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Q8IXK0 (PHC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyhomeotic-like protein 2

Short name=hPH2
Alternative name(s):
Early development regulatory protein 2
Gene names
Name:PHC2
Synonyms:EDR2, PH2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length858 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.

Subunit structure

Component of a PRC1-like complex. Interacts with CBX4. Interacts with BMI1, PCGF2, PHC1 and RNF2. Interacts with CHTOP By similarity. Interacts with the N-terminal region of the SP1 transcription factor and with MAPKAPK2. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.17

Subcellular location

Nucleus Ref.17.

Domain

HD1 motif interacts with SAM domain of PHC1.

Miscellaneous

The hPRC-H complex purification reported by Ref.9 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 AAH68573.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH92492.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAI13956.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IXK0-1)

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.
Isoform 2 (identifier: Q8IXK0-2)

Also known as: isoform b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-535: Missing.
Isoform 3 (identifier: Q8IXK0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-585: Missing.
     586-586: P → M
     809-852: CQEIAEEFRA...GPALKIYARI → LPSSFPKGHE...WPVLRPRPHL
     853-858: Missing.
Isoform 4 (identifier: Q8IXK0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     193-221: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8IXK0-5)

The sequence of this isoform differs from the canonical sequence as follows:
     463-463: P → PV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 858858Polyhomeotic-like protein 2
PRO_0000076286

Regions

Domain794 – 85865SAM
Zinc finger633 – 66735FCS-type
Motif558 – 58730HD1
Compositional bias11 – 3727Ser-rich
Compositional bias55 – 11157Gln-rich
Compositional bias329 – 37749Gln-rich

Amino acid modifications

Modified residue6211Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 585585Missing in isoform 3.
VSP_016914
Alternative sequence1 – 535535Missing in isoform 2.
VSP_016915
Alternative sequence193 – 22129Missing in isoform 4.
VSP_027217
Alternative sequence4631P → PV in isoform 5.
VSP_039755
Alternative sequence5861P → M in isoform 3.
VSP_016916
Alternative sequence809 – 85244CQEIA…IYARI → LPSSFPKGHETSIYSLSKHL RHSRFPQSPSGSCLWPVLRP RPHL in isoform 3.
VSP_016917
Alternative sequence853 – 8586Missing in isoform 3.
VSP_016918
Natural variant2541P → S.
Corresponds to variant rs10914692 [ dbSNP | Ensembl ].
VAR_051276
Natural variant4751V → M. Ref.5
Corresponds to variant rs12026290 [ dbSNP | Ensembl ].
VAR_051277

Experimental info

Sequence conflict7451S → N in BAC87622. Ref.2
Sequence conflict7781D → E in BAC87622. Ref.2
Sequence conflict8131A → E in AAH28396. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 2E3FD3898CFD702B

FASTA85890,713
        10         20         30         40         50         60 
MENELPVPHT SSSACATSST SGASSSSGCN NSSSGGSGRP TGPQISVYSG IPDRQTVQVI 

        70         80         90        100        110        120 
QQALHRQPST AAQYLQQMYA AQQQHLMLQT AALQQQHLSS AQLQSLAAVQ QASLVSNRQG 

       130        140        150        160        170        180 
STSGSNVSAQ APAQSSSINL AASPAAAQLL NRAQSVNSAA ASGIAQQAVL LGNTSSPALT 

       190        200        210        220        230        240 
ASQAQMYLRA QMLIFTPTAT VATVQPELGT GSPARPPTPA QVQNLTLRTQ QTPAAAASGP 

       250        260        270        280        290        300 
TPTQPVLPSL ALKPTPGGSQ PLPTPAQSRN TAQASPAGAK PGIADSVMEP HKKGDGNSSV 

       310        320        330        340        350        360 
PGSMEGRAGL SRTVPAVAAH PLIAPAYAQL QPHQLLPQPS SKHLQPQFVI QQQPQPQQQQ 

       370        380        390        400        410        420 
PPPQQSRPVL QAEPHPQLAS VSPSVALQPS SEAHAMPLGP VTPALPLQCP TANLHKPGGS 

       430        440        450        460        470        480 
QQCHPPTPDT GPQNGHPEGV PHTPQRRFQH TSAVILQLQP ASPPQQCVPD DWKEVAPGEK 

       490        500        510        520        530        540 
SVPETRSGPS PHQQAIVTAM PGGLPVPTSP NIQPSPAHET GQGIVHALTD LSSPGMTSGN 

       550        560        570        580        590        600 
GNSASSIAGT APQNGENKPP QAIVKPQILT HVIEGFVIQE GAEPFPVGRS SLLVGNLKKK 

       610        620        630        640        650        660 
YAQGFLPEKL PQQDHTTTTD SEMEEPYLQE SKEEGAPLKL KCELCGRVDF AYKFKRSKRF 

       670        680        690        700        710        720 
CSMACAKRYN VGCTKRVGLF HSDRSKLQKA GAATHNRRRA SKASLPPLTK DTKKQPTGTV 

       730        740        750        760        770        780 
PLSVTAALQL THSQEDSSRC SDNSSYEEPL SPISASSSTS RRRQGQRDLE LPDMHMRDLV 

       790        800        810        820        830        840 
GMGHHFLPSE PTKWNVEDVY EFIRSLPGCQ EIAEEFRAQE IDGQALLLLK EDHLMSAMNI 

       850 
KLGPALKIYA RISMLKDS 

« Hide

Isoform 2 (isoform b) [UniParc].

Checksum: 3D469465CA2C39AD
Show »

FASTA32335,760
Isoform 3 [UniParc].

Checksum: 2E784C87AA459AD0
Show »

FASTA26730,053
Isoform 4 [UniParc].

Checksum: FFAF6D7224ADBD72
Show »

FASTA82987,812
Isoform 5 [UniParc].

Checksum: 7F6C839B758194DC
Show »

FASTA85990,812

References

« Hide 'large scale' references
[1]"Identification and characterisation of novel mammalian homologues of Drosophila polyhomeotic permits new insights into relationships between members of the polyhomeotic family."
Tonkin E., Hagan D.-M., Li W., Strachan T.
Hum. Genet. 111:435-442(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
Tissue: Testis and Trachea.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[5]"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] (ISOFORMS 2; 4 AND 5), VARIANT MET-475.
Tissue: Cerebellum, Hypothalamus, Placenta, Prostate and Retina.
[6]"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: NUCLEOTIDE SEQUENCE [MRNA] OF 1-266 (ISOFORM 1), INTERACTION WITH SP1.
Tissue: Colon carcinoma.
[7]"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: INTERACTION WITH BMI1 AND PHC1.
[8]"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 RING1; PHC1 AND BMI1.
[9]"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; PHC1; PHC3; RING1 AND RNF2.
[10]"P66(ShcA) interacts with MAPKAP kinase 2 and regulates its activity."
Yannoni Y.M., Gaestel M., Lin L.L.
FEBS Lett. 564:205-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPKAPK2.
[11]"Role of histone H2A ubiquitination in Polycomb silencing."
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.
Nature 431:873-878(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX.
[12]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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.
[15]"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-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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, INTERACTION WITH CBX4, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ419231 mRNA. Translation: CAD11673.1.
AK128821 mRNA. Translation: BAC87622.1.
AK292905 mRNA. Translation: BAF85594.1.
AL513327 Genomic DNA. Translation: CAI13955.1.
AL513327 Genomic DNA. Translation: CAI13956.1. Sequence problems.
AL513327 Genomic DNA. Translation: CAI13957.1.
CH471059 Genomic DNA. Translation: EAX07457.1.
CH471059 Genomic DNA. Translation: EAX07458.1.
CH471059 Genomic DNA. Translation: EAX07459.1.
BC015450 mRNA. Translation: AAH15450.1.
BC028396 mRNA. Translation: AAH28396.3.
BC029269 mRNA. Translation: AAH29269.1.
BC068573 mRNA. Translation: AAH68573.1. Different initiation.
BC092492 mRNA. Translation: AAH92492.1. Different initiation.
BC110863 mRNA. Translation: AAI10864.2.
BC130630 mRNA. Translation: AAI30631.1.
AJ242730 mRNA. Translation: CAB44779.1.
CCDSCCDS378.1. [Q8IXK0-1]
CCDS379.1. [Q8IXK0-2]
RefSeqNP_004418.2. NM_004427.3. [Q8IXK0-2]
NP_932157.1. NM_198040.2. [Q8IXK0-1]
XP_005270627.1. XM_005270570.1. [Q8IXK0-2]
XP_005270628.1. XM_005270571.1. [Q8IXK0-2]
UniGeneHs.524271.

3D structure databases

ProteinModelPortalQ8IXK0.
SMRQ8IXK0. Positions 640-670, 792-852.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108234. 43 interactions.
DIPDIP-34464N.
IntActQ8IXK0. 40 interactions.
MINTMINT-1369031.

PTM databases

PhosphoSiteQ8IXK0.

Polymorphism databases

DMDM74750731.

Proteomic databases

MaxQBQ8IXK0.
PaxDbQ8IXK0.
PRIDEQ8IXK0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257118; ENSP00000257118; ENSG00000134686. [Q8IXK0-1]
ENST00000373418; ENSP00000362517; ENSG00000134686. [Q8IXK0-2]
ENST00000419414; ENSP00000391440; ENSG00000134686. [Q8IXK0-5]
ENST00000431992; ENSP00000389436; ENSG00000134686. [Q8IXK0-4]
GeneID1912.
KEGGhsa:1912.
UCSCuc001bxe.1. human. [Q8IXK0-2]
uc001bxf.1. human. [Q8IXK0-3]
uc001bxg.1. human. [Q8IXK0-1]

Organism-specific databases

CTD1912.
GeneCardsGC01M033789.
HGNCHGNC:3183. PHC2.
HPAHPA047403.
MIM602979. gene.
neXtProtNX_Q8IXK0.
PharmGKBPA27620.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145736.
HOVERGENHBG039325.
InParanoidQ8IXK0.
KOK11457.
OMAHTSSSAC.
OrthoDBEOG789C9Q.
PhylomeDBQ8IXK0.
TreeFamTF331299.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ8IXK0.
BgeeQ8IXK0.
GenevestigatorQ8IXK0.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
InterProIPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR012313. Znf_FCS.
[Graphical view]
PfamPF00536. SAM_1. 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

ChiTaRSPHC2. human.
GeneWikiPHC2.
GenomeRNAi1912.
NextBio35464715.
PROQ8IXK0.
SOURCESearch...

Entry information

Entry namePHC2_HUMAN
AccessionPrimary (citable) accession number: Q8IXK0
Secondary accession number(s): A1L4Q1 expand/collapse secondary AC list , A8KA40, D3DPR2, Q2TAL3, Q5T0C1, Q6NUJ6, Q6ZQR1, Q8N306, Q8TAG8, Q96BL4, Q9Y4Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 105 of the entry and version 1 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM