ID   DUS14_HUMAN             Reviewed;         198 AA.
AC   O95147;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 175.
DE   RecName: Full=Dual specificity protein phosphatase 14;
DE            EC=3.1.3.16 {ECO:0000269|PubMed:24403530};
DE            EC=3.1.3.48;
DE   AltName: Full=MKP-1-like protein tyrosine phosphatase;
DE            Short=MKP-L;
DE   AltName: Full=Mitogen-activated protein kinase phosphatase 6;
DE            Short=MAP kinase phosphatase 6;
DE            Short=MKP-6;
GN   Name=DUSP14; Synonyms=MKP6;
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].
RA   Yuan Y., Suphapeetiporn K., Sun H.;
RT   "MKP-L, a novel MKP-1 like protein tyrosine phosphatase.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11123293; DOI=10.4049/jimmunol.166.1.197;
RA   Marti F., Krause A., Post N.H., Lyddane C., Dupont B., Sadelain M.,
RA   King P.D.;
RT   "Negative-feedback regulation of CD28 costimulation by a novel mitogen-
RT   activated protein kinase phosphatase, MKP6.";
RL   J. Immunol. 166:197-206(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=24403530; DOI=10.4049/jimmunol.1300989;
RA   Yang C.Y., Li J.P., Chiu L.L., Lan J.L., Chen D.Y., Chuang H.C.,
RA   Huang C.Y., Tan T.H.;
RT   "Dual-specificity phosphatase 14 (DUSP14/MKP6) negatively regulates TCR
RT   signaling by inhibiting TAB1 activation.";
RL   J. Immunol. 192:1547-1557(2014).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 2-191 IN COMPLEX WITH PHOSPHATE,
RP   ACTIVE SITE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=19770498; DOI=10.1107/s0907444909023762;
RA   Lountos G.T., Tropea J.E., Cherry S., Waugh D.S.;
RT   "Overproduction, purification and structure determination of human dual-
RT   specificity phosphatase 14.";
RL   Acta Crystallogr. D 65:1013-1020(2009).
CC   -!- FUNCTION: Involved in the inactivation of MAP kinases. Dephosphorylates
CC       ERK, JNK and p38 MAP-kinases. Plays a negative role in TCR signaling by
CC       dephosphorylating MAP3K7 adapter TAB1 leading to its inactivation
CC       (PubMed:24403530). {ECO:0000269|PubMed:24403530}.
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};
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:24403530};
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   -!- SUBUNIT: Interacts with CD28. {ECO:0000269|PubMed:19770498}.
CC   -!- INTERACTION:
CC       O95147; Q8NA61: CBY2; NbExp=3; IntAct=EBI-3922653, EBI-741724;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; AF038844; AAD02105.1; -; mRNA.
DR   EMBL; AF120032; AAF28861.1; -; mRNA.
DR   EMBL; BC000370; AAH00370.1; -; mRNA.
DR   EMBL; BC001894; AAH01894.1; -; mRNA.
DR   EMBL; BC004448; AAH04448.1; -; mRNA.
DR   CCDS; CCDS11320.1; -.
DR   RefSeq; NP_008957.1; NM_007026.3.
DR   RefSeq; XP_005257034.1; XM_005256977.3.
DR   RefSeq; XP_011522536.1; XM_011524234.1.
DR   PDB; 2WGP; X-ray; 1.88 A; A/B=2-191.
DR   PDBsum; 2WGP; -.
DR   AlphaFoldDB; O95147; -.
DR   SMR; O95147; -.
DR   BioGRID; 116255; 245.
DR   IntAct; O95147; 59.
DR   MINT; O95147; -.
DR   STRING; 9606.ENSP00000477653; -.
DR   BindingDB; O95147; -.
DR   ChEMBL; CHEMBL1764941; -.
DR   DEPOD; DUSP14; -.
DR   GlyGen; O95147; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O95147; -.
DR   PhosphoSitePlus; O95147; -.
DR   BioMuta; DUSP14; -.
DR   EPD; O95147; -.
DR   jPOST; O95147; -.
DR   MassIVE; O95147; -.
DR   PaxDb; 9606-ENSP00000477653; -.
DR   PeptideAtlas; O95147; -.
DR   ProteomicsDB; 50661; -.
DR   Pumba; O95147; -.
DR   Antibodypedia; 73139; 375 antibodies from 34 providers.
DR   DNASU; 11072; -.
DR   Ensembl; ENST00000613659.1; ENSP00000484091.1; ENSG00000276023.5.
DR   Ensembl; ENST00000614294.2; ENSP00000478406.1; ENSG00000275932.2.
DR   Ensembl; ENST00000614411.1; ENSP00000477653.1; ENSG00000276023.5.
DR   Ensembl; ENST00000617516.5; ENSP00000478595.1; ENSG00000276023.5.
DR   Ensembl; ENST00000632468.1; ENSP00000487886.1; ENSG00000275932.2.
DR   Ensembl; ENST00000633870.1; ENSP00000488882.1; ENSG00000275932.2.
DR   GeneID; 11072; -.
DR   KEGG; hsa:11072; -.
DR   MANE-Select; ENST00000617516.5; ENSP00000478595.1; NM_007026.4; NP_008957.1.
DR   AGR; HGNC:17007; -.
DR   CTD; 11072; -.
DR   DisGeNET; 11072; -.
DR   GeneCards; DUSP14; -.
DR   HGNC; HGNC:17007; DUSP14.
DR   HPA; ENSG00000276023; Tissue enhanced (skin).
DR   MIM; 606618; gene.
DR   neXtProt; NX_O95147; -.
DR   OpenTargets; ENSG00000276023; -.
DR   PharmGKB; PA27523; -.
DR   VEuPathDB; HostDB:ENSG00000276023; -.
DR   eggNOG; KOG1718; Eukaryota.
DR   GeneTree; ENSGT00940000160675; -.
DR   HOGENOM; CLU_027074_3_2_1; -.
DR   InParanoid; O95147; -.
DR   OMA; IPDVYDR; -.
DR   OrthoDB; 127323at2759; -.
DR   PhylomeDB; O95147; -.
DR   TreeFam; TF316009; -.
DR   PathwayCommons; O95147; -.
DR   SignaLink; O95147; -.
DR   SIGNOR; O95147; -.
DR   BioGRID-ORCS; 11072; 21 hits in 1166 CRISPR screens.
DR   ChiTaRS; DUSP14; human.
DR   EvolutionaryTrace; O95147; -.
DR   GenomeRNAi; 11072; -.
DR   Pharos; O95147; Tbio.
DR   PRO; PR:O95147; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; O95147; Protein.
DR   Bgee; ENSG00000276023; Expressed in olfactory segment of nasal mucosa and 102 other cell types or tissues.
DR   ExpressionAtlas; O95147; baseline and differential.
DR   GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14572; DUSP14; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR020420; Atypical_DUSP_subfamB.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR45961:SF5; DUAL SPECIFICITY PROTEIN PHOSPHATASE 14; 1.
DR   PANTHER; PTHR45961; IP21249P; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   PRINTS; PR01910; ADSPHPHTASEB.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
DR   Genevisible; O95147; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..198
FT                   /note="Dual specificity protein phosphatase 14"
FT                   /id="PRO_0000094822"
FT   DOMAIN          26..167
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        111
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000269|PubMed:19770498"
FT   STRAND          27..31
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   HELIX           39..42
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   HELIX           45..50
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   HELIX           90..102
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   STRAND          107..110
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   STRAND          112..116
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   HELIX           117..130
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   HELIX           134..144
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   HELIX           152..166
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   STRAND          179..182
FT                   /evidence="ECO:0007829|PDB:2WGP"
FT   HELIX           183..189
FT                   /evidence="ECO:0007829|PDB:2WGP"
SQ   SEQUENCE   198 AA;  22255 MW;  6AAFAE1B3A24F9AA CRC64;
     MSSRGHSTLP RTLMAPRMIS EGDIGGIAQI TSSLFLGRGS VASNRHLLQA RGITCIVNAT
     IEIPNFNWPQ FEYVKVPLAD MPHAPIGLYF DTVADKIHSV SRKHGATLVH CAAGVSRSAT
     LCIAYLMKFH NVCLLEAYNW VKARRPVIRP NVGFWRQLID YERQLFGKST VKMVQTPYGI
     VPDVYEKESR HLMPYWGI
//