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Dual specificity protein phosphatase 21 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular weight dual specificity phosphatase 21) (LMW-DSP21)

 DUS21_HUMAN             Reviewed;         190 AA.
Q9H596; Q0VDA6; Q6IAJ6; Q6YDQ8;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
28-FEB-2018, entry version 129.
RecName: Full=Dual specificity protein phosphatase 21;
EC=3.1.3.16;
EC=3.1.3.48;
AltName: Full=Low molecular weight dual specificity phosphatase 21;
Short=LMW-DSP21;
Name=DUSP21; Synonyms=LMWDSP21;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=12408986; DOI=10.1016/S0006-291X(02)02488-9;
Hood K.L., Tobin J.F., Yoon C.;
"Identification and characterization of two novel low-molecular-weight
dual specificity phosphatases.";
Biochem. Biophys. Res. Commun. 298:545-551(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-186.
Mao Y., Xie Y., Dai J.;
"Cloning and characterization of a new DUSP homolog gene.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-186.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
VARIANT [LARGE SCALE ANALYSIS] CYS-167.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Can dephosphorylate single and diphosphorylated
synthetic MAPK peptides, with preference for the phosphotyrosine
and diphosphorylated forms over phosphothreonine.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- INTERACTION:
Q9NP55:BPIFA1; NbExp=4; IntAct=EBI-7357329, EBI-953896;
Q9H8Y8:GORASP2; NbExp=5; IntAct=EBI-7357329, EBI-739467;
Q96MT4:LINC01600; NbExp=4; IntAct=EBI-7357329, EBI-12804988;
Q8IYF3:TEX11; NbExp=3; IntAct=EBI-7357329, EBI-742397;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12408986}.
Nucleus {ECO:0000269|PubMed:12408986}. Mitochondrion inner
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Matrix side {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in testis.
{ECO:0000269|PubMed:12408986}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class dual specificity subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF533018; AAN59788.1; -; mRNA.
EMBL; AY156515; AAO17295.1; -; mRNA.
EMBL; CR457159; CAG33440.1; -; mRNA.
EMBL; AL133545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC119755; AAI19756.1; -; mRNA.
EMBL; BC119756; AAI19757.1; -; mRNA.
CCDS; CCDS14264.1; -.
RefSeq; NP_071359.3; NM_022076.3.
UniGene; Hs.534478; -.
ProteinModelPortal; Q9H596; -.
SMR; Q9H596; -.
BioGrid; 121980; 49.
IntAct; Q9H596; 20.
MINT; Q9H596; -.
STRING; 9606.ENSP00000343244; -.
DEPOD; Q9H596; -.
iPTMnet; Q9H596; -.
PhosphoSitePlus; Q9H596; -.
BioMuta; DUSP21; -.
DMDM; 50400652; -.
PaxDb; Q9H596; -.
PeptideAtlas; Q9H596; -.
PRIDE; Q9H596; -.
DNASU; 63904; -.
Ensembl; ENST00000339042; ENSP00000343244; ENSG00000189037.
GeneID; 63904; -.
KEGG; hsa:63904; -.
UCSC; uc004dgd.4; human.
CTD; 63904; -.
DisGeNET; 63904; -.
EuPathDB; HostDB:ENSG00000189037.7; -.
GeneCards; DUSP21; -.
HGNC; HGNC:20476; DUSP21.
MIM; 300678; gene.
neXtProt; NX_Q9H596; -.
OpenTargets; ENSG00000189037; -.
PharmGKB; PA134967875; -.
eggNOG; KOG1718; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000118853; -.
HOGENOM; HOG000233766; -.
HOVERGEN; HBG051422; -.
InParanoid; Q9H596; -.
KO; K14165; -.
OMA; RMINSPV; -.
OrthoDB; EOG091G0249; -.
PhylomeDB; Q9H596; -.
TreeFam; TF316009; -.
GenomeRNAi; 63904; -.
PRO; PR:Q9H596; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000189037; -.
CleanEx; HS_DUSP21; -.
Genevisible; Q9H596; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
CDD; cd00127; DSPc; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR020417; Atypical_DUSP.
InterPro; IPR020420; Atypical_DUSP_famB.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR024950; DUSP.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR10159; PTHR10159; 1.
Pfam; PF00782; DSPc; 1.
PRINTS; PR01908; ADSPHPHTASE.
PRINTS; PR01910; ADSPHPHTASEB.
SMART; SM00195; DSPc; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Hydrolase; Membrane; Mitochondrion;
Mitochondrion inner membrane; Nucleus; Polymorphism;
Protein phosphatase; Reference proteome.
CHAIN 1 190 Dual specificity protein phosphatase 21.
/FTId=PRO_0000094834.
DOMAIN 21 161 Tyrosine-protein phosphatase.
REGION 43 128 Sufficient for mitochondrial
localization. {ECO:0000250}.
ACT_SITE 106 106 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10044}.
VARIANT 167 167 R -> C (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035644.
VARIANT 186 186 M -> T (in dbSNP:rs1045031).
{ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_019423.
CONFLICT 190 190 M -> I (in Ref. 3; CAG33440).
{ECO:0000305}.
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


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