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Q9H596

- DUS21_HUMAN

UniProt

Q9H596 - DUS21_HUMAN

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Protein

Dual specificity protein phosphatase 21

Gene
DUSP21, LMWDSP21
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061Phosphocysteine intermediate By similarity

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  3. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. peptidyl-tyrosine dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
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 namesi
Name:DUSP21
Synonyms:LMWDSP21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:20476. DUSP21.

Subcellular locationi

Cytoplasm. Nucleus. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. integral component of mitochondrial inner membrane Source: Ensembl
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134967875.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Dual specificity protein phosphatase 21PRO_0000094834Add
BLAST

Proteomic databases

PaxDbiQ9H596.
PRIDEiQ9H596.

Expressioni

Tissue specificityi

Expressed in testis.1 Publication

Gene expression databases

BgeeiQ9H596.
CleanExiHS_DUSP21.
GenevestigatoriQ9H596.

Interactioni

Protein-protein interaction databases

BioGridi121980. 2 interactions.
IntActiQ9H596. 1 interaction.
MINTiMINT-3068077.
STRINGi9606.ENSP00000343244.

Structurei

3D structure databases

ProteinModelPortaliQ9H596.
SMRiQ9H596. Positions 22-181.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 161141Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 12886Sufficient for mitochondrial localization By similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000233766.
HOVERGENiHBG051422.
InParanoidiQ9H596.
KOiK14165.
OMAiFWEQLIN.
OrthoDBiEOG7PK90H.
PhylomeDBiQ9H596.
TreeFamiTF316009.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. 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]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H596-1 [UniParc]FASTAAdd to Basket

« Hide

MTASASSFSS SQGVQQPSIY SFSQITRSLF LSNGVAANDK LLLSSNRITA    50
IVNASVEVVN VFFEGIQYIK VPVTDARDSR LYDFFDPIAD LIHTIDMRQG 100
RTLLHCMAGV SRSASLCLAY LMKYHSMSLL DAHTWTKSRR PIIRPNNGFW 150
EQLINYEFKL FNNNTVRMIN SPVGNIPDIY EKDLRMMISM 190
Length:190
Mass (Da):21,529
Last modified:March 1, 2001 - v1
Checksum:i3E52BA31A4944EE3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035644
Natural varianti186 – 1861M → T.2 Publications
Corresponds to variant rs1045031 [ dbSNP | Ensembl ].
VAR_019423

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti190 – 1901M → I in CAG33440. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14264.1.
RefSeqiNP_071359.3. NM_022076.3.
UniGeneiHs.534478.

Genome annotation databases

EnsembliENST00000339042; ENSP00000343244; ENSG00000189037.
GeneIDi63904.
KEGGihsa:63904.
UCSCiuc004dgd.3. human.

Polymorphism databases

DMDMi50400652.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14264.1.
RefSeqi NP_071359.3. NM_022076.3.
UniGenei Hs.534478.

3D structure databases

ProteinModelPortali Q9H596.
SMRi Q9H596. Positions 22-181.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121980. 2 interactions.
IntActi Q9H596. 1 interaction.
MINTi MINT-3068077.
STRINGi 9606.ENSP00000343244.

Polymorphism databases

DMDMi 50400652.

Proteomic databases

PaxDbi Q9H596.
PRIDEi Q9H596.

Protocols and materials databases

DNASUi 63904.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339042 ; ENSP00000343244 ; ENSG00000189037 .
GeneIDi 63904.
KEGGi hsa:63904.
UCSCi uc004dgd.3. human.

Organism-specific databases

CTDi 63904.
GeneCardsi GC0XP044703.
HGNCi HGNC:20476. DUSP21.
MIMi 300678. gene.
neXtProti NX_Q9H596.
PharmGKBi PA134967875.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
HOGENOMi HOG000233766.
HOVERGENi HBG051422.
InParanoidi Q9H596.
KOi K14165.
OMAi FWEQLIN.
OrthoDBi EOG7PK90H.
PhylomeDBi Q9H596.
TreeFami TF316009.

Miscellaneous databases

GenomeRNAii 63904.
NextBioi 65608.
PROi Q9H596.
SOURCEi Search...

Gene expression databases

Bgeei Q9H596.
CleanExi HS_DUSP21.
Genevestigatori Q9H596.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR020417. 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 ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
PRINTSi PR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-167.

Entry informationi

Entry nameiDUS21_HUMAN
AccessioniPrimary (citable) accession number: Q9H596
Secondary accession number(s): Q0VDA6, Q6IAJ6, Q6YDQ8
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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