SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UNI6

- DUS12_HUMAN

UniProt

Q9UNI6 - DUS12_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Dual specificity protein phosphatase 12
Gene
DUSP12
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei115 – 1151Phosphocysteine intermediate By similarity

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: ProtInc
  2. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  3. zinc ion binding Source: ProtInc

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. peptidyl-tyrosine dephosphorylation Source: GOC
  3. positive regulation of glucokinase activity Source: RefGenome
  4. protein dephosphorylation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:DUSP12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3067. DUSP12.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27522.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Dual specificity protein phosphatase 12
PRO_0000094818Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UNI6.
PaxDbiQ9UNI6.
PeptideAtlasiQ9UNI6.
PRIDEiQ9UNI6.

PTM databases

PhosphoSiteiQ9UNI6.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9UNI6.
CleanExiHS_DUSP12.
GenevestigatoriQ9UNI6.

Organism-specific databases

HPAiHPA008840.

Interactioni

Protein-protein interaction databases

BioGridi116424. 6 interactions.
IntActiQ9UNI6. 7 interactions.
MINTiMINT-1415234.
STRINGi9606.ENSP00000356920.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 314
Beta strandi34 – 374
Helixi39 – 435
Helixi45 – 517
Beta strandi53 – 6210
Beta strandi76 – 816
Helixi91 – 933
Helixi94 – 10613
Beta strandi110 – 1145
Beta strandi116 – 1205
Helixi121 – 13414
Helixi138 – 14811
Helixi156 – 16712
Helixi177 – 18610

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JNBX-ray3.00A27-193[»]
4KI9X-ray2.00A27-189[»]
ProteinModelPortaliQ9UNI6.
SMRiQ9UNI6. Positions 27-186.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 16073Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000243638.
HOVERGENiHBG051421.
InParanoidiQ9UNI6.
KOiK14819.
OMAiKITHILT.
OrthoDBiEOG7Z95MG.
PhylomeDBiQ9UNI6.
TreeFamiTF105123.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR016278. DUSP12.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR007087. Znf_C2H2.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PIRSFiPIRSF000941. DUSP12. 1 hit.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UNI6-1 [UniParc]FASTAAdd to Basket

« Hide

MLEAPGPSDG CELSNPSASR VSCAGQMLEV QPGLYFGGAA AVAEPDHLRE    50
AGITAVLTVD SEEPSFKAGP GVEDLWRLFV PALDKPETDL LSHLDRCVAF 100
IGQARAEGRA VLVHCHAGVS RSVAIITAFL MKTDQLPFEK AYEKLQILKP 150
EAKMNEGFEW QLKLYQAMGY EVDTSSAIYK QYRLQKVTEK YPELQNLPQE 200
LFAVDPTTVS QGLKDEVLYK CRKCRRSLFR SSSILDHREG SGPIAFAHKR 250
MTPSSMLTTG RQAQCTSYFI EPVQWMESAL LGVMDGQLLC PKCSAKLGSF 300
NWYGEQCSCG RWITPAFQIH KNRVDEMKIL PVLGSQTGKI 340
Length:340
Mass (Da):37,687
Last modified:May 1, 2000 - v1
Checksum:i56B52192B42C73EB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511A → E.
Corresponds to variant rs35106830 [ dbSNP | Ensembl ].
VAR_033899

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF119226 mRNA. Translation: AAD51134.1.
BT006633 mRNA. Translation: AAP35279.1.
AL359541 Genomic DNA. Translation: CAH74153.1.
BC006286 mRNA. Translation: AAH06286.1.
CCDSiCCDS1234.1.
RefSeqiNP_009171.1. NM_007240.1.
UniGeneiHs.416216.

Genome annotation databases

EnsembliENST00000367943; ENSP00000356920; ENSG00000081721.
GeneIDi11266.
KEGGihsa:11266.
UCSCiuc001gbo.3. human.

Polymorphism databases

DMDMi9973073.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF119226 mRNA. Translation: AAD51134.1 .
BT006633 mRNA. Translation: AAP35279.1 .
AL359541 Genomic DNA. Translation: CAH74153.1 .
BC006286 mRNA. Translation: AAH06286.1 .
CCDSi CCDS1234.1.
RefSeqi NP_009171.1. NM_007240.1.
UniGenei Hs.416216.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4JNB X-ray 3.00 A 27-193 [» ]
4KI9 X-ray 2.00 A 27-189 [» ]
ProteinModelPortali Q9UNI6.
SMRi Q9UNI6. Positions 27-186.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116424. 6 interactions.
IntActi Q9UNI6. 7 interactions.
MINTi MINT-1415234.
STRINGi 9606.ENSP00000356920.

PTM databases

PhosphoSitei Q9UNI6.

Polymorphism databases

DMDMi 9973073.

Proteomic databases

MaxQBi Q9UNI6.
PaxDbi Q9UNI6.
PeptideAtlasi Q9UNI6.
PRIDEi Q9UNI6.

Protocols and materials databases

DNASUi 11266.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367943 ; ENSP00000356920 ; ENSG00000081721 .
GeneIDi 11266.
KEGGi hsa:11266.
UCSCi uc001gbo.3. human.

Organism-specific databases

CTDi 11266.
GeneCardsi GC01P161719.
HGNCi HGNC:3067. DUSP12.
HPAi HPA008840.
MIMi 604835. gene.
neXtProti NX_Q9UNI6.
PharmGKBi PA27522.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
HOGENOMi HOG000243638.
HOVERGENi HBG051421.
InParanoidi Q9UNI6.
KOi K14819.
OMAi KITHILT.
OrthoDBi EOG7Z95MG.
PhylomeDBi Q9UNI6.
TreeFami TF105123.

Miscellaneous databases

GeneWikii DUSP12.
GenomeRNAii 11266.
NextBioi 42871.
PROi Q9UNI6.
SOURCEi Search...

Gene expression databases

Bgeei Q9UNI6.
CleanExi HS_DUSP12.
Genevestigatori Q9UNI6.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR016278. DUSP12.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR007087. Znf_C2H2.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
PIRSFi PIRSF000941. DUSP12. 1 hit.
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDUS12_HUMAN
AccessioniPrimary (citable) accession number: Q9UNI6
Secondary accession number(s): Q5VXA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 130 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi