ID   E5RHD0_HUMAN            Unreviewed;       145 AA.
AC   E5RHD0;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 8.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Dual specificity protein phosphatase {ECO:0000256|RuleBase:RU366038};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU366038};
DE            EC=3.1.3.48 {ECO:0000256|RuleBase:RU366038};
DE   Flags: Fragment;
GN   Name=DUSP26 {ECO:0000313|Ensembl:ENSP00000430922.1};
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 {ECO:0000313|Ensembl:ENSP00000430922.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000430922.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Glockner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000430922.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Dual specificity phosphatase able to dephosphorylate
CC       phosphotyrosine, phosphoserine and phosphothreonine residues, with a
CC       preference for phosphotyrosine as a substrate.
CC       {ECO:0000256|RuleBase:RU366038}.
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:0000256|RuleBase:RU366038};
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:0000256|RuleBase:RU366038};
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:0000256|RuleBase:RU366038};
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily.
CC       {ECO:0000256|RuleBase:RU366038}.
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DR   EMBL; AC013603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E5RHD0; -.
DR   SMR; E5RHD0; -.
DR   MassIVE; E5RHD0; -.
DR   PeptideAtlas; E5RHD0; -.
DR   ProteomicsDB; 15941; -.
DR   Antibodypedia; 10741; 245 antibodies from 31 providers.
DR   Ensembl; ENST00000522982.1; ENSP00000430922.1; ENSG00000133878.9.
DR   UCSC; uc064lvy.1; human.
DR   HGNC; HGNC:28161; DUSP26.
DR   VEuPathDB; HostDB:ENSG00000133878; -.
DR   GeneTree; ENSGT00940000158107; -.
DR   HOGENOM; CLU_1791276_0_0_1; -.
DR   OMA; MSIHFQA; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; ENSG00000133878; Expressed in hindlimb stylopod muscle and 156 other cell types or tissues.
DR   ExpressionAtlas; E5RHD0; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR020405; Atypical_DUSP_subfamA.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   PANTHER; PTHR45682; AGAP008228-PA; 1.
DR   PANTHER; PTHR45682:SF8; DUAL SPECIFICITY PROTEIN PHOSPHATASE 26; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   PRINTS; PR01909; ADSPHPHTASEA.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
PE   1: Evidence at protein level;
KW   Hydrolase {ECO:0000256|RuleBase:RU366038};
KW   Protein phosphatase {ECO:0000256|RuleBase:RU366038};
KW   Proteomics identification {ECO:0007829|MaxQB:E5RHD0,
KW   ECO:0007829|PeptideAtlas:E5RHD0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT   NON_TER         145
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000430922.1"
SQ   SEQUENCE   145 AA;  16521 MW;  FA1B2FC69052D7A5 CRC64;
     MCPGNWLWAS MTFMARFSRS SSRSPVRTRG TLEEMPTVQH PFLNVFELER LLYTGKTACN
     HADEVWPGLY LGDQDMANNR RELRRLGITH VLNASHSRWR GTPEAYEGLG IRYLGVEAHD
     SPAFDMSIHF QTAADFIHRA LSQPG
//