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P51610

- HCFC1_HUMAN

UniProt

P51610 - HCFC1_HUMAN

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Protein

Host cell factor 1

Gene

HCFC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.13 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1019 – 10202Cleavage; by autolysis
Sitei1081 – 10822Cleavage; by autolysis
Sitei1110 – 11112Cleavage; by autolysis
Sitei1295 – 12962Cleavage; by autolysis
Sitei1323 – 13242Cleavage; by autolysis
Sitei1423 – 14242Cleavage; by autolysis

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  4. sequence-specific DNA binding transcription factor activity Source: ProtInc
  5. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. chromatin organization Source: Reactome
  3. histone H4-K16 acetylation Source: UniProtKB
  4. histone H4-K5 acetylation Source: UniProtKB
  5. histone H4-K8 acetylation Source: UniProtKB
  6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. positive regulation of cell cycle Source: UniProtKB
  8. positive regulation of gene expression Source: UniProtKB
  9. protein stabilization Source: UniProtKB
  10. regulation of protein complex assembly Source: UniProtKB
  11. regulation of transcription, DNA-templated Source: UniProtKB
  12. release from viral latency Source: UniProtKB
  13. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Cell cycle, Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.
REACT_200608. Transcriptional activation of mitochondrial biogenesis.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:HCFC1
Synonyms:HCF1, HFC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:4839. HCFC1.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. histone acetyltransferase complex Source: UniProtKB
  3. membrane Source: UniProtKB
  4. mitochondrion Source: HPA
  5. MLL1 complex Source: UniProtKB
  6. MLL5-L complex Source: UniProtKB
  7. neuronal cell body Source: UniProtKB
  8. nucleoplasm Source: Reactome
  9. nucleus Source: UniProtKB
  10. Set1C/COMPASS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti225 – 2251S → N in MRX3. 1 Publication
Corresponds to variant rs318240758 [ dbSNP | Ensembl ].
VAR_069098

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301P → 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. 1 Publication
Mutagenesisi79 – 791P → S: Severely reduces VIC formation, but retains association with VP16. Severely reduces association with CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi82 – 821C → D: Moderately reduces VIC formation and association with VP16 and CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi105 – 1051K → D: Minor reduction in VIC formation and association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi134 – 1341P → 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. 3 Publications
Mutagenesisi137 – 1371R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi197 – 1971P → S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi200 – 2001R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi228 – 2281R → D: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi252 – 2521P → S: Minor reduction in VIC formation, but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi255 – 2551R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi289 – 2913EWK → 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. 1 Publication
Mutagenesisi319 – 3191P → S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi322 – 3221R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi338 – 3381S → A: Moderately reduces association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. 1 Publication
Mutagenesisi344 – 3452RK → 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. 1 Publication
Mutagenesisi1017 – 10215PCETH → AAAAA: Reduces and disrupts cleavage at HCF repeat. 1 Publication
Mutagenesisi1072 – 10721V → A: No effect on cleavage at HCF repeat.
Mutagenesisi1073 – 10731R → A: No effect on cleavage at HCF repeat.
Mutagenesisi1074 – 10741V → A: No effect on cleavage at HCF repeat.
Mutagenesisi1075 – 10751C → A: No effect on cleavage at HCF repeat.
Mutagenesisi1076 – 10761S → A: No effect on cleavage at HCF repeat.
Mutagenesisi1077 – 10771N → A: No effect on cleavage at HCF repeat.
Mutagenesisi1078 – 10781P → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1079 – 10835PCETH → AAAAA: Reduces and disrupts cleavage at HCF repeat.
Mutagenesisi1079 – 10791P → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1080 – 10801C → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1081 – 10811E → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1081 – 10811E → D: Inactivates cleavage at HCF repeat.
Mutagenesisi1082 – 10821T → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1082 – 10821T → F: Reduces cleavage at HCF repeat.
Mutagenesisi1082 – 10821T → S: Reduces cleavage at HCF repeat.
Mutagenesisi1083 – 10831H → A: Reduces cleavage at HCF repeat.
Mutagenesisi1084 – 10841E → A: No effect on cleavage at HCF repeat.
Mutagenesisi1085 – 10851T → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1086 – 10861G → A: No effect on cleavage at HCF repeat.
Mutagenesisi1087 – 10871T → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1088 – 10881T → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1089 – 10891N → A: Reduces cleavage at HCF repeat.
Mutagenesisi1090 – 10901T → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1092 – 10921T → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1093 – 10931T → A: Inactivates cleavage at HCF repeat.
Mutagenesisi1095 – 10951T → A: Reduces cleavage at HCF repeat.
Mutagenesisi1096 – 10961S → A: No effect on cleavage at HCF repeat.
Mutagenesisi1097 – 10971N → A: No effect on cleavage at HCF repeat.

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi309541. phenotype.
Orphaneti369962. Methylmalonic acidemia with homocystinuria, type cblX.
777. X-linked non-syndromic intellectual disability.
PharmGKBiPA29215.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 14231422HCF N-terminal chain 6PRO_0000016611Add
BLAST
Chaini2 – 13231322HCF N-terminal chain 5PRO_0000016612Add
BLAST
Chaini2 – 12951294HCF N-terminal chain 4PRO_0000016613Add
BLAST
Chaini2 – 11101109HCF N-terminal chain 3PRO_0000016614Add
BLAST
Chaini2 – 10811080HCF N-terminal chain 2PRO_0000016615Add
BLAST
Chaini2 – 10191018HCF N-terminal chain 1PRO_0000016616Add
BLAST
Chaini1020 – 20351016HCF C-terminal chain 1PRO_0000016617Add
BLAST
Chaini1082 – 2035954HCF C-terminal chain 2PRO_0000016618Add
BLAST
Chaini1111 – 2035925HCF C-terminal chain 3PRO_0000016619Add
BLAST
Chaini1296 – 2035740HCF C-terminal chain 4PRO_0000016620Add
BLAST
Chaini1324 – 2035712HCF C-terminal chain 5PRO_0000016621Add
BLAST
Chaini1424 – 2035612HCF C-terminal chain 6PRO_0000016622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei6 – 61Phosphoserine2 Publications
Cross-linki105 – 105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki163 – 163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki244 – 244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei288 – 2881N6-acetyllysine1 Publication
Cross-linki363 – 363Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei411 – 4111Phosphoserine1 Publication
Modified residuei666 – 6661Phosphoserine5 Publications
Modified residuei669 – 6691Phosphoserine1 Publication
Modified residuei813 – 8131N6-acetyllysine1 Publication
Modified residuei1205 – 12051Phosphoserine1 Publication
Modified residuei1491 – 14911Phosphothreonine1 Publication
Modified residuei1507 – 15071Phosphoserine5 Publications
Cross-linki1807 – 1807Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1808 – 1808Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei2005 – 20051N6-acetyllysine1 Publication

Post-translational modificationi

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.1 Publication
O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing.1 Publication
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.2 Publications

Keywords - PTMi

Acetylation, Autocatalytic cleavage, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP51610.
PaxDbiP51610.
PRIDEiP51610.

PTM databases

PhosphoSiteiP51610.

Expressioni

Tissue specificityi

Highly expressed in fetal tissues and the adult kidney. Present in all tissues tested.1 Publication

Gene expression databases

BgeeiP51610.
CleanExiHS_HCFC1.
ExpressionAtlasiP51610. baseline and differential.
GenevestigatoriP51610.

Organism-specific databases

HPAiHPA018312.

Interactioni

Subunit structurei

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, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity By similarity.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-396176,EBI-396176
ASH2LQ9UBL35EBI-396176,EBI-540797
BAP1Q925603EBI-396176,EBI-1791447
CREB3O438895EBI-396176,EBI-625002
CREB3O43889-24EBI-396176,EBI-625022
CREBZFQ9NS378EBI-396176,EBI-632965
FOXO3O435242EBI-396176,EBI-1644164
GABPAQ065462EBI-396176,EBI-638925
GABPB1Q065473EBI-396176,EBI-618165
GABPB1Q06547-26EBI-396176,EBI-618189
HDAC1Q135472EBI-396176,EBI-301834
HDAC2Q927692EBI-396176,EBI-301821
OGTO152949EBI-396176,EBI-539828
SETD1AO150472EBI-396176,EBI-540779
SIN3AQ96ST36EBI-396176,EBI-347218
SIRT1Q96EB62EBI-396176,EBI-1802965
SP1P080474EBI-396176,EBI-298336
SUDS3Q9H7L92EBI-396176,EBI-540496
THAP11Q96EK42EBI-396176,EBI-1790529
WDR5P619644EBI-396176,EBI-540834
ZBTB17Q131059EBI-396176,EBI-372156

Protein-protein interaction databases

BioGridi109304. 84 interactions.
DIPiDIP-32955N.
IntActiP51610. 45 interactions.
MINTiMINT-144367.
STRINGi9606.ENSP00000309555.

Structurei

Secondary structure

1
2035
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi368 – 3758Combined sources
Beta strandi380 – 3856Combined sources
Beta strandi391 – 3999Combined sources
Beta strandi1813 – 182513Combined sources
Beta strandi1827 – 18293Combined sources
Beta strandi1853 – 18553Combined sources
Beta strandi1861 – 187010Combined sources
Beta strandi1873 – 18775Combined sources
Beta strandi1881 – 18844Combined sources
Beta strandi1895 – 19028Combined sources
Beta strandi1905 – 19117Combined sources
Beta strandi1922 – 19298Combined sources
Beta strandi1946 – 196217Combined sources
Helixi1963 – 19664Combined sources
Beta strandi1971 – 198616Combined sources
Beta strandi1995 – 20006Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GO6X-ray2.70A/C360-402[»]
B/D1806-2035[»]
4N39X-ray1.76B1082-1097[»]
4N3AX-ray1.88B1072-1097[»]
4N3BX-ray2.17B1072-1097[»]
4N3CX-ray2.55B1072-1097[»]
ProteinModelPortaliP51610.
SMRiP51610. Positions 360-400, 1811-2010.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati44 – 8946Kelch 1Add
BLAST
Repeati93 – 14048Kelch 2Add
BLAST
Repeati148 – 19447Kelch 3Add
BLAST
Repeati217 – 26549Kelch 4Add
BLAST
Repeati266 – 31348Kelch 5Add
BLAST
Domaini366 – 466101Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Repeati1010 – 103526HCF repeat 1Add
BLAST
Repeati1072 – 109726HCF repeat 2Add
BLAST
Repeati1101 – 112626HCF repeat 3Add
BLAST
Repeati1158 – 118326HCF repeat 4; degenerateAdd
BLAST
Repeati1286 – 131126HCF repeat 5Add
BLAST
Repeati1314 – 133926HCF repeat 6Add
BLAST
Repeati1349 – 137426HCF repeat 7; degenerateAdd
BLAST
Repeati1414 – 143926HCF repeat 8Add
BLAST
Domaini1797 – 188892Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1890 – 2006117Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni500 – 55051Required for interaction with OGTAdd
BLAST
Regioni610 – 722113Interaction with SIN3AAdd
BLAST
Regioni750 – 902153Interaction with ZBTB17Add
BLAST
Regioni813 – 912100Interaction with GABP2Add
BLAST

Domaini

The HCF repeat is a highly specific proteolytic cleavage signal.1 Publication
The kelch repeats fold into a 6-bladed kelch beta-propeller called the beta-propeller domain which mediates interaction with HCFC1R1.1 Publication

Sequence similaritiesi

Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 5 Kelch repeats.Curated

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000119086.
HOGENOMiHOG000293192.
HOVERGENiHBG051888.
InParanoidiP51610.
KOiK14966.
PhylomeDBiP51610.
TreeFamiTF314757.

Family and domain databases

Gene3Di2.120.10.80. 1 hit.
2.130.10.80. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR003961. Fibronectin_type3.
IPR015916. Gal_Oxidase_b-propeller.
IPR013783. Ig-like_fold.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
[Graphical view]
PfamiPF01344. Kelch_1. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P51610-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG
60 70 80 90 100
GNEGIVDELH VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM
110 120 130 140 150
VEYGKYSNDL YELQASRWEW KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY
160 170 180 190 200
LFGGLANDSE DPKNNIPRYL NDLYILELRP GSGVVAWDIP ITYGVLPPPR
210 220 230 240 250
ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIDTL TWNKPSLSGV
260 270 280 290 300
APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN
310 320 330 340 350
LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ
360 370 380 390 400
VCCKDLWYLE TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY
410 420 430 440 450
DIPATAATAT SPTPNPVPSV PANPPKSPAP AAAAPAVQPL TQVGITLLPQ
460 470 480 490 500
AAPAPPTTTT IQVLPTVPGS SISVPTAART QGVPAVLKVT GPQATTGTPL
510 520 530 540 550
VTMRPASQAG KAPVTVTSLP AGVRMVVPTQ SAQGTVIGSS PQMSGMAALA
560 570 580 590 600
AAAAATQKIP PSSAPTVLSV PAGTTIVKTM AVTPGTTTLP ATVKVASSPV
610 620 630 640 650
MVSNPATRML KTAAAQVGTS VSSATNTSTR PIITVHKSGT VTVAQQAQVV
660 670 680 690 700
TTVVGGVTKT ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ
710 720 730 740 750
ASTGPVTQII QTKGPLPAGT ILKLVTSADG KPTTIITTTQ ASGAGTKPTI
760 770 780 790 800
LGISSVSPST TKPGTTTIIK TIPMSAIITQ AGATGVTSSP GIKSPITIIT
810 820 830 840 850
TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG QPGTILRTVP
860 870 880 890 900
MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGGH
910 920 930 940 950
STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT
960 970 980 990 1000
MQPVSQPTQV TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG
1010 1020 1030 1040 1050
QGDVQPGTVT LVCSNPPCET HETGTTNTAT TTVVANLGGH PQPTQVQFVC
1060 1070 1080 1090 1100
DRQEAAASLV TSTVGQQNGS VVRVCSNPPC ETHETGTTNT ATTATSNMAG
1110 1120 1130 1140 1150
QHGCSNPPCE THETGTTNTA TTAMSSVGAN HQRDARRACA AGTPAVIRIS
1160 1170 1180 1190 1200
VATGALEAAQ GSKSQCQTRQ TSATSTTMTV MATGAPCSAG PLLGPSMARE
1210 1220 1230 1240 1250
PGGRSPAFVQ LAPLSSKVRL SSPSIKDLPA GRHSHAVSTA AMTRSSVGAG
1260 1270 1280 1290 1300
EPRMAPVCES LQGGSPSTTV TVTALEALLC PSATVTQVCS NPPCETHETG
1310 1320 1330 1340 1350
TTNTATTSNA GSAQRVCSNP PCETHETGTT HTATTATSNG GTGQPEGGQQ
1360 1370 1380 1390 1400
PPAGRPCETH QTTSTGTTMS VSVGALLPDA TSSHRTVESG LEVAAAPSVT
1410 1420 1430 1440 1450
PQAGTALLAP FPTQRVCSNP PCETHETGTT HTATTVTSNM SSNQDPPPAA
1460 1470 1480 1490 1500
SDQGEVESTQ GDSVNITSSS AITTTVSSTL TRAVTTVTQS TPVPGPSVPP
1510 1520 1530 1540 1550
PEELQVSPGP RQQLPPRQLL QSASTALMGE SAEVLSASQT PELPAAVDLS
1560 1570 1580 1590 1600
STGEPSSGQE SAGSAVVATV VVQPPPPTQS EVDQLSLPQE LMAEAQAGTT
1610 1620 1630 1640 1650
TLMVTGLTPE ELAVTAAAEA AAQAAATEEA QALAIQAVLQ AAQQAVMGTG
1660 1670 1680 1690 1700
EPMDTSEAAA TVTQAELGHL SAEGQEGQAT TIPIVLTQQE LAALVQQQQL
1710 1720 1730 1740 1750
QEAQAQQQHH HLPTEALAPA DSLNDPAIES NCLNELAGTV PSTVALLPST
1760 1770 1780 1790 1800
ATESLAPSNT FVAPQPVVVA SPAKLQAAAT LTEVANGIES LGVKPDLPPP
1810 1820 1830 1840 1850
PSKAPMKKEN QWFDVGVIKG TNVMVTHYFL PPDDAVPSDD DLGTVPDYNQ
1860 1870 1880 1890 1900
LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS
1910 1920 1930 1940 1950
KSPDGAHLTW EPPSVTSGKI IEYSVYLAIQ SSQAGGELKS STPAQLAFMR
1960 1970 1980 1990 2000
VYCGPSPSCL VQSSSLSNAH IDYTTKPAII FRIAARNEKG YGPATQVRWL
2010 2020 2030
QETSKDSSGT KPANKRPMSS PEMKSAPKKS KADGQ
Length:2,035
Mass (Da):208,732
Last modified:November 13, 2007 - v2
Checksum:i0B0C581E2454631E
GO
Isoform 2 (identifier: P51610-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     382-450: Missing.

Note: The N- and the C-terminal fragments fail to associate. No experimental confirmation available.

Show »
Length:1,966
Mass (Da):201,850
Checksum:iA20A8EA295A5D9B5
GO
Isoform 3 (identifier: P51610-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     428-428: P → L
     429-2035: Missing.

Note: No experimental confirmation available.

Show »
Length:428
Mass (Da):47,189
Checksum:iF8514EA1A9FD8D49
GO
Isoform 4 (identifier: P51610-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1499-1499: P → PKISSMTETAPRALTTEVPIPAKITVTIANTETSDMPFSAVDILQ

Note: No experimental confirmation available.

Show »
Length:2,079
Mass (Da):213,405
Checksum:iF4C85542EA495848
GO

Sequence cautioni

The sequence CAA55790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti564 – 5641A → R in CAA55790. (PubMed:7829097)Curated
Sequence conflicti603 – 6031S → SVS in CAA55790. (PubMed:7829097)Curated
Sequence conflicti665 – 6651K → T no nucleotide entry (PubMed:7876203)Curated
Sequence conflicti1638 – 16381V → E no nucleotide entry (PubMed:7876203)Curated
Sequence conflicti1685 – 16851V → A no nucleotide entry (PubMed:7876203)Curated
Sequence conflicti1735 – 17351E → Q no nucleotide entry (PubMed:7876203)Curated
Sequence conflicti1873 – 18731G → A in CAA55790. (PubMed:7829097)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti225 – 2251S → N in MRX3. 1 Publication
Corresponds to variant rs318240758 [ dbSNP | Ensembl ].
VAR_069098
Natural varianti1164 – 11641S → P.1 Publication
Corresponds to variant rs1051152 [ dbSNP | Ensembl ].
VAR_019813
Natural varianti2004 – 20041S → I.
Corresponds to variant rs6643651 [ dbSNP | Ensembl ].
VAR_050043

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei382 – 45069Missing in isoform 2. 1 PublicationVSP_002815Add
BLAST
Alternative sequencei428 – 4281P → L in isoform 3. 1 PublicationVSP_012984
Alternative sequencei429 – 20351607Missing in isoform 3. 1 PublicationVSP_012985Add
BLAST
Alternative sequencei1499 – 14991P → PKISSMTETAPRALTTEVPI PAKITVTIANTETSDMPFSA VDILQ in isoform 4. CuratedVSP_047138

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L20010 mRNA. No translation available.
U52112 Genomic DNA. No translation available.
BC063435 mRNA. Translation: AAH63435.1.
X79198 Genomic DNA. Translation: CAA55790.1. Different initiation.
CCDSiCCDS44020.1. [P51610-1]
PIRiA40718.
RefSeqiNP_005325.2. NM_005334.2. [P51610-1]
XP_006724879.1. XM_006724816.1. [P51610-4]
UniGeneiHs.83634.

Genome annotation databases

EnsembliENST00000310441; ENSP00000309555; ENSG00000172534. [P51610-1]
GeneIDi3054.
KEGGihsa:3054.
UCSCiuc004fjp.3. human. [P51610-1]

Polymorphism databases

DMDMi160332311.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L20010 mRNA. No translation available.
U52112 Genomic DNA. No translation available.
BC063435 mRNA. Translation: AAH63435.1 .
X79198 Genomic DNA. Translation: CAA55790.1 . Different initiation.
CCDSi CCDS44020.1. [P51610-1 ]
PIRi A40718.
RefSeqi NP_005325.2. NM_005334.2. [P51610-1 ]
XP_006724879.1. XM_006724816.1. [P51610-4 ]
UniGenei Hs.83634.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4GO6 X-ray 2.70 A/C 360-402 [» ]
B/D 1806-2035 [» ]
4N39 X-ray 1.76 B 1082-1097 [» ]
4N3A X-ray 1.88 B 1072-1097 [» ]
4N3B X-ray 2.17 B 1072-1097 [» ]
4N3C X-ray 2.55 B 1072-1097 [» ]
ProteinModelPortali P51610.
SMRi P51610. Positions 360-400, 1811-2010.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109304. 84 interactions.
DIPi DIP-32955N.
IntActi P51610. 45 interactions.
MINTi MINT-144367.
STRINGi 9606.ENSP00000309555.

PTM databases

PhosphoSitei P51610.

Polymorphism databases

DMDMi 160332311.

Proteomic databases

MaxQBi P51610.
PaxDbi P51610.
PRIDEi P51610.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310441 ; ENSP00000309555 ; ENSG00000172534 . [P51610-1 ]
GeneIDi 3054.
KEGGi hsa:3054.
UCSCi uc004fjp.3. human. [P51610-1 ]

Organism-specific databases

CTDi 3054.
GeneCardsi GC0XM153213.
H-InvDB HIX0056221.
HGNCi HGNC:4839. HCFC1.
HPAi HPA018312.
MIMi 300019. gene.
309541. phenotype.
neXtProti NX_P51610.
Orphaneti 369962. Methylmalonic acidemia with homocystinuria, type cblX.
777. X-linked non-syndromic intellectual disability.
PharmGKBi PA29215.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000119086.
HOGENOMi HOG000293192.
HOVERGENi HBG051888.
InParanoidi P51610.
KOi K14966.
PhylomeDBi P51610.
TreeFami TF314757.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.
REACT_200608. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

ChiTaRSi HCFC1. human.
GeneWikii Host_cell_factor_C1.
GenomeRNAii 3054.
NextBioi 12089.
PROi P51610.
SOURCEi Search...

Gene expression databases

Bgeei P51610.
CleanExi HS_HCFC1.
ExpressionAtlasi P51610. baseline and differential.
Genevestigatori P51610.

Family and domain databases

Gene3Di 2.120.10.80. 1 hit.
2.130.10.80. 1 hit.
2.60.40.10. 2 hits.
InterProi IPR003961. Fibronectin_type3.
IPR015916. Gal_Oxidase_b-propeller.
IPR013783. Ig-like_fold.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
[Graphical view ]
Pfami PF01344. Kelch_1. 1 hit.
[Graphical view ]
SMARTi SM00060. FN3. 3 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 1 hit.
PROSITEi PS50853. FN3. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein."
    Wilson A.C., Lamarco K., Peterson M.G., Herr W.
    Cell 74:115-125(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PARTIAL PROTEIN SEQUENCE.
    Tissue: Hepatoma.
  2. "The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides."
    Kristie T.M., Pomerantz J.L., Twomey T.C., Parent S.A., Sharp P.A.
    J. Biol. Chem. 270:4387-4394(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The DNA sequence of the human X chromosome."
    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.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Mammary gland.
  5. "Genomic organization of the human VP16 accessory protein, a housekeeping gene (HCFC1) mapping to Xq28."
    Frattini A., Faranda S., Redolfi E., Zucchi I., Villa A., Patrosso M.C., Strina D., Susani L., Vezzoni P.
    Genomics 23:30-35(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-2035, VARIANT PRO-1164.
    Tissue: Fetal brain.
  6. "Autocatalytic proteolysis of the transcription factor-coactivator C1 (HCF): a potential role for proteolytic regulation of coactivator function."
    Vogel J.L., Kristie T.M.
    Proc. Natl. Acad. Sci. U.S.A. 97:9425-9430(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1324-1336; 1424-1436 AND 1446-1457, FUNCTION, AUTOCATALYTIC CLEAVAGE.
  7. "The HCF repeat is an unusual proteolytic cleavage signal."
    Wilson A.C., Peterson M.G., Herr W.
    Genes Dev. 9:2445-2458(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF 1017-PRO--HIS-1021 AND 1072-VAL--ASN-1097.
  8. "Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cellular factor."
    Lu R., Yang P., O'Hare P., Misra V.
    Mol. Cell. Biol. 17:5117-5126(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CREB3 AND VP16, MUTAGENESIS OF PRO-134.
  9. "Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP."
    Freiman R.N., Herr W.
    Genes Dev. 11:3122-3127(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CREB3 AND VP16, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  10. "Nuclear localization of the C1 factor (host cell factor) in sensory neurons correlates with reactivation of herpes simplex virus from latency."
    Kristie T.M., Vogel J.L., Sears A.E.
    Proc. Natl. Acad. Sci. U.S.A. 96:1229-1233(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "The novel coactivator C1 (HCF) coordinates multiprotein enhancer formation and mediates transcription activation by GABP."
    Vogel J.L., Kristie T.M.
    EMBO J. 19:683-690(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GABP2.
  12. "Potential role for luman, the cellular homologue of herpes simplex virus VP16 (alpha gene trans-inducing factor), in herpesvirus latency."
    Lu R., Misra V.
    J. Virol. 74:934-943(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening."
    Gunther M., Laithier M., Brison O.
    Mol. Cell. Biochem. 210:131-142(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SP1.
  14. "Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP."
    Mahajan S.S., Wilson A.C.
    Mol. Cell. Biol. 20:919-928(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH POU2F1; VP16 AND CREB3, 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.
  15. "A novel 50-kilodalton fragment of host cell factor 1 (C1) in G(0) cells."
    Scarr R.B., Smith M.R., Beddall M., Sharp P.A.
    Mol. Cell. Biol. 20:3568-3575(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Zhangfei: a second cellular protein interacts with herpes simplex virus accessory factor HCF in a manner similar to Luman and VP16."
    Lu R., Misra V.
    Nucleic Acids Res. 28:2446-2454(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CREBZF.
  17. "N-terminal transcriptional activation domain of LZIP comprises two LxxLL motifs and the host cell factor-1 binding motif."
    Luciano R.L., Wilson A.C.
    Proc. Natl. Acad. Sci. U.S.A. 97:10757-10762(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CREB3.
  18. "Interaction of HCF-1 with a cellular nuclear export factor."
    Mahajan S.S., Little M.M., Vazquez R., Wilson A.C.
    J. Biol. Chem. 277:44292-44299(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH HCFC1R1.
    Tissue: Brain.
  19. "Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1."
    Piluso D., Bilan P., Capone J.P.
    J. Biol. Chem. 277:46799-46808(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZBTB17.
  20. "HCF-1 functions as a coactivator for the zinc finger protein Krox20."
    Luciano R.L., Wilson A.C.
    J. Biol. Chem. 278:51116-51124(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EGR2 AND E2F4.
  21. "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
    Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
    Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SIN3A; HDAC1; HDAC2; SUDS3; SAP30; SIN3B; OGT; SET1; ASH2 AND WDR5.
  22. "A protein sequestering system reveals control of cellular programs by the transcriptional coactivator HCF-1."
    Khurana B., Kristie T.M.
    J. Biol. Chem. 279:33673-33683(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression."
    Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I., Herr W., Cleary M.L.
    Mol. Cell. Biol. 24:5639-5649(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1 COMPLEX.
  24. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    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.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1 COMPLEX.
  25. "Zhangfei is a potent and specific inhibitor of the host cell factor-binding transcription factor Luman."
    Misra V., Rapin N., Akhova O., Bainbridge M., Korchinski P.
    J. Biol. Chem. 280:15257-15266(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CREBZF AND CREB3.
  26. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; THR-1491 AND SER-1507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Site-specific proteolysis of the transcriptional coactivator HCF-1 can regulate its interaction with protein cofactors."
    Vogel J.L., Kristie T.M.
    Proc. Natl. Acad. Sci. U.S.A. 103:6817-6822(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOCATALYTIC CLEAVAGE, INTERACTION WITH FHL2.
  28. "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."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "The coactivator host cell factor-1 mediates Set1 and MLL1 H3K4 trimethylation at herpesvirus immediate early promoters for initiation of infection."
    Narayanan A., Ruyechan W.T., Kristie T.M.
    Proc. Natl. Acad. Sci. U.S.A. 104:10835-10840(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "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."
    Lee J.H., Skalnik D.G.
    Mol. Cell. Biol. 28:609-618(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SET1 COMPLEX, INTERACTION WITH SETD1A.
  31. "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS."
    Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M., Shilatifard A.
    Mol. Cell. Biol. 28:7337-7344(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SET1 COMPLEX.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-1205 AND SER-1507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  34. "Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
    Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
    J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH ZNF335; MKI67; C11ORF30; MATR3; HSPA8; TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5.
  35. "The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1."
    Machida Y.J., Machida Y., Vashisht A.A., Wohlschlegel J.A., Dutta A.
    J. Biol. Chem. 284:34179-34188(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-105; LYS-163; LYS-244 AND LYS-363, DEUBIQUITINATION BY BAP1, MUTAGENESIS OF PRO-134.
  36. "Association of C-terminal ubiquitin hydrolase BRCA1-associated protein 1 with cell cycle regulator host cell factor 1."
    Misaghi S., Ottosen S., Izrael-Tomasevic A., Arnott D., Lamkanfi M., Lee J., Liu J., O'Rourke K., Dixit V.M., Wilson A.C.
    Mol. Cell. Biol. 29:2181-2192(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-1807 AND LYS-1808, DEUBIQUITINATION BY BAP1, SUBCELLULAR LOCATION.
  37. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
    Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
    Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
  38. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-1507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  39. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-813 AND LYS-2005, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
    Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.
    J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
  41. "The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias."
    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.
    J. Biol. Chem. 285:13364-13371(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT COMPLEX, INTERACTION WITH OGT; THAP1 AND THAP3, GLYCOSYLATION, FUNCTION.
  42. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-666; SER-669 AND SER-1507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  43. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  44. "Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway."
    Daou S., Mashtalir N., Hammond-Martel I., Pak H., Yu H., Sui G., Vogel J.L., Kristie T.M., Affar E.B.
    Proc. Natl. Acad. Sci. U.S.A. 108:2747-2752(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, INTERACTION WITH OGT.
  45. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-666 AND SER-1507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  46. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  47. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  48. Cited for: GLYCOSYLATION, INTERACTION WITH OGT; TET2 AND TET3.
  49. Cited for: VARIANT MRX3 ASN-225.

Entry informationi

Entry nameiHCFC1_HUMAN
AccessioniPrimary (citable) accession number: P51610
Secondary accession number(s): Q6P4G5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 13, 2007
Last modified: October 29, 2014
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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