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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	217 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	JNK cascade Inferred from Biological aspect of Ancestor. Source: RefGenome 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 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
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

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: 11959862] [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: 12479873] [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: 14702039] [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: 15815621] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Liver and Testis.
+	Additional computationally mapped references.

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
ProteinModelPortal	Q8WTR2.
SMR	Q8WTR2. Positions 67-204.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8WTR2.
PTM databases
PhosphoSite	Q8WTR2.
Polymorphism databases
DMDM	29840769.
Proteomic databases
PRIDE	Q8WTR2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000354221; ENSP00000346160; ENSG00000162999.
GeneID	142679.
KEGG	hsa:142679.
UCSC	uc002upd.1. human. uc010frp.1. human.
Organism-specific databases
CTD	142679.
GeneCards	GC02P183907.
H-InvDB	HIX0002652.
HGNC	HGNC:18894. DUSP19.
HPA	HPA021501.
MIM	611437. gene.
neXtProt	NX_Q8WTR2.
PharmGKB	PA134895660.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09966.
GeneTree	ENSGT00590000083109.
HOGENOM	HBG717377.
HOVERGEN	HBG051424.
InParanoid	Q8WTR2.
OMA	FLMNSEE.
PhylomeDB	Q8WTR2.
Gene expression databases
ArrayExpress	Q8WTR2.
Bgee	Q8WTR2.
CleanEx	HS_DUSP19.
Genevestigator	Q8WTR2.
GermOnline	ENSG00000162999. Homo sapiens.
Family and domain databases
InterPro	IPR020417. Dual-sp_phosphatase. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR000387. Tyr/Dual-specificity_Pase. [Graphical view]
KO	K14165.
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
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:	January 25, 2012
This is version 87 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.