Q9UNI6 (DUS12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of glucokinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from direct assay. Source: HPA
Molecular_function	protein tyrosine phosphatase activity Traceable author statement Ref.1. Source: ProtInc protein tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome zinc ion binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 340	340	Dual specificity protein phosphatase 12		PRO_0000094818
Regions
	Domain	88 – 160	73	Tyrosine-protein phosphatase
Sites
	Active site	115	1	Phosphocysteine intermediate By similarity
Natural variations
	Natural variant	51	1	A → E. Corresponds to variant rs35106830 [ dbSNP | Ensembl ].		VAR_033899

Sequences

	Sequence		Length	Mass (Da)
	Q9UNI6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 56B52192B42C73EB	FASTA	340	37,687
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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].
+	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.
IPI	IPI00009210.
RefSeq	NP_009171.1. NM_007240.1.
UniGene	Hs.416216.
3D structure databases
ProteinModelPortal	Q9UNI6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UNI6. 4 interactions.
MINT	MINT-1415234.
STRING	9606.ENSP00000356920.
PTM databases
PhosphoSite	Q9UNI6.
Polymorphism databases
DMDM	9973073.
Proteomic databases
PaxDb	Q9UNI6.
PeptideAtlas	Q9UNI6.
PRIDE	Q9UNI6.
Protocols and materials databases
DNASU	11266.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367943; ENSP00000356920; ENSG00000081721.
GeneID	11266.
KEGG	hsa:11266.
UCSC	uc001gbo.3. human.
Organism-specific databases
CTD	11266.
GeneCards	GC01P161719.
HGNC	HGNC:3067. DUSP12.
HPA	HPA008840.
MIM	604835. gene.
neXtProt	NX_Q9UNI6.
PharmGKB	PA27522.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2453.
HOGENOM	HOG000243638.
HOVERGEN	HBG051421.
InParanoid	Q9UNI6.
KO	K14819.
OMA	VTAYLMK.
OrthoDB	EOG4GXFNM.
PhylomeDB	Q9UNI6.
Gene expression databases
Bgee	Q9UNI6.
CleanEx	HS_DUSP12.
Genevestigator	Q9UNI6.
GermOnline	ENSG00000081721. Homo sapiens.
Family and domain databases
InterPro	IPR000340. 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]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PIRSF	PIRSF000941. DUSP12. 1 hit.
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. 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]
ProtoNet	Search...
Other
GenomeRNAi	11266.
NextBio	42871.
SOURCE	Search...

Entry information

Entry name

DUS12_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 120 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.