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Q9H596 (DUS21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190Dual specificity protein phosphatase 21
PRO_0000094834

Regions

Domain21 – 161141Tyrosine-protein phosphatase
Region43 – 12886Sufficient for mitochondrial localization By similarity

Sites

Active site1061Phosphocysteine intermediate By similarity

Natural variations

Natural variant1671R → C in a colorectal cancer sample; somatic mutation. Ref.6
VAR_035644
Natural variant1861M → T. Ref.2 Ref.3
Corresponds to variant rs1045031 [ dbSNP | Ensembl ].
VAR_019423

Experimental info

Sequence conflict1901M → I in CAG33440. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9H596 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 3E52BA31A4944EE3

FASTA19021,529
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-167.

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.
CCDSCCDS14264.1.
RefSeqNP_071359.3. NM_022076.3.
UniGeneHs.534478.

3D structure databases

ProteinModelPortalQ9H596.
SMRQ9H596. Positions 22-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121980. 2 interactions.
IntActQ9H596. 1 interaction.
MINTMINT-3068077.
STRING9606.ENSP00000343244.

Polymorphism databases

DMDM50400652.

Proteomic databases

PaxDbQ9H596.
PRIDEQ9H596.

Protocols and materials databases

DNASU63904.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339042; ENSP00000343244; ENSG00000189037.
GeneID63904.
KEGGhsa:63904.
UCSCuc004dgd.3. human.

Organism-specific databases

CTD63904.
GeneCardsGC0XP044703.
HGNCHGNC:20476. DUSP21.
MIM300678. gene.
neXtProtNX_Q9H596.
PharmGKBPA134967875.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000233766.
HOVERGENHBG051422.
InParanoidQ9H596.
KOK14165.
OMAFWEQLIN.
OrthoDBEOG7PK90H.
PhylomeDBQ9H596.
TreeFamTF316009.

Gene expression databases

BgeeQ9H596.
CleanExHS_DUSP21.
GenevestigatorQ9H596.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi63904.
NextBio65608.
PROQ9H596.
SOURCESearch...

Entry information

Entry nameDUS21_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM