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   24-JAN-2024, entry version 148.
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; 40.
DR   IntAct; Q68J44; 28.
DR   MINT; Q68J44; -.
DR   STRING; 9606.ENSP00000340609; -.
DR   DEPOD; DUPD1; -.
DR   GlyGen; Q68J44; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q68J44; -.
DR   PhosphoSitePlus; Q68J44; -.
DR   BioMuta; DUPD1; -.
DR   DMDM; 74748317; -.
DR   MassIVE; Q68J44; -.
DR   PaxDb; 9606-ENSP00000340609; -.
DR   PeptideAtlas; Q68J44; -.
DR   Antibodypedia; 29633; 134 antibodies from 13 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   AGR; HGNC:23481; -.
DR   CTD; 338599; -.
DR   DisGeNET; 338599; -.
DR   GeneCards; DUSP29; -.
DR   HGNC; HGNC:23481; DUSP29.
DR   HPA; ENSG00000188716; Tissue enriched (skeletal).
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; 1082488at2759; -.
DR   PhylomeDB; Q68J44; -.
DR   TreeFam; TF105128; -.
DR   PathwayCommons; Q68J44; -.
DR   SignaLink; Q68J44; -.
DR   BioGRID-ORCS; 338599; 10 hits in 1160 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 cell types or 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   CDD; cd14575; DUPD1; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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; AGAP008228-PA; 1.
DR   PANTHER; PTHR45682:SF6; DUAL SPECIFICITY PHOSPHATASE 29; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   PRINTS; PR01909; ADSPHPHTASEA.
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.
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
//