal chain 4"
FT /evidence="ECO:0000305|PubMed:7590226"
FT /id="PRO_0000016620"
FT CHAIN 1324..2035
FT /note="HCF C-terminal chain 5"
FT /evidence="ECO:0000305|PubMed:7590226"
FT /id="PRO_0000016621"
FT CHAIN 1424..2035
FT /note="HCF C-terminal chain 6"
FT /evidence="ECO:0000305|PubMed:7590226"
FT /id="PRO_0000016622"
FT REPEAT 44..89
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 93..140
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 148..194
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 217..265
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 266..313
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT DOMAIN 366..466
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 1010..1035
FT /note="HCF repeat 1"
FT /evidence="ECO:0000305|PubMed:7590226"
FT REPEAT 1072..1097
FT /note="HCF repeat 2"
FT /evidence="ECO:0000305|PubMed:7590226"
FT REPEAT 1101..1126
FT /note="HCF repeat 3"
FT /evidence="ECO:0000305|PubMed:7590226"
FT REPEAT 1158..1183
FT /note="HCF repeat 4; degenerate"
FT /evidence="ECO:0000305|PubMed:7590226"
FT REPEAT 1286..1311
FT /note="HCF repeat 5"
FT /evidence="ECO:0000305|PubMed:7590226"
FT REPEAT 1314..1339
FT /note="HCF repeat 6"
FT /evidence="ECO:0000305|PubMed:7590226"
FT REPEAT 1349..1374
FT /note="HCF repeat 7; degenerate"
FT /evidence="ECO:0000305|PubMed:7590226"
FT REPEAT 1414..1439
FT /note="HCF repeat 8"
FT /evidence="ECO:0000305|PubMed:7590226"
FT DOMAIN 1797..1888
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1890..2006
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 407..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..550
FT /note="Required for interaction with OGT"
FT /evidence="ECO:0000269|PubMed:21285374"
FT REGION 610..722
FT /note="Interaction with SIN3A"
FT /evidence="ECO:0000269|PubMed:12670868"
FT REGION 750..902
FT /note="Interaction with ZBTB17"
FT /evidence="ECO:0000269|PubMed:12244100"
FT REGION 813..912
FT /note="Interaction with GABP2"
FT /evidence="ECO:0000269|PubMed:10675337"
FT REGION 1292..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1487..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1997..2015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1019..1020
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:7590226"
FT SITE 1081..1082
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:7590226"
FT SITE 1110..1111
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000305|PubMed:7590226"
FT SITE 1295..1296
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000305|PubMed:7590226"
FT SITE 1323..1324
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:10920196,
FT ECO:0000305|PubMed:7590226"
FT SITE 1423..1424
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:10920196,
FT ECO:0000305|PubMed:7590226"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 504
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 524
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 813
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1219
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1491
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 1497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1838
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61191"
FT MOD_RES 2005
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 105
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19815555"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19815555"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19815555"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 363
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19815555"
FT CROSSLNK 1807
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19188440"
FT CROSSLNK 1808
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19188440"
FT CROSSLNK 2024
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 382..450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8392914"
FT /id="VSP_002815"
FT VAR_SEQ 428
FT /note="P -> L (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012984"
FT VAR_SEQ 429..2035
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012985"
FT VAR_SEQ 1499
FT /note="P -> PKISSMTETAPRALTTEVPIPAKITVTIANTETSDMPFSAVDILQ
FT (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047138"
FT VARIANT 225
FT /note="S -> N (in MAHCX; unknown pathological significance;
FT dbSNP:rs318240758)"
FT /evidence="ECO:0000269|PubMed:23000143"
FT /id="VAR_069098"
FT VARIANT 1164
FT /note="S -> P (in dbSNP:rs1051152)"
FT /evidence="ECO:0000269|PubMed:7829097"
FT /id="VAR_019813"
FT VARIANT 2004
FT /note="S -> I (in dbSNP:rs6643651)"
FT /id="VAR_050043"
FT MUTAGEN 30
FT /note="P->S: Severely reduces VP16-induced complex (VIC)
FT formation, but retains association with VP16. Unable to
FT rescue proliferation in temperature-sensitive arrested
FT cells. Abolishes interaction with CREB3."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 79
FT /note="P->S: Severely reduces VIC formation, but retains
FT association with VP16. Severely reduces association with
FT CREB3. Unable to rescue proliferation in temperature-
FT sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 82
FT /note="C->D: Moderately reduces VIC formation and
FT association with VP16 and CREB3. Unable to rescue
FT proliferation in temperature-sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 105
FT /note="K->D: Minor reduction in VIC formation and
FT association with VP16 and CREB3. Able to rescue
FT proliferation in temperature-sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 134
FT /note="P->S: Eliminates VIC formation and association with
FT VP16. Weak association with POU2F1. Unable to associate
FT with CREBZF and BAP1. Unable to rescue proliferation in
FT temperature-sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049,
FT ECO:0000269|PubMed:19815555, ECO:0000269|PubMed:9271389"
FT MUTAGEN 137
FT /note="R->D: Eliminates VIC formation. Unable to rescue
FT proliferation in temperature-sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 197
FT /note="P->S: Eliminates VIC formation and association with
FT VP16. Unable to rescue proliferation in temperature-
FT sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 200
FT /note="R->D: Eliminates VIC formation. Unable to rescue
FT proliferation in temperature-sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 228
FT /note="R->D: Eliminates VIC formation and association with
FT VP16. Unable to rescue proliferation in temperature-
FT sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 252
FT /note="P->S: Minor reduction in VIC formation, but retains
FT association with VP16. Unable to rescue proliferation in
FT temperature-sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 255
FT /note="R->D: Eliminates VIC formation. Unable to rescue
FT proliferation in temperature-sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 289..291
FT /note="EWK->AAA: Minor reduction in VIC formation and
FT association with VP16. Weak association with POU2F1.
FT Severely reduces association with CREB3. Able to rescue
FT proliferation in temperature-sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 319
FT /note="P->S: Eliminates VIC formation and association with
FT VP16. Unable to rescue proliferation in temperature-
FT sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 322
FT /note="R->D: Eliminates VIC formation. Unable to rescue
FT proliferation in temperature-sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 338
FT /note="S->A: Moderately reduces association with VP16 and
FT CREB3. Able to rescue proliferation in temperature-
FT sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 344..345
FT /note="RK->AA: Eliminates VIC formation, but only minor
FT reduction in association with VP16. Unable to associate
FT with POU2F1, but only minor reduction in association with
FT CREB3. Able to rescue proliferation in temperature-
FT sensitive arrested cells."
FT /evidence="ECO:0000269|PubMed:10629049"
FT MUTAGEN 1017..1021
FT /note="PCETH->AAAAA: Reduces and disrupts cleavage at HCF
FT repeat."
FT /evidence="ECO:0000269|PubMed:7590226"
FT MUTAGEN 1072
FT /note="V->A: No effect on cleavage at HCF repeat."
FT MUTAGEN 1073
FT /note="R->A: No effect on cleavage at HCF repeat."
FT MUTAGEN 1074
FT /note="V->A: No effect on cleavage at HCF repeat."
FT MUTAGEN 1075
FT /note="C->A: No effect on cleavage at HCF repeat."
FT MUTAGEN 1076
FT /note="S->A: No effect on cleavage at HCF repeat."
FT MUTAGEN 1077
FT /note="N->A: No effect on cleavage at HCF repeat."
FT MUTAGEN 1078
FT /note="P->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1079..1083
FT /note="PCETH->AAAAA: Reduces and disrupts cleavage at HCF
FT repeat."
FT MUTAGEN 1079
FT /note="P->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1080
FT /note="C->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1081
FT /note="E->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1081
FT /note="E->D: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1082
FT /note="T->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1082
FT /note="T->F: Reduces cleavage at HCF repeat."
FT MUTAGEN 1082
FT /note="T->S: Reduces cleavage at HCF repeat."
FT MUTAGEN 1083
FT /note="H->A: Reduces cleavage at HCF repeat."
FT MUTAGEN 1084
FT /note="E->A: No effect on cleavage at HCF repeat."
FT MUTAGEN 1085
FT /note="T->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1086
FT /note="G->A: No effect on cleavage at HCF repeat."
FT MUTAGEN 1087
FT /note="T->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1088
FT /note="T->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1089
FT /note="N->A: Reduces cleavage at HCF repeat."
FT MUTAGEN 1090
FT /note="T->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1092
FT /note="T->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1093
FT /note="T->A: Inactivates cleavage at HCF repeat."
FT MUTAGEN 1095
FT /note="T->A: Reduces cleavage at HCF repeat."
FT MUTAGEN 1096
FT /note="S->A: No effect on cleavage at HCF repeat."
FT MUTAGEN 1097
FT /note="N->A: No effect on cleavage at HCF repeat."
FT CONFLICT 564
FT /note="A -> R (in Ref. 5; CAA55790)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="S -> SVS (in Ref. 5; CAA55790)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="K -> T (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1638
FT /note="V -> E (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1685
FT /note="V -> A (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1735
FT /note="E -> Q (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1873
FT /note="G -> A (in Ref. 5; CAA55790)"
FT /evidence="ECO:0000305"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1813..1825
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1827..1829
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1853..1855
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1861..1870
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1873..1877
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1881..1884
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1895..1902
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1905..1911
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1922..1929
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1935..1937
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1946..1962
FT /evidence="ECO:0007829|PDB:4GO6"
FT HELIX 1963..1966
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1971..1986
FT /evidence="ECO:0007829|PDB:4GO6"
FT STRAND 1995..2000
FT /evidence="ECO:0007829|PDB:4GO6"
SQ SEQUENCE 2035 AA; 208732 MW; 0B0C581E2454631E CRC64;
MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG GNEGIVDELH
VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM VEYGKYSNDL YELQASRWEW
KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY LFGGLANDSE DPKNNIPRYL NDLYILELRP
GSGVVAWDIP ITYGVLPPPR ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIDTL
TWNKPSLSGV APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN
LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ VCCKDLWYLE
TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY DIPATAATAT SPTPNPVPSV
PANPPKSPAP AAAAPAVQPL TQVGITLLPQ AAPAPPTTTT IQVLPTVPGS SISVPTAART
QGVPAVLKVT GPQATTGTPL VTMRPASQAG KAPVTVTSLP AGVRMVVPTQ SAQGTVIGSS
PQMSGMAALA AAAAATQKIP PSSAPTVLSV PAGTTIVKTM AVTPGTTTLP ATVKVASSPV
MVSNPATRML KTAAAQVGTS VSSATNTSTR PIITVHKSGT VTVAQQAQVV TTVVGGVTKT
ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ ASTGPVTQII QTKGPLPAGT
ILKLVTSADG KPTTIITTTQ ASGAGTKPTI LGISSVSPST TKPGTTTIIK TIPMSAIITQ
AGATGVTSSP GIKSPITIIT TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG
QPGTILRTVP MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGGH
STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT MQPVSQPTQV
TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG QGDVQPGTVT LVCSNPPCET
HETGTTNTAT TTVVANLGGH PQPTQVQFVC DRQEAAASLV TSTVGQQNGS VVRVCSNPPC
ETHETGTTNT ATTATSNMAG QHGCSNPPCE THETGTTNTA TTAMSSVGAN HQRDARRACA
AGTPAVIRIS VATGALEAAQ GSKSQCQTRQ TSATSTTMTV MATGAPCSAG PLLGPSMARE
PGGRSPAFVQ LAPLSSKVRL SSPSIKDLPA GRHSHAVSTA AMTRSSVGAG EPRMAPVCES
LQGGSPSTTV TVTALEALLC PSATVTQVCS NPPCETHETG TTNTATTSNA GSAQRVCSNP
PCETHETGTT HTATTATSNG GTGQPEGGQQ PPAGRPCETH QTTSTGTTMS VSVGALLPDA
TSSHRTVESG LEVAAAPSVT PQAGTALLAP FPTQRVCSNP PCETHETGTT HTATTVTSNM
SSNQDPPPAA SDQGEVESTQ GDSVNITSSS AITTTVSSTL TRAVTTVTQS TPVPGPSVPP
PEELQVSPGP RQQLPPRQLL QSASTALMGE SAEVLSASQT PELPAAVDLS STGEPSSGQE
SAGSAVVATV VVQPPPPTQS EVDQLSLPQE LMAEAQAGTT TLMVTGLTPE ELAVTAAAEA
AAQAAATEEA QALAIQAVLQ AAQQAVMGTG EPMDTSEAAA TVTQAELGHL SAEGQEGQAT
TIPIVLTQQE LAALVQQQQL QEAQAQQQHH HLPTEALAPA DSLNDPAIES NCLNELAGTV
PSTVALLPST ATESLAPSNT FVAPQPVVVA SPAKLQAAAT LTEVANGIES LGVKPDLPPP
PSKAPMKKEN QWFDVGVIKG TNVMVTHYFL PPDDAVPSDD DLGTVPDYNQ LKKQELQPGT
AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS KSPDGAHLTW EPPSVTSGKI
IEYSVYLAIQ SSQAGGELKS STPAQLAFMR VYCGPSPSCL VQSSSLSNAH IDYTTKPAII
FRIAARNEKG YGPATQVRWL QETSKDSSGT KPANKRPMSS PEMKSAPKKS KADGQ
