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Host cell factor 1 (HCF) (HCF-1) (C1 factor) (CFF) (VCAF) (VP16 accessory protein) [Cleaved into: HCF N-terminal chain 1; HCF N-terminal chain 2; HCF N-terminal chain 3; HCF N-terminal chain 4; HCF N-terminal chain 5; HCF N-terminal chain 6; HCF C-terminal chain 1; HCF C-terminal chain 2; HCF C-terminal chain 3; HCF C-terminal chain 4; HCF C-terminal chain 5; HCF C-terminal chain 6]

 HCFC1_HUMAN             Reviewed;        2035 AA.
P51610; Q6P4G5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
30-AUG-2017, entry version 195.
RecName: Full=Host cell factor 1;
Short=HCF;
Short=HCF-1;
AltName: Full=C1 factor;
AltName: Full=CFF;
AltName: Full=VCAF;
AltName: Full=VP16 accessory protein;
Contains:
RecName: Full=HCF N-terminal chain 1;
Contains:
RecName: Full=HCF N-terminal chain 2;
Contains:
RecName: Full=HCF N-terminal chain 3;
Contains:
RecName: Full=HCF N-terminal chain 4;
Contains:
RecName: Full=HCF N-terminal chain 5;
Contains:
RecName: Full=HCF N-terminal chain 6;
Contains:
RecName: Full=HCF C-terminal chain 1;
Contains:
RecName: Full=HCF C-terminal chain 2;
Contains:
RecName: Full=HCF C-terminal chain 3;
Contains:
RecName: Full=HCF C-terminal chain 4;
Contains:
RecName: Full=HCF C-terminal chain 5;
Contains:
RecName: Full=HCF C-terminal chain 6;
Name=HCFC1; Synonyms=HCF1, HFC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Hepatoma;
PubMed=8392914; DOI=10.1016/0092-8674(93)90299-6;
Wilson A.C., Lamarco K., Peterson M.G., Herr W.;
"The VP16 accessory protein HCF is a family of polypeptides processed
from a large precursor protein.";
Cell 74:115-125(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7876203; DOI=10.1074/jbc.270.9.4387;
Kristie T.M., Pomerantz J.L., Twomey T.C., Parent S.A., Sharp P.A.;
"The cellular C1 factor of the herpes simplex virus enhancer complex
is a family of polypeptides.";
J. Biol. Chem. 270:4387-4394(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-2035, AND VARIANT PRO-1164.
TISSUE=Fetal brain;
PubMed=7829097; DOI=10.1006/geno.1994.1455;
Frattini A., Faranda S., Redolfi E., Zucchi I., Villa A.,
Patrosso M.C., Strina D., Susani L., Vezzoni P.;
"Genomic organization of the human VP16 accessory protein, a
housekeeping gene (HCFC1) mapping to Xq28.";
Genomics 23:30-35(1994).
[6]
PROTEIN SEQUENCE OF 1324-1336; 1424-1436 AND 1446-1457, FUNCTION, AND
AUTOCATALYTIC CLEAVAGE.
PubMed=10920196; DOI=10.1073/pnas.160266697;
Vogel J.L., Kristie T.M.;
"Autocatalytic proteolysis of the transcription factor-coactivator C1
(HCF): a potential role for proteolytic regulation of coactivator
function.";
Proc. Natl. Acad. Sci. U.S.A. 97:9425-9430(2000).
[7]
AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF 1017-PRO--HIS-1021 AND
1072-VAL--ASN-1097.
PubMed=7590226; DOI=10.1101/gad.9.20.2445;
Wilson A.C., Peterson M.G., Herr W.;
"The HCF repeat is an unusual proteolytic cleavage signal.";
Genes Dev. 9:2445-2458(1995).
[8]
INTERACTION WITH CREB3 AND VP16, AND MUTAGENESIS OF PRO-134.
PubMed=9271389; DOI=10.1128/MCB.17.9.5117;
Lu R., Yang P., O'Hare P., Misra V.;
"Luman, a new member of the CREB/ATF family, binds to herpes simplex
virus VP16-associated host cellular factor.";
Mol. Cell. Biol. 17:5117-5126(1997).
[9]
INTERACTION WITH CREB3 AND VP16, AND TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=9389645; DOI=10.1101/gad.11.23.3122;
Freiman R.N., Herr W.;
"Viral mimicry: common mode of association with HCF by VP16 and the
cellular protein LZIP.";
Genes Dev. 11:3122-3127(1997).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9990006; DOI=10.1073/pnas.96.4.1229;
Kristie T.M., Vogel J.L., Sears A.E.;
"Nuclear localization of the C1 factor (host cell factor) in sensory
neurons correlates with reactivation of herpes simplex virus from
latency.";
Proc. Natl. Acad. Sci. U.S.A. 96:1229-1233(1999).
[11]
FUNCTION, AND INTERACTION WITH GABP2.
PubMed=10675337; DOI=10.1093/emboj/19.4.683;
Vogel J.L., Kristie T.M.;
"The novel coactivator C1 (HCF) coordinates multiprotein enhancer
formation and mediates transcription activation by GABP.";
EMBO J. 19:683-690(2000).
[12]
SUBCELLULAR LOCATION.
PubMed=10623756; DOI=10.1128/JVI.74.2.934-943.2000;
Lu R., Misra V.;
"Potential role for luman, the cellular homologue of herpes simplex
virus VP16 (alpha gene trans-inducing factor), in herpesvirus
latency.";
J. Virol. 74:934-943(2000).
[13]
INTERACTION WITH SP1.
PubMed=10976766; DOI=10.1023/A:1007177623283;
Gunther M., Laithier M., Brison O.;
"A set of proteins interacting with transcription factor Sp1
identified in a two-hybrid screening.";
Mol. Cell. Biochem. 210:131-142(2000).
[14]
FUNCTION, INTERACTION WITH POU2F1; VP16 AND CREB3, AND MUTAGENESIS OF
PRO-30; PRO-79; CYS-82; LYS-105; PRO-134; ARG-137; PRO-197; ARG-200;
ARG-228; PRO-252; ARG-255; 289-GLU--LYS-291; PRO-319; ARG-322; SER-338
AND 344-ARG-LYS-345.
PubMed=10629049; DOI=10.1128/MCB.20.3.919-928.2000;
Mahajan S.S., Wilson A.C.;
"Mutations in host cell factor 1 separate its role in cell
proliferation from recruitment of VP16 and LZIP.";
Mol. Cell. Biol. 20:919-928(2000).
[15]
FUNCTION.
PubMed=10779346; DOI=10.1128/MCB.20.10.3568-3575.2000;
Scarr R.B., Smith M.R., Beddall M., Sharp P.A.;
"A novel 50-kilodalton fragment of host cell factor 1 (C1) in G(0)
cells.";
Mol. Cell. Biol. 20:3568-3575(2000).
[16]
INTERACTION WITH CREBZF.
PubMed=10871379; DOI=10.1093/nar/28.12.2446;
Lu R., Misra V.;
"Zhangfei: a second cellular protein interacts with herpes simplex
virus accessory factor HCF in a manner similar to Luman and VP16.";
Nucleic Acids Res. 28:2446-2454(2000).
[17]
INTERACTION WITH CREB3.
PubMed=10984507; DOI=10.1073/pnas.190062797;
Luciano R.L., Wilson A.C.;
"N-terminal transcriptional activation domain of LZIP comprises two
LxxLL motifs and the host cell factor-1 binding motif.";
Proc. Natl. Acad. Sci. U.S.A. 97:10757-10762(2000).
[18]
SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH HCFC1R1.
TISSUE=Brain;
PubMed=12235138; DOI=10.1074/jbc.M205440200;
Mahajan S.S., Little M.M., Vazquez R., Wilson A.C.;
"Interaction of HCF-1 with a cellular nuclear export factor.";
J. Biol. Chem. 277:44292-44299(2002).
[19]
FUNCTION, AND INTERACTION WITH ZBTB17.
PubMed=12244100; DOI=10.1074/jbc.M206226200;
Piluso D., Bilan P., Capone J.P.;
"Host cell factor-1 interacts with and antagonizes transactivation by
the cell cycle regulatory factor Miz-1.";
J. Biol. Chem. 277:46799-46808(2002).
[20]
FUNCTION, AND INTERACTION WITH EGR2 AND E2F4.
PubMed=14532282; DOI=10.1074/jbc.M303470200;
Luciano R.L., Wilson A.C.;
"HCF-1 functions as a coactivator for the zinc finger protein
Krox20.";
J. Biol. Chem. 278:51116-51124(2003).
[21]
FUNCTION, AND INTERACTION WITH SIN3A; HDAC1; HDAC2; SUDS3; SAP30;
SIN3B; OGT; SET1; ASH2 AND WDR5.
PubMed=12670868; DOI=10.1101/gad.252103;
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
methyltransferase are tethered together selectively by the cell-
proliferation factor HCF-1.";
Genes Dev. 17:896-911(2003).
[22]
FUNCTION.
PubMed=15190068; DOI=10.1074/jbc.M401255200;
Khurana B., Kristie T.M.;
"A protein sequestering system reveals control of cellular programs by
the transcriptional coactivator HCF-1.";
J. Biol. Chem. 279:33673-33683(2004).
[23]
IDENTIFICATION IN THE MLL1 COMPLEX.
PubMed=15199122; DOI=10.1128/MCB.24.13.5639-5649.2004;
Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J.,
Kitabayashi I., Herr W., Cleary M.L.;
"Leukemia proto-oncoprotein MLL forms a SET1-like histone
methyltransferase complex with menin to regulate Hox gene
expression.";
Mol. Cell. Biol. 24:5639-5649(2004).
[24]
IDENTIFICATION IN THE MLL1 COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[25]
INTERACTION WITH CREBZF AND CREB3.
PubMed=15705566; DOI=10.1074/jbc.M500728200;
Misra V., Rapin N., Akhova O., Bainbridge M., Korchinski P.;
"Zhangfei is a potent and specific inhibitor of the host cell factor-
binding transcription factor Luman.";
J. Biol. Chem. 280:15257-15266(2005).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; THR-1491 AND
SER-1507, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[27]
FUNCTION, AUTOCATALYTIC CLEAVAGE, AND INTERACTION WITH FHL2.
PubMed=16624878; DOI=10.1073/pnas.0602109103;
Vogel J.L., Kristie T.M.;
"Site-specific proteolysis of the transcriptional coactivator HCF-1
can regulate its interaction with protein cofactors.";
Proc. Natl. Acad. Sci. U.S.A. 103:6817-6822(2006).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[29]
FUNCTION.
PubMed=17578910; DOI=10.1073/pnas.0704351104;
Narayanan A., Ruyechan W.T., Kristie T.M.;
"The coactivator host cell factor-1 mediates Set1 and MLL1 H3K4
trimethylation at herpesvirus immediate early promoters for initiation
of infection.";
Proc. Natl. Acad. Sci. U.S.A. 104:10835-10840(2007).
[30]
IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH SETD1A.
PubMed=17998332; DOI=10.1128/MCB.01356-07;
Lee J.H., Skalnik D.G.;
"Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
Histone H3-Lys4 methyltransferase complex to transcription start sites
of transcribed human genes.";
Mol. Cell. Biol. 28:609-618(2008).
[31]
IDENTIFICATION IN SET1 COMPLEX.
PubMed=18838538; DOI=10.1128/MCB.00976-08;
Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
Shilatifard A.;
"Molecular regulation of H3K4 trimethylation by Wdr82, a component of
human Set1/COMPASS.";
Mol. Cell. Biol. 28:7337-7344(2008).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-1205 AND
SER-1507, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[33]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[34]
IDENTIFICATION IN A COMPLEX WITH ZNF335; MKI67; EMSY; MATR3; HSPA8;
TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5.
PubMed=19131338; DOI=10.1074/jbc.M805872200;
Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A.,
Samuels H.H.;
"Identification and characterization of a novel nuclear protein
complex involved in nuclear hormone receptor-mediated gene
regulation.";
J. Biol. Chem. 284:7542-7552(2009).
[35]
UBIQUITINATION AT LYS-105; LYS-163; LYS-244 AND LYS-363,
DEUBIQUITINATION BY BAP1, AND MUTAGENESIS OF PRO-134.
PubMed=19815555; DOI=10.1074/jbc.M109.046755;
Machida Y.J., Machida Y., Vashisht A.A., Wohlschlegel J.A., Dutta A.;
"The deubiquitinating enzyme BAP1 regulates cell growth via
interaction with HCF-1.";
J. Biol. Chem. 284:34179-34188(2009).
[36]
UBIQUITINATION AT LYS-1807 AND LYS-1808, DEUBIQUITINATION BY BAP1, AND
SUBCELLULAR LOCATION.
PubMed=19188440; DOI=10.1128/MCB.01517-08;
Misaghi S., Ottosen S., Izrael-Tomasevic A., Arnott D., Lamkanfi M.,
Lee J., Liu J., O'Rourke K., Dixit V.M., Wilson A.C.;
"Association of C-terminal ubiquitin hydrolase BRCA1-associated
protein 1 with cell cycle regulator host cell factor 1.";
Mol. Cell. Biol. 29:2181-2192(2009).
[37]
IDENTIFICATION IN THE MLL5-L COMPLEX.
PubMed=19377461; DOI=10.1038/nature07954;
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
Kitagawa H., Kato S.;
"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
granulopoiesis.";
Nature 459:455-459(2009).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-1507, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[39]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-813 AND LYS-2005,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[40]
FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, AND
SUBCELLULAR LOCATION.
PubMed=20018852; DOI=10.1074/jbc.C109.087981;
Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L.,
Washburn M.P., Conaway J.W., Conaway R.C.;
"Subunit composition and substrate specificity of a MOF-containing
histone acetyltransferase distinct from the male-specific lethal (MSL)
complex.";
J. Biol. Chem. 285:4268-4272(2010).
[41]
IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT
COMPLEX, INTERACTION WITH OGT; THAP1 AND THAP3, GLYCOSYLATION, AND
FUNCTION.
PubMed=20200153; DOI=10.1074/jbc.M109.072579;
Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L.,
Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B.,
Kristie T.M., Girard J.P.;
"The THAP-zinc finger protein THAP1 associates with coactivator HCF-1
and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias.";
J. Biol. Chem. 285:13364-13371(2010).
[42]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-6; SER-666; SER-669 AND SER-1507, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[44]
GLYCOSYLATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND
INTERACTION WITH OGT.
PubMed=21285374; DOI=10.1073/pnas.1013822108;
Daou S., Mashtalir N., Hammond-Martel I., Pak H., Yu H., Sui G.,
Vogel J.L., Kristie T.M., Affar E.B.;
"Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates
the host cell factor-1 maturation pathway.";
Proc. Natl. Acad. Sci. U.S.A. 108:2747-2752(2011).
[45]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-6; SER-666 AND SER-1507, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[46]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[47]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[48]
GLYCOSYLATION, AND INTERACTION WITH OGT; TET2 AND TET3.
PubMed=23353889; DOI=10.1038/emboj.2012.357;
Deplus R., Delatte B., Schwinn M.K., Defrance M., Mendez J.,
Murphy N., Dawson M.A., Volkmar M., Putmans P., Calonne E., Shih A.H.,
Levine R.L., Bernard O., Mercher T., Solary E., Urh M., Daniels D.L.,
Fuks F.;
"TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT
and SET1/COMPASS.";
EMBO J. 32:645-655(2013).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-598; SER-666;
SER-1205 AND SER-1224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1497; SER-1507 AND
SER-1771, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[51]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-504; ARG-524 AND ARG-1219,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[52]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-282 AND LYS-2024, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[53]
VARIANT MRX3 ASN-225.
PubMed=23000143; DOI=10.1016/j.ajhg.2012.08.011;
Huang L., Jolly L.A., Willis-Owen S., Gardner A., Kumar R.,
Douglas E., Shoubridge C., Wieczorek D., Tzschach A., Cohen M.,
Hackett A., Field M., Froyen G., Hu H., Haas S.A., Ropers H.H.,
Kalscheuer V.M., Corbett M.A., Gecz J.;
"A noncoding, regulatory mutation implicates HCFC1 in nonsyndromic
intellectual disability.";
Am. J. Hum. Genet. 91:694-702(2012).
-!- FUNCTION: Involved in control of the cell cycle. Also antagonizes
transactivation by ZBTB17 and GABP2; represses ZBTB17 activation
of the p15(INK4b) promoter and inhibits its ability to recruit
p300. Coactivator for EGR2 and GABP2. Tethers the chromatin
modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me)
and Sin3 histone deacetylase (HDAC) complexes (involved in the
activation and repression of transcription, respectively)
together. Component of a THAP1/THAP3-HCFC1-OGT complex that is
required for the regulation of the transcriptional activity of
RRM1. As part of the NSL complex it may be involved in acetylation
of nucleosomal histone H4 on several lysine residues. In case of
human herpes simplex virus (HSV) infection, HCFC1 forms a
multiprotein-DNA complex with the viral transactivator protein
VP16 and POU2F1 thereby enabling the transcription of the viral
immediate early genes. {ECO:0000269|PubMed:10629049,
ECO:0000269|PubMed:10675337, ECO:0000269|PubMed:10779346,
ECO:0000269|PubMed:10920196, ECO:0000269|PubMed:12244100,
ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:14532282,
ECO:0000269|PubMed:15190068, ECO:0000269|PubMed:16624878,
ECO:0000269|PubMed:17578910, ECO:0000269|PubMed:20018852,
ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:9990006}.
-!- SUBUNIT: Composed predominantly of six polypeptides ranging from
110 to 150 kDa and a minor 300 kDa polypeptide. The majority of
N- and C-terminal cleavage products remain tightly, albeit non-
covalently, associated. Interacts with POU2F1, CREB3, ZBTB17,
EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A, HDAC1,
HDAC2, SUDS3), SAP30, SIN3B and FHL2. Component of a MLL1 complex,
composed of at least the core components KMT2A/MLL1, ASH2L, HCFC1,
WDR5 and RBBP5, as well as the facultative components BAP18, CHD8,
DPY30, E2F6, HCFC2, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
MEN1, MGA, KAT8, PELP1, PHF20, PRP31, RING2, RUVBL1, RUVBL2,
SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the
MLL5-L complex, composed of at least KMT2E/MLL5, STK38, PPP1CA,
PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Component of a THAP1/THAP3-
HCFC1-OGT complex that is required for the regulation of the
transcriptional activity of RRM1. Interacts directly with OGT; the
interaction, which requires the HCFC1 cleavage site domain,
glycosylates and promotes the proteolytic processing of HCFC1,
retains OGT in the nucleus and impacts the expression of herpes
simplex virus immediate early viral genes. Interacts with TET2 and
TET3. Interacts directly with THAP3 (via its HBM). Interacts (via
the Kelch-repeat domain) with THAP1 (via the HBM); the interaction
recruits HCHC1 to the RRM1. Interacts with HCFC1R1 and THAP11.
Associates with the VP16-induced complex; binding to HCFC1
activates the viral transcriptional activator VP16 for association
with POU2F1, to form a multiprotein-DNA complex responsible for
activating transcription of the viral immediate early genes.
Component of the SET1 complex, at least composed of the catalytic
subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L, CXXC1,
HCFC1 and DPY30. Component of the NSL complex at least composed of
MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and
HCFC1. Interacts with the viral transactivator protein VP16. Part
of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8,
CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex
may have a histone H3-specific methyltransferase activity (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-396176, EBI-396176;
Q9UBL3:ASH2L; NbExp=5; IntAct=EBI-396176, EBI-540797;
Q92560:BAP1; NbExp=4; IntAct=EBI-396176, EBI-1791447;
O43889:CREB3; NbExp=5; IntAct=EBI-396176, EBI-625002;
O43889-2:CREB3; NbExp=4; IntAct=EBI-396176, EBI-625022;
Q9NS37:CREBZF; NbExp=10; IntAct=EBI-396176, EBI-632965;
O43524:FOXO3; NbExp=2; IntAct=EBI-396176, EBI-1644164;
Q06546:GABPA; NbExp=2; IntAct=EBI-396176, EBI-638925;
Q06547:GABPB1; NbExp=3; IntAct=EBI-396176, EBI-618165;
Q06547-2:GABPB1; NbExp=6; IntAct=EBI-396176, EBI-618189;
Q13547:HDAC1; NbExp=2; IntAct=EBI-396176, EBI-301834;
Q92769:HDAC2; NbExp=2; IntAct=EBI-396176, EBI-301821;
O15294:OGT; NbExp=10; IntAct=EBI-396176, EBI-539828;
O15047:SETD1A; NbExp=2; IntAct=EBI-396176, EBI-540779;
Q96ST3:SIN3A; NbExp=6; IntAct=EBI-396176, EBI-347218;
Q96EB6:SIRT1; NbExp=2; IntAct=EBI-396176, EBI-1802965;
P08047:SP1; NbExp=4; IntAct=EBI-396176, EBI-298336;
Q9H7L9:SUDS3; NbExp=2; IntAct=EBI-396176, EBI-540496;
Q96EK4:THAP11; NbExp=2; IntAct=EBI-396176, EBI-1790529;
P61964:WDR5; NbExp=5; IntAct=EBI-396176, EBI-540834;
Q13105:ZBTB17; NbExp=9; IntAct=EBI-396176, EBI-372156;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=HCFC1R1 modulates
its subcellular localization and overexpression of HCFC1R1 leads
to accumulation of HCFC1 in the cytoplasm. Nuclear in general, but
uniquely cytoplasmic in trigeminal ganglia, becoming nuclear upon
HSV reactivation from the latent state. Non-processed HCFC1
associates with chromatin. Colocalizes with CREB3 and CANX in the
ER.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P51610-1; Sequence=Displayed;
Name=2;
IsoId=P51610-2; Sequence=VSP_002815;
Note=The N- and the C-terminal fragments fail to associate. No
experimental confirmation available.;
Name=3;
IsoId=P51610-3; Sequence=VSP_012984, VSP_012985;
Note=No experimental confirmation available.;
Name=4;
IsoId=P51610-4; Sequence=VSP_047138;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in fetal tissues and the
adult kidney. Present in all tissues tested.
{ECO:0000269|PubMed:9389645}.
-!- DOMAIN: The HCF repeat is a highly specific proteolytic cleavage
signal. {ECO:0000269|PubMed:12235138}.
-!- DOMAIN: The kelch repeats fold into a 6-bladed kelch beta-
propeller called the beta-propeller domain which mediates
interaction with HCFC1R1. {ECO:0000269|PubMed:12235138}.
-!- PTM: Proteolytically cleaved at one or several PPCE--THET sites
within the HCF repeats. Further cleavage of the primary N- and C-
terminal chains results in a 'trimming' and accumulation of the
smaller chains. Cleavage is promoted by O-glycosylation.
{ECO:0000269|PubMed:21285374}.
-!- PTM: O-glycosylated. GlcNAcylation by OGT promotes proteolytic
processing. {ECO:0000269|PubMed:21285374}.
-!- PTM: Ubiquitinated. Lys-1807 and Lys-1808 are ubiquitinated both
via 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. BAP1
mediated deubiquitination of 'Lys-48'-linked polyubiquitin chains;
deubiquitination by BAP1 does not seem to stabilize the protein.
{ECO:0000269|PubMed:19188440, ECO:0000269|PubMed:19815555}.
-!- DISEASE: Mental retardation, X-linked 3 (MRX3) [MIM:309541]: A
disorder characterized by significantly below average general
intellectual functioning associated with impairments in adaptive
behavior and manifested during the developmental period.
Intellectual deficiency is the only primary symptom of non-
syndromic X-linked mental retardation, while syndromic mental
retardation presents with associated physical, neurological and/or
psychiatric manifestations. {ECO:0000269|PubMed:23000143}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=CAA55790.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; L20010; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC063435; AAH63435.1; -; mRNA.
EMBL; X79198; CAA55790.1; ALT_INIT; Genomic_DNA.
CCDS; CCDS44020.1; -. [P51610-1]
PIR; A40718; A40718.
RefSeq; NP_005325.2; NM_005334.2. [P51610-1]
RefSeq; XP_006724879.1; XM_006724816.2. [P51610-4]
UniGene; Hs.83634; -.
PDB; 4GO6; X-ray; 2.70 A; A/C=360-402, B/D=1806-2035.
PDB; 4N39; X-ray; 1.76 A; B=1082-1097.
PDB; 4N3A; X-ray; 1.88 A; B=1072-1097.
PDB; 4N3B; X-ray; 2.17 A; B=1072-1097.
PDB; 4N3C; X-ray; 2.55 A; B=1072-1097.
PDBsum; 4GO6; -.
PDBsum; 4N39; -.
PDBsum; 4N3A; -.
PDBsum; 4N3B; -.
PDBsum; 4N3C; -.
ProteinModelPortal; P51610; -.
SMR; P51610; -.
BioGrid; 109304; 109.
DIP; DIP-32955N; -.
ELM; P51610; -.
IntAct; P51610; 55.
MINT; MINT-144367; -.
STRING; 9606.ENSP00000309555; -.
iPTMnet; P51610; -.
PhosphoSitePlus; P51610; -.
BioMuta; HCFC1; -.
DMDM; 160332311; -.
EPD; P51610; -.
MaxQB; P51610; -.
PaxDb; P51610; -.
PeptideAtlas; P51610; -.
PRIDE; P51610; -.
TopDownProteomics; P51610-2; -. [P51610-2]
Ensembl; ENST00000310441; ENSP00000309555; ENSG00000172534. [P51610-1]
GeneID; 3054; -.
KEGG; hsa:3054; -.
UCSC; uc004fjp.4; human. [P51610-1]
CTD; 3054; -.
DisGeNET; 3054; -.
GeneCards; HCFC1; -.
H-InvDB; HIX0056221; -.
HGNC; HGNC:4839; HCFC1.
HPA; HPA018312; -.
MalaCards; HCFC1; -.
MIM; 300019; gene.
MIM; 309541; phenotype.
neXtProt; NX_P51610; -.
OpenTargets; ENSG00000172534; -.
Orphanet; 369962; Methylmalonic acidemia with homocystinuria, type cblX.
Orphanet; 777; X-linked non-syndromic intellectual disability.
PharmGKB; PA29215; -.
eggNOG; KOG4152; Eukaryota.
eggNOG; ENOG410Y5AC; LUCA.
GeneTree; ENSGT00760000119086; -.
HOGENOM; HOG000293192; -.
HOVERGEN; HBG051888; -.
InParanoid; P51610; -.
KO; K14966; -.
PhylomeDB; P51610; -.
TreeFam; TF314757; -.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-5689603; UCH proteinases.
SIGNOR; P51610; -.
ChiTaRS; HCFC1; human.
GeneWiki; Host_cell_factor_C1; -.
GenomeRNAi; 3054; -.
PRO; PR:P51610; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000172534; -.
CleanEx; HS_HCFC1; -.
ExpressionAtlas; P51610; baseline and differential.
Genevisible; P51610; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; IPI:CAFA.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:ProtInc.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; TAS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0043254; P:regulation of protein complex assembly; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0019046; P:release from viral latency; NAS:UniProtKB.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
CDD; cd00063; FN3; 2.
Gene3D; 2.120.10.80; -; 1.
Gene3D; 2.130.10.80; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR015916; Gal_Oxidase_b-propeller.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR015915; Kelch-typ_b-propeller.
InterPro; IPR006652; Kelch_1.
Pfam; PF01344; Kelch_1; 1.
SMART; SM00060; FN3; 3.
SUPFAM; SSF49265; SSF49265; 1.
PROSITE; PS50853; FN3; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Autocatalytic cleavage; Cell cycle; Chromatin regulator;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Glycoprotein; Host-virus interaction;
Isopeptide bond; Kelch repeat; Mental retardation; Methylation;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 1423 HCF N-terminal chain 6.
/FTId=PRO_0000016611.
CHAIN 2 1323 HCF N-terminal chain 5.
/FTId=PRO_0000016612.
CHAIN 2 1295 HCF N-terminal chain 4.
/FTId=PRO_0000016613.
CHAIN 2 1110 HCF N-terminal chain 3.
/FTId=PRO_0000016614.
CHAIN 2 1081 HCF N-terminal chain 2.
/FTId=PRO_0000016615.
CHAIN 2 1019 HCF N-terminal chain 1.
/FTId=PRO_0000016616.
CHAIN 1020 2035 HCF C-terminal chain 1.
/FTId=PRO_0000016617.
CHAIN 1082 2035 HCF C-terminal chain 2.
/FTId=PRO_0000016618.
CHAIN 1111 2035 HCF C-terminal chain 3.
/FTId=PRO_0000016619.
CHAIN 1296 2035 HCF C-terminal chain 4.
/FTId=PRO_0000016620.
CHAIN 1324 2035 HCF C-terminal chain 5.
/FTId=PRO_0000016621.
CHAIN 1424 2035 HCF C-terminal chain 6.
/FTId=PRO_0000016622.
REPEAT 44 89 Kelch 1.
REPEAT 93 140 Kelch 2.
REPEAT 148 194 Kelch 3.
REPEAT 217 265 Kelch 4.
REPEAT 266 313 Kelch 5.
DOMAIN 366 466 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REPEAT 1010 1035 HCF repeat 1.
REPEAT 1072 1097 HCF repeat 2.
REPEAT 1101 1126 HCF repeat 3.
REPEAT 1158 1183 HCF repeat 4; degenerate.
REPEAT 1286 1311 HCF repeat 5.
REPEAT 1314 1339 HCF repeat 6.
REPEAT 1349 1374 HCF repeat 7; degenerate.
REPEAT 1414 1439 HCF repeat 8.
DOMAIN 1797 1888 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1890 2006 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 500 550 Required for interaction with OGT.
REGION 610 722 Interaction with SIN3A.
{ECO:0000269|PubMed:12670868}.
REGION 750 902 Interaction with ZBTB17.
{ECO:0000269|PubMed:12244100}.
REGION 813 912 Interaction with GABP2.
{ECO:0000269|PubMed:10675337}.
SITE 1019 1020 Cleavage; by autolysis.
SITE 1081 1082 Cleavage; by autolysis.
SITE 1110 1111 Cleavage; by autolysis.
SITE 1295 1296 Cleavage; by autolysis.
SITE 1323 1324 Cleavage; by autolysis.
SITE 1423 1424 Cleavage; by autolysis.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 288 288 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 504 504 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 524 524 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 666 666 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 813 813 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1205 1205 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1219 1219 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1224 1224 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1491 1491 Phosphothreonine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 1497 1497 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1507 1507 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 1771 1771 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1838 1838 Phosphoserine.
{ECO:0000250|UniProtKB:Q61191}.
MOD_RES 2005 2005 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 105 105 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19815555}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19815555}.
CROSSLNK 244 244 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19815555}.
CROSSLNK 282 282 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 363 363 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19815555}.
CROSSLNK 1807 1807 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19188440}.
CROSSLNK 1808 1808 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19188440}.
CROSSLNK 2024 2024 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 382 450 Missing (in isoform 2).
{ECO:0000303|PubMed:8392914}.
/FTId=VSP_002815.
VAR_SEQ 428 428 P -> L (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012984.
VAR_SEQ 429 2035 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012985.
VAR_SEQ 1499 1499 P -> PKISSMTETAPRALTTEVPIPAKITVTIANTETSDM
PFSAVDILQ (in isoform 4). {ECO:0000305}.
/FTId=VSP_047138.
VARIANT 225 225 S -> N (in MRX3; dbSNP:rs318240758).
{ECO:0000269|PubMed:23000143}.
/FTId=VAR_069098.
VARIANT 1164 1164 S -> P (in dbSNP:rs1051152).
{ECO:0000269|PubMed:7829097}.
/FTId=VAR_019813.
VARIANT 2004 2004 S -> I (in dbSNP:rs6643651).
/FTId=VAR_050043.
MUTAGEN 30 30 P->S: Severely reduces VP16-induced
complex (VIC) formation, but retains
association with VP16. Unable to rescue
proliferation in temperature-sensitive
arrested cells. Abolishes interaction
with CREB3.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 79 79 P->S: Severely reduces VIC formation, but
retains association with VP16. Severely
reduces association with CREB3. Unable to
rescue proliferation in temperature-
sensitive arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 82 82 C->D: Moderately reduces VIC formation
and association with VP16 and CREB3.
Unable to rescue proliferation in
temperature-sensitive arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 105 105 K->D: Minor reduction in VIC formation
and association with VP16 and CREB3. Able
to rescue proliferation in temperature-
sensitive arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 134 134 P->S: Eliminates VIC formation and
association with VP16. Weak association
with POU2F1. Unable to associate with
CREBZF and BAP1. Unable to rescue
proliferation in temperature-sensitive
arrested cells.
{ECO:0000269|PubMed:10629049,
ECO:0000269|PubMed:19815555,
ECO:0000269|PubMed:9271389}.
MUTAGEN 137 137 R->D: Eliminates VIC formation. Unable to
rescue proliferation in temperature-
sensitive arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 197 197 P->S: Eliminates VIC formation and
association with VP16. Unable to rescue
proliferation in temperature-sensitive
arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 200 200 R->D: Eliminates VIC formation. Unable to
rescue proliferation in temperature-
sensitive arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 228 228 R->D: Eliminates VIC formation and
association with VP16. Unable to rescue
proliferation in temperature-sensitive
arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 252 252 P->S: Minor reduction in VIC formation,
but retains association with VP16. Unable
to rescue proliferation in temperature-
sensitive arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 255 255 R->D: Eliminates VIC formation. Unable to
rescue proliferation in temperature-
sensitive arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 289 291 EWK->AAA: Minor reduction in VIC
formation and association with VP16. Weak
association with POU2F1. Severely reduces
association with CREB3. Able to rescue
proliferation in temperature-sensitive
arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 319 319 P->S: Eliminates VIC formation and
association with VP16. Unable to rescue
proliferation in temperature-sensitive
arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 322 322 R->D: Eliminates VIC formation. Unable to
rescue proliferation in temperature-
sensitive arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 338 338 S->A: Moderately reduces association with
VP16 and CREB3. Able to rescue
proliferation in temperature-sensitive
arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 344 345 RK->AA: Eliminates VIC formation, but
only minor reduction in association with
VP16. Unable to associate with POU2F1,
but only minor reduction in association
with CREB3. Able to rescue proliferation
in temperature-sensitive arrested cells.
{ECO:0000269|PubMed:10629049}.
MUTAGEN 1017 1021 PCETH->AAAAA: Reduces and disrupts
cleavage at HCF repeat.
{ECO:0000269|PubMed:7590226}.
MUTAGEN 1072 1072 V->A: No effect on cleavage at HCF
repeat.
MUTAGEN 1073 1073 R->A: No effect on cleavage at HCF
repeat.
MUTAGEN 1074 1074 V->A: No effect on cleavage at HCF
repeat.
MUTAGEN 1075 1075 C->A: No effect on cleavage at HCF
repeat.
MUTAGEN 1076 1076 S->A: No effect on cleavage at HCF
repeat.
MUTAGEN 1077 1077 N->A: No effect on cleavage at HCF
repeat.
MUTAGEN 1078 1078 P->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1079 1083 PCETH->AAAAA: Reduces and disrupts
cleavage at HCF repeat.
MUTAGEN 1079 1079 P->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1080 1080 C->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1081 1081 E->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1081 1081 E->D: Inactivates cleavage at HCF repeat.
MUTAGEN 1082 1082 T->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1082 1082 T->F: Reduces cleavage at HCF repeat.
MUTAGEN 1082 1082 T->S: Reduces cleavage at HCF repeat.
MUTAGEN 1083 1083 H->A: Reduces cleavage at HCF repeat.
MUTAGEN 1084 1084 E->A: No effect on cleavage at HCF
repeat.
MUTAGEN 1085 1085 T->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1086 1086 G->A: No effect on cleavage at HCF
repeat.
MUTAGEN 1087 1087 T->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1088 1088 T->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1089 1089 N->A: Reduces cleavage at HCF repeat.
MUTAGEN 1090 1090 T->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1092 1092 T->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1093 1093 T->A: Inactivates cleavage at HCF repeat.
MUTAGEN 1095 1095 T->A: Reduces cleavage at HCF repeat.
MUTAGEN 1096 1096 S->A: No effect on cleavage at HCF
repeat.
MUTAGEN 1097 1097 N->A: No effect on cleavage at HCF
repeat.
CONFLICT 564 564 A -> R (in Ref. 5; CAA55790).
{ECO:0000305}.
CONFLICT 603 603 S -> SVS (in Ref. 5; CAA55790).
{ECO:0000305}.
CONFLICT 665 665 K -> T (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1638 1638 V -> E (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1685 1685 V -> A (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1735 1735 E -> Q (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1873 1873 G -> A (in Ref. 5; CAA55790).
{ECO:0000305}.
STRAND 368 375 {ECO:0000244|PDB:4GO6}.
STRAND 380 385 {ECO:0000244|PDB:4GO6}.
STRAND 391 399 {ECO:0000244|PDB:4GO6}.
STRAND 1813 1825 {ECO:0000244|PDB:4GO6}.
STRAND 1827 1829 {ECO:0000244|PDB:4GO6}.
STRAND 1853 1855 {ECO:0000244|PDB:4GO6}.
STRAND 1861 1870 {ECO:0000244|PDB:4GO6}.
STRAND 1873 1877 {ECO:0000244|PDB:4GO6}.
STRAND 1881 1884 {ECO:0000244|PDB:4GO6}.
STRAND 1895 1902 {ECO:0000244|PDB:4GO6}.
STRAND 1905 1911 {ECO:0000244|PDB:4GO6}.
STRAND 1922 1929 {ECO:0000244|PDB:4GO6}.
STRAND 1935 1937 {ECO:0000244|PDB:4GO6}.
STRAND 1946 1962 {ECO:0000244|PDB:4GO6}.
HELIX 1963 1966 {ECO:0000244|PDB:4GO6}.
STRAND 1971 1986 {ECO:0000244|PDB:4GO6}.
STRAND 1995 2000 {ECO:0000244|PDB:4GO6}.
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


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