WBP11_MOUSE
ID WBP11_MOUSE Reviewed; 641 AA.
AC Q923D5; O88539; Q3UMD8; Q8VDI0;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=WW domain-binding protein 11;
DE Short=WBP-11;
DE AltName: Full=Splicing factor that interacts with PQBP-1 and PP1;
GN Name=Wbp11; Synonyms=Sipp1;
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; TISSUE=Aorta, Mammary gland, Testis, and Vein;
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=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 213-641.
RX PubMed=9724750; DOI=10.1073/pnas.95.18.10602;
RA Bedford M.T., Reed R., Leder P.;
RT "WW domain-mediated interactions reveal a spliceosome-associated protein
RT that binds a third class of proline-rich motif: the proline glycine and
RT methionine-rich motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10602-10607(1998).
RN [4]
RP FUNCTION, INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC, MUTAGENESIS OF
RP VAL-219; PHE-221; VAL-308 AND PHE-310, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14640981; DOI=10.1042/bj20030950;
RA Llorian M., Beullens M., Andres I., Ortiz J.M., Bollen M.;
RT "SIPP1, a novel pre-mRNA splicing factor and interactor of protein
RT phosphatase-1.";
RL Biochem. J. 378:229-238(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16162498; DOI=10.1074/jbc.m509185200;
RA Llorian M., Beullens M., Lesage B., Nicolaescu E., Beke L., Landuyt W.,
RA Ortiz J.M., Bollen M.;
RT "Nucleocytoplasmic shuttling of the splicing factor SIPP1.";
RL J. Biol. Chem. 280:38862-38869(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; TYR-236; SER-237;
RP SER-353; SER-361 AND SER-364, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13 AND LYS-565, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=33276377; DOI=10.1093/hmg/ddaa258;
RA Martin E.M.M.A., Enriquez A., Sparrow D.B., Humphreys D.T.,
RA McInerney-Leo A.M., Leo P.J., Duncan E.L., Iyer K.R., Greasby J.A., Ip E.,
RA Giannoulatou E., Sheng D., Wohler E., Dimartino C., Amiel J., Capri Y.,
RA Lehalle D., Mory A., Wilnai Y., Lebenthal Y., Gharavi A.G., Krzemien G.G.,
RA Miklaszewska M., Steiner R.D., Raggio C., Blank R., Baris Feldman H.,
RA Milo Rasouly H., Sobreira N.L.M., Jobling R., Gordon C.T., Giampietro P.F.,
RA Dunwoodie S.L., Chapman G.;
RT "Heterozygous loss of WBP11 function causes multiple congenital defects in
RT humans and mice.";
RL Hum. Mol. Genet. 29:3662-3678(2020).
CC -!- FUNCTION: Activates pre-mRNA splicing. May inhibit PP1 phosphatase
CC activity. {ECO:0000269|PubMed:14640981, ECO:0000269|PubMed:16162498}.
CC -!- SUBUNIT: Interacts via the PGR motif with PQBP1 in the nucleus.
CC Interacts with the WW domains of WBP4 (By similarity). Interacts with
CC PPP1CA, PPP1CB and PPP1CC. {ECO:0000250, ECO:0000269|PubMed:14640981}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly located in
CC the nucleus with granular heterogeneous distribution. Excluded from
CC nucleoli in interphase cells, distributed throughout cytoplasm in
CC dividing cells. Colocalized with SC35 and U2B in the nucleus. In the
CC cytoplasm, associates with the intermediate filament protein vimentin.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC testis. {ECO:0000269|PubMed:14640981}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos die prior to 8.5 dpc
CC (PubMed:33276377). Heterozygous null mice are small and exhibit defects
CC in axial skeleton, kidneys and esophagus (PubMed:33276377).
CC {ECO:0000269|PubMed:33276377}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34812.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK031678; BAC27508.1; -; mRNA.
DR EMBL; AK041079; BAC30812.1; -; mRNA.
DR EMBL; AK144968; BAE26160.1; -; mRNA.
DR EMBL; BC006600; AAH06600.1; -; mRNA.
DR EMBL; BC021823; AAH21823.1; -; mRNA.
DR EMBL; AF071186; AAC34812.1; ALT_SEQ; mRNA.
DR CCDS; CCDS20655.1; -.
DR RefSeq; NP_068360.4; NM_021714.4.
DR RefSeq; XP_017177182.1; XM_017321693.1.
DR AlphaFoldDB; Q923D5; -.
DR SMR; Q923D5; -.
DR BioGRID; 208550; 16.
DR ELM; Q923D5; -.
DR IntAct; Q923D5; 12.
DR MINT; Q923D5; -.
DR STRING; 10090.ENSMUSP00000112213; -.
DR iPTMnet; Q923D5; -.
DR PhosphoSitePlus; Q923D5; -.
DR EPD; Q923D5; -.
DR jPOST; Q923D5; -.
DR MaxQB; Q923D5; -.
DR PaxDb; Q923D5; -.
DR PRIDE; Q923D5; -.
DR ProteomicsDB; 297843; -.
DR DNASU; 60321; -.
DR Ensembl; ENSMUST00000116514; ENSMUSP00000112213; ENSMUSG00000030216.
DR GeneID; 60321; -.
DR KEGG; mmu:60321; -.
DR UCSC; uc009emf.2; mouse.
DR CTD; 51729; -.
DR MGI; MGI:1891823; Wbp11.
DR VEuPathDB; HostDB:ENSMUSG00000030216; -.
DR eggNOG; KOG4672; Eukaryota.
DR GeneTree; ENSGT01050000245409; -.
DR HOGENOM; CLU_028337_1_0_1; -.
DR InParanoid; Q923D5; -.
DR OMA; NKEPPGV; -.
DR OrthoDB; 1304995at2759; -.
DR PhylomeDB; Q923D5; -.
DR TreeFam; TF323226; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 60321; 28 hits in 74 CRISPR screens.
DR ChiTaRS; Wbp11; mouse.
DR PRO; PR:Q923D5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q923D5; protein.
DR Bgee; ENSMUSG00000030216; Expressed in embryonic post-anal tail and 259 other tissues.
DR ExpressionAtlas; Q923D5; baseline and differential.
DR Genevisible; Q923D5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:MGI.
DR GO; GO:0050699; F:WW domain binding; ISO:MGI.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IDA:MGI.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR019007; WW_dom-bd_prot_11.
DR PANTHER; PTHR13361; PTHR13361; 1.
DR Pfam; PF09429; Wbp11; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; rRNA processing; Ubl conjugation.
FT CHAIN 1..641
FT /note="WW domain-binding protein 11"
FT /id="PRO_0000065946"
FT REGION 1..45
FT /note="Required for nuclear import"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..221
FT /note="Interaction with PP1"
FT REGION 236..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..310
FT /note="Interaction with PP1"
FT REGION 588..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..641
FT /note="Required for nuclear export"
FT COILED 75..133
FT /evidence="ECO:0000255"
FT MOTIF 455..466
FT /note="PGR"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..364
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W2"
FT MOD_RES 236
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W2"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W2"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 565
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W2"
FT CROSSLNK 557
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W2"
FT CROSSLNK 572
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W2"
FT MUTAGEN 219
FT /note="V->A: Impairs interaction with PP1; when associated
FT with A-221."
FT /evidence="ECO:0000269|PubMed:14640981"
FT MUTAGEN 221
FT /note="F->A: Impairs interaction with PP1; when associated
FT with A-219."
FT /evidence="ECO:0000269|PubMed:14640981"
FT MUTAGEN 308
FT /note="V->A: Impairs interaction with PP1; when associated
FT with A-310."
FT /evidence="ECO:0000269|PubMed:14640981"
FT MUTAGEN 310
FT /note="F->A: Impairs interaction with PP1; when associated
FT with A-308."
FT /evidence="ECO:0000269|PubMed:14640981"
FT CONFLICT 378
FT /note="G -> A (in Ref. 2; AAH06600 and 3; AAC34812)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 69875 MW; 9C97281B4257B1F6 CRC64;
MGRRSTSSTK SGKFMNPTDQ ARKEARKREL KKNKKQRMMV RAAVLKMKDP KQIIRDMEKL
DEMEFNPVQQ PQLNEKVLKD KRKKLRETFE RILRLYEKEN PDIYKELRKL EVEYEQKRAQ
LSQYFDAVKN AQHVEVESIP LPDMPHAPSN ILIQDIPLPG AQPPSILKKT SAYGPPARAV
SILPLLGHGV PRLPPGRKPP GPPPGPPPPQ VLQMYGRKVG FALDLPPRRR DEDMLYSPEL
AQRGHDDDMS STSEDDGYPE DMDQDKHDDS TEDSDTDRSD AESDGDEFGH REDSERDNTE
EKKSGLSVRF ADMPGKSRKK KKNMKELTPL QAMMLRMAGQ EIPEEGREVE EFSEEEDADD
SDDSEAEKQS QKQHKDDGHS DSTAAASSQQ QAPPQSAPAS QIQAPPMPGP PPLGPPPAPP
LRPPGPPTGL PPGPPPGAPP FLRPPGMPGI RGPLPRLLPP GPPPGRPPGP PPGPPPGLPP
GPPPRGPPPR LPPPAPPGIP PPRPGMMRPP LVPPLGPAPP GLFPPAPLPN PGVLSAPPSL
IQRPKADDAS AATIEKKATA TISAKPQITN PKAEVTRFVP TALRVRRENK GATAVPQRRS
EDDSAVPVAK AAPRSGPSVA VSVQTKDDVY EAFMKEMEGL L
