DUS28_HUMAN
ID DUS28_HUMAN Reviewed; 176 AA.
AC Q4G0W2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Dual specificity phosphatase 28;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
GN Name=DUSP28;
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 [LARGE SCALE MRNA].
RC TISSUE=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 [2]
RP FUNCTION.
RX PubMed=24531476; DOI=10.1107/s1399004713029866;
RA Jeong D.G., Wei C.H., Ku B., Jeon T.J., Chien P.N., Kim J.K., Park S.Y.,
RA Hwang H.S., Ryu S.Y., Park H., Kim D.S., Kim S.J., Ryu S.E.;
RT "The family-wide structure and function of human dual-specificity protein
RT phosphatases.";
RL Acta Crystallogr. D 70:421-435(2014).
RN [3] {ECO:0007744|PDB:5Y15, ECO:0007744|PDB:5Y16}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP TYR-102; CYS-103; ASN-105 AND ARG-107.
RX PubMed=29121083; DOI=10.1371/journal.pone.0187701;
RA Ku B., Hong W., Keum C.W., Kim M., Ryu H., Jeon D., Shin H.C., Kim J.H.,
RA Kim S.J., Ryu S.E.;
RT "Structural and biochemical analysis of atypically low dephosphorylating
RT activity of human dual-specificity phosphatase 28.";
RL PLoS ONE 12:E0187701-E0187701(2017).
CC -!- FUNCTION: Has phosphatase activity with the synthetic substrate 6,8-
CC difluoro-4-methylumbelliferyl phosphate (in vitro) (PubMed:24531476,
CC PubMed:29121083). Has almost no detectable activity with
CC phosphotyrosine, even less activity with phosphothreonine and displays
CC complete lack of activity with phosphoserine (PubMed:29121083). The
CC poor activity with phosphotyrosine may be due to steric hindrance by
CC bulky amino acid sidechains that obstruct access to the active site
CC (PubMed:29121083). {ECO:0000269|PubMed:24531476,
CC ECO:0000269|PubMed:29121083}.
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 -!- 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:29121083};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:29121083}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; BC036198; AAH36198.1; -; mRNA.
DR CCDS; CCDS33418.1; -.
DR RefSeq; NP_001028747.1; NM_001033575.1.
DR PDB; 5Y15; X-ray; 2.10 A; A/B=1-176.
DR PDB; 5Y16; X-ray; 2.40 A; A/B=1-176.
DR PDBsum; 5Y15; -.
DR PDBsum; 5Y16; -.
DR AlphaFoldDB; Q4G0W2; -.
DR SMR; Q4G0W2; -.
DR BioGRID; 130042; 63.
DR IntAct; Q4G0W2; 4.
DR MINT; Q4G0W2; -.
DR STRING; 9606.ENSP00000385885; -.
DR DEPOD; DUSP28; -.
DR iPTMnet; Q4G0W2; -.
DR PhosphoSitePlus; Q4G0W2; -.
DR SwissPalm; Q4G0W2; -.
DR BioMuta; DUSP28; -.
DR DMDM; 121943916; -.
DR EPD; Q4G0W2; -.
DR jPOST; Q4G0W2; -.
DR MassIVE; Q4G0W2; -.
DR PaxDb; Q4G0W2; -.
DR PeptideAtlas; Q4G0W2; -.
DR PRIDE; Q4G0W2; -.
DR ProteomicsDB; 62133; -.
DR Antibodypedia; 50666; 26 antibodies from 12 providers.
DR DNASU; 285193; -.
DR Ensembl; ENST00000343217.6; ENSP00000344235.2; ENSG00000188542.10.
DR Ensembl; ENST00000405954.2; ENSP00000385885.2; ENSG00000188542.10.
DR GeneID; 285193; -.
DR KEGG; hsa:285193; -.
DR MANE-Select; ENST00000405954.2; ENSP00000385885.2; NM_001370465.2; NP_001357394.1.
DR UCSC; uc002vzg.3; human.
DR CTD; 285193; -.
DR DisGeNET; 285193; -.
DR GeneCards; DUSP28; -.
DR HGNC; HGNC:33237; DUSP28.
DR HPA; ENSG00000188542; Low tissue specificity.
DR neXtProt; NX_Q4G0W2; -.
DR OpenTargets; ENSG00000188542; -.
DR PharmGKB; PA162384124; -.
DR VEuPathDB; HostDB:ENSG00000188542; -.
DR eggNOG; KOG1718; Eukaryota.
DR GeneTree; ENSGT00940000161528; -.
DR InParanoid; Q4G0W2; -.
DR OMA; EPNLGFW; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q4G0W2; -.
DR TreeFam; TF105128; -.
DR PathwayCommons; Q4G0W2; -.
DR SignaLink; Q4G0W2; -.
DR BioGRID-ORCS; 285193; 18 hits in 1075 CRISPR screens.
DR GenomeRNAi; 285193; -.
DR Pharos; Q4G0W2; Tbio.
DR PRO; PR:Q4G0W2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q4G0W2; protein.
DR Bgee; ENSG00000188542; Expressed in vastus lateralis and 170 other tissues.
DR ExpressionAtlas; Q4G0W2; baseline and differential.
DR Genevisible; Q4G0W2; HS.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
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; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..176
FT /note="Dual specificity phosphatase 28"
FT /id="PRO_0000302840"
FT DOMAIN 17..159
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 103
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000305|PubMed:29121083"
FT MUTAGEN 102
FT /note="Y->H: Decreases the already low catalytic activity."
FT /evidence="ECO:0000269|PubMed:29121083"
FT MUTAGEN 103
FT /note="C->S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29121083"
FT MUTAGEN 105
FT /note="N->A: Increases activity with phosphotyrosine; when
FT associated with V-107."
FT /evidence="ECO:0000269|PubMed:29121083"
FT MUTAGEN 107
FT /note="R->V: Increases activity with phosphotyrosine; when
FT associated with A-105."
FT /evidence="ECO:0000269|PubMed:29121083"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:5Y15"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:5Y15"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:5Y15"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:5Y15"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:5Y15"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:5Y15"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5Y15"
FT HELIX 79..94
FT /evidence="ECO:0007829|PDB:5Y15"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:5Y15"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5Y15"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:5Y15"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:5Y15"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:5Y15"
SQ SEQUENCE 176 AA; 18324 MW; 3BB208F7373814B0 CRC64;
MGPAEAGRRG AASPVPPPLV RVAPSLFLGS ARAAGAEEQL ARAGVTLCVN VSRQQPGPRA
PGVAELRVPV FDDPAEDLLA HLEPTCAAME AAVRAGGACL VYCKNGRSRS AAVCTAYLMR
HRGLSLAKAF QMVKSARPVA EPNPGFWSQL QKYEEALQAQ SCLQGEPPAL GLGPEA
