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 16-SEP-2015, entry version 103. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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 RT 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 -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O CC = [a protein]-serine/threonine + phosphate. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Non-receptor class dual specificity subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Mm.46179; -. DR PDB; 2HCM; X-ray; 2.00 A; A=2-163. DR PDBsum; 2HCM; -. DR ProteinModelPortal; Q8BTR5; -. DR SMR; Q8BTR5; 1-158. DR STRING; 10090.ENSMUSP00000057690; -. DR PaxDb; Q8BTR5; -. DR PRIDE; Q8BTR5; -. 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 eggNOG; NOG313004; -. DR GeneTree; ENSGT00760000118853; -. DR HOGENOM; HOG000233766; -. DR HOVERGEN; HBG051422; -. DR InParanoid; Q8BTR5; -. DR KO; K14165; -. DR OMA; AKAFQMV; -. DR OrthoDB; EOG715Q5Z; -. DR PhylomeDB; Q8BTR5; -. DR TreeFam; TF105128; -. DR EvolutionaryTrace; Q8BTR5; -. DR NextBio; 324594; -. DR PRO; PR:Q8BTR5; -. DR Proteomes; UP000000589; Chromosome 1. DR Bgee; Q8BTR5; -. DR CleanEx; MM_DUSP28; -. DR Genevisible; Q8BTR5; MM. DR GO; GO:0005622; C:intracellular; IBA:GOC. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0007254; P:JNK cascade; IBA:GO_Central. DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. DR InterPro; IPR024950; DUSP. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR10159; PTHR10159; 1. 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; Complete proteome; Hydrolase; Protein phosphatase; KW Reference proteome. FT CHAIN 1 163 Dual specificity phosphatase 28. FT /FTId=PRO_0000302841. FT DOMAIN 68 130 Tyrosine-protein phosphatase. FT ACT_SITE 95 95 Phosphocysteine intermediate. FT {ECO:0000250}. FT STRAND 10 15 {ECO:0000244|PDB:2HCM}. FT STRAND 18 22 {ECO:0000244|PDB:2HCM}. FT HELIX 23 27 {ECO:0000244|PDB:2HCM}. FT HELIX 29 34 {ECO:0000244|PDB:2HCM}. FT STRAND 37 42 {ECO:0000244|PDB:2HCM}. FT STRAND 44 46 {ECO:0000244|PDB:2HCM}. FT STRAND 56 59 {ECO:0000244|PDB:2HCM}. FT HELIX 71 86 {ECO:0000244|PDB:2HCM}. FT STRAND 90 99 {ECO:0000244|PDB:2HCM}. FT HELIX 100 113 {ECO:0000244|PDB:2HCM}. FT HELIX 118 128 {ECO:0000244|PDB:2HCM}. FT HELIX 136 151 {ECO:0000244|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 //