Q9H596 (DUS21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 21
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
Low molecular weight dual specificity phosphatase 21
Short name=LMW-DSP21

Gene names

Name:	DUSP21
Synonyms:	LMWDSP21

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	190 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subcellular location	Cytoplasm. Nucleus. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity Ref.1.
Tissue specificity	Expressed in testis. Ref.1
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane Mitochondrion Mitochondrion inner membrane Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 190	190	Dual specificity protein phosphatase 21		PRO_0000094834
Regions
	Domain	21 – 161	141	Tyrosine-protein phosphatase
	Region	43 – 128	86	Sufficient for mitochondrial localization By similarity
Sites
	Active site	106	1	Phosphocysteine intermediate By similarity
Natural variations
	Natural variant	167	1	R → C in a colorectal cancer sample; somatic mutation. Ref.6		VAR_035644
	Natural variant	186	1	M → T. Ref.2 Ref.3 Corresponds to variant rs1045031 [ dbSNP | Ensembl ].		VAR_019423
Experimental info
	Sequence conflict	190	1	M → I in CAG33440. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9H596 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 3E52BA31A4944EE3	FASTA	190	21,529
	10 20 30 40 50 60 MTASASSFSS SQGVQQPSIY SFSQITRSLF LSNGVAANDK LLLSSNRITA IVNASVEVVN 70 80 90 100 110 120 VFFEGIQYIK VPVTDARDSR LYDFFDPIAD LIHTIDMRQG RTLLHCMAGV SRSASLCLAY 130 140 150 160 170 180 LMKYHSMSLL DAHTWTKSRR PIIRPNNGFW EQLINYEFKL FNNNTVRMIN SPVGNIPDIY 190 EKDLRMMISM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of two novel low-molecular-weight dual specificity phosphatases." Hood K.L., Tobin J.F., Yoon C. Biochem. Biophys. Res. Commun. 298:545-551(2002) [PubMed: 12408986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Liver.
[2]	"Cloning and characterization of a new DUSP homolog gene." Mao Y., Xie Y., Dai J. Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-186.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-186.
[4]	"The DNA sequence of the human X chromosome." 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. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-167.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF533018 mRNA. Translation: AAN59788.1. AY156515 mRNA. Translation: AAO17295.1. CR457159 mRNA. Translation: CAG33440.1. AL133545 Genomic DNA. Translation: CAC10195.1. BC119755 mRNA. Translation: AAI19756.1. BC119756 mRNA. Translation: AAI19757.1.
IPI	IPI00419454.
RefSeq	NP_071359.3. NM_022076.3.
UniGene	Hs.534478.
3D structure databases
ProteinModelPortal	Q9H596.
SMR	Q9H596. Positions 22-181.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9H596.
Polymorphism databases
DMDM	50400652.
Proteomic databases
PRIDE	Q9H596.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000339042; ENSP00000343244; ENSG00000189037.
GeneID	63904.
KEGG	hsa:63904.
UCSC	uc004dgd.1. human.
Organism-specific databases
CTD	63904.
GeneCards	GC0XP044703.
H-InvDB	HIX0203318.
HGNC	HGNC:20476. DUSP21.
MIM	300678. gene.
neXtProt	NX_Q9H596.
PharmGKB	PA134967875.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15017.
HOGENOM	HBG717377.
HOVERGEN	HBG051422.
InParanoid	Q9H596.
OMA	AYLMELM.
OrthoDB	EOG4FBHV2.
PhylomeDB	Q9H596.
Gene expression databases
ArrayExpress	Q9H596.
Bgee	Q9H596.
CleanEx	HS_DUSP21.
Genevestigator	Q9H596.
GermOnline	ENSG00000189037. Homo sapiens.
Family and domain databases
InterPro	IPR020417. Dual-sp_phosphatase. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020420. Dual-sp_phosphatase_famB. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR000387. Tyr/Dual-specificity_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
KO	K14165.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PRINTS	PR01908. ADSPHPHTASE. PR01910. ADSPHPHTASEB.
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	65608.
SOURCE	Search...

Entry information

Entry name

DUS21_HUMAN

Accession

Primary (citable) accession number: Q9H596
Secondary accession number(s): Q0VDA6, Q6IAJ6, Q6YDQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.