DUS11_MOUSE
ID DUS11_MOUSE Reviewed; 321 AA.
AC Q6NXK5; Q8BTR4; Q8BYE4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=RNA/RNP complex-1-interacting phosphatase;
DE EC=3.1.3.-;
DE AltName: Full=Dual specificity protein phosphatase 11;
DE AltName: Full=Phosphatase that interacts with RNA/RNP complex 1;
GN Name=Dusp11; Synonyms=Pir1;
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=NOD; TISSUE=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 STRAIN=C57BL/6J; 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).
CC -!- FUNCTION: Possesses RNA 5'-triphosphatase and diphosphatase activities,
CC but displays a poor protein-tyrosine phosphatase activity. In addition,
CC has phosphatase activity with ATP, ADP and O-methylfluorescein
CC phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA
CC metabolism. {ECO:0000250|UniProtKB:O75319}.
CC -!- SUBUNIT: Monomer. May interact with SFRS7 and SFRS9/SRP30C.
CC {ECO:0000250|UniProtKB:O75319}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75319}. Nucleus
CC speckle {ECO:0000250|UniProtKB:O75319}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AK040232; BAC30546.1; -; mRNA.
DR EMBL; AK088941; BAC40665.1; -; mRNA.
DR EMBL; BC067028; AAH67028.1; -; mRNA.
DR CCDS; CCDS20306.1; -.
DR RefSeq; NP_082375.4; NM_028099.4.
DR AlphaFoldDB; Q6NXK5; -.
DR SMR; Q6NXK5; -.
DR STRING; 10090.ENSMUSP00000032071; -.
DR iPTMnet; Q6NXK5; -.
DR PhosphoSitePlus; Q6NXK5; -.
DR EPD; Q6NXK5; -.
DR MaxQB; Q6NXK5; -.
DR PaxDb; Q6NXK5; -.
DR PeptideAtlas; Q6NXK5; -.
DR PRIDE; Q6NXK5; -.
DR ProteomicsDB; 279820; -.
DR Antibodypedia; 31366; 123 antibodies from 23 providers.
DR DNASU; 72102; -.
DR Ensembl; ENSMUST00000032071; ENSMUSP00000032071; ENSMUSG00000030002.
DR GeneID; 72102; -.
DR KEGG; mmu:72102; -.
DR UCSC; uc009cqp.1; mouse.
DR CTD; 8446; -.
DR MGI; MGI:1919352; Dusp11.
DR VEuPathDB; HostDB:ENSMUSG00000030002; -.
DR eggNOG; KOG2386; Eukaryota.
DR GeneTree; ENSGT00940000155847; -.
DR HOGENOM; CLU_057587_1_1_1; -.
DR InParanoid; Q6NXK5; -.
DR OMA; NRIPERW; -.
DR OrthoDB; 1544021at2759; -.
DR PhylomeDB; Q6NXK5; -.
DR TreeFam; TF105124; -.
DR BioGRID-ORCS; 72102; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Dusp11; mouse.
DR PRO; PR:Q6NXK5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6NXK5; protein.
DR Bgee; ENSMUSG00000030002; Expressed in retinal neural layer and 256 other tissues.
DR ExpressionAtlas; Q6NXK5; baseline and differential.
DR Genevisible; Q6NXK5; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; ISS:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0098507; P:polynucleotide 5' dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0016070; P:RNA metabolic process; ISS:UniProtKB.
DR Gene3D; 3.90.190.10; -; 1.
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 Pfam; PF00782; DSPc; 1.
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 2: Evidence at transcript level;
KW Hydrolase; Nucleus; Protein phosphatase; Reference proteome; RNA-binding.
FT CHAIN 1..321
FT /note="RNA/RNP complex-1-interacting phosphatase"
FT /id="PRO_0000094817"
FT DOMAIN 60..207
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 157
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 152..157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O75319"
FT CONFLICT 159
FT /note="G -> A (in Ref. 1; BAC40665)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="R -> T (in Ref. 1; BAC40665)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="I -> N (in Ref. 1; BAC40665)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="N -> D (in Ref. 1; BAC40665)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="K -> E (in Ref. 1; BAC40665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 37851 MW; 5C757545FBA235E1 CRC64;
MNQHYGRHGR GRGRDFAACA PPKKKGRNHI PERWKDYLPV GQRMPGTRFI AFKVPLQKKF
EAKLMPEECF SPLDLFNKIQ EQNEELGLII DLTYTQRYYK VEDLPETISY IKIFTVGHQI
PDNDTIFQFK CAVKEFLKKN KNNDKLIGVH CTHGLNRTGY LICRYLIDVE GMRPDDAIEL
FNSCRGHCIE RQNYIENLQK RHVRKNRNVS APRTDGLEDS ADPTEQVYTN NKPVKKKPRK
NRRGGHLAPS QHFQHQTQSS PYSLRKWSQN QSVYQRGLVP PPGPAGEDYS QRRFFWSARP
NKWTAESYQR PFYPYYWEWN L
