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Q9UNI6 (DUS12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 12

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Dual specificity tyrosine phosphatase YVH1
Gene names
Name:DUSP12
OrganismHomo sapiens (Human) [Reference 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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.

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.5 Ref.7 Ref.8

Natural variations

Natural variant511A → E.
Corresponds to variant rs35106830 [ dbSNP | Ensembl ].
VAR_033899

Sequences

Sequence LengthMass (Da)Tools
Q9UNI6 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[5]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_009171.1. NM_007240.1.
UniGeneHs.416216.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4KI9X-ray2.00A27-189[»]
ProteinModelPortalQ9UNI6.
SMRQ9UNI6. Positions 30-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116424. 6 interactions.
IntActQ9UNI6. 7 interactions.
MINTMINT-1415234.
STRING9606.ENSP00000356920.

PTM databases

PhosphoSiteQ9UNI6.

Polymorphism databases

DMDM9973073.

Proteomic databases

PaxDbQ9UNI6.
PeptideAtlasQ9UNI6.
PRIDEQ9UNI6.

Protocols and materials databases

DNASU11266.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367943; ENSP00000356920; ENSG00000081721.
GeneID11266.
KEGGhsa:11266.
UCSCuc001gbo.3. human.

Organism-specific databases

CTD11266.
GeneCardsGC01P161719.
HGNCHGNC:3067. DUSP12.
HPAHPA008840.
MIM604835. gene.
neXtProtNX_Q9UNI6.
PharmGKBPA27522.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000243638.
HOVERGENHBG051421.
InParanoidQ9UNI6.
KOK14819.
OMAKITHILT.
OrthoDBEOG7Z95MG.
PhylomeDBQ9UNI6.
TreeFamTF105123.

Gene expression databases

BgeeQ9UNI6.
CleanExHS_DUSP12.
GenevestigatorQ9UNI6.

Family and domain databases

InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR016278. DUSP12.
IPR000387. Tyr/Dual-sp_Pase.
IPR007087. Znf_C2H2.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PIRSFPIRSF000941. DUSP12. 1 hit.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDUSP12.
GenomeRNAi11266.
NextBio42871.
PROQ9UNI6.
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: April 16, 2014
This is version 127 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 1

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