ID DUS21_HUMAN Reviewed; 190 AA. AC Q9H596; Q0VDA6; Q6IAJ6; Q6YDQ8; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 164. DE RecName: Full=Dual specificity protein phosphatase 21; DE EC=3.1.3.16; DE EC=3.1.3.48; DE AltName: Full=Low molecular weight dual specificity phosphatase 21; DE Short=LMW-DSP21; GN Name=DUSP21; Synonyms=LMWDSP21; 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], CHARACTERIZATION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=12408986; DOI=10.1016/s0006-291x(02)02488-9; RA Hood K.L., Tobin J.F., Yoon C.; RT "Identification and characterization of two novel low-molecular-weight dual RT specificity phosphatases."; RL Biochem. Biophys. Res. Commun. 298:545-551(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-186. RA Mao Y., Xie Y., Dai J.; RT "Cloning and characterization of a new DUSP homolog gene."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-186. 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=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [6] RP VARIANT [LARGE SCALE ANALYSIS] CYS-167. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Can dephosphorylate single and diphosphorylated synthetic CC MAPK peptides, with preference for the phosphotyrosine and CC diphosphorylated forms over phosphothreonine. 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}; 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 Q9H596; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-7357329, EBI-12811889; CC Q9H596; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-7357329, EBI-953896; CC Q9H596; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-7357329, EBI-12012272; CC Q9H596; P56545-3: CTBP2; NbExp=3; IntAct=EBI-7357329, EBI-10171902; CC Q9H596; O00167-2: EYA2; NbExp=3; IntAct=EBI-7357329, EBI-12807776; CC Q9H596; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-7357329, EBI-12013806; CC Q9H596; Q7L5D6: GET4; NbExp=3; IntAct=EBI-7357329, EBI-711823; CC Q9H596; Q9H8Y8: GORASP2; NbExp=7; IntAct=EBI-7357329, EBI-739467; CC Q9H596; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-7357329, EBI-14103818; CC Q9H596; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-7357329, EBI-10693436; CC Q9H596; Q14525: KRT33B; NbExp=3; IntAct=EBI-7357329, EBI-1049638; CC Q9H596; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-7357329, EBI-1052037; CC Q9H596; Q13163: MAP2K5; NbExp=3; IntAct=EBI-7357329, EBI-307294; CC Q9H596; O43482: OIP5; NbExp=3; IntAct=EBI-7357329, EBI-536879; CC Q9H596; Q15319: POU4F3; NbExp=3; IntAct=EBI-7357329, EBI-12033574; CC Q9H596; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-7357329, EBI-746118; CC Q9H596; P51687: SUOX; NbExp=3; IntAct=EBI-7357329, EBI-3921347; CC Q9H596; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-7357329, EBI-742397; CC Q9H596; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-7357329, EBI-11523345; CC Q9H596; Q13077: TRAF1; NbExp=3; IntAct=EBI-7357329, EBI-359224; CC Q9H596; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-7357329, EBI-947187; CC Q9H596; O75604: USP2; NbExp=3; IntAct=EBI-7357329, EBI-743272; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12408986}. Nucleus CC {ECO:0000269|PubMed:12408986}. Mitochondrion inner membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side CC {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12408986}. 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; AF533018; AAN59788.1; -; mRNA. DR EMBL; AY156515; AAO17295.1; -; mRNA. DR EMBL; CR457159; CAG33440.1; -; mRNA. DR EMBL; AL133545; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC119755; AAI19756.1; -; mRNA. DR EMBL; BC119756; AAI19757.1; -; mRNA. DR CCDS; CCDS14264.1; -. DR RefSeq; NP_071359.3; NM_022076.3. DR AlphaFoldDB; Q9H596; -. DR SMR; Q9H596; -. DR BioGRID; 121980; 85. DR IntAct; Q9H596; 38. DR MINT; Q9H596; -. DR STRING; 9606.ENSP00000343244; -. DR DEPOD; DUSP21; -. DR iPTMnet; Q9H596; -. DR PhosphoSitePlus; Q9H596; -. DR BioMuta; DUSP21; -. DR DMDM; 50400652; -. DR jPOST; Q9H596; -. DR MassIVE; Q9H596; -. DR PaxDb; 9606-ENSP00000343244; -. DR PeptideAtlas; Q9H596; -. DR ProteomicsDB; 80901; -. DR Antibodypedia; 25173; 75 antibodies from 11 providers. DR DNASU; 63904; -. DR Ensembl; ENST00000339042.6; ENSP00000343244.4; ENSG00000189037.8. DR GeneID; 63904; -. DR KEGG; hsa:63904; -. DR MANE-Select; ENST00000339042.6; ENSP00000343244.4; NM_022076.4; NP_071359.3. DR UCSC; uc004dgd.4; human. DR AGR; HGNC:20476; -. DR CTD; 63904; -. DR DisGeNET; 63904; -. DR GeneCards; DUSP21; -. DR HGNC; HGNC:20476; DUSP21. DR HPA; ENSG00000189037; Tissue enriched (testis). DR MIM; 300678; gene. DR neXtProt; NX_Q9H596; -. DR OpenTargets; ENSG00000189037; -. DR PharmGKB; PA134967875; -. DR VEuPathDB; HostDB:ENSG00000189037; -. DR eggNOG; KOG1718; Eukaryota. DR GeneTree; ENSGT00940000163638; -. DR HOGENOM; CLU_027074_3_2_1; -. DR InParanoid; Q9H596; -. DR OMA; CVINCAY; -. DR OrthoDB; 127323at2759; -. DR PhylomeDB; Q9H596; -. DR TreeFam; TF316009; -. DR PathwayCommons; Q9H596; -. DR SignaLink; Q9H596; -. DR BioGRID-ORCS; 63904; 13 hits in 786 CRISPR screens. DR GenomeRNAi; 63904; -. DR Pharos; Q9H596; Tdark. DR PRO; PR:Q9H596; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9H596; Protein. DR Bgee; ENSG00000189037; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 22 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB. DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB. DR CDD; cd14573; DUSP18_21; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR020420; Atypical_DUSP_subfamB. 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; PTHR46495; DUAL SPECIFICITY PROTEIN PHOSPHATASE 21; 1. DR PANTHER; PTHR46495:SF1; DUAL SPECIFICITY PROTEIN PHOSPHATASE 21; 1. DR Pfam; PF00782; DSPc; 1. DR PRINTS; PR01908; ADSPHPHTASE. DR PRINTS; PR01910; ADSPHPHTASEB. 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; Q9H596; HS. PE 1: Evidence at protein level; KW Cytoplasm; Hydrolase; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Nucleus; Protein phosphatase; KW Reference proteome. FT CHAIN 1..190 FT /note="Dual specificity protein phosphatase 21" FT /id="PRO_0000094834" FT DOMAIN 21..162 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 43..128 FT /note="Sufficient for mitochondrial localization" FT /evidence="ECO:0000250" FT ACT_SITE 106 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT VARIANT 167 FT /note="R -> C (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs1372839121)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035644" FT VARIANT 186 FT /note="M -> T (in dbSNP:rs1045031)" FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3" FT /id="VAR_019423" FT CONFLICT 190 FT /note="M -> I (in Ref. 3; CAG33440)" FT /evidence="ECO:0000305" SQ SEQUENCE 190 AA; 21529 MW; 3E52BA31A4944EE3 CRC64; MTASASSFSS SQGVQQPSIY SFSQITRSLF LSNGVAANDK LLLSSNRITA IVNASVEVVN VFFEGIQYIK VPVTDARDSR LYDFFDPIAD LIHTIDMRQG RTLLHCMAGV SRSASLCLAY LMKYHSMSLL DAHTWTKSRR PIIRPNNGFW EQLINYEFKL FNNNTVRMIN SPVGNIPDIY EKDLRMMISM //