DUS11_HUMAN
ID DUS11_HUMAN Reviewed; 377 AA.
AC O75319; B2RCT8; C9JYA6; Q6AI47; Q9BWE3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 03-AUG-2022, entry version 175.
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 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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-377 (ISOFORM 1), FUNCTION, INTERACTION WITH
RP SFRS7 AND SFRS9, MUTAGENESIS OF CYS-199, ACTIVE SITE, AND SUBCELLULAR
RP 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-377 (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-377 (ISOFORM 1).
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-199, 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 75-255 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-199 IN
RP COMPLEX WITH PHOSPHATE, MUTAGENESIS OF HIS-166; CYS-199; HIS-201; ASN-204
RP AND ARG-239, 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; Named isoforms=2;
CC Name=1;
CC IsoId=O75319-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75319-2; Sequence=VSP_014136, VSP_014137;
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-48 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39925.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH00346.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG37685.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR627368; CAH10467.1; -; mRNA.
DR EMBL; AC092653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF023917; AAC39925.1; ALT_INIT; mRNA.
DR EMBL; AK315271; BAG37685.1; ALT_INIT; mRNA.
DR EMBL; BC000346; AAH00346.1; ALT_INIT; mRNA.
DR RefSeq; NP_003575.2; NM_003584.2. [O75319-1]
DR PDB; 4JMJ; X-ray; 2.38 A; A=75-255.
DR PDB; 4MBB; X-ray; 1.85 A; A=76-254.
DR PDB; 4NYH; X-ray; 1.20 A; A/B/C=76-252.
DR PDBsum; 4JMJ; -.
DR PDBsum; 4MBB; -.
DR PDBsum; 4NYH; -.
DR AlphaFoldDB; O75319; -.
DR SMR; O75319; -.
DR BioGRID; 114024; 86.
DR IntAct; O75319; 19.
DR MINT; O75319; -.
DR STRING; 9606.ENSP00000272444; -.
DR DEPOD; DUSP11; -.
DR iPTMnet; O75319; -.
DR PhosphoSitePlus; O75319; -.
DR BioMuta; DUSP11; -.
DR EPD; O75319; -.
DR jPOST; O75319; -.
DR MassIVE; O75319; -.
DR MaxQB; O75319; -.
DR PaxDb; O75319; -.
DR PeptideAtlas; O75319; -.
DR PRIDE; O75319; -.
DR ProteomicsDB; 12230; -.
DR ProteomicsDB; 49891; -. [O75319-1]
DR ProteomicsDB; 49892; -. [O75319-2]
DR Antibodypedia; 31366; 123 antibodies from 23 providers.
DR DNASU; 8446; -.
DR Ensembl; ENST00000272444.7; ENSP00000272444.3; ENSG00000144048.10. [O75319-1]
DR Ensembl; ENST00000443070.5; ENSP00000413444.1; ENSG00000144048.10. [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. [O75319-1]
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; 1544021at2759; -.
DR PhylomeDB; O75319; -.
DR TreeFam; TF105124; -.
DR PathwayCommons; O75319; -.
DR SignaLink; O75319; -.
DR BioGRID-ORCS; 8446; 27 hits in 1085 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 204 other 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:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IMP:UniProtKB.
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:0098507; P:polynucleotide 5' dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0016070; P:RNA metabolic process; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Nucleus;
KW Protein phosphatase; Reference proteome; RNA-binding.
FT CHAIN 1..377
FT /note="RNA/RNP complex-1-interacting phosphatase"
FT /id="PRO_0000094816"
FT DOMAIN 108..255
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 53..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 199
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000269|PubMed:24447265, ECO:0000305|PubMed:9685386"
FT ACT_SITE 205
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 200..205
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:24531476"
FT VAR_SEQ 213..273
FT /note="YLIDVEGVRPDDAIELFNRCRGHCLERQNYIEDLQNGPIRKNWNSSVPRSSD
FT FEDSAHLMQ -> RSLALSPRLECSGTISTHSKFCFPGSRRSPASASQVAGTTGARHHA
FT RLIFCIFSRDVVSPC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_014136"
FT VAR_SEQ 274..377
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_014137"
FT MUTAGEN 166
FT /note="H->G: No effect on phosphatase activity with ATP and
FT ADP."
FT /evidence="ECO:0000269|PubMed:24447265"
FT MUTAGEN 199
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 201
FT /note="H->A: Strongly decreases phosphatase activity with
FT ATP and ADP."
FT /evidence="ECO:0000269|PubMed:24447265"
FT MUTAGEN 204
FT /note="N->A: Strongly decreases phosphatase activity with
FT ATP and ADP."
FT /evidence="ECO:0000269|PubMed:24447265"
FT MUTAGEN 239
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 7
FT /note="L -> W (in Ref. 3; AAC39925)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="D -> G (in Ref. 1; CAH10467, 3; AAC39925, 4;
FT BAG37685 and 5; AAH00346)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
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 O75319-2:215
FT /note="L -> R (in Ref. 1; CAH10467)"
FT /evidence="ECO:0000305"
FT CONFLICT O75319-2:237
FT /note="G -> S (in Ref. 1; CAH10467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 43710 MW; 61002BD1E2B06A5D CRC64;
MRNSETLERG VGGCRVFSCL GSYPGIEGAG LALLADLALG GRLLGTHMSQ WHHPRSGWGR
RRDFSGRSSA KKKGGNHIPE RWKDYLPVGQ RMPGTRFIAF KVPLQKSFEK KLAPEECFSP
LDLFNKIREQ NEELGLIIDL TYTQRYYKPE DLPETVPYLK IFTVGHQVPD DETIFKFKHA
VNGFLKENKD NDKLIGVHCT HGLNRTGYLI CRYLIDVEGV RPDDAIELFN RCRGHCLERQ
NYIEDLQNGP IRKNWNSSVP RSSDFEDSAH LMQPVHNKPV KQGPRYNLHQ IQGHSAPRHF
HTQTQSLQQS VRKFSENPHV YQRHHLPPPG PPGEDYSHRR YSWNVKPNAS RAAQDRRRWY
PYNYSRLSYP ACWEWTQ
