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P51610

- HCFC1_HUMAN

UniProt

P51610 - HCFC1_HUMAN

Protein

Host cell factor 1

Gene

HCFC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    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

    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

    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. 2 Publications
    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. 2 Publications
    Mutagenesisi82 – 821C → D: Moderately reduces VIC formation and association with VP16 and CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells. 2 Publications
    Mutagenesisi105 – 1051K → D: Minor reduction in VIC formation and association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. 2 Publications
    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. 4 Publications
    Mutagenesisi137 – 1371R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 2 Publications
    Mutagenesisi197 – 1971P → S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 2 Publications
    Mutagenesisi200 – 2001R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 2 Publications
    Mutagenesisi228 – 2281R → D: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 2 Publications
    Mutagenesisi252 – 2521P → S: Minor reduction in VIC formation, but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 2 Publications
    Mutagenesisi255 – 2551R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 2 Publications
    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. 2 Publications
    Mutagenesisi322 – 3221R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 2 Publications
    Mutagenesisi338 – 3381S → A: Moderately reduces association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. 2 Publications
    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. 1 Publication
    Mutagenesisi1073 – 10731R → A: No effect on cleavage at HCF repeat. 1 Publication
    Mutagenesisi1074 – 10741V → A: No effect on cleavage at HCF repeat. 1 Publication
    Mutagenesisi1075 – 10751C → A: No effect on cleavage at HCF repeat. 1 Publication
    Mutagenesisi1076 – 10761S → A: No effect on cleavage at HCF repeat. 1 Publication
    Mutagenesisi1077 – 10771N → A: No effect on cleavage at HCF repeat. 1 Publication
    Mutagenesisi1078 – 10781P → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1079 – 10835PCETH → AAAAA: Reduces and disrupts cleavage at HCF repeat. 1 Publication
    Mutagenesisi1079 – 10791P → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1080 – 10801C → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1081 – 10811E → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1081 – 10811E → D: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1082 – 10821T → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1082 – 10821T → F: Reduces cleavage at HCF repeat. 1 Publication
    Mutagenesisi1082 – 10821T → S: Reduces cleavage at HCF repeat. 1 Publication
    Mutagenesisi1083 – 10831H → A: Reduces cleavage at HCF repeat. 1 Publication
    Mutagenesisi1084 – 10841E → A: No effect on cleavage at HCF repeat. 1 Publication
    Mutagenesisi1085 – 10851T → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1086 – 10861G → A: No effect on cleavage at HCF repeat. 1 Publication
    Mutagenesisi1087 – 10871T → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1088 – 10881T → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1089 – 10891N → A: Reduces cleavage at HCF repeat. 1 Publication
    Mutagenesisi1090 – 10901T → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1092 – 10921T → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1093 – 10931T → A: Inactivates cleavage at HCF repeat. 1 Publication
    Mutagenesisi1095 – 10951T → A: Reduces cleavage at HCF repeat. 1 Publication
    Mutagenesisi1096 – 10961S → A: No effect on cleavage at HCF repeat. 1 Publication
    Mutagenesisi1097 – 10971N → A: No effect on cleavage at HCF repeat. 1 Publication

    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

    ArrayExpressiP51610.
    BgeeiP51610.
    CleanExiHS_HCFC1.
    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. 81 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 – 3758
    Beta strandi380 – 3856
    Beta strandi391 – 3999
    Beta strandi1813 – 182513
    Beta strandi1827 – 18293
    Beta strandi1853 – 18553
    Beta strandi1861 – 187010
    Beta strandi1873 – 18775
    Beta strandi1881 – 18844
    Beta strandi1895 – 19028
    Beta strandi1905 – 19117
    Beta strandi1922 – 19298
    Beta strandi1946 – 196217
    Helixi1963 – 19664
    Beta strandi1971 – 198616
    Beta strandi1995 – 20006

    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.
    HOGENOMiHOG000293192.
    HOVERGENiHBG051888.
    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

    MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG     50
    GNEGIVDELH VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM 100
    VEYGKYSNDL YELQASRWEW KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY 150
    LFGGLANDSE DPKNNIPRYL NDLYILELRP GSGVVAWDIP ITYGVLPPPR 200
    ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIDTL TWNKPSLSGV 250
    APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN 300
    LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ 350
    VCCKDLWYLE TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY 400
    DIPATAATAT SPTPNPVPSV PANPPKSPAP AAAAPAVQPL TQVGITLLPQ 450
    AAPAPPTTTT IQVLPTVPGS SISVPTAART QGVPAVLKVT GPQATTGTPL 500
    VTMRPASQAG KAPVTVTSLP AGVRMVVPTQ SAQGTVIGSS PQMSGMAALA 550
    AAAAATQKIP PSSAPTVLSV PAGTTIVKTM AVTPGTTTLP ATVKVASSPV 600
    MVSNPATRML KTAAAQVGTS VSSATNTSTR PIITVHKSGT VTVAQQAQVV 650
    TTVVGGVTKT ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ 700
    ASTGPVTQII QTKGPLPAGT ILKLVTSADG KPTTIITTTQ ASGAGTKPTI 750
    LGISSVSPST TKPGTTTIIK TIPMSAIITQ AGATGVTSSP GIKSPITIIT 800
    TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG QPGTILRTVP 850
    MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGGH 900
    STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT 950
    MQPVSQPTQV TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG 1000
    QGDVQPGTVT LVCSNPPCET HETGTTNTAT TTVVANLGGH PQPTQVQFVC 1050
    DRQEAAASLV TSTVGQQNGS VVRVCSNPPC ETHETGTTNT ATTATSNMAG 1100
    QHGCSNPPCE THETGTTNTA TTAMSSVGAN HQRDARRACA AGTPAVIRIS 1150
    VATGALEAAQ GSKSQCQTRQ TSATSTTMTV MATGAPCSAG PLLGPSMARE 1200
    PGGRSPAFVQ LAPLSSKVRL SSPSIKDLPA GRHSHAVSTA AMTRSSVGAG 1250
    EPRMAPVCES LQGGSPSTTV TVTALEALLC PSATVTQVCS NPPCETHETG 1300
    TTNTATTSNA GSAQRVCSNP PCETHETGTT HTATTATSNG GTGQPEGGQQ 1350
    PPAGRPCETH QTTSTGTTMS VSVGALLPDA TSSHRTVESG LEVAAAPSVT 1400
    PQAGTALLAP FPTQRVCSNP PCETHETGTT HTATTVTSNM SSNQDPPPAA 1450
    SDQGEVESTQ GDSVNITSSS AITTTVSSTL TRAVTTVTQS TPVPGPSVPP 1500
    PEELQVSPGP RQQLPPRQLL QSASTALMGE SAEVLSASQT PELPAAVDLS 1550
    STGEPSSGQE SAGSAVVATV VVQPPPPTQS EVDQLSLPQE LMAEAQAGTT 1600
    TLMVTGLTPE ELAVTAAAEA AAQAAATEEA QALAIQAVLQ AAQQAVMGTG 1650
    EPMDTSEAAA TVTQAELGHL SAEGQEGQAT TIPIVLTQQE LAALVQQQQL 1700
    QEAQAQQQHH HLPTEALAPA DSLNDPAIES NCLNELAGTV PSTVALLPST 1750
    ATESLAPSNT FVAPQPVVVA SPAKLQAAAT LTEVANGIES LGVKPDLPPP 1800
    PSKAPMKKEN QWFDVGVIKG TNVMVTHYFL PPDDAVPSDD DLGTVPDYNQ 1850
    LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS 1900
    KSPDGAHLTW EPPSVTSGKI IEYSVYLAIQ SSQAGGELKS STPAQLAFMR 1950
    VYCGPSPSCL VQSSSLSNAH IDYTTKPAII FRIAARNEKG YGPATQVRWL 2000
    QETSKDSSGT KPANKRPMSS PEMKSAPKKS KADGQ 2035
    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. 81 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.
    HOGENOMi HOG000293192.
    HOVERGENi HBG051888.
    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

    ArrayExpressi P51610.
    Bgeei P51610.
    CleanExi HS_HCFC1.
    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

    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 1, 2014
    This is version 167 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

    Dasty 3