ID DUS11_HUMAN Reviewed; 330 AA.
AC O75319; B2RCT8; C9JYA6; Q6AI47; Q9BWE3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2024, sequence version 3.
DT 27-MAR-2024, entry version 184.
DE RecName: Full=RNA/RNP complex-1-interacting phosphatase {ECO:0000305};
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 {ECO:0000312|HGNC:HGNC:3066}; Synonyms=PIR1;
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] (ISOFORM 3), FUNCTION, INTERACTION WITH SFRS7
RP AND SFRS9, MUTAGENESIS OF CYS-152, ACTIVE SITE, AND SUBCELLULAR LOCATION.
RX PubMed=9685386; DOI=10.1074/jbc.273.32.20347;
RA Yuan Y., Li D.-M., Sun H.;
RT "PIR1, a novel phosphatase that exhibits high affinity to RNA
RT ribonucleoprotein complexes.";
RL J. Biol. Chem. 273:20347-20353(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Muscle;
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 [6]
RP CHARACTERIZATION, MUTAGENESIS OF CYS-152, AND FUNCTION.
RX PubMed=10347225; DOI=10.1074/jbc.274.23.16590;
RA Deshpande T., Takagi T., Hao L., Buratowski S., Charbonneau H.;
RT "Human PIR1 of the protein-tyrosine phosphatase superfamily has RNA 5'-
RT triphosphatase and diphosphatase activities.";
RL J. Biol. Chem. 274:16590-16594(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 28-208 IN COMPLEX WITH THE
RP SUBSTRATE ANALOG PHOSPHATE, AND SUBUNIT.
RX PubMed=24531476; DOI=10.1107/s1399004713029866;
RA Jeong D.G., Wei C.H., Ku B., Jeon T.J., Chien P.N., Kim J.K., Park S.Y.,
RA Hwang H.S., Ryu S.Y., Park H., Kim D.S., Kim S.J., Ryu S.E.;
RT "The family-wide structure and function of human dual-specificity protein
RT phosphatases.";
RL Acta Crystallogr. D 70:421-435(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 76-254 OF MUTANT SER-152 IN
RP COMPLEX WITH PHOSPHATE, MUTAGENESIS OF HIS-119; CYS-152; HIS-154; ASN-157
RP AND ARG-192, ACTIVE SITE, AND FUNCTION.
RX PubMed=24447265; DOI=10.1021/bi401240x;
RA Sankhala R.S., Lokareddy R.K., Cingolani G.;
RT "Structure of human PIR1, an atypical dual-specificity phosphatase.";
RL Biochemistry 53:862-871(2014).
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:0000269|PubMed:10347225, ECO:0000269|PubMed:24447265,
CC ECO:0000269|PubMed:9685386}.
CC -!- SUBUNIT: Monomer (PubMed:24531476). May interact with SFRS7 and
CC SFRS9/SRP30C (PubMed:24447265). {ECO:0000269|PubMed:24447265,
CC ECO:0000269|PubMed:24531476}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9685386}. Nucleus
CC speckle {ECO:0000269|PubMed:9685386}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=3;
CC IsoId=O75319-3; Sequence=Displayed;
CC Name=1;
CC IsoId=O75319-1; Sequence=VSP_062169;
CC Name=2;
CC IsoId=O75319-2; Sequence=VSP_062170, VSP_062171;
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative initiation
CC (Probable). Based on proteomic data (Probable). {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Major isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH10467.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF023917; AAC39925.1; -; mRNA.
DR EMBL; AK315271; BAG37685.1; -; mRNA.
DR EMBL; CR627368; CAH10467.1; ALT_INIT; mRNA.
DR EMBL; AC092653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000346; AAH00346.1; -; mRNA.
DR RefSeq; NP_003575.2; NM_003584.2. [O75319-3]
DR PDB; 4JMJ; X-ray; 2.38 A; A=28-208.
DR PDB; 4MBB; X-ray; 1.85 A; A=29-207.
DR PDB; 4NYH; X-ray; 1.20 A; A/B/C=29-205.
DR PDBsum; 4JMJ; -.
DR PDBsum; 4MBB; -.
DR PDBsum; 4NYH; -.
DR AlphaFoldDB; O75319; -.
DR SMR; O75319; -.
DR BioGRID; 114024; 89.
DR IntAct; O75319; 19.
DR MINT; O75319; -.
DR STRING; 9606.ENSP00000272444; -.
DR DEPOD; DUSP11; -.
DR GlyGen; O75319; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75319; -.
DR PhosphoSitePlus; O75319; -.
DR BioMuta; DUSP11; -.
DR EPD; O75319; -.
DR jPOST; O75319; -.
DR MassIVE; O75319; -.
DR MaxQB; O75319; -.
DR PaxDb; 9606-ENSP00000272444; -.
DR PeptideAtlas; O75319; -.
DR ProteomicsDB; 12230; -.
DR ProteomicsDB; 49891; -. [O75319-1]
DR ProteomicsDB; 49892; -. [O75319-2]
DR Pumba; O75319; -.
DR Antibodypedia; 31366; 141 antibodies from 24 providers.
DR DNASU; 8446; -.
DR Ensembl; ENST00000272444.8; ENSP00000272444.4; ENSG00000144048.11. [O75319-3]
DR Ensembl; ENST00000443070.5; ENSP00000413444.2; ENSG00000144048.11. [O75319-2]
DR Ensembl; ENST00000707649.1; ENSP00000516943.1; ENSG00000291483.1. [O75319-3]
DR Ensembl; ENST00000707657.1; ENSP00000516949.1; ENSG00000291483.1. [O75319-2]
DR GeneID; 8446; -.
DR KEGG; hsa:8446; -.
DR MANE-Select; ENST00000272444.8; ENSP00000272444.4; NM_003584.3; NP_003575.3.
DR UCSC; uc002sjp.4; human. [O75319-3]
DR AGR; HGNC:3066; -.
DR CTD; 8446; -.
DR DisGeNET; 8446; -.
DR GeneCards; DUSP11; -.
DR HGNC; HGNC:3066; DUSP11.
DR HPA; ENSG00000144048; Low tissue specificity.
DR MIM; 603092; gene.
DR neXtProt; NX_O75319; -.
DR OpenTargets; ENSG00000144048; -.
DR PharmGKB; PA27521; -.
DR VEuPathDB; HostDB:ENSG00000144048; -.
DR eggNOG; KOG2386; Eukaryota.
DR GeneTree; ENSGT00940000155847; -.
DR HOGENOM; CLU_057587_1_1_1; -.
DR InParanoid; O75319; -.
DR OMA; NRIPERW; -.
DR OrthoDB; 49440at2759; -.
DR PhylomeDB; O75319; -.
DR TreeFam; TF105124; -.
DR PathwayCommons; O75319; -.
DR SignaLink; O75319; -.
DR BioGRID-ORCS; 8446; 28 hits in 1176 CRISPR screens.
DR ChiTaRS; DUSP11; human.
DR GenomeRNAi; 8446; -.
DR Pharos; O75319; Tbio.
DR PRO; PR:O75319; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O75319; Protein.
DR Bgee; ENSG00000144048; Expressed in esophagus squamous epithelium and 206 other cell types or tissues.
DR ExpressionAtlas; O75319; baseline and differential.
DR Genevisible; O75319; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR CDD; cd17665; DSP_DUSP11; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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 PANTHER; PTHR10367; MRNA-CAPPING ENZYME; 1.
DR PANTHER; PTHR10367:SF18; RNA_RNP COMPLEX-1-INTERACTING PHOSPHATASE; 1.
DR Pfam; PF00782; DSPc; 1.
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; Alternative initiation; Alternative splicing; Hydrolase;
KW Nucleus; Protein phosphatase; Reference proteome; RNA-binding.
FT CHAIN 1..330
FT /note="RNA/RNP complex-1-interacting phosphatase"
FT /id="PRO_0000094816"
FT DOMAIN 61..208
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000269|PubMed:24447265, ECO:0000305|PubMed:9685386"
FT ACT_SITE 158
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 153..158
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:24531476"
FT VAR_SEQ 1
FT /note="M -> MRNSETLERGVGGCRVFSCLGSYPGIEGAGLALLADLALGGRLLGTH
FT M (in isoform 1)"
FT /id="VSP_062169"
FT VAR_SEQ 166..226
FT /note="YLIDVEGVRPDDAIELFNRCRGHCLERQNYIEDLQNGPIRKNWNSSVPRSSD
FT FEDSAHLMQ -> RSLALSPRLECSGTISTHSKFCFPGSRRSPASASQVAGTTGARHHA
FT RLIFCIFSRDVVSPC (in isoform 2)"
FT /id="VSP_062170"
FT VAR_SEQ 227..330
FT /note="Missing (in isoform 2)"
FT /id="VSP_062171"
FT MUTAGEN 119
FT /note="H->G: No effect on phosphatase activity with ATP and
FT ADP."
FT /evidence="ECO:0000269|PubMed:24447265"
FT MUTAGEN 152
FT /note="C->S: Loss of activity. No effect in RNA-binding."
FT /evidence="ECO:0000269|PubMed:10347225,
FT ECO:0000269|PubMed:24447265, ECO:0000269|PubMed:9685386"
FT MUTAGEN 154
FT /note="H->A: Strongly decreases phosphatase activity with
FT ATP and ADP."
FT /evidence="ECO:0000269|PubMed:24447265"
FT MUTAGEN 157
FT /note="N->A: Strongly decreases phosphatase activity with
FT ATP and ADP."
FT /evidence="ECO:0000269|PubMed:24447265"
FT MUTAGEN 192
FT /note="R->K: Slightly decreases phosphatase activity with
FT ATP. Strongly decreases phosphatase activity with ADP."
FT /evidence="ECO:0000269|PubMed:24447265"
FT CONFLICT 165
FT /note="R -> I (in Ref. 5; AAH00346)"
FT /evidence="ECO:0000305"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4NYH"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:4NYH"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:4NYH"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4NYH"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:4NYH"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4NYH"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:4NYH"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4NYH"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4NYH"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:4NYH"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4NYH"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4NYH"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:4NYH"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:4NYH"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:4NYH"
FT CONFLICT O75319-2:168
FT /note="L -> R (in Ref. 3; CAH10467)"
FT /evidence="ECO:0000305"
FT CONFLICT O75319-2:190
FT /note="G -> S (in Ref. 3; CAH10467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 38939 MW; 0C397F43043B450A CRC64;
MSQWHHPRSG WGRRRDFSGR SSAKKKGGNH IPERWKDYLP VGQRMPGTRF IAFKVPLQKS
FEKKLAPEEC FSPLDLFNKI REQNEELGLI IDLTYTQRYY KPEDLPETVP YLKIFTVGHQ
VPDDETIFKF KHAVNGFLKE NKDNDKLIGV HCTHGLNRTG YLICRYLIDV EGVRPDDAIE
LFNRCRGHCL ERQNYIEDLQ NGPIRKNWNS SVPRSSDFED SAHLMQPVHN KPVKQGPRYN
LHQIQGHSAP RHFHTQTQSL QQSVRKFSEN PHVYQRHHLP PPGPPGEDYS HRRYSWNVKP
NASRAAQDRR RWYPYNYSRL SYPACWEWTQ
//
