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Reviewed, UniProtKB/Swiss-Prot Q9UNI6 (DUS12_HUMAN)

Last modified January 19, 2010. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dual specificity protein phosphatase 12
    EC=3.1.3.48
    EC=3.1.3.16
Alternative name(s):
    Dual specificity tyrosine phosphatase YVH1
Gene names
Name: DUSP12
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

A phosphoprotein + H2O = a protein + phosphate.

Cofactor

Binds 2 zinc ions per subunit.

Subcellular location

Nucleus.

Tissue specificity

Ubiquitous, highest expression in spleen, testis, ovary, and peripheral blood leukocytes and lower expression in liver and lung.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein amino acid dephosphorylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from direct assay. Source: HPA

   Molecular functionprotein tyrosine phosphatase activity Ref.1

Traceable author statement. Source: ProtInc

zinc ion binding Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Dual specificity protein phosphatase 12
PRO_0000094818

Regions

Domain88 – 16073Tyrosine-protein phosphatase

Sites

Active site1151Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6

Natural variations

Natural variant511A → E: dbSNP rs35106830.
VAR_033899

Sequences

Sequence LengthMass (Da)Tools
Q9UNI6-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 56B52192B42C73EB

FASTA34037,687
        10         20         30         40         50         60 
MLEAPGPSDG CELSNPSASR VSCAGQMLEV QPGLYFGGAA AVAEPDHLRE AGITAVLTVD 

        70         80         90        100        110        120 
SEEPSFKAGP GVEDLWRLFV PALDKPETDL LSHLDRCVAF IGQARAEGRA VLVHCHAGVS 

       130        140        150        160        170        180 
RSVAIITAFL MKTDQLPFEK AYEKLQILKP EAKMNEGFEW QLKLYQAMGY EVDTSSAIYK 

       190        200        210        220        230        240 
QYRLQKVTEK YPELQNLPQE LFAVDPTTVS QGLKDEVLYK CRKCRRSLFR SSSILDHREG 

       250        260        270        280        290        300 
SGPIAFAHKR MTPSSMLTTG RQAQCTSYFI EPVQWMESAL LGVMDGQLLC PKCSAKLGSF 

       310        320        330        340 
NWYGEQCSCG RWITPAFQIH KNRVDEMKIL PVLGSQTGKI 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the human YVH1 protein-tyrosine phosphatase orthologue reveals a novel zinc binding domain essential for in vivo function."
Muda M., Manning E.R., Orth K., Dixon J.E.
J. Biol. Chem. 274:23991-23995(1999) [PubMed: 10446167] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Placenta.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF119226 mRNA. Translation: AAD51134.1.
BT006633 mRNA. Translation: AAP35279.1.
AL359541 Genomic DNA. Translation: CAH74153.1.
BC006286 mRNA. Translation: AAH06286.1.
IPIIPI00009210.
RefSeqNP_009171.1.
UniGeneHs.416216

3D structure databases

SMRQ9UNI6. Positions 26-168.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9UNI6. 4 interactions.
STRINGQ9UNI6.

Proteomic databases

PeptideAtlasQ9UNI6.
PRIDEQ9UNI6.

Genome annotation databases

EnsemblENST00000367943; ENSP00000356920; ENSG00000081721; Homo sapiens. [Genome view]
GeneID11266.
KEGGhsa:11266.
UCSCuc001gbo.1. human.

Organism-specific databases

CTD11266.
GeneCardsGC01P159989.
H-InvDBHIX0001252.
HGNCHGNC:3067. DUSP12.
HPAHPA008840.
MIM604835. gene.
PharmGKBPA27522.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08569.
HOGENOMHBG588460.
HOVERGENQ9UNI6.
InParanoidQ9UNI6.
OMAVTAYLMK.
OrthoDBEOG9KPWX9.
PhylomeDBQ9UNI6.

Enzyme and pathway databases

BRENDA3.1.3.16. 247.
3.1.3.48. 247.

Gene expression databases

ArrayExpressQ9UNI6.
BgeeQ9UNI6.
CleanExHS_DUSP12.
GenevestigatorQ9UNI6.
GermOnlineENSG00000081721. Homo sapiens.

Family and domain databases

InterProIPR000387. Dual-sp/Tyr_phosphatase.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR016278. Tyr_Pase_dual_specific_12.
IPR007087. Znf_C2H2.
[Graphical view]
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PIRSFPIRSF000941. DUSP12. 1 hit.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. False negative.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit. Uncertain.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio42871.
SOURCESearch...

Entry information

Entry nameDUS12_HUMAN
AccessionPrimary (citable) accession number: Q9UNI6
Secondary accession number(s): Q5VXA8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: January 19, 2010
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents