DUS14_HUMAN
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 03-AUG-2022, entry version 167.
DE RecName: Full=Dual specificity protein phosphatase 14;
DE EC=3.1.3.16;
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 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.
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 -!- 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; 241.
DR IntAct; O95147; 59.
DR MINT; O95147; -.
DR STRING; 9606.ENSP00000477653; -.
DR BindingDB; O95147; -.
DR ChEMBL; CHEMBL1764941; -.
DR DEPOD; DUSP14; -.
DR iPTMnet; O95147; -.
DR PhosphoSitePlus; O95147; -.
DR BioMuta; DUSP14; -.
DR EPD; O95147; -.
DR jPOST; O95147; -.
DR MassIVE; O95147; -.
DR PaxDb; O95147; -.
DR PeptideAtlas; O95147; -.
DR PRIDE; O95147; -.
DR ProteomicsDB; 50661; -.
DR Antibodypedia; 73139; 350 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 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; 1576308at2759; -.
DR PhylomeDB; O95147; -.
DR TreeFam; TF316009; -.
DR PathwayCommons; O95147; -.
DR SignaLink; O95147; -.
DR BioGRID-ORCS; 11072; 21 hits in 1076 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 101 other tissues.
DR ExpressionAtlas; O95147; baseline and differential.
DR Genevisible; O95147; HS.
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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01910; ADSPHPHTASEB.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 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; 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
