DUS21_HUMAN
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 03-AUG-2022, entry version 155.
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}.
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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; Q9H596; -.
DR PeptideAtlas; Q9H596; -.
DR PRIDE; Q9H596; -.
DR ProteomicsDB; 80901; -.
DR Antibodypedia; 25173; 55 antibodies from 10 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 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; QLIRYEM; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q9H596; -.
DR TreeFam; TF316009; -.
DR PathwayCommons; Q9H596; -.
DR SignaLink; Q9H596; -.
DR BioGRID-ORCS; 63904; 13 hits in 704 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 sperm and 21 other tissues.
DR Genevisible; Q9H596; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:Ensembl.
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 Gene3D; 3.90.190.10; -; 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 Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01910; ADSPHPHTASEB.
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 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
