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Protein

Dual specificity protein phosphatase 12

Gene

DUSP12

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

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

GO - Molecular functioni

  1. protein tyrosine/serine/threonine phosphatase activity Source: GO_Central
  2. protein tyrosine phosphatase activity Source: ProtInc
  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: GO_Central
  4. protein dephosphorylation Source: GO_Central
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 12PRO_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

DEPODiQ9UNI6.
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.
ExpressionAtlasiQ9UNI6. baseline and differential.
GenevestigatoriQ9UNI6.

Organism-specific databases

HPAiHPA008840.

Interactioni

Protein-protein interaction databases

BioGridi116424. 13 interactions.
IntActiQ9UNI6. 7 interactions.
MINTiMINT-1415234.
STRINGi9606.ENSP00000356920.

Structurei

Secondary structure

1
340
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 314Combined sources
Beta strandi34 – 374Combined sources
Helixi39 – 435Combined sources
Helixi45 – 517Combined sources
Beta strandi53 – 6210Combined sources
Beta strandi76 – 816Combined sources
Helixi91 – 933Combined sources
Helixi94 – 10613Combined sources
Beta strandi110 – 1145Combined sources
Beta strandi116 – 1205Combined sources
Helixi121 – 13414Combined sources
Helixi138 – 14811Combined sources
Helixi156 – 16712Combined sources
Helixi177 – 18610Combined sources

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00740000115610.
HOGENOMiHOG000243638.
HOVERGENiHBG051421.
InParanoidiQ9UNI6.
KOiK14819.
OMAiFAWQGMQ.
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

        10         20         30         40         50
MLEAPGPSDG CELSNPSASR VSCAGQMLEV QPGLYFGGAA AVAEPDHLRE
60 70 80 90 100
AGITAVLTVD SEEPSFKAGP GVEDLWRLFV PALDKPETDL LSHLDRCVAF
110 120 130 140 150
IGQARAEGRA VLVHCHAGVS RSVAIITAFL MKTDQLPFEK AYEKLQILKP
160 170 180 190 200
EAKMNEGFEW QLKLYQAMGY EVDTSSAIYK QYRLQKVTEK YPELQNLPQE
210 220 230 240 250
LFAVDPTTVS QGLKDEVLYK CRKCRRSLFR SSSILDHREG SGPIAFAHKR
260 270 280 290 300
MTPSSMLTTG RQAQCTSYFI EPVQWMESAL LGVMDGQLLC PKCSAKLGSF
310 320 330 340
NWYGEQCSCG RWITPAFQIH KNRVDEMKIL PVLGSQTGKI
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:
EMBLi
GenBanki
DDBJi
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_007240.2.
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:
EMBLi
GenBanki
DDBJi
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_007240.2.
UniGeneiHs.416216.

3D structure databases

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

Protein-protein interaction databases

BioGridi116424. 13 interactions.
IntActiQ9UNI6. 7 interactions.
MINTiMINT-1415234.
STRINGi9606.ENSP00000356920.

PTM databases

DEPODiQ9UNI6.
PhosphoSiteiQ9UNI6.

Polymorphism databases

DMDMi9973073.

Proteomic databases

MaxQBiQ9UNI6.
PaxDbiQ9UNI6.
PeptideAtlasiQ9UNI6.
PRIDEiQ9UNI6.

Protocols and materials databases

DNASUi11266.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi11266.
GeneCardsiGC01P161719.
HGNCiHGNC:3067. DUSP12.
HPAiHPA008840.
MIMi604835. gene.
neXtProtiNX_Q9UNI6.
PharmGKBiPA27522.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00740000115610.
HOGENOMiHOG000243638.
HOVERGENiHBG051421.
InParanoidiQ9UNI6.
KOiK14819.
OMAiFAWQGMQ.
OrthoDBiEOG7Z95MG.
PhylomeDBiQ9UNI6.
TreeFamiTF105123.

Miscellaneous databases

GeneWikiiDUSP12.
GenomeRNAii11266.
NextBioi42871.
PROiQ9UNI6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UNI6.
CleanExiHS_DUSP12.
ExpressionAtlasiQ9UNI6. baseline and differential.
GenevestigatoriQ9UNI6.

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]
ProtoNetiSearch...

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: March 4, 2015
This is version 136 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.