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P78364

- PHC1_HUMAN

UniProt

P78364 - PHC1_HUMAN

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Protein

Polyhomeotic-like protein 1

Gene
PHC1, EDR1, PH1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-typeAdd
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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini940 – 100465SAMAdd
BLAST

Compositional bias

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

Sequence similaritiesi

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1673LGR → PGS in AAC51169. 1 Publication
Sequence conflicti568 – 5692HL → LK in AAC51169. 1 Publication
Sequence conflicti613 – 6131S → T in AAC51169. 1 Publication
Sequence conflicti752 – 7521V → G in AAC51169. 1 Publication
Sequence conflicti782 – 7821L → F in AAC51169. 1 Publication
Sequence conflicti972 – 9721L → F in AAC51169. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 135 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 1 Publication 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

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