CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008395
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Host cell factor 1 
Protein Synonyms/Alias
 HCF; HCF-1; C1 factor; CFF; VCAF; VP16 accessory protein; 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 
Gene Name
 HCFC1 
Gene Synonyms/Alias
 HCF1; HFC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
105GGMVEYGKYSNDLYEubiquitination[1]
148SFSLVGNKCYLFGGLubiquitination[1, 2]
163ANDSEDPKNNIPRYLubiquitination[1]
244IDTLTWNKPSLSGVAubiquitination[1]
288VKVATHEKEWKCTNTacetylation[3]
363LWYLETEKPPPPARVubiquitination[1, 4]
665TKTITLVKSPISVPGubiquitination[1, 2]
813SGTGAPAKIITAVPKacetylation[3]
813SGTGAPAKIITAVPKubiquitination[1, 2]
836GVTQVVLKGAPGQPGacetylation[3]
836GVTQVVLKGAPGQPGubiquitination[1, 2]
1807PPSKAPMKKENQWFDubiquitination[1]
1808PSKAPMKKENQWFDVubiquitination[1]
1863LQPGTAYKFRVAGINubiquitination[1, 2]
1901PCAIKISKSPDGAHLubiquitination[1, 2]
2005RWLQETSKDSSGTKPacetylation[3]
2028PEMKSAPKKSKADGQacetylation[3]
Reference
 [1] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 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. 
Sequence Annotation
 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.
 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.
 REGION 500 550 Required for interaction with OGT.
 REGION 610 722 Interaction with SIN3A.
 REGION 750 902 Interaction with ZBTB17.
 REGION 813 912 Interaction with GABP2.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 6 6 Phosphoserine.
 MOD_RES 288 288 N6-acetyllysine.
 MOD_RES 411 411 Phosphoserine.
 MOD_RES 666 666 Phosphoserine.
 MOD_RES 669 669 Phosphoserine.
 MOD_RES 813 813 N6-acetyllysine.
 MOD_RES 1205 1205 Phosphoserine.
 MOD_RES 1491 1491 Phosphothreonine.
 MOD_RES 1507 1507 Phosphoserine.
 MOD_RES 2005 2005 N6-acetyllysine.
 CROSSLNK 105 105 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 244 244 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 363 363 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1807 1807 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1808 1808 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 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; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2035 AA 
Protein Sequence
MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG GNEGIVDELH 60
VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM VEYGKYSNDL YELQASRWEW 120
KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY LFGGLANDSE DPKNNIPRYL NDLYILELRP 180
GSGVVAWDIP ITYGVLPPPR ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIDTL 240
TWNKPSLSGV APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN 300
LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ VCCKDLWYLE 360
TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY DIPATAATAT SPTPNPVPSV 420
PANPPKSPAP AAAAPAVQPL TQVGITLLPQ AAPAPPTTTT IQVLPTVPGS SISVPTAART 480
QGVPAVLKVT GPQATTGTPL VTMRPASQAG KAPVTVTSLP AGVRMVVPTQ SAQGTVIGSS 540
PQMSGMAALA AAAAATQKIP PSSAPTVLSV PAGTTIVKTM AVTPGTTTLP ATVKVASSPV 600
MVSNPATRML KTAAAQVGTS VSSATNTSTR PIITVHKSGT VTVAQQAQVV TTVVGGVTKT 660
ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ ASTGPVTQII QTKGPLPAGT 720
ILKLVTSADG KPTTIITTTQ ASGAGTKPTI LGISSVSPST TKPGTTTIIK TIPMSAIITQ 780
AGATGVTSSP GIKSPITIIT TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG 840
QPGTILRTVP MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGGH 900
STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT MQPVSQPTQV 960
TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG QGDVQPGTVT LVCSNPPCET 1020
HETGTTNTAT TTVVANLGGH PQPTQVQFVC DRQEAAASLV TSTVGQQNGS VVRVCSNPPC 1080
ETHETGTTNT ATTATSNMAG QHGCSNPPCE THETGTTNTA TTAMSSVGAN HQRDARRACA 1140
AGTPAVIRIS VATGALEAAQ GSKSQCQTRQ TSATSTTMTV MATGAPCSAG PLLGPSMARE 1200
PGGRSPAFVQ LAPLSSKVRL SSPSIKDLPA GRHSHAVSTA AMTRSSVGAG EPRMAPVCES 1260
LQGGSPSTTV TVTALEALLC PSATVTQVCS NPPCETHETG TTNTATTSNA GSAQRVCSNP 1320
PCETHETGTT HTATTATSNG GTGQPEGGQQ PPAGRPCETH QTTSTGTTMS VSVGALLPDA 1380
TSSHRTVESG LEVAAAPSVT PQAGTALLAP FPTQRVCSNP PCETHETGTT HTATTVTSNM 1440
SSNQDPPPAA SDQGEVESTQ GDSVNITSSS AITTTVSSTL TRAVTTVTQS TPVPGPSVPP 1500
PEELQVSPGP RQQLPPRQLL QSASTALMGE SAEVLSASQT PELPAAVDLS STGEPSSGQE 1560
SAGSAVVATV VVQPPPPTQS EVDQLSLPQE LMAEAQAGTT TLMVTGLTPE ELAVTAAAEA 1620
AAQAAATEEA QALAIQAVLQ AAQQAVMGTG EPMDTSEAAA TVTQAELGHL SAEGQEGQAT 1680
TIPIVLTQQE LAALVQQQQL QEAQAQQQHH HLPTEALAPA DSLNDPAIES NCLNELAGTV 1740
PSTVALLPST ATESLAPSNT FVAPQPVVVA SPAKLQAAAT LTEVANGIES LGVKPDLPPP 1800
PSKAPMKKEN QWFDVGVIKG TNVMVTHYFL PPDDAVPSDD DLGTVPDYNQ LKKQELQPGT 1860
AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS KSPDGAHLTW EPPSVTSGKI 1920
IEYSVYLAIQ SSQAGGELKS STPAQLAFMR VYCGPSPSCL VQSSSLSNAH IDYTTKPAII 1980
FRIAARNEKG YGPATQVRWL QETSKDSSGT KPANKRPMSS PEMKSAPKKS KADGQ 2035 
Gene Ontology
 GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0071339; C:MLL1 complex; IDA:UniProtKB.
 GO:0070688; C:MLL5-L complex; IDA:UniProtKB.
 GO:0043025; C:neuronal cell body; IDA:UniProtKB.
 GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; NAS:ProtInc.
 GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0045787; P:positive regulation of cell cycle; TAS:UniProtKB.
 GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
 GO:0050821; P:protein stabilization; IDA:UniProtKB.
 GO:0043254; P:regulation of protein complex assembly; IDA:UniProtKB.
 GO:0019046; P:release from viral latency; NAS:UniProtKB.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR003961; Fibronectin_type3.
 IPR015916; Gal_Oxidase_b-propeller.
 IPR013783; Ig-like_fold.
 IPR015915; Kelch-typ_b-propeller.
 IPR006652; Kelch_1. 
Pfam
 PF01344; Kelch_1 
SMART
 SM00060; FN3 
PROSITE
  
PRINTS