Q9H1R2 (DUS15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	295 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.
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.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protein phosphatase
PTM	Lipoprotein Myristate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	2	EBI-1752795,EBI-389883
PLCG1	P19174	2	EBI-1752795,EBI-79387

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 295

295

Dual specificity protein phosphatase 15

PRO_0000094824

Regions

Domain

62 – 132

71

Tyrosine-protein phosphatase

Sites

Active site

85

1

Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence

1 – 100

100

Missing in isoform 4.

VSP_043107

Alternative sequence

1 – 4

4

MTEG → MGNGMTK in isoform 3.

VSP_019228

Alternative sequence

143 – 232

90

GARHR…PGPTQ → LRRQLEERFGESPFRDEEEL RALLPLCKRCRQGSATSASS AGPHSAASEGTVQRLVPRTP REAHRPLPLLARVKQTFSCL PRCLSRKGGK in isoform 2, isoform 3 and isoform 4.

VSP_007292

Alternative sequence

233 – 295

63

Missing in isoform 2, isoform 3 and isoform 4.

VSP_007293

Experimental info

Mutagenesis

85

1

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

Secondary structure

1

.

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295

Helix Strand Turn

Details...

Beta strand

9 – 12

4

Helix

16 – 18

3

Helix

20 – 25

6

Beta strand

30 – 34

5

Beta strand

46 – 50

5

Helix

60 – 63

4

Helix

64 – 76

13

Beta strand

81 – 85

5

Beta strand

88 – 90

3

Helix

91 – 104

14

Helix

108 – 117

10

Helix

126 – 137

12

Helix

139 – 142

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 30, 2003. Version 4. Checksum: 28F8A687ECB5C219	FASTA	295	31,882
	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
	Isoform 2 [UniParc]. Checksum: 806EB3DFA4167D76	FASTA	232	25,851
	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 QKLRRQLEER FGESPFRDEE ELRALLPLCK RCRQGSATSA 190 200 210 220 230 SSAGPHSAAS EGTVQRLVPR TPREAHRPLP LLARVKQTFS CLPRCLSRKG GK
	Isoform 3 (A) [UniParc]. Checksum: A3AF26789894FECB	FASTA	235	26,152
	10 20 30 40 50 60 MGNGMTKVLP GLYLGNFIDA KDLDQLGRNK ITHIISIHES PQPLLQDITY LRIPVADTPE 70 80 90 100 110 120 VPIKKHFKEC INFIHCCRLN GGNCLVHCFA GISRSTTIVT AYVMTVTGLG WRDVLEAIKA 130 140 150 160 170 180 TRPIANPNPG FRQQLEEFGW ASSQKLRRQL EERFGESPFR DEEELRALLP LCKRCRQGSA 190 200 210 220 230 TSASSAGPHS AASEGTVQRL VPRTPREAHR PLPLLARVKQ TFSCLPRCLS RKGGK
	Isoform 4 [UniParc]. Checksum: F1690DF488891012	FASTA	132	14,721
	10 20 30 40 50 60 MTVTGLGWRD VLEAIKATRP IANPNPGFRQ QLEEFGWASS QKLRRQLEER FGESPFRDEE 70 80 90 100 110 120 ELRALLPLCK RCRQGSATSA SSAGPHSAAS EGTVQRLVPR TPREAHRPLP LLARVKQTFS 130 CLPRCLSRKG GK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

IPI

IPI00171178.
IPI00414846.
IPI00419331.

RefSeq

NP_001012662.1. NM_001012644.1.
NP_542178.2. NM_080611.3.
NP_817130.1. NM_177991.1.

UniGene

Hs.434108.
Hs.585017.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YZ4	X-ray	2.40	A/B	5-142	[»]

ProteinModelPortal

Q9H1R2.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H1R2. 9 interactions.

MINT

MINT-7241177.

PTM databases

PhosphoSite

Q9H1R2.

Polymorphism databases

DMDM

30316387.

Proteomic databases

PaxDb

Q9H1R2.

PRIDE

Q9H1R2.

Protocols and materials databases

DNASU

128853.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000278979; ENSP00000278979; ENSG00000149599.
ENST00000339738; ENSP00000341658; ENSG00000149599.
ENST00000375966; ENSP00000365133; ENSG00000149599.
ENST00000398083; ENSP00000381157; ENSG00000149599.
ENST00000398084; ENSP00000381158; ENSG00000149599.
ENST00000486996; ENSP00000419818; ENSG00000149599.

GeneID

128853.

KEGG

hsa:128853.

UCSC

uc002wwu.1. human.
uc002wwx.1. human.

Organism-specific databases

CTD

128853.

GeneCards

GC20M030435.
GC20M030437.

H-InvDB

HIX0015716.

HGNC

HGNC:16190. C20orf57.
HGNC:16236. DUSP15.

HPA

HPA031114.

neXtProt

NX_Q9H1R2.

PharmGKB

PA27524.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2453.

HOGENOM

HOG000007880.

HOVERGEN

HBG054344.

InParanoid

Q9H1R2.

KO

K14165.

OMA

CRQGSAT.

OrthoDB

EOG4RFKT3.

PhylomeDB

Q9H1R2.

Gene expression databases

ArrayExpress

Q9H1R2.

Bgee

Q9H1R2.

CleanEx

HS_C20orf57.
HS_DUSP15.

Genevestigator

Q9H1R2.

GermOnline

ENSG00000149599. Homo sapiens.

Family and domain databases

Gene3D

2.60.200.10. 1 hit.

InterPro

IPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR017855. SMAD_dom-like.
IPR008984. SMAD_FHA_domain.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]

PANTHER

PTHR10159. PTHR10159. 1 hit.

Pfam

PF00782. DSPc. 1 hit.
[Graphical view]

PRINTS

PR01908. ADSPHPHTASE.

SMART

SM00195. DSPc. 1 hit.
[Graphical view]

SUPFAM

SSF49879. SMAD_FHA. 1 hit.

PROSITE

PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9H1R2.

GenomeRNAi

128853.

NextBio

82475.

Entry information

Entry name

DUS15_HUMAN

Accession

Primary (citable) accession number: Q9H1R2
Secondary accession number(s): A6NH79 , 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:	May 1, 2013
This is version 117 of the entry and version 4 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.