HCFC1_MOUSE
ID HCFC1_MOUSE Reviewed; 2045 AA.
AC Q61191; B1AUX1; Q684R1; Q7TSB0; Q8C2D0; Q9QWH2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Host cell factor 1 {ECO:0000303|PubMed:9334261};
DE Short=HCF {ECO:0000303|PubMed:9334261};
DE Short=HCF-1 {ECO:0000250|UniProtKB:P51610};
DE AltName: Full=C1 factor {ECO:0000303|PubMed:9334261};
DE Contains:
DE RecName: Full=HCF N-terminal chain 1 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF N-terminal chain 2 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF N-terminal chain 3 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF N-terminal chain 4 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF N-terminal chain 5 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF N-terminal chain 6 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF C-terminal chain 1 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF C-terminal chain 2 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF C-terminal chain 3 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF C-terminal chain 4 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF C-terminal chain 5 {ECO:0000250|UniProtKB:P51610};
DE Contains:
DE RecName: Full=HCF C-terminal chain 6 {ECO:0000250|UniProtKB:P51610};
GN Name=Hcfc1 {ECO:0000312|MGI:MGI:105942};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB01163.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal liver {ECO:0000269|PubMed:9334261};
RX PubMed=9334261; DOI=10.1074/jbc.272.42.26749;
RA Kristie T.M.;
RT "The mouse homologue of the human transcription factor C1 (host cell
RT factor). Conservation of forms and function.";
RL J. Biol. Chem. 272:26749-26755(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAF25305.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH53742.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb mesenchyme {ECO:0000269|PubMed:15489334};
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 [LARGE SCALE MRNA] OF 1-209.
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6] {ECO:0000305, ECO:0000312|EMBL:CAF25305.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-520.
RC STRAIN=NMRI; TISSUE=Embryo;
RA Kolb A.A., Mehrle A., Bechtel S., Wellenreuther R., Simpson J.,
RA Pepperkok R., Wiemann S., Poustka A.;
RT "Towards functional annotation of all Xq28 genes: expression and
RT intracellular localization analyses reveal novel candidates for disease
RT genes.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000269|PubMed:9990006};
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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [9]
RP INTERACTION WITH THAP11.
RX PubMed=18585351; DOI=10.1016/j.cell.2008.05.047;
RA Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F.,
RA Songyang Z., Thomson J.A., Zwaka T.P.;
RT "Ronin is essential for embryogenesis and the pluripotency of mouse
RT embryonic stem cells.";
RL Cell 133:1162-1174(2008).
RN [10]
RP ERRATUM OF PUBMED:18585351.
RA Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F.,
RA Songyang Z., Thomson J.A., Zwaka T.P.;
RL Cell 134:692-692(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-1516 AND SER-1848,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-504; ARG-524 AND ARG-1216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
CC -!- FUNCTION: Transcriptional coregulator (By similarity). Involved in
CC control of the cell cycle (PubMed:9334261, PubMed:9990006). Also
CC antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17
CC activation of the p15(INK4b) promoter and inhibits its ability to
CC recruit p300 (By similarity). Coactivator for EGR2 and GABP2 (By
CC similarity). Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-
CC 4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC)
CC complexes (involved in the activation and repression of transcription
CC respectively) together (By similarity). As part of the NSL complex it
CC may be involved in acetylation of nucleosomal histone H4 on several
CC lysine residues (By similarity). Recruits KMT2E to E2F1 responsive
CC promoters promoting transcriptional activation and thereby facilitates
CC G1 to S phase transition (By similarity). Modulates expression of
CC homeobox protein PDX1, perhaps acting in concert with transcription
CC factor E2F1, thereby regulating pancreatic beta-cell growth and
CC glucose-stimulated insulin secretion (By similarity). May negatively
CC modulate transcriptional activity of FOXO3 (By similarity).
CC {ECO:0000250|UniProtKB:D3ZN95, ECO:0000250|UniProtKB:P51610,
CC ECO:0000269|PubMed:9334261, ECO:0000269|PubMed:9990006}.
CC -!- SUBUNIT: Composed predominantly of six polypeptides ranging from 110 to
CC 150 kDa and a minor 300 kDa polypeptide (PubMed:9334261). The majority
CC of N- and C-terminal cleavage products remain tightly, albeit non-
CC covalently, associated (By similarity). Interacts with POU2F1, CREB3,
CC ZBTB17, EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A,
CC HDAC1, HDAC2, SUDS3), SAP30, SIN3B and FHL2 (By similarity). Component
CC of a MLL1 complex, composed of at least the core components KMT2A/MLL1,
CC ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components
CC BAP18, CHD8, DPY30, E2F6, HCFC2, HSP70, INO80C, KANSL1, LAS1L, MAX,
CC MCRS1, MEN1, MGA, KAT8, PELP1, PHF20, PRP31, RING2, RUVBL1, RUVBL2,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (By similarity).
CC Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the
CC regulation of the transcriptional activity of RRM1 (By similarity).
CC Interacts directly with THAP3 (via its HBM) (By similarity). Interacts
CC (via the Kelch-repeat domain) with THAP1 (via the HBM); the interaction
CC recruits HCHC1 to the RRM1 (By similarity). Interacts directly with
CC OGT; the interaction, which requires the HCFC1 cleavage site domain,
CC glycosylates and promotes the proteolytic processing of HCFC1 and
CC retains OGT in the nucleus (By similarity). Component of the SET1
CC complex, at least composed of the catalytic subunit (SETD1A or SETD1B),
CC WDR5, WDR82, RBBP5, ASH2L, CXXC1, HCFC1 and DPY30 (By similarity).
CC Component of the NSL complex at least composed of MOF/KAT8, KANSL1,
CC KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (By similarity).
CC Component of a complex at least composed of ZNF335, HCFC1, CCAR2, EMSY,
CC MKI67, RBBP5, ASH2L and WDR5; the complex is formed as a result of
CC interactions between components of a nuclear receptor-mediated
CC transcription complex and a histone methylation complex (By
CC similarity). Within the complex interacts with ZNF335 (By similarity).
CC Interacts with TET2 and TET3 (By similarity). Interacts with HCFC1R1
CC (By similarity). Interacts with THAP11 (PubMed:18585351). Interacts
CC (via Kelch domain) with KMT2E (via HBM motif) (By similarity).
CC Interacts with E2F1 (By similarity). {ECO:0000250|UniProtKB:P51610,
CC ECO:0000269|PubMed:18585351, ECO:0000269|PubMed:9334261}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51610}. Cytoplasm
CC {ECO:0000269|PubMed:9990006}. Note=HCFC1R1 modulates its subcellular
CC localization and overexpression of HCFC1R1 leads to accumulation of
CC HCFC1 in the cytoplasm (By similarity). Localizes to cytoplasm in
CC trigeminal ganglia (PubMed:9990006). Non-processed HCFC1 associates
CC with chromatin. Colocalizes with CREB3 and CANX in the ER.
CC {ECO:0000250|UniProtKB:P51610, ECO:0000269|PubMed:9990006}.
CC -!- SUBCELLULAR LOCATION: Note=(Microbial infection) In trigeminal ganglia,
CC becoming nuclear upon HSV reactivation from the latent state.
CC {ECO:0000269|PubMed:9990006}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, pituitary gland, skeletal
CC muscle, kidney, eye and brain (at protein level). Also observed at low
CC level in heart, spleen and lung. {ECO:0000269|PubMed:9334261,
CC ECO:0000269|PubMed:9990006}.
CC -!- DOMAIN: The HCF repeat is a highly specific proteolytic cleavage
CC signal. {ECO:0000250|UniProtKB:P51610}.
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:0000250|UniProtKB:P51610}.
CC -!- PTM: Proteolytically cleaved at one or several PPCE--THET sites within
CC the HCF repeats. Further cleavage of the primary N- and C-terminal
CC chains results in a 'trimming' and accumulation of the smaller chains.
CC Cleavage is promoted by O-glycosylation.
CC {ECO:0000250|UniProtKB:P51610}.
CC -!- PTM: O-glycosylated. GlcNAcylation by OGT promotes proteolytic
CC processing. {ECO:0000250|UniProtKB:P51610}.
CC -!- PTM: Ubiquitinated. Lys-1817 and Lys-1818 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:0000250|UniProtKB:P51610}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF25305.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U53925; AAB01163.1; -; Genomic_DNA.
DR EMBL; U80821; AAD09225.1; -; Genomic_DNA.
DR EMBL; AL672002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466650; EDL29851.1; -; Genomic_DNA.
DR EMBL; BC053742; AAH53742.1; -; mRNA.
DR EMBL; AK088827; BAC40597.1; -; mRNA.
DR EMBL; AJ627036; CAF25305.1; ALT_FRAME; mRNA.
DR CCDS; CCDS30218.1; -.
DR RefSeq; NP_032250.2; NM_008224.4.
DR PDB; 2M26; NMR; -; A=1896-2020.
DR PDBsum; 2M26; -.
DR AlphaFoldDB; Q61191; -.
DR BMRB; Q61191; -.
DR SMR; Q61191; -.
DR BioGRID; 200248; 27.
DR ComplexPortal; CPX-875; NSL histone acetyltransferase complex.
DR IntAct; Q61191; 3.
DR MINT; Q61191; -.
DR STRING; 10090.ENSMUSP00000033761; -.
DR iPTMnet; Q61191; -.
DR PhosphoSitePlus; Q61191; -.
DR SwissPalm; Q61191; -.
DR EPD; Q61191; -.
DR jPOST; Q61191; -.
DR MaxQB; Q61191; -.
DR PaxDb; Q61191; -.
DR PeptideAtlas; Q61191; -.
DR PRIDE; Q61191; -.
DR ProteomicsDB; 269817; -.
DR Antibodypedia; 7165; 260 antibodies from 33 providers.
DR DNASU; 15161; -.
DR Ensembl; ENSMUST00000033761; ENSMUSP00000033761; ENSMUSG00000031386.
DR GeneID; 15161; -.
DR KEGG; mmu:15161; -.
DR UCSC; uc009tnm.2; mouse.
DR CTD; 3054; -.
DR MGI; MGI:105942; Hcfc1.
DR VEuPathDB; HostDB:ENSMUSG00000031386; -.
DR eggNOG; KOG4152; Eukaryota.
DR GeneTree; ENSGT00940000161383; -.
DR HOGENOM; CLU_002603_0_0_1; -.
DR InParanoid; Q61191; -.
DR OMA; GPCGTIH; -.
DR TreeFam; TF314757; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR BioGRID-ORCS; 15161; 28 hits in 77 CRISPR screens.
DR ChiTaRS; Hcfc1; mouse.
DR PRO; PR:Q61191; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q61191; protein.
DR Bgee; ENSMUSG00000031386; Expressed in undifferentiated genital tubercle and 256 other tissues.
DR ExpressionAtlas; Q61191; baseline and differential.
DR Genevisible; Q61191; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0044665; C:MLL1/2 complex; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0044545; C:NSL complex; ISO:MGI.
DR GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IDA:ComplexPortal.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0019046; P:release from viral latency; IDA: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; 2.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Autocatalytic cleavage; Cell cycle;
KW Chromatin regulator; Cytoplasm; Glycoprotein; Isopeptide bond;
KW Kelch repeat; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CHAIN 2..1432
FT /note="HCF N-terminal chain 6"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016635"
FT CHAIN 2..1332
FT /note="HCF N-terminal chain 5"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016636"
FT CHAIN 2..1304
FT /note="HCF N-terminal chain 4"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016637"
FT CHAIN 2..1110
FT /note="HCF N-terminal chain 3"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016638"
FT CHAIN 2..1081
FT /note="HCF N-terminal chain 2"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016639"
FT CHAIN 2..1019
FT /note="HCF N-terminal chain 1"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016640"
FT CHAIN 1020..2045
FT /note="HCF C-terminal chain 1"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016641"
FT CHAIN 1082..2045
FT /note="HCF C-terminal chain 2"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016642"
FT CHAIN 1111..2045
FT /note="HCF C-terminal chain 3"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016643"
FT CHAIN 1305..2045
FT /note="HCF C-terminal chain 4"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016644"
FT CHAIN 1333..2045
FT /note="HCF C-terminal chain 5"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016645"
FT CHAIN 1433..2045
FT /note="HCF C-terminal chain 6"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000016646"
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..457
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:0000250|UniProtKB:P51610"
FT REPEAT 1072..1097
FT /note="HCF repeat 2"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT REPEAT 1101..1126
FT /note="HCF repeat 3"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT REPEAT 1157..1182
FT /note="HCF repeat 4; degenerate"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT REPEAT 1295..1320
FT /note="HCF repeat 5"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT REPEAT 1323..1348
FT /note="HCF repeat 6"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT REPEAT 1358..1383
FT /note="HCF repeat 7; degenerate"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT REPEAT 1423..1448
FT /note="HCF repeat 8"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT DOMAIN 1808..1898
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1900..2016
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:0000250|UniProtKB:P51610"
FT REGION 610..722
FT /note="Interaction with SIN3A"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT REGION 750..902
FT /note="Interaction with ZBTB17"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT REGION 813..912
FT /note="Interaction with GABP2"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT REGION 1219..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1494..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2004..2045
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 1225..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2007..2025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1019..1020
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT SITE 1081..1082
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT SITE 1110..1111
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT SITE 1304..1305
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT SITE 1332..1333
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT SITE 1432..1433
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
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:0000250|UniProtKB:P51610"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 813
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 1204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 1216
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 1500
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 1506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 1516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 1848
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2015
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CROSSLNK 105
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CROSSLNK 363
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CROSSLNK 1817
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CROSSLNK 1818
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CROSSLNK 2034
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CONFLICT 483
FT /note="V -> R (in Ref. 1; AAB01163/AAD09225)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="P -> S (in Ref. 6; CAF25305)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..568
FT /note="VL -> AW (in Ref. 1; AAB01163/AAD09225)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="Q -> H (in Ref. 1; AAD09225)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104
FT /note="C -> S (in Ref. 1; AAB01163/AAD09225)"
FT /evidence="ECO:0000305"
FT CONFLICT 1230
FT /note="G -> A (in Ref. 1; AAB01163/AAD09225)"
FT /evidence="ECO:0000305"
FT STRAND 1897..1899
FT /evidence="ECO:0007829|PDB:2M26"
FT STRAND 1905..1912
FT /evidence="ECO:0007829|PDB:2M26"
FT STRAND 1915..1921
FT /evidence="ECO:0007829|PDB:2M26"
FT STRAND 1924..1926
FT /evidence="ECO:0007829|PDB:2M26"
FT STRAND 1930..1938
FT /evidence="ECO:0007829|PDB:2M26"
FT STRAND 1965..1968
FT /evidence="ECO:0007829|PDB:2M26"
FT HELIX 1973..1977
FT /evidence="ECO:0007829|PDB:2M26"
FT STRAND 1984..1997
FT /evidence="ECO:0007829|PDB:2M26"
FT STRAND 2005..2010
FT /evidence="ECO:0007829|PDB:2M26"
SQ SEQUENCE 2045 AA; 210437 MW; AD0EC38C9DB19F22 CRC64;
MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG GNEGIVDELH
VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM VEYGKYSNDL YELQASRWEW
KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY LFGGLANDSE DPKNNIPRYL NDLYILELRP
GSGVVAWDIP ITYGVLPPPR ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIETL
TWNKPSLSGV APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN
LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ VCCKDLWYLE
TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY DIPATAATAT SPTPNPVPSV
PANPPKSPAP AAAAPAVQPL TQVGITLVPQ AATAPPSTTT IQVLPTVPGS SISVPTAART
QGVPAVLKVT GPQATTGTPL VTMRPASQAG KAPVTVTSLP ASVRMVVPTQ SAQGTVIGSN
PQMSGMAALA AAAAATQKIP PSSAPTVLSV PAGTTIVKTV AVTPGTTTLP ATVKVASSPV
MVSNPATRML KTAAAQVGTS VSSAANTSTR 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 STSLAGAGAH
STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT MQPVSQPTQV
TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG QGDVQPGTVT LVCSNPPCET
HETGTTNTAT TTVVANLGGH PQPTQVQFVC DRQETAASLV TSAVGQQNGN VVRVCSNPPC
ETHETGTTNT ATTATSNMAG QHGCSNPPCE THETGTTSTA TTAMSSMGTG QQRDTRRTTN
TPTVVRITVA PGALERVQGT VKPQCQTQQT NMTTTTMTVQ ATGAPCSAGP LLRPSVALES
GSHSPAFVQL ALPSVRVGLS GPSSKDMPTG RQPETYHTYT TNTPTTTRSI MVAGELGAAR
VVPTSTYESL QASSPSSTMT MTALEALLCP SATVTQVCSN PPCETHETGT TNTATTSNAG
SAQRVCSNPP CETHETGTTH TATTATSNGG AGQPEGGQQP ASGHPCETHQ TTSTGTTMSV
SVGTLIPDAT SSHGTLESGL EVVAVPTVTS QAGSTLLASF PTQRVCSNPP CETHETGTTH
TATTVTSNMS SNQDPPPAAS DQGEVASTQG DSTNITSASA ITTSVSSTLP RAVTTVTQST
PVPGPSVPPP EELQVSPGPR QQLPPRQLLQ SASTPLMGES TEVLSASQTP ELQAAVDLSS
TGDPSSGQEP TTSAVVATVV VQPPPPTQSE VDQLSLPQEL MAEAQAGTTT LMVTGLTPEE
LAVTAAAEAA AQAAATEEAQ ALAIQAVLQA AQQAVMGTGE PMDTSEAAAA VTQAELGHLS
AEGQEGQATT IPIVLTQQEL AALVQQQQQL QEAQAQAQQQ HHLPTEALAP ADSLNDPSIE
SNCLNELASA VPSTVALLPS TATESLAPSN TFVAPQPVVA SPAKMQAAAT LTEVANGIES
LGVKPDLPPP PSKAPVKKEN QWFDVGVIKG TSVMVTHYFL PPDDAVQSDD DSGTVPDYNQ
LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS KSPDGAHLTW
EPPSVTSGKI IEYSVYLAIQ SSQASGEPKS STPAQLAFMR VYCGPSPSCL VQSSSLSNAH
IDYTTKPAII FRIAARNEKG YGPATQVRWL QETSKDSSGT KPASKRPMSS PEMKSAPKKS
KADGQ
