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   10-FEB-2009, entry version 56.
DE   RecName: Full=Dual specificity protein phosphatase 21;
DE            EC=3.1.3.48;
DE            EC=3.1.3.16;
DE   AltName: Full=Low molecular weight dual specificity phosphatase 21;
GN   Name=DUSP21; Synonyms=LMWDSP21;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, CHARACTERIZATION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   MEDLINE=22296578; 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
RT   dual 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.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   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.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   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.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   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.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   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.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., 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
RT   project: 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.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Can dephosphorylate single and diphosphorylated
CC       synthetic MAPK peptides, with preference for the phosphotyrosine
CC       and diphosphorylated forms over phosphothreonine.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in testis.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class dual specificity subfamily.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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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; CAC10195.1; -; Genomic_DNA.
DR   EMBL; BC119755; AAI19756.1; -; mRNA.
DR   EMBL; BC119756; AAI19757.1; -; mRNA.
DR   IPI; IPI00419454; -.
DR   RefSeq; NP_071359.2; -.
DR   UniGene; Hs.534478; -.
DR   HSSP; Q05923; 1M3G.
DR   SMR; Q9H596; 22-181.
DR   PRIDE; Q9H596; -.
DR   Ensembl; ENSG00000189037; Homo sapiens.
DR   GeneID; 63904; -.
DR   KEGG; hsa:63904; -.
DR   GeneCards; GC0XP044588; -.
DR   H-InvDB; HIX0056144; -.
DR   HGNC; HGNC:20476; DUSP21.
DR   MIM; 300678; gene.
DR   PharmGKB; PA134967875; -.
DR   HOGENOM; Q9H596; -.
DR   HOVERGEN; Q9H596; -.
DR   BRENDA; 3.1.3.16; 247.
DR   BRENDA; 3.1.3.48; 247.
DR   NextBio; 65608; -.
DR   ArrayExpress; Q9H596; -.
DR   Bgee; Q9H596; -.
DR   CleanEx; HS_DUSP21; -.
DR   GermOnline; ENSG00000189037; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphata...; IEA:InterPro.
DR   GO; GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR   InterPro; IPR000387; Tyr_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000340; Tyr_Pase_dual_specific.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 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; Nucleus; Polymorphism; Protein phosphatase.
FT   CHAIN         1    190       Dual specificity protein phosphatase 21.
FT                                /FTId=PRO_0000094834.
FT   DOMAIN       21    161       Tyrosine-protein phosphatase.
FT   ACT_SITE    106    106       Phosphocysteine intermediate (By
FT                                similarity).
FT   VARIANT     167    167       R -> C (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_035644.
FT   VARIANT     186    186       M -> T (in dbSNP:rs1045031).
FT                                /FTId=VAR_019423.
FT   CONFLICT    190    190       M -> I (in Ref. 3; CAG33440).
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
//