DS13B_HUMAN
ID DS13B_HUMAN Reviewed; 198 AA.
AC Q9UII6; A0A024QZR6; A8K776; A8K782; B3KPY1; B3KXT0; B4DUK0; Q5JSC6; Q6IAR0;
AC Q96GC2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 176.
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:0000250|UniProtKB:Q9QYJ7};
DE AltName: Full=Dual specificity phosphatase SKRP4;
DE AltName: Full=Testis- and skeletal-muscle-specific DSP;
GN Name=DUSP13; Synonyms=DUSP13B, TMDP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RA Zama T., Aoki R., Murata M., Ikeda Y.;
RT "Identification of a novel dual specificity phosphatase, SKRP4.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-156.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 4), ALTERNATIVE PROMOTER USAGE, AND
RP TISSUE SPECIFICITY.
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 [7]
RP FUNCTION AS MAPK8 AND MAPK14 PHOSPHATASE.
RX PubMed=21360282; DOI=10.1007/s11010-011-0749-x;
RA Katagiri C., Masuda K., Nomura M., Tanoue K., Fujita S., Yamashita Y.,
RA Katakura R., Shiiba K., Nomura E., Sato M., Tanuma N., Shima H.;
RT "DUSP13B/TMDP inhibits stress-activated MAPKs and suppresses AP-1-dependent
RT gene expression.";
RL Mol. Cell. Biochem. 352:155-162(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=17044055; DOI=10.1002/prot.21197;
RA Kim S.J., Jeong D.G., Yoon T.S., Son J.H., Cho S.K., Ryu S.E., Kim J.H.;
RT "Crystal structure of human TMDP, a testis-specific dual specificity
RT protein phosphatase: implications for substrate specificity.";
RL Proteins 66:239-245(2007).
CC -!- FUNCTION: Dual specificity phosphatase that dephosphorylates MAPK8/JNK
CC and MAPK14/p38, but not MAPK1/ERK2, in vitro (PubMed:21360282).
CC Exhibits intrinsic phosphatase activity towards both phospho-
CC seryl/threonyl and -tyrosyl residues, with similar specific activities
CC in vitro (PubMed:10585869). {ECO:0000269|PubMed:10585869,
CC ECO:0000269|PubMed:21360282}.
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:Q9QYJ7, ECO:0000255|PROSITE-
CC ProRule:PRU10044};
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 -!- INTERACTION:
CC Q9UII6; Q9P1Z2: CALCOCO1; NbExp=6; IntAct=EBI-749800, EBI-749920;
CC Q9UII6; Q9H257: CARD9; NbExp=3; IntAct=EBI-749800, EBI-751319;
CC Q9UII6; Q9H257-2: CARD9; NbExp=8; IntAct=EBI-749800, EBI-11530605;
CC Q9UII6; Q96ED9: HOOK2; NbExp=3; IntAct=EBI-749800, EBI-743290;
CC Q9UII6; O75031: HSF2BP; NbExp=3; IntAct=EBI-749800, EBI-7116203;
CC Q9UII6; Q0VD86: INCA1; NbExp=3; IntAct=EBI-749800, EBI-6509505;
CC Q9UII6; P02545: LMNA; NbExp=7; IntAct=EBI-749800, EBI-351935;
CC Q9UII6; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-749800, EBI-949255;
CC Q9UII6; O14492-2: SH2B2; NbExp=3; IntAct=EBI-749800, EBI-19952306;
CC Q9UII6; Q13077: TRAF1; NbExp=3; IntAct=EBI-749800, EBI-359224;
CC Q9UII6; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-749800, EBI-527853;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=TMDP;
CC IsoId=Q9UII6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6B8I1-5; Sequence=External;
CC Name=4; Synonyms=TMDP-L2;
CC IsoId=Q9UII6-4; Sequence=VSP_037858;
CC Name=5;
CC IsoId=Q6B8I1-1; Sequence=External;
CC Name=6;
CC IsoId=Q6B8I1-2; Sequence=External;
CC Name=7;
CC IsoId=Q6B8I1-3; Sequence=External;
CC Name=8;
CC IsoId=Q6B8I1-4; Sequence=External;
CC -!- TISSUE SPECIFICITY: Highly expressed in the testis (at protein level)
CC (PubMed:10585869, PubMed:15252030). Also found in the skeletal muscle
CC (PubMed:15252030). {ECO:0000269|PubMed:10585869,
CC ECO:0000269|PubMed:15252030}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AB027004; BAA89412.1; -; mRNA.
DR EMBL; AB103375; BAD91014.1; -; mRNA.
DR EMBL; CR457094; CAG33375.1; -; mRNA.
DR EMBL; AL392111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54561.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54563.1; -; Genomic_DNA.
DR CCDS; CCDS31224.1; -. [Q9UII6-4]
DR CCDS; CCDS7346.1; -. [Q9UII6-1]
DR RefSeq; NP_001307772.1; NM_001320843.1. [Q9UII6-1]
DR RefSeq; NP_057448.3; NM_016364.3. [Q9UII6-1]
DR RefSeq; XP_005269947.1; XM_005269890.1. [Q9UII6-1]
DR RefSeq; XP_011538156.1; XM_011539854.2. [Q9UII6-1]
DR RefSeq; XP_011538157.1; XM_011539855.1. [Q9UII6-1]
DR RefSeq; XP_011538158.1; XM_011539856.2. [Q9UII6-1]
DR PDB; 2GWO; X-ray; 2.40 A; A/B/C/D=1-198.
DR PDB; 2PQ5; X-ray; 2.30 A; A/B/C/D=1-198.
DR PDBsum; 2GWO; -.
DR PDBsum; 2PQ5; -.
DR AlphaFoldDB; Q9UII6; -.
DR SMR; Q9UII6; -.
DR BioGRID; 119380; 103.
DR IntAct; Q9UII6; 15.
DR MINT; Q9UII6; -.
DR STRING; 9606.ENSP00000361785; -.
DR DEPOD; DUSP13; -.
DR iPTMnet; Q9UII6; -.
DR PhosphoSitePlus; Q9UII6; -.
DR BioMuta; DUSP13; -.
DR DMDM; 257051044; -.
DR MassIVE; Q9UII6; -.
DR PaxDb; Q9UII6; -.
DR PeptideAtlas; Q9UII6; -.
DR PRIDE; Q9UII6; -.
DR ProteomicsDB; 84529; -. [Q9UII6-1]
DR ProteomicsDB; 84532; -. [Q9UII6-4]
DR Antibodypedia; 15503; 269 antibodies from 27 providers.
DR DNASU; 51207; -.
DR Ensembl; ENST00000372700.7; ENSP00000361785.2; ENSG00000079393.21. [Q9UII6-4]
DR Ensembl; ENST00000472493.6; ENSP00000444580.1; ENSG00000079393.21. [Q9UII6-1]
DR Ensembl; ENST00000491677.6; ENSP00000436312.3; ENSG00000079393.21. [Q9UII6-1]
DR Ensembl; ENST00000607131.5; ENSP00000475801.2; ENSG00000079393.21. [Q9UII6-1]
DR GeneID; 51207; -.
DR UCSC; uc001jwr.4; human. [Q9UII6-1]
DR CTD; 51207; -.
DR DisGeNET; 51207; -.
DR GeneCards; DUSP13; -.
DR HGNC; HGNC:19681; DUSP13.
DR HPA; ENSG00000079393; Tissue enhanced (skeletal muscle, testis, tongue).
DR MIM; 613191; gene.
DR neXtProt; NX_Q9UII6; -.
DR OpenTargets; ENSG00000079393; -.
DR PharmGKB; PA134939640; -.
DR VEuPathDB; HostDB:ENSG00000079393; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000154628; -.
DR HOGENOM; CLU_027074_4_0_1; -.
DR InParanoid; Q9UII6; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q9UII6; -.
DR TreeFam; TF105128; -.
DR PathwayCommons; Q9UII6; -.
DR SignaLink; Q9UII6; -.
DR BioGRID-ORCS; 51207; 13 hits in 1080 CRISPR screens.
DR ChiTaRS; DUSP13; human.
DR EvolutionaryTrace; Q9UII6; -.
DR GenomeRNAi; 51207; -.
DR Pharos; Q9UII6; Tbio.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9UII6; protein.
DR Bgee; ENSG00000079393; Expressed in hindlimb stylopod muscle and 125 other tissues.
DR ExpressionAtlas; Q9UII6; baseline and differential.
DR Genevisible; Q9UII6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; TAS:ProtInc.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
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 3D-structure; Alternative promoter usage; Alternative splicing; Hydrolase;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..198
FT /note="Dual specificity protein phosphatase 13 isoform B"
FT /id="PRO_0000094820"
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"
FT VAR_SEQ 1
FT /note="M -> MAETSLPELGGEDKATPCPSILELEELLRAGKSSCSRVDEVWPNLFI
FT GDAM (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_037858"
FT VARIANT 62
FT /note="R -> Q (in dbSNP:rs16932004)"
FT /id="VAR_057130"
FT VARIANT 156
FT /note="C -> Y (in dbSNP:rs3088142)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025431"
FT VARIANT 190
FT /note="R -> G (in dbSNP:rs16931996)"
FT /id="VAR_057131"
FT CONFLICT 82
FT /note="K -> E (in Ref. 3; CAG33375)"
FT /evidence="ECO:0000305"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:2PQ5"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:2PQ5"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2PQ5"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:2PQ5"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:2PQ5"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2PQ5"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:2PQ5"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2PQ5"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2PQ5"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:2PQ5"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:2PQ5"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2GWO"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2PQ5"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2PQ5"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:2PQ5"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:2PQ5"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2PQ5"
FT HELIX 178..192
FT /evidence="ECO:0007829|PDB:2PQ5"
SQ SEQUENCE 198 AA; 22149 MW; 82EF05AB74E031EB CRC64;
MDSLQKQDLR RPKIHGAVQA SPYQPPTLAS LQRLLWVRQA ATLNHIDEVW PSLFLGDAYA
ARDKSKLIQL GITHVVNAAA GKFQVDTGAK FYRGMSLEYY GIEADDNPFF DLSVYFLPVA
RYIRAALSVP QGRVLVHCAM GVSRSATLVL AFLMICENMT LVEAIQTVQA HRNICPNSGF
LRQLQVLDNR LGRETGRF
