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Dual specificity protein phosphatase 19 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase TS-DSP1) (Low molecular weight dual specificity phosphatase 3) (LMW-DSP3) (Protein phosphatase SKRP1) (Stress-activated protein kinase pathway-regulating phosphatase 1) (SAPK pathway-regulating phosphatase 1)

 DUS19_HUMAN             Reviewed;         217 AA.
Q8WTR2; B2RA79; Q547H4; Q8WYN4;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
28-FEB-2018, entry version 140.
RecName: Full=Dual specificity protein phosphatase 19;
EC=3.1.3.16;
EC=3.1.3.48;
AltName: Full=Dual specificity phosphatase TS-DSP1;
AltName: Full=Low molecular weight dual specificity phosphatase 3;
Short=LMW-DSP3;
AltName: Full=Protein phosphatase SKRP1;
AltName: Full=Stress-activated protein kinase pathway-regulating phosphatase 1;
Short=SAPK pathway-regulating phosphatase 1;
Name=DUSP19; Synonyms=DUSP17, LMWDSP3, SKRP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=11959862; DOI=10.1074/jbc.M200838200;
Zama T., Aoki R., Kamimoto T., Inoue K., Ikeda Y., Hagiwara M.;
"Scaffold role of a mitogen-activated protein kinase phosphatase,
SKRP1, for the JNK signaling pathway.";
J. Biol. Chem. 277:23919-23926(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kikuchi K., Nakamura K., Sato T., Shima H.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=12479873; DOI=10.1016/S1357-2725(02)00127-9;
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.;
"Molecular cloning and characterization of a novel human protein
phosphatase, LMW-DSP3.";
Int. J. Biochem. Cell Biol. 35:226-234(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[8]
X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 65-206.
PubMed=21989941; DOI=10.1002/prot.23156;
Wei C.H., Ryu S.Y., Jeon Y.H., Yoon M.Y., Jeong D.G., Kim S.J.,
Ryu S.E.;
"Crystal structure of a novel mitogen-activated protein kinase
phosphatase, SKRP1.";
Proteins 79:3242-3246(2011).
-!- FUNCTION: Has a dual specificity toward Ser/Thr and Tyr-containing
proteins. {ECO:0000269|PubMed:12479873}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- INTERACTION:
P13196:ALAS1; NbExp=6; IntAct=EBI-8654968, EBI-3905054;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=Q8WTR2-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=Q8WTR2-2; Sequence=VSP_005138;
-!- TISSUE SPECIFICITY: Expressed in the heart, lung, liver, and
pancreas. The expression level in the pancreas is the highest.
{ECO:0000269|PubMed:12479873}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class dual specificity subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB063186; BAB83498.1; -; mRNA.
EMBL; AB063187; BAB83499.1; -; mRNA.
EMBL; AB038770; BAB82499.1; -; mRNA.
EMBL; AF486808; AAO49450.1; -; mRNA.
EMBL; AK314078; BAG36776.1; -; mRNA.
EMBL; AC064871; AAY24197.1; -; Genomic_DNA.
EMBL; BC035000; AAH35000.1; -; mRNA.
EMBL; BC093958; AAH93958.1; -; mRNA.
EMBL; BC112005; AAI12006.1; -; mRNA.
CCDS; CCDS2289.1; -. [Q8WTR2-1]
CCDS; CCDS46469.1; -. [Q8WTR2-2]
RefSeq; NP_001135786.1; NM_001142314.1. [Q8WTR2-2]
RefSeq; NP_001308448.1; NM_001321519.1.
RefSeq; NP_543152.1; NM_080876.3. [Q8WTR2-1]
UniGene; Hs.132237; -.
PDB; 3S4E; X-ray; 1.26 A; A=65-206.
PDB; 4D3P; X-ray; 1.27 A; A=65-205.
PDB; 4D3Q; X-ray; 1.64 A; A/B=65-205.
PDB; 4D3R; X-ray; 1.67 A; A=65-204.
PDBsum; 3S4E; -.
PDBsum; 4D3P; -.
PDBsum; 4D3Q; -.
PDBsum; 4D3R; -.
ProteinModelPortal; Q8WTR2; -.
SMR; Q8WTR2; -.
BioGrid; 126770; 73.
IntAct; Q8WTR2; 5.
MINT; Q8WTR2; -.
STRING; 9606.ENSP00000346160; -.
DEPOD; Q8WTR2; -.
iPTMnet; Q8WTR2; -.
PhosphoSitePlus; Q8WTR2; -.
BioMuta; DUSP19; -.
DMDM; 29840769; -.
EPD; Q8WTR2; -.
MaxQB; Q8WTR2; -.
PaxDb; Q8WTR2; -.
PeptideAtlas; Q8WTR2; -.
PRIDE; Q8WTR2; -.
DNASU; 142679; -.
Ensembl; ENST00000342619; ENSP00000343905; ENSG00000162999. [Q8WTR2-2]
Ensembl; ENST00000354221; ENSP00000346160; ENSG00000162999. [Q8WTR2-1]
GeneID; 142679; -.
KEGG; hsa:142679; -.
UCSC; uc002upd.4; human. [Q8WTR2-1]
CTD; 142679; -.
DisGeNET; 142679; -.
EuPathDB; HostDB:ENSG00000162999.12; -.
GeneCards; DUSP19; -.
HGNC; HGNC:18894; DUSP19.
HPA; HPA021501; -.
MIM; 611437; gene.
neXtProt; NX_Q8WTR2; -.
OpenTargets; ENSG00000162999; -.
PharmGKB; PA134895660; -.
eggNOG; KOG1716; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000118902; -.
HOGENOM; HOG000233765; -.
HOVERGEN; HBG051424; -.
InParanoid; Q8WTR2; -.
KO; K14165; -.
OMA; MEQLRTY; -.
OrthoDB; EOG091G0249; -.
PhylomeDB; Q8WTR2; -.
TreeFam; TF354211; -.
SignaLink; Q8WTR2; -.
SIGNOR; Q8WTR2; -.
GeneWiki; DUSP19; -.
GenomeRNAi; 142679; -.
PRO; PR:Q8WTR2; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000162999; -.
CleanEx; HS_DUSP19; -.
Genevisible; Q8WTR2; HS.
GO; GO:0008579; F:JUN kinase phosphatase activity; IBA:GO_Central.
GO; GO:0005078; F:MAP-kinase scaffold activity; ISS:BHF-UCL.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISS:BHF-UCL.
GO; GO:0030295; F:protein kinase activator activity; ISS:BHF-UCL.
GO; GO:0004860; F:protein kinase inhibitor activity; ISS:BHF-UCL.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0046329; P:negative regulation of JNK cascade; ISS:BHF-UCL.
GO; GO:0043508; P:negative regulation of JUN kinase activity; ISS:BHF-UCL.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:BHF-UCL.
GO; GO:0046330; P:positive regulation of JNK cascade; ISS:BHF-UCL.
GO; GO:0043507; P:positive regulation of JUN kinase activity; ISS:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:BHF-UCL.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:BHF-UCL.
CDD; cd00127; DSPc; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR020417; Atypical_DUSP.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR024950; DUSP.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR10159; PTHR10159; 1.
Pfam; PF00782; DSPc; 1.
PRINTS; PR01908; ADSPHPHTASE.
SMART; SM00195; DSPc; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Hydrolase; Polymorphism; Protein phosphatase; Reference proteome.
CHAIN 1 217 Dual specificity protein phosphatase 19.
/FTId=PRO_0000094832.
DOMAIN 133 197 Tyrosine-protein phosphatase.
ACT_SITE 150 150 Phosphocysteine intermediate.
{ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
VAR_SEQ 91 141 Missing (in isoform 2).
{ECO:0000303|PubMed:11959862}.
/FTId=VSP_005138.
VARIANT 216 216 S -> R (in dbSNP:rs16823987).
/FTId=VAR_051755.
STRAND 67 70 {ECO:0000244|PDB:3S4E}.
STRAND 73 76 {ECO:0000244|PDB:3S4E}.
HELIX 78 81 {ECO:0000244|PDB:3S4E}.
HELIX 84 89 {ECO:0000244|PDB:3S4E}.
STRAND 94 97 {ECO:0000244|PDB:3S4E}.
STRAND 99 101 {ECO:0000244|PDB:3S4E}.
TURN 107 109 {ECO:0000244|PDB:3S4E}.
STRAND 110 114 {ECO:0000244|PDB:3S4E}.
HELIX 125 128 {ECO:0000244|PDB:3S4E}.
HELIX 129 141 {ECO:0000244|PDB:3S4E}.
STRAND 146 149 {ECO:0000244|PDB:3S4E}.
STRAND 151 155 {ECO:0000244|PDB:3S4E}.
HELIX 156 169 {ECO:0000244|PDB:3S4E}.
HELIX 173 183 {ECO:0000244|PDB:3S4E}.
HELIX 191 199 {ECO:0000244|PDB:3S4E}.
HELIX 202 205 {ECO:0000244|PDB:3S4E}.
SEQUENCE 217 AA; 24194 MW; A9FAB082D35EC442 CRC64;
MYSLNQEIKA FSRNNLRKQC TRVTTLTGKK IIETWKDARI HVVEEVEPSS GGGCGYVQDL
SSDLQVGVIK PWLLLGSQDA AHDLDTLKKN KVTHILNVAY GVENAFLSDF TYKSISILDL
PETNILSYFP ECFEFIEEAK RKDGVVLVHC NAGVSRAAAI VIGFLMNSEQ TSFTSAFSLV
KNARPSICPN SGFMEQLRTY QEGKESNKCD RIQENSS


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