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P78364

- PHC1_HUMAN

UniProt

P78364 - PHC1_HUMAN

Protein

Polyhomeotic-like protein 1

Gene

PHC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (03 Mar 2009)
      Previous versions | rss
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    Functioni

    Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Required for proper control of cellular levels of GMNN expression.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri791 – 82535FCS-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. DNA binding Source: UniProtKB-KW
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to retinoic acid Source: Ensembl
    2. histone ubiquitination Source: UniProtKB
    3. multicellular organismal development Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_169436. Oxidative Stress Induced Senescence.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyhomeotic-like protein 1
    Short name:
    hPH1
    Alternative name(s):
    Early development regulatory protein 1
    Gene namesi
    Name:PHC1
    Synonyms:EDR1, PH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:3182. PHC1.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nuclear body Source: Ensembl
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. PcG protein complex Source: UniProtKB
    5. PRC1 complex Source: UniProtKB
    6. sex chromatin Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Microcephaly 11, primary, autosomal recessive (MCPH11) [MIM:615414]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti992 – 9921L → F in MCPH11; significant reduction in mutant protein levels which is shown to result from proteasome-mediated degradation; patient cells show increased expression of GMNN and decreased interaction between the protein and ubiquitinated HIST1H2AM compared to control cells. 1 Publication
    VAR_070566

    Keywords - Diseasei

    Disease mutation, Primary microcephaly

    Organism-specific databases

    MIMi615414. phenotype.
    Orphaneti2512. Autosomal recessive primary microcephaly.
    PharmGKBiPA27619.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10041004Polyhomeotic-like protein 1PRO_0000058375Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei645 – 6451Phosphoserine1 Publication
    Modified residuei898 – 8981Phosphoserine1 Publication
    Modified residuei922 – 9221Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP78364.
    PaxDbiP78364.
    PRIDEiP78364.

    PTM databases

    PhosphoSiteiP78364.

    Expressioni

    Gene expression databases

    BgeeiP78364.
    CleanExiHS_PHC1.
    GenevestigatoriP78364.

    Organism-specific databases

    HPAiHPA006973.

    Interactioni

    Subunit structurei

    Homodimer. Component of a PRC1-like complex.3 Publications

    Protein-protein interaction databases

    BioGridi108233. 22 interactions.
    DIPiDIP-44567N.
    IntActiP78364. 14 interactions.
    MINTiMINT-3023129.
    STRINGi9606.ENSP00000251757.

    Structurei

    Secondary structure

    1
    1004
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi783 – 7853
    Helixi789 – 7946
    Beta strandi796 – 7994
    Turni801 – 8033
    Beta strandi806 – 8083
    Helixi809 – 8113
    Turni813 – 8153
    Beta strandi816 – 8183
    Helixi821 – 8277

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L8ENMR-A783-828[»]
    ProteinModelPortaliP78364.
    SMRiP78364. Positions 780-828, 938-998.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini940 – 100465SAMPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi425 – 44117Poly-GlnAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FCS-type zinc finger.PROSITE-ProRule annotation
    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri791 – 82535FCS-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG145736.
    HOGENOMiHOG000115526.
    HOVERGENiHBG039325.
    InParanoidiP78364.
    KOiK11456.
    OMAiQGTAHVV.
    PhylomeDBiP78364.
    TreeFamiTF331299.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    InterProiIPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR012313. Znf_FCS.
    IPR010507. Znf_MYM.
    [Graphical view]
    PfamiPF00536. SAM_1. 1 hit.
    PF06467. zf-FCS. 1 hit.
    [Graphical view]
    SMARTiSM00454. SAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    PROSITEiPS50105. SAM_DOMAIN. 1 hit.
    PS51024. ZF_FCS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P78364-1 [UniParc]FASTAAdd to Basket

    « Hide

    METESEQNSN STNGSSSSGG SSRPQIAQMS LYERQAVQAL QALQRQPNAA     50
    QYFHQFMLQQ QLSNAQLHSL AAVQQATIAA SRQASSPNTS TTQQQTTTTQ 100
    ASINLATTSA AQLISRSQSV SSPSATTLTQ SVLLGNTTSP PLNQSQAQMY 150
    LRPQLGNLLQ VNRTLGRNVP LASQLILMPN GAVAAVQQEV PSAQSPGVHA 200
    DADQVQNLAV RNQQASAQGP QMQGSTQKAI PPGASPVSSL SQASSQALAV 250
    AQASSGATNQ SLNLSQAGGG SGNSIPGSMG PGGGGQAHGG LGQLPSSGMG 300
    GGSCPRKGTG VVQPLPAAQT VTVSQGSQTE AESAAAKKAE ADGSGQQNVG 350
    MNLTRTATPA PSQTLISSAT YTQIQPHSLI QQQQQIHLQQ KQVVIQQQIA 400
    IHHQQQFQHR QSQLLHTATH LQLAQQQQQQ QQQQQQQQQP QATTLTAPQP 450
    PQVPPTQQVP PSQSQQQAQT LVVQPMLQSS PLSLPPDAAP KPPIPIQSKP 500
    PVAPIKPPQL GAAKMSAAQQ PPPHIPVQVV GTRQPGTAQA QALGLAQLAA 550
    AVPTSRGMPG TVQSGQAHLA SSPPSSQAPG ALQECPPTLA PGMTLAPVQG 600
    TAHVVKGGAT TSSPVVAQVP AAFYMQSVHL PGKPQTLAVK RKADSEEERD 650
    DVSTLGSMLP AKASPVAESP KVMDEKSSLG EKAESVANVN ANTPSSELVA 700
    LTPAPSVPPP TLAMVSRQMG DSKPPQAIVK PQILTHIIEG FVIQEGAEPF 750
    PVGCSQLLKE SEKPLQTGLP TGLTENQSGG PLGVDSPSAE LDKKANLLKC 800
    EYCGKYAPAE QFRGSKRFCS MTCAKRYNVS CSHQFRLKRK KMKEFQEANY 850
    ARVRRRGPRR SSSDIARAKI QGKCHRGQED SSRGSDNSSY DEALSPTSPG 900
    PLSVRAGHGE RDLGNPNTAP PTPELHGINP VFLSSNPSRW SVEEVYEFIA 950
    SLQGCQEIAE EFRSQEIDGQ ALLLLKEEHL MSAMNIKLGP ALKICAKINV 1000
    LKET 1004
    Length:1,004
    Mass (Da):105,534
    Last modified:March 3, 2009 - v3
    Checksum:iD53764F80931A938
    GO

    Sequence cautioni

    The sequence AAH17748.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti165 – 1673LGR → PGS in AAC51169. (PubMed:9121482)Curated
    Sequence conflicti568 – 5692HL → LK in AAC51169. (PubMed:9121482)Curated
    Sequence conflicti613 – 6131S → T in AAC51169. (PubMed:9121482)Curated
    Sequence conflicti752 – 7521V → G in AAC51169. (PubMed:9121482)Curated
    Sequence conflicti782 – 7821L → F in AAC51169. (PubMed:9121482)Curated
    Sequence conflicti972 – 9721L → F in AAC51169. (PubMed:9121482)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti693 – 6931T → A.2 Publications
    Corresponds to variant rs1049925 [ dbSNP | Ensembl ].
    VAR_054503
    Natural varianti992 – 9921L → F in MCPH11; significant reduction in mutant protein levels which is shown to result from proteasome-mediated degradation; patient cells show increased expression of GMNN and decreased interaction between the protein and ubiquitinated HIST1H2AM compared to control cells. 1 Publication
    VAR_070566

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89277 mRNA. Translation: AAC51169.1.
    AC006581 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88600.1.
    CH471116 Genomic DNA. Translation: EAW88601.1.
    BC002871 mRNA. Translation: AAH02871.2.
    BC017748 mRNA. Translation: AAH17748.1. Different initiation.
    CCDSiCCDS8597.1.
    RefSeqiNP_004417.2. NM_004426.2.
    UniGeneiHs.744902.

    Genome annotation databases

    EnsembliENST00000543824; ENSP00000440674; ENSG00000111752.
    ENST00000544916; ENSP00000437659; ENSG00000111752.
    GeneIDi1911.
    KEGGihsa:1911.
    UCSCiuc001qvd.3. human.

    Polymorphism databases

    DMDMi224471881.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89277 mRNA. Translation: AAC51169.1 .
    AC006581 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88600.1 .
    CH471116 Genomic DNA. Translation: EAW88601.1 .
    BC002871 mRNA. Translation: AAH02871.2 .
    BC017748 mRNA. Translation: AAH17748.1 . Different initiation.
    CCDSi CCDS8597.1.
    RefSeqi NP_004417.2. NM_004426.2.
    UniGenei Hs.744902.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L8E NMR - A 783-828 [» ]
    ProteinModelPortali P78364.
    SMRi P78364. Positions 780-828, 938-998.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108233. 22 interactions.
    DIPi DIP-44567N.
    IntActi P78364. 14 interactions.
    MINTi MINT-3023129.
    STRINGi 9606.ENSP00000251757.

    PTM databases

    PhosphoSitei P78364.

    Polymorphism databases

    DMDMi 224471881.

    Proteomic databases

    MaxQBi P78364.
    PaxDbi P78364.
    PRIDEi P78364.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000543824 ; ENSP00000440674 ; ENSG00000111752 .
    ENST00000544916 ; ENSP00000437659 ; ENSG00000111752 .
    GeneIDi 1911.
    KEGGi hsa:1911.
    UCSCi uc001qvd.3. human.

    Organism-specific databases

    CTDi 1911.
    GeneCardsi GC12P009067.
    HGNCi HGNC:3182. PHC1.
    HPAi HPA006973.
    MIMi 602978. gene.
    615414. phenotype.
    neXtProti NX_P78364.
    Orphaneti 2512. Autosomal recessive primary microcephaly.
    PharmGKBi PA27619.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145736.
    HOGENOMi HOG000115526.
    HOVERGENi HBG039325.
    InParanoidi P78364.
    KOi K11456.
    OMAi QGTAHVV.
    PhylomeDBi P78364.
    TreeFami TF331299.

    Enzyme and pathway databases

    Reactomei REACT_169436. Oxidative Stress Induced Senescence.

    Miscellaneous databases

    GeneWikii PHC1.
    GenomeRNAii 1911.
    NextBioi 7785.
    PROi P78364.
    SOURCEi Search...

    Gene expression databases

    Bgeei P78364.
    CleanExi HS_PHC1.
    Genevestigatori P78364.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    InterProi IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR012313. Znf_FCS.
    IPR010507. Znf_MYM.
    [Graphical view ]
    Pfami PF00536. SAM_1. 1 hit.
    PF06467. zf-FCS. 1 hit.
    [Graphical view ]
    SMARTi SM00454. SAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    PROSITEi PS50105. SAM_DOMAIN. 1 hit.
    PS51024. ZF_FCS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of interactions between the vertebrate polycomb-group protein BMI1 and human homologs of polyhomeotic."
      Gunster M.J., Satijn D.P.E., Hamer K.M., den Blaauwen J.L., de Bruijn D., Alkema M.J., van Lohuizen M., van Driel R., Otte A.P.
      Mol. Cell. Biol. 17:2326-2335(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH BMI1 AND PHC2.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-693.
    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] OF 504-1004, VARIANT ALA-693.
      Tissue: Lung and Lymph.
    5. "RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor."
      Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W., Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.
      Mol. Cell. Biol. 17:4105-4113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHC2.
    6. "The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans."
      Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P., Kingston R.E.
      Mol. Cell. Biol. 22:6070-6078(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX WITH BMI1; CBX2; CBX4; CBX8; PHC2; PHC3; RING1 AND RNF2.
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus."
      Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.
      PLoS ONE 4:E6380-E6380(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX.
    9. "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-898 AND THR-922, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Interaction proteomics analysis of polycomb proteins defines distinct PRC1 Complexes in mammalian cells."
      Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, SUBCELLULAR LOCATION.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Mutation in PHC1 implicates chromatin remodeling in primary microcephaly pathogenesis."
      Awad S., Al-Dosari M.S., Al-Yacoub N., Colak D., Salih M.A., Alkuraya F.S., Poizat C.
      Hum. Mol. Genet. 22:2200-2213(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, VARIANT MCPH11 PHE-992.

    Entry informationi

    Entry nameiPHC1_HUMAN
    AccessioniPrimary (citable) accession number: P78364
    Secondary accession number(s): D3DUV4, Q8WVM3, Q9BU63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 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

    Miscellaneous

    The hPRC-H complex purification reported by PubMed:12167701 probably presents a mixture of different PRC1-like complexes.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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