DUS28_MOUSE
ID DUS28_MOUSE Reviewed; 163 AA.
AC Q8BTR5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dual specificity phosphatase 28;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
GN Name=Dusp28;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
RA Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
RA Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
RA Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
RA Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
RA Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
RT "Structural genomics of protein phosphatases.";
RL J. Struct. Funct. Genomics 8:121-140(2007).
CC -!- FUNCTION: Has phosphatase activity with the synthetic substrate 6,8-
CC difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no
CC detectable activity with phosphotyrosine, even less activity with
CC phosphothreonine and displays complete lack of activity with
CC phosphoserine. The poor activity with phosphotyrosine may be due to
CC steric hindrance by bulky amino acid sidechains that obstruct access to
CC the active site. {ECO:0000250|UniProtKB:Q4G0W2}.
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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q4G0W2}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AK088940; BAC40664.1; -; mRNA.
DR EMBL; AK163560; BAE37397.1; -; mRNA.
DR EMBL; BC119127; AAI19128.1; -; mRNA.
DR CCDS; CCDS15179.1; -.
DR RefSeq; NP_780327.1; NM_175118.3.
DR PDB; 2HCM; X-ray; 2.00 A; A=2-163.
DR PDBsum; 2HCM; -.
DR AlphaFoldDB; Q8BTR5; -.
DR SMR; Q8BTR5; -.
DR STRING; 10090.ENSMUSP00000057690; -.
DR PhosphoSitePlus; Q8BTR5; -.
DR EPD; Q8BTR5; -.
DR MaxQB; Q8BTR5; -.
DR PaxDb; Q8BTR5; -.
DR PeptideAtlas; Q8BTR5; -.
DR PRIDE; Q8BTR5; -.
DR ProteomicsDB; 277532; -.
DR Antibodypedia; 50666; 26 antibodies from 12 providers.
DR DNASU; 67446; -.
DR Ensembl; ENSMUST00000060913; ENSMUSP00000057690; ENSMUSG00000047067.
DR GeneID; 67446; -.
DR KEGG; mmu:67446; -.
DR UCSC; uc007cbu.1; mouse.
DR CTD; 285193; -.
DR MGI; MGI:1914696; Dusp28.
DR VEuPathDB; HostDB:ENSMUSG00000047067; -.
DR eggNOG; KOG1718; Eukaryota.
DR GeneTree; ENSGT00940000161528; -.
DR HOGENOM; CLU_027074_3_3_1; -.
DR InParanoid; Q8BTR5; -.
DR OMA; EPNLGFW; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q8BTR5; -.
DR TreeFam; TF105128; -.
DR BioGRID-ORCS; 67446; 3 hits in 71 CRISPR screens.
DR EvolutionaryTrace; Q8BTR5; -.
DR PRO; PR:Q8BTR5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BTR5; protein.
DR Bgee; ENSMUSG00000047067; Expressed in interventricular septum and 152 other tissues.
DR Genevisible; Q8BTR5; MM.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; ISS: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; ISS: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..163
FT /note="Dual specificity phosphatase 28"
FT /id="PRO_0000302841"
FT DOMAIN 10..151
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 95
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:2HCM"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:2HCM"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:2HCM"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:2HCM"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2HCM"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2HCM"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2HCM"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:2HCM"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:2HCM"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:2HCM"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:2HCM"
FT HELIX 136..151
FT /evidence="ECO:0007829|PDB:2HCM"
SQ SEQUENCE 163 AA; 17505 MW; 40259C4C084B0696 CRC64;
MGTSEAAPPP FARVAPALFI GNARAAGATE LLVRAGITLC VNVSRQQPGP RAPGVAELRV
PVFDDPAEDL LTHLEPTCAA MEAAVRDGGS CLVYCKNGRS RSAAVCTAYL MRHRGHSLDR
AFQMVKSARP VAEPNLGFWA QLQKYEQTLQ AQAILPREPI DPE
