ID DS13B_HUMAN Reviewed; 198 AA. AC Q9UII6; A0A024QZR6; A8K776; A8K782; B3KPY1; B3KXT0; B4DUK0; Q5JSC6; Q6IAR0; AC Q96GC2; U3KQ82; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 3. DT 24-JAN-2024, entry version 183. DE RecName: Full=Dual specificity protein phosphatase 13B {ECO:0000305}; DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9QYJ7}; 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=DUSP13B {ECO:0000312|HGNC:HGNC:19681}; GN Synonyms=DUSP13, SKRP4, 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), AND 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 Evidence={ECO:0000250|UniProtKB:Q9QYJ7}; 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 Evidence={ECO:0000250|UniProtKB:Q9QYJ7}; 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 splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=TMDP; CC IsoId=Q9UII6-1; Sequence=Displayed; CC Name=4; Synonyms=TMDP-L2; CC IsoId=Q9UII6-4; Sequence=VSP_037858; CC Name=5; CC IsoId=Q9UII6-5; Sequence=VSP_061945; 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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class dual specificity subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS86105.1; -. [Q9UII6-5] DR RefSeq; NP_001307772.1; NM_001320843.1. [Q9UII6-1] DR RefSeq; NP_057448.3; NM_016364.3. [Q9UII6-1] DR RefSeq; XP_005269941.3; XM_005269884.4. DR RefSeq; XP_005269947.1; XM_005269890.1. DR RefSeq; XP_011538156.1; XM_011539854.2. DR RefSeq; XP_011538157.1; XM_011539855.1. DR RefSeq; XP_011538158.1; XM_011539856.2. 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.ENSP00000475626; -. DR DEPOD; DUSP13; -. DR iPTMnet; Q9UII6; -. DR PhosphoSitePlus; Q9UII6; -. DR BioMuta; DUSP13; -. DR DMDM; 257051044; -. DR MassIVE; Q9UII6; -. DR PaxDb; 9606-ENSP00000361785; -. DR PeptideAtlas; Q9UII6; -. DR ProteomicsDB; 84529; -. [Q9UII6-1] DR ProteomicsDB; 84532; -. [Q9UII6-4] DR Antibodypedia; 15503; 303 antibodies from 27 providers. DR DNASU; 51207; -. DR Ensembl; ENST00000372700.8; ENSP00000361785.2; ENSG00000079393.21. [Q9UII6-4] DR Ensembl; ENST00000472493.6; ENSP00000444580.1; ENSG00000079393.21. [Q9UII6-1] DR Ensembl; ENST00000478873.7; ENSP00000475626.1; ENSG00000079393.21. [Q9UII6-5] DR Ensembl; ENST00000707121.1; ENSP00000516749.1; ENSG00000079393.21. [Q9UII6-1] DR GeneID; 51207; -. DR KEGG; hsa:51207; -. DR MANE-Select; ENST00000478873.7; ENSP00000475626.1; NM_001363514.2; NP_001350443.1. [Q9UII6-5] DR UCSC; uc001jwr.4; human. [Q9UII6-1] DR AGR; HGNC:19681; -. DR CTD; 51207; -. DR DisGeNET; 51207; -. DR GeneCards; DUSP13B; -. DR HGNC; HGNC:19681; DUSP13B. 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; 1082488at2759; -. DR PhylomeDB; Q9UII6; -. DR TreeFam; TF105128; -. DR PathwayCommons; Q9UII6; -. DR SignaLink; Q9UII6; -. DR BioGRID-ORCS; 51207; 20 hits in 1170 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 127 other cell types or tissues. DR ExpressionAtlas; Q9UII6; baseline and differential. 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 CDD; cd14577; DUSP13B; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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; AGAP008228-PA; 1. DR PANTHER; PTHR45682:SF10; DUAL SPECIFICITY PROTEIN PHOSPHATASE 13 ISOFORM B; 1. DR Pfam; PF00782; DSPc; 1. DR PRINTS; PR01908; ADSPHPHTASE. DR PRINTS; PR01909; ADSPHPHTASEA. DR SMART; SM00195; DSPc; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. DR Genevisible; Q9UII6; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Hydrolase; Protein phosphatase; KW Reference proteome. FT CHAIN 1..198 FT /note="Dual specificity protein phosphatase 13B" 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 VAR_SEQ 1 FT /note="M -> MPQVGGRPLSHLERSQWGMRRTAWSSLPPCPTASHWVSLAKPAASWV FT PVSFSGPGTAYQREKMFFPVCTFPSHWSRGSGAVSKDRTPSPTRHQAHILVPLKIQLRR FT VPDSFSQQMPETSYLTRVGPDIQCWPESWGM (in isoform 5)" FT /id="VSP_061945" 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 //