CDKN3_MOUSE
ID CDKN3_MOUSE Reviewed; 211 AA.
AC Q810P3; Q9CWS3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cyclin-dependent kinase inhibitor 3 {ECO:0000250|UniProtKB:Q16667, ECO:0000312|EMBL:AAH49694.1};
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=CDK2-associated dual-specificity phosphatase {ECO:0000250|UniProtKB:Q16667};
DE AltName: Full=Kinase-associated phosphatase {ECO:0000250|UniProtKB:Q16667};
GN Name=Cdkn3 {ECO:0000312|MGI:MGI:1919641};
GN Synonyms=Kap {ECO:0000250|UniProtKB:Q16667};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAE27067.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB26929.1}, and
RC DBA/2J {ECO:0000312|EMBL:BAE27067.1};
RC TISSUE=Embryonic stem cell {ECO:0000312|EMBL:BAB26929.1}, and
RC Embryonic testis {ECO:0000312|EMBL:BAC28238.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|EMBL:AAH49694.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH49694.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May play a role in cell cycle regulation. Dual specificity
CC phosphatase active toward substrates containing either phosphotyrosine
CC or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a
CC cyclin-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q16667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000250|UniProtKB:Q16667};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Interacts with cyclin-dependent kinases such as CDK1, CDK2 and
CC CDK3. Does not interact with CDK4. Interacts (via C-terminus) with
CC phosphorylated CDK2 (via C-terminal helix). Interacts with MS4A3 (via
CC C-terminus); the interaction enhances CDKN3 enzymatic activity (By
CC similarity). {ECO:0000250|UniProtKB:Q16667}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q16667}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26929.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAC28238.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AK010426; BAB26929.1; ALT_SEQ; mRNA.
DR EMBL; AK033341; BAC28238.1; ALT_SEQ; mRNA.
DR EMBL; AK146312; BAE27067.1; -; mRNA.
DR EMBL; BC049694; AAH49694.1; -; mRNA.
DR CCDS; CCDS49466.1; -.
DR RefSeq; NP_082498.1; NM_028222.1.
DR AlphaFoldDB; Q810P3; -.
DR SMR; Q810P3; -.
DR STRING; 10090.ENSMUSP00000070575; -.
DR PhosphoSitePlus; Q810P3; -.
DR PaxDb; Q810P3; -.
DR PRIDE; Q810P3; -.
DR ProteomicsDB; 281519; -.
DR Antibodypedia; 3940; 532 antibodies from 31 providers.
DR DNASU; 72391; -.
DR Ensembl; ENSMUST00000067426; ENSMUSP00000070575; ENSMUSG00000037628.
DR GeneID; 72391; -.
DR KEGG; mmu:72391; -.
DR UCSC; uc007the.2; mouse.
DR CTD; 1033; -.
DR MGI; MGI:1919641; Cdkn3.
DR VEuPathDB; HostDB:ENSMUSG00000037628; -.
DR eggNOG; KOG1720; Eukaryota.
DR GeneTree; ENSGT00390000004717; -.
DR HOGENOM; CLU_047330_1_0_1; -.
DR InParanoid; Q810P3; -.
DR OMA; PFHISWL; -.
DR OrthoDB; 1539111at2759; -.
DR PhylomeDB; Q810P3; -.
DR TreeFam; TF101040; -.
DR BioGRID-ORCS; 72391; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Cdkn3; mouse.
DR PRO; PR:Q810P3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q810P3; protein.
DR Bgee; ENSMUSG00000037628; Expressed in seminiferous tubule of testis and 159 other tissues.
DR ExpressionAtlas; Q810P3; baseline and differential.
DR Genevisible; Q810P3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
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_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_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.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..211
FT /note="Cyclin-dependent kinase inhibitor 3"
FT /id="PRO_0000396637"
FT DOMAIN 32..200
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..34
FT /note="Interaction with CDK2"
FT /evidence="ECO:0000250|UniProtKB:Q16667"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 211 AA; 23793 MW; A119D81C61A7F20F CRC64;
MKPPISIQAS EFDSSDEEPV DEEQTPIQIS WLPLSRVNCS QFLGLCALPG CKFKDVRRNI
QKDTEELKSY GIQDVFVFCT RGELSKYRVP NLLDLYQQYG IVTHHHPIPD GGTPDIGSCW
EIMEELATCL KNNRKTLIHC YGGLGRSCLA ACLLLYLSDS ISPQQAIDSL RDVRGSGAIQ
TIKQYNYLHE FRDKLAAYLS SRDSLSRSVS R
