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Q61191

- HCFC1_MOUSE

UniProt

Q61191 - HCFC1_MOUSE

Protein

Host cell factor 1

Gene

Hcfc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1019 – 10202Cleavage; by autolysisBy similarity
    Sitei1081 – 10822Cleavage; by autolysisBy similarity
    Sitei1110 – 11112Cleavage; by autolysisBy similarity
    Sitei1304 – 13052Cleavage; by autolysisBy similarity
    Sitei1332 – 13332Cleavage; by autolysisBy similarity
    Sitei1432 – 14332Cleavage; by autolysisBy similarity

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. histone acetyltransferase activity (H4-K16 specific) Source: Ensembl
    3. histone acetyltransferase activity (H4-K5 specific) Source: Ensembl
    4. histone acetyltransferase activity (H4-K8 specific) Source: Ensembl
    5. protein binding Source: UniProtKB
    6. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    7. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. histone H4-K16 acetylation Source: UniProtKB
    3. histone H4-K5 acetylation Source: UniProtKB
    4. histone H4-K8 acetylation Source: UniProtKB
    5. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    6. positive regulation of transcription from RNA polymerase II promoter Source: GOC
    7. protein stabilization Source: UniProtKB
    8. regulation of protein complex assembly Source: Ensembl
    9. release from viral latency Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Cell cycle

    Enzyme and pathway databases

    ReactomeiREACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_226917. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Gene namesi
    Name:Hcfc1Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:105942. Hcfc1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: HCFC1R1 modulates its subcellular localization and overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm. Non-processed HCFC1 associates with chromatin. Colocalizes with CREB3 and CANX in the ER By similarity.By similarity

    GO - Cellular componenti

    1. Ada2/Gcn5/Ada3 transcription activator complex Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. histone acetyltransferase complex Source: UniProtKB
    4. mitochondrion Source: Ensembl
    5. MLL1 complex Source: UniProtKB
    6. MLL5-L complex Source: Ensembl
    7. neuronal cell body Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. SAGA-type complex Source: Ensembl
    10. Set1C/COMPASS complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 14321431HCF N-terminal chain 6By similarityPRO_0000016635Add
    BLAST
    Chaini2 – 13321331HCF N-terminal chain 5By similarityPRO_0000016636Add
    BLAST
    Chaini2 – 13041303HCF N-terminal chain 4By similarityPRO_0000016637Add
    BLAST
    Chaini2 – 11101109HCF N-terminal chain 3By similarityPRO_0000016638Add
    BLAST
    Chaini2 – 10811080HCF N-terminal chain 2By similarityPRO_0000016639Add
    BLAST
    Chaini2 – 10191018HCF N-terminal chain 1By similarityPRO_0000016640Add
    BLAST
    Chaini1020 – 20451026HCF C-terminal chain 1By similarityPRO_0000016641Add
    BLAST
    Chaini1082 – 2045964HCF C-terminal chain 2By similarityPRO_0000016642Add
    BLAST
    Chaini1111 – 2045935HCF C-terminal chain 3By similarityPRO_0000016643Add
    BLAST
    Chaini1305 – 2045741HCF C-terminal chain 4By similarityPRO_0000016644Add
    BLAST
    Chaini1333 – 2045713HCF C-terminal chain 5By similarityPRO_0000016645Add
    BLAST
    Chaini1433 – 2045613HCF C-terminal chain 6By similarityPRO_0000016646Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei6 – 61PhosphoserineBy similarity
    Cross-linki105 – 105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki163 – 163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki244 – 244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei288 – 2881N6-acetyllysine1 Publication
    Cross-linki363 – 363Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei411 – 4111PhosphoserineBy similarity
    Modified residuei666 – 6661PhosphoserineBy similarity
    Modified residuei669 – 6691PhosphoserineBy similarity
    Modified residuei813 – 8131N6-acetyllysineBy similarity
    Modified residuei1204 – 12041PhosphoserineBy similarity
    Modified residuei1500 – 15001PhosphothreonineBy similarity
    Modified residuei1516 – 15161PhosphoserineBy similarity
    Cross-linki1817 – 1817Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki1818 – 1818Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei2015 – 20151N6-acetyllysineBy similarity

    Post-translational modificationi

    Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats. Cleavage is promoted by O-glycosylation By similarity.By similarity
    O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing By similarity.By similarity
    Ubiquitinated. Lys-1817 and Lys-1818 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 By similarity.By similarity

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiQ61191.
    PaxDbiQ61191.
    PRIDEiQ61191.

    PTM databases

    PhosphoSiteiQ61191.

    Expressioni

    Tissue specificityi

    Expressed in liver, pituitary gland, skeletal muscle, kidney, eye and brain (at protein level). Also observed at low level in heart, spleen and lung.2 Publications

    Gene expression databases

    ArrayExpressiQ61191.
    BgeeiQ61191.
    CleanExiMM_HCFC1.
    GenevestigatoriQ61191.

    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. Interacts directly with OGT; the interaction, which requires the cleavage site domain, glycosylates and promotes proteolytic processing of HCFC1 and retains OGT in the nucleus. Interacts with TET2 and TET3. Interacts with HCFC1R1. Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L, CXXC1, HCFC1 and DPY30. Interacts (via HBM motif) with SETD1A. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 By similarity. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity By similarity. Interacts with THAP11.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi200248. 9 interactions.
    IntActiQ61191. 4 interactions.
    MINTiMINT-4097262.
    STRINGi10090.ENSMUSP00000110012.

    Structurei

    Secondary structure

    1
    2045
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1897 – 18993
    Beta strandi1905 – 19128
    Beta strandi1915 – 19217
    Beta strandi1924 – 19263
    Beta strandi1930 – 19389
    Beta strandi1965 – 19684
    Helixi1973 – 19775
    Beta strandi1984 – 199714
    Beta strandi2005 – 20106

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2M26NMR-A1896-2020[»]
    ProteinModelPortaliQ61191.
    SMRiQ61191. Positions 360-400, 1821-2020.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati44 – 8946Kelch 1Sequence AnalysisAdd
    BLAST
    Repeati93 – 14048Kelch 2Sequence AnalysisAdd
    BLAST
    Repeati148 – 19447Kelch 3Sequence AnalysisAdd
    BLAST
    Repeati217 – 26549Kelch 4Sequence AnalysisAdd
    BLAST
    Repeati266 – 31348Kelch 5Sequence AnalysisAdd
    BLAST
    Domaini366 – 45792Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati1010 – 103526HCF repeat 1Sequence AnalysisAdd
    BLAST
    Repeati1072 – 109726HCF repeat 2Sequence AnalysisAdd
    BLAST
    Repeati1101 – 112626HCF repeat 3Sequence AnalysisAdd
    BLAST
    Repeati1157 – 118226HCF repeat 4; degenerateAdd
    BLAST
    Repeati1295 – 132026HCF repeat 5Sequence AnalysisAdd
    BLAST
    Repeati1323 – 134826HCF repeat 6Sequence AnalysisAdd
    BLAST
    Repeati1358 – 138326HCF repeat 7; degenerateAdd
    BLAST
    Repeati1423 – 144826HCF repeat 8Sequence AnalysisAdd
    BLAST
    Domaini1808 – 189891Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1900 – 2016117Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni500 – 55051Required for interaction with OGTBy similarityAdd
    BLAST
    Regioni610 – 722113Interaction with SIN3ABy similarityAdd
    BLAST
    Regioni750 – 902153Interaction with ZBTB17By similarityAdd
    BLAST
    Regioni813 – 912100Interaction with GABP2By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi574 – 1500927Thr-richSequence AnalysisAdd
    BLAST
    Compositional biasi1622 – 167453Ala-richSequence AnalysisAdd
    BLAST
    Compositional biasi1684 – 172037Gln-richSequence AnalysisAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

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

    Keywords - Domaini

    Kelch repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00720000108539.
    HOGENOMiHOG000293192.
    HOVERGENiHBG051888.
    KOiK14966.
    OrthoDBiEOG790G05.
    TreeFamiTF314757.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    Q61191-1 [UniParc]FASTAAdd to Basket

    « 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 DLWTLDIETL TWNKPSLSGV 250
    APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN 300
    LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ 350
    VCCKDLWYLE TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY 400
    DIPATAATAT SPTPNPVPSV PANPPKSPAP AAAAPAVQPL TQVGITLVPQ 450
    AATAPPSTTT IQVLPTVPGS SISVPTAART QGVPAVLKVT GPQATTGTPL 500
    VTMRPASQAG KAPVTVTSLP ASVRMVVPTQ SAQGTVIGSN PQMSGMAALA 550
    AAAAATQKIP PSSAPTVLSV PAGTTIVKTV AVTPGTTTLP ATVKVASSPV 600
    MVSNPATRML KTAAAQVGTS VSSAANTSTR 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 STSLAGAGAH 900
    STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT 950
    MQPVSQPTQV TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG 1000
    QGDVQPGTVT LVCSNPPCET HETGTTNTAT TTVVANLGGH PQPTQVQFVC 1050
    DRQETAASLV TSAVGQQNGN VVRVCSNPPC ETHETGTTNT ATTATSNMAG 1100
    QHGCSNPPCE THETGTTSTA TTAMSSMGTG QQRDTRRTTN TPTVVRITVA 1150
    PGALERVQGT VKPQCQTQQT NMTTTTMTVQ ATGAPCSAGP LLRPSVALES 1200
    GSHSPAFVQL ALPSVRVGLS GPSSKDMPTG RQPETYHTYT TNTPTTTRSI 1250
    MVAGELGAAR VVPTSTYESL QASSPSSTMT MTALEALLCP SATVTQVCSN 1300
    PPCETHETGT TNTATTSNAG SAQRVCSNPP CETHETGTTH TATTATSNGG 1350
    AGQPEGGQQP ASGHPCETHQ TTSTGTTMSV SVGTLIPDAT SSHGTLESGL 1400
    EVVAVPTVTS QAGSTLLASF PTQRVCSNPP CETHETGTTH TATTVTSNMS 1450
    SNQDPPPAAS DQGEVASTQG DSTNITSASA ITTSVSSTLP RAVTTVTQST 1500
    PVPGPSVPPP EELQVSPGPR QQLPPRQLLQ SASTPLMGES TEVLSASQTP 1550
    ELQAAVDLSS TGDPSSGQEP TTSAVVATVV VQPPPPTQSE VDQLSLPQEL 1600
    MAEAQAGTTT LMVTGLTPEE LAVTAAAEAA AQAAATEEAQ ALAIQAVLQA 1650
    AQQAVMGTGE PMDTSEAAAA VTQAELGHLS AEGQEGQATT IPIVLTQQEL 1700
    AALVQQQQQL QEAQAQAQQQ HHLPTEALAP ADSLNDPSIE SNCLNELASA 1750
    VPSTVALLPS TATESLAPSN TFVAPQPVVA SPAKMQAAAT LTEVANGIES 1800
    LGVKPDLPPP PSKAPVKKEN QWFDVGVIKG TSVMVTHYFL PPDDAVQSDD 1850
    DSGTVPDYNQ LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF 1900
    PGAPCAIKIS KSPDGAHLTW EPPSVTSGKI IEYSVYLAIQ SSQASGEPKS 1950
    STPAQLAFMR VYCGPSPSCL VQSSSLSNAH IDYTTKPAII FRIAARNEKG 2000
    YGPATQVRWL QETSKDSSGT KPASKRPMSS PEMKSAPKKS KADGQ 2045
    Length:2,045
    Mass (Da):210,437
    Last modified:July 27, 2011 - v2
    Checksum:iAD0EC38C9DB19F22
    GO

    Sequence cautioni

    The sequence CAF25305.1 differs from that shown. Reason: Frameshift at position 339.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti483 – 4831V → R in AAB01163. (PubMed:9334261)Curated
    Sequence conflicti483 – 4831V → R in AAD09225. (PubMed:9334261)Curated
    Sequence conflicti520 – 5201P → S in CAF25305. 1 PublicationCurated
    Sequence conflicti567 – 5682VL → AW in AAB01163. (PubMed:9334261)Curated
    Sequence conflicti567 – 5682VL → AW in AAD09225. (PubMed:9334261)Curated
    Sequence conflicti711 – 7111Q → H in AAD09225. (PubMed:9334261)Curated
    Sequence conflicti1104 – 11041C → S in AAB01163. (PubMed:9334261)Curated
    Sequence conflicti1104 – 11041C → S in AAD09225. (PubMed:9334261)Curated
    Sequence conflicti1230 – 12301G → A in AAB01163. (PubMed:9334261)Curated
    Sequence conflicti1230 – 12301G → A in AAD09225. (PubMed:9334261)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53925 Genomic DNA. Translation: AAB01163.1.
    U80821 Genomic DNA. Translation: AAD09225.1.
    AL672002 Genomic DNA. Translation: CAM18726.1.
    CH466650 Genomic DNA. Translation: EDL29851.1.
    BC053742 mRNA. Translation: AAH53742.1.
    AK088827 mRNA. Translation: BAC40597.1.
    AJ627036 mRNA. Translation: CAF25305.1. Frameshift.
    CCDSiCCDS30218.1.
    RefSeqiNP_032250.2. NM_008224.4.
    UniGeneiMm.491126.

    Genome annotation databases

    EnsembliENSMUST00000033761; ENSMUSP00000033761; ENSMUSG00000031386.
    GeneIDi15161.
    KEGGimmu:15161.
    UCSCiuc009tnm.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53925 Genomic DNA. Translation: AAB01163.1 .
    U80821 Genomic DNA. Translation: AAD09225.1 .
    AL672002 Genomic DNA. Translation: CAM18726.1 .
    CH466650 Genomic DNA. Translation: EDL29851.1 .
    BC053742 mRNA. Translation: AAH53742.1 .
    AK088827 mRNA. Translation: BAC40597.1 .
    AJ627036 mRNA. Translation: CAF25305.1 . Frameshift.
    CCDSi CCDS30218.1.
    RefSeqi NP_032250.2. NM_008224.4.
    UniGenei Mm.491126.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2M26 NMR - A 1896-2020 [» ]
    ProteinModelPortali Q61191.
    SMRi Q61191. Positions 360-400, 1821-2020.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200248. 9 interactions.
    IntActi Q61191. 4 interactions.
    MINTi MINT-4097262.
    STRINGi 10090.ENSMUSP00000110012.

    PTM databases

    PhosphoSitei Q61191.

    Proteomic databases

    MaxQBi Q61191.
    PaxDbi Q61191.
    PRIDEi Q61191.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033761 ; ENSMUSP00000033761 ; ENSMUSG00000031386 .
    GeneIDi 15161.
    KEGGi mmu:15161.
    UCSCi uc009tnm.1. mouse.

    Organism-specific databases

    CTDi 3054.
    MGIi MGI:105942. Hcfc1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00720000108539.
    HOGENOMi HOG000293192.
    HOVERGENi HBG051888.
    KOi K14966.
    OrthoDBi EOG790G05.
    TreeFami TF314757.

    Enzyme and pathway databases

    Reactomei REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_226917. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi HCFC1. mouse.
    NextBioi 287652.
    PROi Q61191.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61191.
    Bgeei Q61191.
    CleanExi MM_HCFC1.
    Genevestigatori Q61191.

    Family and domain databases

    Gene3Di 2.120.10.80. 2 hits.
    2.60.40.10. 2 hits.
    InterProi IPR003961. Fibronectin_type3.
    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. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    PROSITEi PS50853. FN3. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The mouse homologue of the human transcription factor C1 (host cell factor). Conservation of forms and function."
      Kristie T.M.
      J. Biol. Chem. 272:26749-26755(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
      Tissue: Fetal liver1 Publication.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      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].
      Tissue: Limb mesenchyme1 Publication.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-209.
      Strain: NOD.
      Tissue: Thymus.
    6. "Towards functional annotation of all Xq28 genes: expression and intracellular localization analyses reveal novel candidates for disease genes."
      Kolb A.A., Mehrle A., Bechtel S., Wellenreuther R., Simpson J., Pepperkok R., Wiemann S., Poustka A.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 165-520.
      Strain: NMRI.
      Tissue: Embryo.
    7. "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, TISSUE SPECIFICITY.
      Strain: BALB/c1 Publication.
    8. "O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry."
      Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    9. "Ronin is essential for embryogenesis and the pluripotency of mouse embryonic stem cells."
      Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F., Songyang Z., Thomson J.A., Zwaka T.P.
      Cell 133:1162-1174(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THAP11.
    10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiHCFC1_MOUSE
    AccessioniPrimary (citable) accession number: Q61191
    Secondary accession number(s): B1AUX1
    , Q684R1, Q7TSB0, Q8C2D0, Q9QWH2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3