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Q9H1R2 (DUS15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 15

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
VH1-related member Y
Vaccinia virus VH1-related dual-specific protein phosphatase Y
Gene names
Name:DUSP15
Synonyms:C20orf57, VHY
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length295 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.

Subcellular location

Cytoplasm Probable Ref.5.

Isoform 3: Cell membrane; Lipid-anchor; Cytoplasmic side Ref.5.

Tissue specificity

Highly expressed in testis. Ref.5

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Caution

Although assigned as two separate genes (c20orf57 and DUSP15), it is probable that C20orf57 does not exist by itself and is a part of the DUSP15 gene.

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H1R2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9H1R2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     143-232: GARHRTSKTS...FGEEDPGPTQ → LRRQLEERFG...PRCLSRKGGK
     233-295: Missing.
Note: Derived from EST data.
Isoform 3 (identifier: Q9H1R2-3)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MTEG → MGNGMTK
     143-232: GARHRTSKTS...FGEEDPGPTQ → LRRQLEERFG...PRCLSRKGGK
     233-295: Missing.
Note: Initiator Met-1 is removed. Myristoylated on Gly-2.
Isoform 4 (identifier: Q9H1R2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     143-232: GARHRTSKTS...FGEEDPGPTQ → LRRQLEERFG...PRCLSRKGGK
     233-295: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Dual specificity protein phosphatase 15
PRO_0000094824

Regions

Domain62 – 13271Tyrosine-protein phosphatase

Sites

Active site851Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence1 – 100100Missing in isoform 4.
VSP_043107
Alternative sequence1 – 44MTEG → MGNGMTK in isoform 3.
VSP_019228
Alternative sequence143 – 23290GARHR…PGPTQ → LRRQLEERFGESPFRDEEEL RALLPLCKRCRQGSATSASS AGPHSAASEGTVQRLVPRTP REAHRPLPLLARVKQTFSCL PRCLSRKGGK in isoform 2, isoform 3 and isoform 4.
VSP_007292
Alternative sequence233 – 29563Missing in isoform 2, isoform 3 and isoform 4.
VSP_007293

Experimental info

Mutagenesis851C → S: Loss of phosphatase activity. Ref.5

Secondary structure

......................... 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 30, 2003. Version 4.
Checksum: 28F8A687ECB5C219

FASTA29531,882
        10         20         30         40         50         60 
MTEGVLPGLY LGNFIDAKDL DQLGRNKITH IISIHESPQP LLQDITYLRI PVADTPEVPI 

        70         80         90        100        110        120 
KKHFKECINF IHCCRLNGGN CLVHCFAGIS RSTTIVTAYV MTVTGLGWRD VLEAIKATRP 

       130        140        150        160        170        180 
IANPNPGFRQ QLEEFGWASS QKGARHRTSK TSGAQCPPMT SATCLLAARV ALLSAALVRE 

       190        200        210        220        230        240 
ATGRTAQRCR LSPRAAAERL LGPPPHVAAG WSPDPKYQIC LCFGEEDPGP TQHPKEQLIM 

       250        260        270        280        290 
ADVQVQLRPG SSSCTLSAST ERPDGSSTPG NPDGITHLQC SCLHPKRAAS SSCTR 

« Hide

Isoform 2 [UniParc].

Checksum: 806EB3DFA4167D76
Show »

FASTA23225,851
Isoform 3 (A) [UniParc].

Checksum: A3AF26789894FECB
Show »

FASTA23526,152
Isoform 4 [UniParc].

Checksum: F1690DF488891012
Show »

FASTA13214,721

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
Tissue: Testis.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORMS 2 AND 3).
Tissue: Brain and PNS.
[5]"VHY, a novel myristoylated testis-restricted dual specificity protein phosphatase related to VHX."
Alonso A., Narisawa S., Bogetz J., Tautz L., Hadzic R., Huynh H., Williams S., Gjoerloff-Wingren A., Bremer M.C.D., Holsinger L.J., Millan J.L., Mustelin T.
J. Biol. Chem. 279:32586-32591(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-85, MYRISTOYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"Crystal structure of the catalytic domain of human VHY, a dual-specificity protein phosphatase."
Yoon T.-S., Jeong D.G., Kim J.H., Cho Y.H., Son J.H., Lee J.W., Ryu S.E., Kim S.J.
Proteins 61:694-697(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-157 (ISOFORM 3).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK091960 mRNA. Translation: BAG52450.1.
AK097430 mRNA. Translation: BAC05048.1.
AL160175 Genomic DNA. Translation: CAI12819.1.
AL160175 Genomic DNA. Translation: CAI12821.1.
AL160175 Genomic DNA. Translation: CAI12822.1.
CH471077 Genomic DNA. Translation: EAW76410.1.
BC056911 mRNA. Translation: AAH56911.1.
BM554314 mRNA. No translation available.
CCDSCCDS13193.1. [Q9H1R2-3]
CCDS42862.1. [Q9H1R2-4]
RefSeqNP_001012662.1. NM_001012644.1. [Q9H1R2-4]
NP_542178.2. NM_080611.3. [Q9H1R2-3]
NP_817130.1. NM_177991.1. [Q9H1R2-4]
UniGeneHs.434108.
Hs.585017.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZ4X-ray2.40A/B5-145[»]
ProteinModelPortalQ9H1R2.
SMRQ9H1R2. Positions 5-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126164. 2 interactions.
IntActQ9H1R2. 9 interactions.
MINTMINT-7241177.

Chemistry

ChEMBLCHEMBL2396507.

PTM databases

PhosphoSiteQ9H1R2.

Polymorphism databases

DMDM30316387.

Proteomic databases

PaxDbQ9H1R2.
PRIDEQ9H1R2.

Protocols and materials databases

DNASU128853.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278979; ENSP00000278979; ENSG00000149599. [Q9H1R2-1]
ENST00000339738; ENSP00000341658; ENSG00000149599. [Q9H1R2-3]
ENST00000375966; ENSP00000365133; ENSG00000149599. [Q9H1R2-2]
ENST00000398083; ENSP00000381157; ENSG00000149599. [Q9H1R2-4]
ENST00000398084; ENSP00000381158; ENSG00000149599. [Q9H1R2-4]
ENST00000486996; ENSP00000419818; ENSG00000149599. [Q9H1R2-4]
GeneID128853.
KEGGhsa:128853.
UCSCuc002wwu.1. human. [Q9H1R2-1]
uc002wwv.1. human. [Q9H1R2-4]
uc002wwx.1. human. [Q9H1R2-3]

Organism-specific databases

CTD128853.
GeneCardsGC20M030443.
GC20U990068.
H-InvDBHIX0015716.
HGNCHGNC:16190. C20orf57.
HGNC:16236. DUSP15.
HPAHPA031114.
neXtProtNX_Q9H1R2.
PharmGKBPA27524.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000007880.
HOVERGENHBG054344.
InParanoidQ9H1R2.
KOK14165.
OMACRQGSAT.
OrthoDBEOG7966HM.
PhylomeDBQ9H1R2.
TreeFamTF105126.

Enzyme and pathway databases

SABIO-RKQ9H1R2.

Gene expression databases

ArrayExpressQ9H1R2.
BgeeQ9H1R2.
CleanExHS_C20orf57.
HS_DUSP15.
GenevestigatorQ9H1R2.

Family and domain databases

Gene3D2.60.200.10. 1 hit.
3.90.190.10. 1 hit.
InterProIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR017855. SMAD_dom-like.
IPR008984. SMAD_FHA_domain.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9H1R2.
GeneWikiDUSP15.
GenomeRNAi128853.
NextBio82475.
PROQ9H1R2.

Entry information

Entry nameDUS15_HUMAN
AccessionPrimary (citable) accession number: Q9H1R2
Secondary accession number(s): A6NH79 expand/collapse secondary AC list , A8MVC8, Q5QP62, Q5QP63, Q5QP65, Q6PGN7, Q8N826, Q9BX24
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: April 30, 2003
Last modified: July 9, 2014
This is version 130 of the entry and version 4 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

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM