DUS19_HUMAN
ID DUS19_HUMAN Reviewed; 217 AA.
AC Q8WTR2; B2RA79; Q547H4; Q8WYN4;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Dual specificity protein phosphatase 19 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:12479873};
DE EC=3.1.3.48 {ECO:0000269|PubMed:12479873};
DE AltName: Full=Dual specificity phosphatase TS-DSP1;
DE AltName: Full=Low molecular weight dual specificity phosphatase 3;
DE Short=LMW-DSP3;
DE AltName: Full=Protein phosphatase SKRP1;
DE AltName: Full=Stress-activated protein kinase pathway-regulating phosphatase 1;
DE Short=SAPK pathway-regulating phosphatase 1;
GN Name=DUSP19 {ECO:0000312|HGNC:HGNC:18894}; Synonyms=DUSP17, LMWDSP3, SKRP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=11959862; DOI=10.1074/jbc.m200838200;
RA Zama T., Aoki R., Kamimoto T., Inoue K., Ikeda Y., Hagiwara M.;
RT "Scaffold role of a mitogen-activated protein kinase phosphatase, SKRP1,
RT for the JNK signaling pathway.";
RL J. Biol. Chem. 277:23919-23926(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Kikuchi K., Nakamura K., Sato T., Shima H.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=12479873; DOI=10.1016/s1357-2725(02)00127-9;
RA Cheng H., Gao Q., Jiang M., Ma Y., Ni X., Guo L., Jin W., Cao G., Ji C.,
RA Ying K., Xu W., Gu S., Ma Y., Xie Y., Mao Y.;
RT "Molecular cloning and characterization of a novel human protein
RT phosphatase, LMW-DSP3.";
RL Int. J. Biochem. Cell Biol. 35:226-234(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 65-206.
RX PubMed=21989941; DOI=10.1002/prot.23156;
RA Wei C.H., Ryu S.Y., Jeon Y.H., Yoon M.Y., Jeong D.G., Kim S.J., Ryu S.E.;
RT "Crystal structure of a novel mitogen-activated protein kinase phosphatase,
RT SKRP1.";
RL Proteins 79:3242-3246(2011).
CC -!- FUNCTION: Has a dual specificity toward Ser/Thr and Tyr-containing
CC proteins. {ECO:0000269|PubMed:12479873}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:12479873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC Evidence={ECO:0000269|PubMed:12479873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:12479873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000269|PubMed:12479873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:12479873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC Evidence={ECO:0000269|PubMed:12479873};
CC -!- ACTIVITY REGULATION: Phosphatase activity is enhanced by Ca(2+) and
CC Mn(2+). {ECO:0000269|PubMed:12479873}.
CC -!- INTERACTION:
CC Q8WTR2; P60709: ACTB; NbExp=4; IntAct=EBI-8654968, EBI-353944;
CC Q8WTR2; P13196: ALAS1; NbExp=8; IntAct=EBI-8654968, EBI-3905054;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q8WTR2-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q8WTR2-2; Sequence=VSP_005138;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, lung, liver, and pancreas.
CC The expression level in the pancreas is the highest.
CC {ECO:0000269|PubMed:12479873}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AB063186; BAB83498.1; -; mRNA.
DR EMBL; AB063187; BAB83499.1; -; mRNA.
DR EMBL; AB038770; BAB82499.1; -; mRNA.
DR EMBL; AF486808; AAO49450.1; -; mRNA.
DR EMBL; AK314078; BAG36776.1; -; mRNA.
DR EMBL; AC064871; AAY24197.1; -; Genomic_DNA.
DR EMBL; BC035000; AAH35000.1; -; mRNA.
DR EMBL; BC093958; AAH93958.1; -; mRNA.
DR EMBL; BC112005; AAI12006.1; -; mRNA.
DR CCDS; CCDS2289.1; -. [Q8WTR2-1]
DR CCDS; CCDS46469.1; -. [Q8WTR2-2]
DR RefSeq; NP_001135786.1; NM_001142314.1. [Q8WTR2-2]
DR RefSeq; NP_001308448.1; NM_001321519.1.
DR RefSeq; NP_543152.1; NM_080876.3. [Q8WTR2-1]
DR PDB; 3S4E; X-ray; 1.26 A; A=65-206.
DR PDB; 4D3P; X-ray; 1.27 A; A=65-205.
DR PDB; 4D3Q; X-ray; 1.64 A; A/B=65-205.
DR PDB; 4D3R; X-ray; 1.67 A; A=65-204.
DR PDBsum; 3S4E; -.
DR PDBsum; 4D3P; -.
DR PDBsum; 4D3Q; -.
DR PDBsum; 4D3R; -.
DR AlphaFoldDB; Q8WTR2; -.
DR SMR; Q8WTR2; -.
DR BioGRID; 126770; 96.
DR IntAct; Q8WTR2; 33.
DR MINT; Q8WTR2; -.
DR STRING; 9606.ENSP00000346160; -.
DR DEPOD; DUSP19; -.
DR iPTMnet; Q8WTR2; -.
DR PhosphoSitePlus; Q8WTR2; -.
DR BioMuta; DUSP19; -.
DR DMDM; 29840769; -.
DR EPD; Q8WTR2; -.
DR MassIVE; Q8WTR2; -.
DR MaxQB; Q8WTR2; -.
DR PaxDb; Q8WTR2; -.
DR PeptideAtlas; Q8WTR2; -.
DR PRIDE; Q8WTR2; -.
DR ProteomicsDB; 74584; -. [Q8WTR2-1]
DR ProteomicsDB; 74585; -. [Q8WTR2-2]
DR Antibodypedia; 19768; 192 antibodies from 26 providers.
DR DNASU; 142679; -.
DR Ensembl; ENST00000342619.10; ENSP00000343905.6; ENSG00000162999.13. [Q8WTR2-2]
DR Ensembl; ENST00000354221.5; ENSP00000346160.4; ENSG00000162999.13. [Q8WTR2-1]
DR GeneID; 142679; -.
DR KEGG; hsa:142679; -.
DR MANE-Select; ENST00000354221.5; ENSP00000346160.4; NM_080876.4; NP_543152.1.
DR UCSC; uc002upd.4; human. [Q8WTR2-1]
DR CTD; 142679; -.
DR DisGeNET; 142679; -.
DR GeneCards; DUSP19; -.
DR HGNC; HGNC:18894; DUSP19.
DR HPA; ENSG00000162999; Low tissue specificity.
DR MIM; 611437; gene.
DR neXtProt; NX_Q8WTR2; -.
DR OpenTargets; ENSG00000162999; -.
DR PharmGKB; PA134895660; -.
DR VEuPathDB; HostDB:ENSG00000162999; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000156472; -.
DR HOGENOM; CLU_027074_10_0_1; -.
DR InParanoid; Q8WTR2; -.
DR OMA; TWKDARM; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q8WTR2; -.
DR TreeFam; TF354211; -.
DR PathwayCommons; Q8WTR2; -.
DR SignaLink; Q8WTR2; -.
DR SIGNOR; Q8WTR2; -.
DR BioGRID-ORCS; 142679; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; DUSP19; human.
DR GeneWiki; DUSP19; -.
DR GenomeRNAi; 142679; -.
DR Pharos; Q8WTR2; Tbio.
DR PRO; PR:Q8WTR2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WTR2; protein.
DR Bgee; ENSG00000162999; Expressed in oocyte and 117 other tissues.
DR Genevisible; Q8WTR2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008579; F:JUN kinase phosphatase activity; IBA:GO_Central.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISS:BHF-UCL.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISS:BHF-UCL.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:BHF-UCL.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:BHF-UCL.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISS:BHF-UCL.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; ISS:BHF-UCL.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:BHF-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISS:BHF-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:BHF-UCL.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:BHF-UCL.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0043405; P:regulation of MAP kinase activity; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Hydrolase;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..217
FT /note="Dual specificity protein phosphatase 19"
FT /id="PRO_0000094832"
FT DOMAIN 65..206
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 150
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 91..141
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11959862"
FT /id="VSP_005138"
FT VARIANT 216
FT /note="S -> R (in dbSNP:rs16823987)"
FT /id="VAR_051755"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:3S4E"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3S4E"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:3S4E"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:3S4E"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3S4E"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3S4E"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3S4E"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:3S4E"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:3S4E"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:3S4E"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:3S4E"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:3S4E"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:3S4E"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:3S4E"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:3S4E"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3S4E"
SQ 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
