DUS29_HUMAN
ID DUS29_HUMAN Reviewed; 220 AA.
AC Q68J44; B2RP93;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Dual specificity phosphatase 29 {ECO:0000312|HGNC:HGNC:23481};
DE AltName: Full=Dual specificity phosphatase 27 {ECO:0000303|PubMed:17498703, ECO:0000303|PubMed:21543850};
DE AltName: Full=Dual specificity phosphatase DUPD1 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:17498703};
DE EC=3.1.3.48 {ECO:0000269|PubMed:17498703};
GN Name=DUSP29 {ECO:0000312|HGNC:HGNC:23481};
GN Synonyms=DUPD1, DUSP27 {ECO:0000303|PubMed:17498703,
GN ECO:0000303|PubMed:21543850};
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], FUNCTION, SUBCELLULAR LOCATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=17498703; DOI=10.1016/j.febslet.2007.04.059;
RA Friedberg I., Nika K., Tautz L., Saito K., Cerignoli F., Friedberg I.,
RA Godzik A., Mustelin T.;
RT "Identification and characterization of DUSP27, a novel dual-specific
RT protein phosphatase.";
RL FEBS Lett. 581:2527-2533(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH SULFATE, AND
RP SUBUNIT.
RX PubMed=21543850; DOI=10.1107/s090744491100970x;
RA Lountos G.T., Tropea J.E., Waugh D.S.;
RT "Structure of human dual-specificity phosphatase 27 at 2.38 A resolution.";
RL Acta Crystallogr. D 67:471-479(2011).
CC -!- FUNCTION: Dual specificity phosphatase able to dephosphorylate
CC phosphotyrosine, phosphoserine and phosphothreonine residues within the
CC same substrate, with a preference for phosphotyrosine as a substrate
CC (PubMed:17498703). Involved in the modulation of intracellular
CC signaling cascades. In skeletal muscle regulates systemic glucose
CC homeostasis by activating, AMPK, an energy sensor protein kinase (By
CC similarity). Affects MAP kinase signaling though modulation of the
CC MAPK1/2 cascade in skeletal muscle promoting muscle cell
CC differentiation, development and atrophy (By similarity).
CC {ECO:0000250|UniProtKB:Q8BK84, ECO:0000269|PubMed:17498703}.
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:17498703};
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:17498703};
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:17498703};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.02 mM for para-nitrophenylphosphate (at pH 5.5)
CC {ECO:0000269|PubMed:17498703};
CC Note=kcat is 0.330 sec(-1) for para-nitrophenylphosphate.
CC {ECO:0000269|PubMed:17498703};
CC -!- SUBUNIT: Homodimer (PubMed:21543850). Interacts with PRKAA2 (By
CC similarity). {ECO:0000250|UniProtKB:Q8BK84,
CC ECO:0000269|PubMed:21543850}.
CC -!- INTERACTION:
CC Q68J44; O15145: ARPC3; NbExp=3; IntAct=EBI-1054321, EBI-351829;
CC Q68J44; P45381: ASPA; NbExp=3; IntAct=EBI-1054321, EBI-750475;
CC Q68J44; Q9HAS0: C17orf75; NbExp=3; IntAct=EBI-1054321, EBI-12954949;
CC Q68J44; Q8N137: CNTROB; NbExp=3; IntAct=EBI-1054321, EBI-947360;
CC Q68J44; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-1054321, EBI-742054;
CC Q68J44; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-1054321, EBI-11163335;
CC Q68J44; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-1054321, EBI-739832;
CC Q68J44; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-1054321, EBI-740897;
CC Q68J44; Q9BVI4: NOC4L; NbExp=3; IntAct=EBI-1054321, EBI-395927;
CC Q68J44; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1054321, EBI-79165;
CC Q68J44; P62487: POLR2G; NbExp=3; IntAct=EBI-1054321, EBI-347928;
CC Q68J44; P28074: PSMB5; NbExp=3; IntAct=EBI-1054321, EBI-357828;
CC Q68J44; O75150: RNF40; NbExp=3; IntAct=EBI-1054321, EBI-744408;
CC Q68J44; Q05519-2: SRSF11; NbExp=3; IntAct=EBI-1054321, EBI-11975029;
CC Q68J44; O75558: STX11; NbExp=3; IntAct=EBI-1054321, EBI-714135;
CC Q68J44; P15884-3: TCF4; NbExp=3; IntAct=EBI-1054321, EBI-13636688;
CC Q68J44; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-1054321, EBI-11139477;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17498703}. Nucleus
CC {ECO:0000250|UniProtKB:Q8BK84}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AY686755; AAT94288.1; -; mRNA.
DR EMBL; BC137321; AAI37322.1; -; mRNA.
DR EMBL; BC137322; AAI37323.1; -; mRNA.
DR CCDS; CCDS31223.1; -.
DR RefSeq; NP_001003892.1; NM_001003892.1.
DR RefSeq; XP_011538049.1; XM_011539747.2.
DR PDB; 2Y96; X-ray; 2.38 A; A/B=2-220.
DR PDBsum; 2Y96; -.
DR AlphaFoldDB; Q68J44; -.
DR SMR; Q68J44; -.
DR BioGRID; 130766; 39.
DR IntAct; Q68J44; 28.
DR MINT; Q68J44; -.
DR STRING; 9606.ENSP00000340609; -.
DR DEPOD; DUPD1; -.
DR iPTMnet; Q68J44; -.
DR PhosphoSitePlus; Q68J44; -.
DR BioMuta; DUPD1; -.
DR DMDM; 74748317; -.
DR MassIVE; Q68J44; -.
DR PaxDb; Q68J44; -.
DR PeptideAtlas; Q68J44; -.
DR PRIDE; Q68J44; -.
DR Antibodypedia; 29633; 107 antibodies from 12 providers.
DR DNASU; 338599; -.
DR Ensembl; ENST00000338487.6; ENSP00000340609.5; ENSG00000188716.6.
DR Ensembl; ENST00000625469.1; ENSP00000487404.1; ENSG00000281660.1.
DR GeneID; 338599; -.
DR KEGG; hsa:338599; -.
DR MANE-Select; ENST00000338487.6; ENSP00000340609.5; NM_001003892.3; NP_001003892.1.
DR UCSC; uc001jwq.1; human.
DR CTD; 338599; -.
DR DisGeNET; 338599; -.
DR GeneCards; DUSP29; -.
DR HGNC; HGNC:23481; DUSP29.
DR HPA; ENSG00000188716; Tissue enriched (skeletal).
DR MalaCards; DUSP29; -.
DR MIM; 618574; gene.
DR neXtProt; NX_Q68J44; -.
DR OpenTargets; ENSG00000188716; -.
DR VEuPathDB; HostDB:ENSG00000188716; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000160190; -.
DR HOGENOM; CLU_027074_11_3_1; -.
DR InParanoid; Q68J44; -.
DR OMA; NAAHGQR; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q68J44; -.
DR TreeFam; TF105128; -.
DR PathwayCommons; Q68J44; -.
DR SignaLink; Q68J44; -.
DR BioGRID-ORCS; 338599; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; DUPD1; human.
DR GenomeRNAi; 338599; -.
DR Pharos; Q68J44; Tbio.
DR PRO; PR:Q68J44; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q68J44; protein.
DR Bgee; ENSG00000188716; Expressed in hindlimb stylopod muscle and 40 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization 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; IDA:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0042692; P:muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020405; Atypical_DUSP_subfamA.
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; PTHR45682; PTHR45682; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01909; ADSPHPHTASEA.
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; Cytoplasm; Hydrolase; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..220
FT /note="Dual specificity phosphatase 29"
FT /id="PRO_0000295877"
FT DOMAIN 54..202
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 146..153
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT VARIANT 66
FT /note="D -> N (in dbSNP:rs11594934)"
FT /id="VAR_051757"
FT VARIANT 137
FT /note="S -> R (in dbSNP:rs16931938)"
FT /id="VAR_033376"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:2Y96"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2Y96"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2Y96"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:2Y96"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:2Y96"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:2Y96"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:2Y96"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2Y96"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2Y96"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:2Y96"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:2Y96"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2Y96"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:2Y96"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:2Y96"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:2Y96"
FT HELIX 187..205
FT /evidence="ECO:0007829|PDB:2Y96"
SQ SEQUENCE 220 AA; 25336 MW; A4DA1E37FD39D5A3 CRC64;
MTSGEVKTSL KNAYSSAKRL SPKMEEEGEE EDYCTPGAFE LERLFWKGSP QYTHVNEVWP
KLYIGDEATA LDRYRLQKAG FTHVLNAAHG RWNVDTGPDY YRDMDIQYHG VEADDLPTFD
LSVFFYPAAA FIDRALSDDH SKILVHCVMG RSRSATLVLA YLMIHKDMTL VDAIQQVAKN
RCVLPNRGFL KQLRELDKQL VQQRRRSQRQ DGEEEDGREL
