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Database: UniProt
Entry: H0ZS88_TAEGU
LinkDB: H0ZS88_TAEGU
Original site: H0ZS88_TAEGU 
ID   H0ZS88_TAEGU            Unreviewed;       211 AA.
AC   H0ZS88;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   16-OCT-2019, entry version 37.
DE   RecName: Full=Cyclin-dependent kinase inhibitor 3 {ECO:0000256|PIRNR:PIRNR037322};
DE            EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR037322};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR037322};
GN   Name=CDKN3 {ECO:0000313|Ensembl:ENSTGUP00000013484};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea;
OC   Estrildidae; Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000013484, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000013484, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C.,
RA   London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B.,
RA   Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B.,
RA   Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M.,
RA   Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P.,
RA   Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T.,
RA   Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A.,
RA   Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E.,
RA   Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D.,
RA   Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H.,
RA   Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J.,
RA   Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000013484}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2012) to UniProtKB.
CC   -!- FUNCTION: May play a role in cell cycle regulation. Dual
CC       specificity phosphatase active toward substrates containing either
CC       phosphotyrosine or phosphoserine residues.
CC       {ECO:0000256|PIRNR:PIRNR037322}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
CC         [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC         COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC         EC=3.1.3.16; Evidence={ECO:0000256|PIRNR:PIRNR037322};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000256|PIRNR:PIRNR037322}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000256|PIRNR:PIRNR037322}.
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DR   EMBL; ABQF01004137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABQF01004138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABQF01004139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABQF01004140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSTGUT00000013637; ENSTGUP00000013484; ENSTGUG00000013094.
DR   eggNOG; KOG1720; Eukaryota.
DR   eggNOG; COG2453; LUCA.
DR   GeneTree; ENSGT00390000004717; -.
DR   InParanoid; H0ZS88; -.
DR   OMA; ALPGCKY; -.
DR   TreeFam; TF101040; -.
DR   Proteomes; UP000007754; Chromosome 5.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:Ensembl.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR008425; CDK_inhib_3.
DR   InterPro; IPR022778; CDKN3.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; TYR_PHOSPHATASE_dom.
DR   Pfam; PF05706; CDKN3; 1.
DR   PIRSF; PIRSF037322; CDKN3; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|PIRNR:PIRNR037322};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007754};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR037322};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037322};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR037322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007754}.
FT   DOMAIN      119    186       TYR_PHOSPHATASE_2. {ECO:0000259|PROSITE:
FT                                PS50056}.
FT   ACT_SITE    139    139       Phosphocysteine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR037322-1}.
SQ   SEQUENCE   211 AA;  23256 MW;  8CBB35A7E352451A CRC64;
     PQPAAAPADG FASSDDEAAE EEPSPLHISW LSLSPLYSSE FLGLCSLPGC RFKDVRRNLQ
     KDIGELKSCG IQDIFVLCTR GELSKYRVPN LLDTYQQHGM CVHHHPIPDG NAPDIATCCK
     ILEELRTCLE NKQKAMIHCY GGLGRSCLVA ACLLLQLSDT LAPQQVIESL RNLRGSGAIQ
     TIKQYNFLHD FRENLAAHLA TKDPVLRSAS R
//
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