Q8WTR2 (DUS19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 19
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
Dual specificity phosphatase TS-DSP1
Low molecular weight dual specificity phosphatase 3
Short name=LMW-DSP3
Protein phosphatase SKRP1
Stress-activated protein kinase pathway-regulating phosphatase 1
Short name=SAPK pathway-regulating phosphatase 1

Gene names

Name:	DUSP19
Synonyms:	DUSP17, LMWDSP3, SKRP1

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	217 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a dual specificity toward Ser/Thr and Tyr-containing proteins. Ref.3
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Tissue specificity	Expressed in the heart, lung, liver, and pancreas. The expression level in the pancreas is the highest. Ref.3
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JNK cascade Inferred from Biological aspect of Ancestor. Source: RefGenome inactivation of MAPK activity Inferred from electronic annotation. Source: Compara negative regulation of JNK cascade Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of JUN kinase activity Inferred from sequence or structural similarity. Source: BHF-UCL peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC positive regulation of JNK cascade Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of JUN kinase activity Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	JUN kinase phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome MAP-kinase scaffold activity Inferred from sequence or structural similarity. Source: BHF-UCL mitogen-activated protein kinase kinase kinase binding Inferred from sequence or structural similarity. Source: BHF-UCL protein kinase activator activity Inferred from sequence or structural similarity. Source: BHF-UCL protein kinase inhibitor activity Inferred from sequence or structural similarity. Source: BHF-UCL protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/threonine phosphatase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8WTR2-1)

Also known as: Long;

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: Q8WTR2-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     91-141: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 217

217

Dual specificity protein phosphatase 19

PRO_0000094832

Regions

Domain

133 – 197

65

Tyrosine-protein phosphatase

Sites

Active site

150

1

Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence

91 – 141

51

Missing in isoform 2.

VSP_005138

Natural variant

216

1

S → R.
Corresponds to variant rs16823987 [ dbSNP | Ensembl ].

VAR_051755

Secondary structure

1

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217

Helix Strand Turn

Details...

Beta strand

67 – 70

4

Beta strand

73 – 76

4

Helix

78 – 81

4

Helix

84 – 89

6

Beta strand

94 – 97

4

Beta strand

99 – 101

3

Turn

107 – 109

3

Beta strand

110 – 114

5

Helix

125 – 128

4

Helix

129 – 141

13

Beta strand

146 – 149

4

Beta strand

151 – 155

5

Helix

156 – 169

14

Helix

173 – 183

11

Helix

191 – 199

9

Helix

202 – 205

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified March 1, 2002. Version 1. Checksum: A9FAB082D35EC442	FASTA	217	24,194
	10 20 30 40 50 60 MYSLNQEIKA FSRNNLRKQC TRVTTLTGKK IIETWKDARI HVVEEVEPSS GGGCGYVQDL 70 80 90 100 110 120 SSDLQVGVIK PWLLLGSQDA AHDLDTLKKN KVTHILNVAY GVENAFLSDF TYKSISILDL 130 140 150 160 170 180 PETNILSYFP ECFEFIEEAK RKDGVVLVHC NAGVSRAAAI VIGFLMNSEQ TSFTSAFSLV 190 200 210 KNARPSICPN SGFMEQLRTY QEGKESNKCD RIQENSS
	Isoform 2 (Short) [UniParc]. Checksum: 76E894A1DF10E70F	FASTA	166	18,296
	10 20 30 40 50 60 MYSLNQEIKA FSRNNLRKQC TRVTTLTGKK IIETWKDARI HVVEEVEPSS GGGCGYVQDL 70 80 90 100 110 120 SSDLQVGVIK PWLLLGSQDA AHDLDTLKKN KDGVVLVHCN AGVSRAAAIV IGFLMNSEQT 130 140 150 160 SFTSAFSLVK NARPSICPNS GFMEQLRTYQ EGKESNKCDR IQENSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Scaffold role of a mitogen-activated protein kinase phosphatase, SKRP1, for the JNK signaling pathway." Zama T., Aoki R., Kamimoto T., Inoue K., Ikeda Y., Hagiwara M. J. Biol. Chem. 277:23919-23926(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]	Kikuchi K., Nakamura K., Sato T., Shima H. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Molecular cloning and characterization of a novel human protein phosphatase, LMW-DSP3." Cheng H., Gao Q., Jiang M., Ma Y., Ni X., Guo L., Jin W., Cao G., Ji C., Ying K., Xu W., Gu S., Ma Y., Xie Y., Mao Y. Int. J. Biochem. Cell Biol. 35:226-234(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[4]	"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] (ISOFORM 1). Tissue: Uterus.
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORM 1). Tissue: Liver and Testis.
[7]	"Crystal structure of a novel mitogen-activated protein kinase phosphatase, SKRP1." Wei C.H., Ryu S.Y., Jeon Y.H., Yoon M.Y., Jeong D.G., Kim S.J., Ryu S.E. Proteins 79:3242-3246(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 65-206.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB063186 mRNA. Translation: BAB83498.1.
AB063187 mRNA. Translation: BAB83499.1.
AB038770 mRNA. Translation: BAB82499.1.
AF486808 mRNA. Translation: AAO49450.1.
AK314078 mRNA. Translation: BAG36776.1.
AC064871 Genomic DNA. Translation: AAY24197.1.
BC035000 mRNA. Translation: AAH35000.1.
BC093958 mRNA. Translation: AAH93958.1.
BC112005 mRNA. Translation: AAI12006.1.

IPI

IPI00102808.
IPI00218179.

RefSeq

NP_001135786.1. NM_001142314.1.
NP_543152.1. NM_080876.3.

UniGene

Hs.132237.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3S4E	X-ray	1.26	A	65-206	[»]

ProteinModelPortal

Q8WTR2.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000346160.

PTM databases

PhosphoSite

Q8WTR2.

Polymorphism databases

DMDM

29840769.

Proteomic databases

PaxDb

Q8WTR2.

PRIDE

Q8WTR2.

Protocols and materials databases

DNASU

142679.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000342619; ENSP00000343905; ENSG00000162999.
ENST00000354221; ENSP00000346160; ENSG00000162999.

GeneID

142679.

KEGG

hsa:142679.

UCSC

uc002upd.3. human.
uc002upe.3. human.

Organism-specific databases

CTD

142679.

GeneCards

GC02P183907.

HGNC

HGNC:18894. DUSP19.

HPA

HPA021501.

MIM

611437. gene.

neXtProt

NX_Q8WTR2.

PharmGKB

PA134895660.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2453.

HOGENOM

HOG000233765.

HOVERGEN

HBG051424.

InParanoid

Q8WTR2.

KO

K14165.

OMA

FLMNSEE.

PhylomeDB

Q8WTR2.

Gene expression databases

Bgee

Q8WTR2.

CleanEx

HS_DUSP19.

Genevestigator

Q8WTR2.

GermOnline

ENSG00000162999. Homo sapiens.

Family and domain databases

InterPro

IPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]

PANTHER

PTHR10159. PTHR10159. 1 hit.

Pfam

PF00782. DSPc. 1 hit.
[Graphical view]

PRINTS

PR01908. ADSPHPHTASE.

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.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

142679.

NextBio

84595.

SOURCE

Search...

Entry information

Entry name

DUS19_HUMAN

Accession

Primary (citable) accession number: Q8WTR2
Secondary accession number(s): B2RA79, Q547H4, Q8WYN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 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.