Reviewed, UniProtKB/Swiss-Prot Q9UNI6 (DUS12_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from direct assay. Source: HPA
Molecular function	protein 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 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
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.6
Natural variations
	Natural variant	51	1	A → E: dbSNP rs35106830.		VAR_033899

Sequences

	Sequence		Length	Mass (Da)
	Q9UNI6-1 [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: 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. , 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.
IPI	IPI00009210.
RefSeq	NP_009171.1.
UniGene	Hs.416216
3D structure databases
SMR	Q9UNI6. Positions 26-168.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UNI6. 4 interactions.
STRING	Q9UNI6.
Proteomic databases
PeptideAtlas	Q9UNI6.
PRIDE	Q9UNI6.
Genome annotation databases
Ensembl	ENST00000367943; ENSP00000356920; ENSG00000081721; Homo sapiens. [Genome view]
GeneID	11266.
KEGG	hsa:11266.
UCSC	uc001gbo.1. human.
Organism-specific databases
CTD	11266.
GeneCards	GC01P159989.
H-InvDB	HIX0001252.
HGNC	HGNC:3067. DUSP12.
HPA	HPA008840.
MIM	604835. gene.
PharmGKB	PA27522.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08569.
HOGENOM	HBG588460.
HOVERGEN	Q9UNI6.
InParanoid	Q9UNI6.
OMA	VTAYLMK.
OrthoDB	EOG9KPWX9.
PhylomeDB	Q9UNI6.
Enzyme and pathway databases
BRENDA	3.1.3.16. 247. 3.1.3.48. 247.
Gene expression databases
ArrayExpress	Q9UNI6.
Bgee	Q9UNI6.
CleanEx	HS_DUSP12.
Genevestigator	Q9UNI6.
GermOnline	ENSG00000081721. Homo sapiens.
Family and domain databases
InterPro	IPR000387. 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]
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 Resources
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:	January 19, 2010
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.