DS13B_MOUSE
ID DS13B_MOUSE Reviewed; 198 AA.
AC Q9QYJ7; Q497R2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Dual specificity protein phosphatase 13 isoform B;
DE Short=DUSP13B;
DE EC=3.1.3.16;
DE EC=3.1.3.48 {ECO:0000269|PubMed:10585869};
DE AltName: Full=Dual specificity tyrosine phosphatase TS-DSP6;
DE AltName: Full=Testis- and skeletal muscle-specific DSP;
GN Name=Dusp13; Synonyms=Gm1203, Tmdp;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10585869; DOI=10.1042/bj3440819;
RA Nakamura K., Shima H., Watanabe M., Haneji T., Kikuchi K.;
RT "Molecular cloning and characterization of a novel dual-specificity protein
RT phosphatase possibly involved in spermatogenesis.";
RL Biochem. J. 344:819-825(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
RN [3]
RP ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15252030; DOI=10.1074/jbc.m405286200;
RA Chen H.-H., Luche R., Wei B., Tonks N.K.;
RT "Characterization of two distinct dual specificity phosphatases encoded in
RT alternative open reading frames of a single gene located on human
RT chromosome 10q22.2.";
RL J. Biol. Chem. 279:41404-41413(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Dual specificity phosphatase that dephosphorylates MAPK8/JNK
CC and MAPK14/p38, but not MAPK1/ERK2, in vitro (By similarity). Exhibits
CC intrinsic phosphatase activity towards both phospho-seryl/threonyl and
CC -tyrosyl residues, with similar specific activities in vitro
CC (PubMed:10585869). {ECO:0000250|UniProtKB:Q9UII6,
CC ECO:0000269|PubMed:10585869}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:10585869};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=2;
CC IsoId=Q9QYJ7-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q6B8I0-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in the testis.
CC {ECO:0000269|PubMed:15252030}.
CC -!- DEVELOPMENTAL STAGE: Not detectable in testis in the first 3 weeks of
CC life. The expression markedly increases at approximately the 3rd week
CC after birth and continues to increase gradually into adulthood.
CC {ECO:0000269|PubMed:15252030}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AB027003; BAA89411.1; -; mRNA.
DR EMBL; AF237620; AAK15037.1; -; mRNA.
DR EMBL; BC100421; AAI00422.1; -; mRNA.
DR CCDS; CCDS88592.1; -. [Q9QYJ7-1]
DR RefSeq; NP_038877.2; NM_013849.3.
DR RefSeq; XP_006519139.1; XM_006519076.3.
DR AlphaFoldDB; Q9QYJ7; -.
DR SMR; Q9QYJ7; -.
DR BioGRID; 205196; 1.
DR STRING; 10090.ENSMUSP00000113305; -.
DR PaxDb; Q9QYJ7; -.
DR PRIDE; Q9QYJ7; -.
DR ProteomicsDB; 275402; -. [Q9QYJ7-1]
DR Antibodypedia; 15503; 269 antibodies from 27 providers.
DR DNASU; 27389; -.
DR Ensembl; ENSMUST00000120984; ENSMUSP00000113985; ENSMUSG00000021768. [Q9QYJ7-1]
DR Ensembl; ENSMUST00000184703; ENSMUSP00000138972; ENSMUSG00000021768. [Q9QYJ7-1]
DR GeneID; 27389; -.
DR UCSC; uc007slm.2; mouse. [Q9QYJ7-1]
DR CTD; 51207; -.
DR MGI; MGI:1351599; Dusp13.
DR VEuPathDB; HostDB:ENSMUSG00000021768; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000154628; -.
DR HOGENOM; CLU_027074_4_0_1; -.
DR InParanoid; Q9QYJ7; -.
DR OrthoDB; 1576308at2759; -.
DR BioGRID-ORCS; 27389; 2 hits in 58 CRISPR screens.
DR ChiTaRS; Dusp13; mouse.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9QYJ7; protein.
DR Bgee; ENSMUSG00000021768; Expressed in spermatid and 47 other tissues.
DR ExpressionAtlas; Q9QYJ7; baseline and differential.
DR Genevisible; Q9QYJ7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0016311; P:dephosphorylation; ISO:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020405; Atypical_DUSP_subfamA.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45682; PTHR45682; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01909; ADSPHPHTASEA.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Hydrolase; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..198
FT /note="Dual specificity protein phosphatase 13 isoform B"
FT /id="PRO_0000094821"
FT DOMAIN 45..193
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 138
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 198 AA; 22481 MW; C2493597D6D3732B CRC64;
MDSLQKQELR RPKIHGAVQV SPYQPPTLAS LQRLLWVRRT ATLTHINEVW PNLFLGDAYA
ARDKGRLIQL GITHVVNVAA GKFQVDTGAK FYRGTPLEYY GIEADDNPFF DLSVHFLPVA
RYIRDALNIP RSRVLVHCAM GVSRSATIVL AFLMIFENMT LVDAIQTVQA HRDICPNSGF
LRQLQVLDNR LRRETGRL
