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P78364 (PHC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyhomeotic-like protein 1

Short name=hPH1
Alternative name(s):
Early development regulatory protein 1
Gene names
Name:PHC1
Synonyms:EDR1, PH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1004 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12

Subunit structure

Homodimer. Component of a PRC1-like complex. Ref.6 Ref.8 Ref.10

Subcellular location

Nucleus Ref.1 Ref.10.

Involvement in disease

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. Ref.12

Miscellaneous

The hPRC-H complex purification reported by Ref.6 probably presents a mixture of different PRC1-like complexes.

Sequence similarities

Contains 1 FCS-type zinc finger.

Contains 1 SAM (sterile alpha motif) domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10041004Polyhomeotic-like protein 1
PRO_0000058375

Regions

Domain940 – 100465SAM
Zinc finger791 – 82535FCS-type
Compositional bias425 – 44117Poly-Gln

Amino acid modifications

Modified residue6451Phosphoserine Ref.11
Modified residue8981Phosphoserine Ref.9
Modified residue9221Phosphothreonine Ref.9

Natural variations

Natural variant6931T → A. Ref.3 Ref.4
Corresponds to variant rs1049925 [ dbSNP | Ensembl ].
VAR_054503
Natural variant9921L → 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. Ref.12
VAR_070566

Experimental info

Sequence conflict165 – 1673LGR → PGS in AAC51169. Ref.1
Sequence conflict568 – 5692HL → LK in AAC51169. Ref.1
Sequence conflict6131S → T in AAC51169. Ref.1
Sequence conflict7521V → G in AAC51169. Ref.1
Sequence conflict7821L → F in AAC51169. Ref.1
Sequence conflict9721L → F in AAC51169. Ref.1

Secondary structure

................. 1004
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P78364 [UniParc].

Last modified March 3, 2009. Version 3.
Checksum: D53764F80931A938

FASTA1,004105,534
        10         20         30         40         50         60 
METESEQNSN STNGSSSSGG SSRPQIAQMS LYERQAVQAL QALQRQPNAA QYFHQFMLQQ 

        70         80         90        100        110        120 
QLSNAQLHSL AAVQQATIAA SRQASSPNTS TTQQQTTTTQ ASINLATTSA AQLISRSQSV 

       130        140        150        160        170        180 
SSPSATTLTQ SVLLGNTTSP PLNQSQAQMY LRPQLGNLLQ VNRTLGRNVP LASQLILMPN 

       190        200        210        220        230        240 
GAVAAVQQEV PSAQSPGVHA DADQVQNLAV RNQQASAQGP QMQGSTQKAI PPGASPVSSL 

       250        260        270        280        290        300 
SQASSQALAV AQASSGATNQ SLNLSQAGGG SGNSIPGSMG PGGGGQAHGG LGQLPSSGMG 

       310        320        330        340        350        360 
GGSCPRKGTG VVQPLPAAQT VTVSQGSQTE AESAAAKKAE ADGSGQQNVG MNLTRTATPA 

       370        380        390        400        410        420 
PSQTLISSAT YTQIQPHSLI QQQQQIHLQQ KQVVIQQQIA IHHQQQFQHR QSQLLHTATH 

       430        440        450        460        470        480 
LQLAQQQQQQ QQQQQQQQQP QATTLTAPQP PQVPPTQQVP PSQSQQQAQT LVVQPMLQSS 

       490        500        510        520        530        540 
PLSLPPDAAP KPPIPIQSKP PVAPIKPPQL GAAKMSAAQQ PPPHIPVQVV GTRQPGTAQA 

       550        560        570        580        590        600 
QALGLAQLAA AVPTSRGMPG TVQSGQAHLA SSPPSSQAPG ALQECPPTLA PGMTLAPVQG 

       610        620        630        640        650        660 
TAHVVKGGAT TSSPVVAQVP AAFYMQSVHL PGKPQTLAVK RKADSEEERD DVSTLGSMLP 

       670        680        690        700        710        720 
AKASPVAESP KVMDEKSSLG EKAESVANVN ANTPSSELVA LTPAPSVPPP TLAMVSRQMG 

       730        740        750        760        770        780 
DSKPPQAIVK PQILTHIIEG FVIQEGAEPF PVGCSQLLKE SEKPLQTGLP TGLTENQSGG 

       790        800        810        820        830        840 
PLGVDSPSAE LDKKANLLKC EYCGKYAPAE QFRGSKRFCS MTCAKRYNVS CSHQFRLKRK 

       850        860        870        880        890        900 
KMKEFQEANY ARVRRRGPRR SSSDIARAKI QGKCHRGQED SSRGSDNSSY DEALSPTSPG 

       910        920        930        940        950        960 
PLSVRAGHGE RDLGNPNTAP PTPELHGINP VFLSSNPSRW SVEEVYEFIA SLQGCQEIAE 

       970        980        990       1000 
EFRSQEIDGQ ALLLLKEEHL MSAMNIKLGP ALKICAKINV LKET 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_004417.2. NM_004426.2.
UniGeneHs.744902.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L8ENMR-A783-828[»]
ProteinModelPortalP78364.
SMRP78364. Positions 780-828, 938-998.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108233. 21 interactions.
DIPDIP-44567N.
IntActP78364. 14 interactions.
MINTMINT-3023129.
STRING9606.ENSP00000251757.

PTM databases

PhosphoSiteP78364.

Polymorphism databases

DMDM224471881.

Proteomic databases

PaxDbP78364.
PRIDEP78364.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000543824; ENSP00000440674; ENSG00000111752.
ENST00000544916; ENSP00000437659; ENSG00000111752.
GeneID1911.
KEGGhsa:1911.
UCSCuc001qvd.3. human.

Organism-specific databases

CTD1911.
GeneCardsGC12P009067.
HGNCHGNC:3182. PHC1.
HPAHPA006973.
MIM602978. gene.
615414. phenotype.
neXtProtNX_P78364.
Orphanet2512. Autosomal recessive primary microcephaly.
PharmGKBPA27619.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145736.
HOGENOMHOG000115526.
HOVERGENHBG039325.
InParanoidP78364.
KOK11456.
OMAQGTAHVV.
PhylomeDBP78364.
TreeFamTF331299.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

BgeeP78364.
CleanExHS_PHC1.
GenevestigatorP78364.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
InterProIPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR012313. Znf_FCS.
IPR010507. Znf_MYM.
[Graphical view]
PfamPF00536. SAM_1. 1 hit.
PF06467. zf-FCS. 1 hit.
[Graphical view]
SMARTSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
PROSITEPS50105. SAM_DOMAIN. 1 hit.
PS51024. ZF_FCS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPHC1.
GenomeRNAi1911.
NextBio7785.
PROP78364.
SOURCESearch...

Entry information

Entry namePHC1_HUMAN
AccessionPrimary (citable) accession number: P78364
Secondary accession number(s): D3DUV4, Q8WVM3, Q9BU63
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM