HCFC2_HUMAN
ID HCFC2_HUMAN Reviewed; 792 AA.
AC Q9Y5Z7; B2R8Q5; C0H5X3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Host cell factor 2;
DE Short=HCF-2;
DE AltName: Full=C2 factor;
GN Name=HCFC2;
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] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10196288; DOI=10.1128/jvi.73.5.3930-3940.1999;
RA Johnson K.M., Mahajan S.S., Wilson A.C.;
RT "Herpes simplex virus transactivator VP16 discriminates between HCF-1 and a
RT novel family member, HCF-2.";
RL J. Virol. 73:3930-3940(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Lung;
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 [6]
RP IDENTIFICATION IN A COMPLEX WITH KMT2A.
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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-553, AND IDENTIFICATION BY MASS
RP 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).
CC -!- SUBUNIT: Binds KMT2A/MLL1. Component of the MLL1/MLL complex, at least
CC composed of KMT2A/MLL1, ASH2L, RBBP5, DPY30, WDR5, MEN1, HCFC1 and
CC HCFC2 (PubMed:15199122). Interacts with TASOR (By similarity).
CC {ECO:0000250|UniProtKB:Q9D968, ECO:0000269|PubMed:15199122}.
CC -!- INTERACTION:
CC Q9Y5Z7; Q8IVD9: NUDCD3; NbExp=2; IntAct=EBI-592728, EBI-744342;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10196288}. Nucleus
CC {ECO:0000269|PubMed:10196288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5Z7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5Z7-2; Sequence=VSP_057024, VSP_057025;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Detected at lower
CC levels in spleen, thymus, prostate, ovary, small intestine and colon.
CC {ECO:0000269|PubMed:10196288}.
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DR EMBL; AF117210; AAD27814.1; -; mRNA.
DR EMBL; AK313466; BAG36252.1; -; mRNA.
DR EMBL; AC078819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC089983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97736.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97737.1; -; Genomic_DNA.
DR EMBL; BC006558; AAH06558.1; -; mRNA.
DR EMBL; BC033799; AAH33799.1; -; mRNA.
DR CCDS; CCDS9097.1; -. [Q9Y5Z7-1]
DR RefSeq; NP_037452.1; NM_013320.2. [Q9Y5Z7-1]
DR AlphaFoldDB; Q9Y5Z7; -.
DR SMR; Q9Y5Z7; -.
DR BioGRID; 118959; 93.
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 CORUM; Q9Y5Z7; -.
DR IntAct; Q9Y5Z7; 45.
DR MINT; Q9Y5Z7; -.
DR STRING; 9606.ENSP00000229330; -.
DR iPTMnet; Q9Y5Z7; -.
DR PhosphoSitePlus; Q9Y5Z7; -.
DR BioMuta; HCFC2; -.
DR DMDM; 62900381; -.
DR EPD; Q9Y5Z7; -.
DR jPOST; Q9Y5Z7; -.
DR MassIVE; Q9Y5Z7; -.
DR MaxQB; Q9Y5Z7; -.
DR PaxDb; Q9Y5Z7; -.
DR PeptideAtlas; Q9Y5Z7; -.
DR PRIDE; Q9Y5Z7; -.
DR ProteomicsDB; 7569; -.
DR ProteomicsDB; 86554; -. [Q9Y5Z7-1]
DR Antibodypedia; 1771; 170 antibodies from 21 providers.
DR DNASU; 29915; -.
DR Ensembl; ENST00000229330.9; ENSP00000229330.4; ENSG00000111727.12. [Q9Y5Z7-1]
DR Ensembl; ENST00000544223.6; ENSP00000442942.2; ENSG00000111727.12. [Q9Y5Z7-2]
DR GeneID; 29915; -.
DR KEGG; hsa:29915; -.
DR MANE-Select; ENST00000229330.9; ENSP00000229330.4; NM_013320.3; NP_037452.1.
DR UCSC; uc001tkj.5; human. [Q9Y5Z7-1]
DR CTD; 29915; -.
DR DisGeNET; 29915; -.
DR GeneCards; HCFC2; -.
DR HGNC; HGNC:24972; HCFC2.
DR HPA; ENSG00000111727; Low tissue specificity.
DR MIM; 607926; gene.
DR neXtProt; NX_Q9Y5Z7; -.
DR OpenTargets; ENSG00000111727; -.
DR PharmGKB; PA134868925; -.
DR VEuPathDB; HostDB:ENSG00000111727; -.
DR eggNOG; KOG4152; Eukaryota.
DR GeneTree; ENSGT00940000160733; -.
DR HOGENOM; CLU_002603_1_0_1; -.
DR InParanoid; Q9Y5Z7; -.
DR OMA; GWIPVPE; -.
DR OrthoDB; 416932at2759; -.
DR PhylomeDB; Q9Y5Z7; -.
DR TreeFam; TF314757; -.
DR PathwayCommons; Q9Y5Z7; -.
DR SignaLink; Q9Y5Z7; -.
DR BioGRID-ORCS; 29915; 18 hits in 1084 CRISPR screens.
DR ChiTaRS; HCFC2; human.
DR GenomeRNAi; 29915; -.
DR Pharos; Q9Y5Z7; Tbio.
DR PRO; PR:Q9Y5Z7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y5Z7; protein.
DR Bgee; ENSG00000111727; Expressed in calcaneal tendon and 178 other tissues.
DR ExpressionAtlas; Q9Y5Z7; baseline and differential.
DR Genevisible; Q9Y5Z7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
DR GO; GO:0071339; C:MLL1 complex; IPI:ComplexPortal.
DR GO; GO:0044665; C:MLL1/2 complex; IPI:ComplexPortal.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IPI:ComplexPortal.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0051568; P:histone H3-K4 methylation; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0016032; P:viral process; TAS:ProtInc.
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; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR043536; HCF1/2.
DR InterPro; IPR037932; HCF2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR PANTHER; PTHR46003; PTHR46003; 1.
DR PANTHER; PTHR46003:SF2; PTHR46003:SF2; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR PROSITE; PS50853; FN3; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Isopeptide bond; Kelch repeat; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..792
FT /note="Host cell factor 2"
FT /id="PRO_0000119072"
FT REPEAT 34..79
FT /note="Kelch 1"
FT REPEAT 83..130
FT /note="Kelch 2"
FT REPEAT 207..255
FT /note="Kelch 3"
FT REPEAT 257..303
FT /note="Kelch 4"
FT DOMAIN 359..449
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 583..675
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 677..787
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 399..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 411..412
FT /note="GV -> DQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057024"
FT VAR_SEQ 413..792
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057025"
FT VARIANT 46
FT /note="A -> S (in dbSNP:rs2700500)"
FT /id="VAR_050044"
FT VARIANT 268
FT /note="G -> A (in dbSNP:rs17035206)"
FT /id="VAR_033984"
SQ SEQUENCE 792 AA; 86779 MW; EADF5FF25F70856C CRC64;
MAAPSLLNWR RVSSFTGPVP RARHGHRAVA IRELMIIFGG GNEGIADELH VYNTATNQWF
LPAVRGDIPP GCAAHGFVCD GTRILVFGGM VEYGRYSNEL YELQASRWLW KKVKPHPPPS
GLPPCPRLGH SFSLYGNKCY LFGGLANESE DSNNNVPRYL NDFYELELQH GSGVVGWSIP
VTKGVVPSPR ESHTAVIYCK KDSGSPKMYV FGGMCGARLD DLWQLDLETM SWSKPETKGT
VPLPRSLHTA SVIGNKMYIF GGWVPHKGEN TETSPHDCEW RCTSSFSYLN LDTTEWTTLV
SDSQEDKKNS RPRPRAGHCA VAIGTRLYFW SGRDGYKKAL NSQVCCKDLW YLDTEKPPAP
SQVQLIKATT NSFHVKWDEV STVEGYLLQL STDLPYQAAS SDSSAAPNMQ GVRMDPHRQG
SNNIVPNSIN DTINSTKTEQ PATKETSMKN KPDFKALTDS NAILYPSLAS NASNHNSHVV
DMLRKNEGPH TSANVGVLSS CLDVRTVIPE TSVSSTVSST QTMVTQQTIK TESSSTNGAV
VKDETSLTTF STKSEVDETY ALPATKISRV ETHATATPFS KETPSNPVAT VKAGERQWCD
VGIFKNNTAL VSQFYLLPKG KQSISKVGNA DVPDYSLLKK QDLVPGTGYR FRVAAINGCG
IGPFSKISEF KTCIPGFPGA PSAVRISKNV EGIHLSWEPP TSPSGNILEY SAYLAIRTAQ
IQDNPSQLVF MRIYCGLKTS CIVTAGQLAN AHIDYTSRPA IVFRISAKNE KGYGPATQVR
WLQGNNKKAP LN
