DUS4_HUMAN
ID DUS4_HUMAN Reviewed; 394 AA.
AC Q13115; B2RBU5; D3DSU4; G5E930; Q13524;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Dual specificity protein phosphatase 4;
DE EC=3.1.3.16 {ECO:0000269|PubMed:7535768};
DE EC=3.1.3.48 {ECO:0000269|PubMed:7535768};
DE AltName: Full=Dual specificity protein phosphatase hVH2;
DE AltName: Full=Mitogen-activated protein kinase phosphatase 2;
DE Short=MAP kinase phosphatase 2;
DE Short=MKP-2;
GN Name=DUSP4; Synonyms=MKP2, VH2;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7535768; DOI=10.1074/jbc.270.13.7197;
RA Guan K.-L., Butch E.;
RT "Isolation and characterization of a novel dual specific phosphatase, HVH2,
RT which selectively dephosphorylates the mitogen-activated protein kinase.";
RL J. Biol. Chem. 270:7197-7203(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8626452; DOI=10.1074/jbc.271.11.6497;
RA Chu Y., Solski P.A., Khosravi-Far R., Der C.J., Kelly K.;
RT "The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2
RT have unique substrate specificities and reduced activity in vivo toward the
RT ERK2 sevenmaker mutation.";
RL J. Biol. Chem. 271:6497-6501(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, and Uterus;
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 [8]
RP PHOSPHORYLATION AT SER-386 AND SER-391.
RX PubMed=21084841; DOI=10.4161/cc.9.23.13957;
RA Peng D.J., Zhou J.Y., Wu G.S.;
RT "Post-translational regulation of mitogen-activated protein kinase
RT phosphatase-2 (MKP-2) by ERK.";
RL Cell Cycle 9:4650-4655(2010).
RN [9]
RP ALTERNATIVE SPLICING.
RX PubMed=19843478; DOI=10.1016/j.cellsig.2009.10.002;
RA Cadalbert L.C., Sloss C.M., Cunningham M.R., Al-Mutairi M., McIntire A.,
RA Shipley J., Plevin R.;
RT "Differential regulation of MAP kinase activation by a novel splice variant
RT of human MAP kinase phosphatase-2.";
RL Cell. Signal. 22:357-365(2010).
RN [10]
RP IDENTIFICATION BY MASS 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 [11]
RP ACETYLATION AT VAL-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-336, AND SUBUNIT.
RX PubMed=19415758; DOI=10.1002/prot.22423;
RA Jeong D.G., Jung S.K., Yoon T.S., Woo E.J., Kim J.H., Park B.C., Ryu S.E.,
RA Kim S.J.;
RT "Crystal structure of the catalytic domain of human MKP-2 reveals a 24-mer
RT assembly.";
RL Proteins 76:763-767(2009).
CC -!- FUNCTION: Regulates mitogenic signal transduction by dephosphorylating
CC both Thr and Tyr residues on MAP kinases ERK1 and ERK2.
CC {ECO:0000269|PubMed:7535768}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:7535768};
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:7535768};
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:7535768};
CC -!- SUBUNIT: Hollow spherical complex composed of 24 subunits with
CC pseudooctahedral symmetry, has a tetramer as the basic unit.
CC {ECO:0000269|PubMed:19415758}.
CC -!- INTERACTION:
CC Q13115; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-6591081, EBI-739467;
CC Q13115; Q96S90: LYSMD1; NbExp=3; IntAct=EBI-6591081, EBI-10293291;
CC Q13115; Q8IV50-2: LYSMD2; NbExp=3; IntAct=EBI-6591081, EBI-19761491;
CC Q13115; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-6591081, EBI-741037;
CC Q13115; P28482: MAPK1; NbExp=6; IntAct=EBI-6591081, EBI-959949;
CC Q13115; P45984: MAPK9; NbExp=4; IntAct=EBI-6591081, EBI-713568;
CC Q13115; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-6591081, EBI-12025760;
CC Q13115; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-6591081, EBI-742388;
CC Q13115; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-6591081, EBI-11139477;
CC Q13115; Q13077: TRAF1; NbExp=3; IntAct=EBI-6591081, EBI-359224;
CC Q13115; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-6591081, EBI-743265;
CC Q13115; Q8N720: ZNF655; NbExp=3; IntAct=EBI-6591081, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7535768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=MKP-2-L;
CC IsoId=Q13115-1; Sequence=Displayed;
CC Name=2; Synonyms=MKP-2-S;
CC IsoId=Q13115-2; Sequence=VSP_044667, VSP_044668;
CC -!- PTM: Phosphorylation in the C-terminus by ERK1/2 inhibits proteasomal
CC degradation and stabilizes the protein. {ECO:0000269|PubMed:21084841}.
CC -!- MISCELLANEOUS: [Isoform 2]: Does not bind to JNK or ERK, and is more
CC susceptible to proteosomal degradation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; U21108; AAA85119.1; -; mRNA.
DR EMBL; U48807; AAC50452.1; -; mRNA.
DR EMBL; AK314820; BAG37342.1; -; mRNA.
DR EMBL; AL137704; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC084262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63481.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63482.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63483.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63484.1; -; Genomic_DNA.
DR EMBL; BC002671; AAH02671.1; -; mRNA.
DR EMBL; BC014565; AAH14565.1; -; mRNA.
DR CCDS; CCDS6072.1; -. [Q13115-1]
DR CCDS; CCDS6073.1; -. [Q13115-2]
DR RefSeq; NP_001385.1; NM_001394.6. [Q13115-1]
DR RefSeq; NP_476499.1; NM_057158.3. [Q13115-2]
DR RefSeq; XP_011542730.1; XM_011544428.2. [Q13115-2]
DR PDB; 3EZZ; X-ray; 2.90 A; A/B/C/D/E/F=194-336.
DR PDBsum; 3EZZ; -.
DR AlphaFoldDB; Q13115; -.
DR SMR; Q13115; -.
DR BioGRID; 108179; 121.
DR IntAct; Q13115; 67.
DR MINT; Q13115; -.
DR STRING; 9606.ENSP00000240100; -.
DR BindingDB; Q13115; -.
DR ChEMBL; CHEMBL2146343; -.
DR DEPOD; DUSP4; -.
DR GlyGen; Q13115; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13115; -.
DR PhosphoSitePlus; Q13115; -.
DR BioMuta; DUSP4; -.
DR DMDM; 2499745; -.
DR CPTAC; CPTAC-1565; -.
DR EPD; Q13115; -.
DR jPOST; Q13115; -.
DR MassIVE; Q13115; -.
DR MaxQB; Q13115; -.
DR PaxDb; Q13115; -.
DR PeptideAtlas; Q13115; -.
DR PRIDE; Q13115; -.
DR ProteomicsDB; 33812; -.
DR ProteomicsDB; 59167; -. [Q13115-1]
DR Antibodypedia; 10497; 435 antibodies from 33 providers.
DR DNASU; 1846; -.
DR Ensembl; ENST00000240100.7; ENSP00000240100.2; ENSG00000120875.9. [Q13115-1]
DR Ensembl; ENST00000240101.2; ENSP00000240101.2; ENSG00000120875.9. [Q13115-2]
DR GeneID; 1846; -.
DR KEGG; hsa:1846; -.
DR MANE-Select; ENST00000240100.7; ENSP00000240100.2; NM_001394.7; NP_001385.1.
DR UCSC; uc003xhl.4; human. [Q13115-1]
DR CTD; 1846; -.
DR DisGeNET; 1846; -.
DR GeneCards; DUSP4; -.
DR HGNC; HGNC:3070; DUSP4.
DR HPA; ENSG00000120875; Tissue enhanced (brain, pancreas, stomach).
DR MIM; 602747; gene.
DR neXtProt; NX_Q13115; -.
DR OpenTargets; ENSG00000120875; -.
DR PharmGKB; PA27527; -.
DR VEuPathDB; HostDB:ENSG00000120875; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000159066; -.
DR HOGENOM; CLU_027074_0_2_1; -.
DR InParanoid; Q13115; -.
DR OMA; ELGEMDC; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q13115; -.
DR TreeFam; TF105122; -.
DR PathwayCommons; Q13115; -.
DR Reactome; R-HSA-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-HSA-202670; ERKs are inactivated.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR SignaLink; Q13115; -.
DR SIGNOR; Q13115; -.
DR BioGRID-ORCS; 1846; 52 hits in 1083 CRISPR screens.
DR ChiTaRS; DUSP4; human.
DR EvolutionaryTrace; Q13115; -.
DR GeneWiki; DUSP4; -.
DR GenomeRNAi; 1846; -.
DR Pharos; Q13115; Tbio.
DR PRO; PR:Q13115; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q13115; protein.
DR Bgee; ENSG00000120875; Expressed in pigmented layer of retina and 151 other tissues.
DR Genevisible; Q13115; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990439; F:MAP kinase serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0001706; P:endoderm formation; IBA:GO_Central.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 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; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052"
FT CHAIN 2..394
FT /note="Dual specificity protein phosphatase 4"
FT /id="PRO_0000094798"
FT DOMAIN 41..159
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 195..336
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 280
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000269|PubMed:25489052"
FT MOD_RES 386
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:21084841"
FT MOD_RES 391
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:21084841"
FT VAR_SEQ 1..53
FT /note="MVTMEELREMDCSVLKRLMNRDENGGGAGGSGSHGTLGLPSGGKCLLLDCRP
FT F -> MGRKVHSNGSQFAEHSRSPRRTGRDCKPVRAPSMALGVSQLAGRSRCLCSESQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_044667"
FT VAR_SEQ 54..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_044668"
FT CONFLICT 111
FT /note="R -> G (in Ref. 2; AAC50452)"
FT /evidence="ECO:0000305"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:3EZZ"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:3EZZ"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:3EZZ"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:3EZZ"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3EZZ"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3EZZ"
FT TURN 235..239
FT /evidence="ECO:0007829|PDB:3EZZ"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3EZZ"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:3EZZ"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:3EZZ"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:3EZZ"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:3EZZ"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:3EZZ"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:3EZZ"
FT HELIX 321..335
FT /evidence="ECO:0007829|PDB:3EZZ"
SQ SEQUENCE 394 AA; 42953 MW; 0603971759B6952E CRC64;
MVTMEELREM DCSVLKRLMN RDENGGGAGG SGSHGTLGLP SGGKCLLLDC RPFLAHSAGY
ILGSVNVRCN TIVRRRAKGS VSLEQILPAE EEVRARLRSG LYSAVIVYDE RSPRAESLRE
DSTVSLVVQA LRRNAERTDI CLLKGGYERF SSEYPEFCSK TKALAAIPPP VPPSATEPLD
LGCSSCGTPL HDQGGPVEIL PFLYLGSAYH AARRDMLDAL GITALLNVSS DCPNHFEGHY
QYKCIPVEDN HKADISSWFM EAIEYIDAVK DCRGRVLVHC QAGISRSATI CLAYLMMKKR
VRLEEAFEFV KQRRSIISPN FSFMGQLLQF ESQVLATSCA AEAASPSGPL RERGKTPATP
TSQFVFSFPV SVGVHSAPSS LPYLHSPITT SPSC
