WBP11_RAT
ID WBP11_RAT Reviewed; 641 AA.
AC Q5PQQ2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-353; SER-361 AND
RP SER-364, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Activates pre-mRNA splicing. May inhibit PP1 phosphatase
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and PPP1CC. Interacts via the
CC PGR motif with PQBP1 in the nucleus. Interacts with the WW domains of
CC WBP4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Predominantly located in the nucleus with granular heterogeneous
CC distribution. Excluded from nucleoli in interphase cells, distributed
CC throughout cytoplasm in dividing cells. Colocalized with SC35 and U2B
CC in the nucleus. In the cytoplasm, associates with the intermediate
CC filament protein vimentin (By similarity). {ECO:0000250}.
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DR EMBL; BC087082; AAH87082.1; -; mRNA.
DR RefSeq; NP_001009661.1; NM_001009661.2.
DR RefSeq; NP_001289946.1; NM_001303017.1.
DR RefSeq; XP_008761671.1; XM_008763449.2.
DR RefSeq; XP_008761672.1; XM_008763450.2.
DR AlphaFoldDB; Q5PQQ2; -.
DR SMR; Q5PQQ2; -.
DR STRING; 10116.ENSRNOP00000007402; -.
DR iPTMnet; Q5PQQ2; -.
DR PhosphoSitePlus; Q5PQQ2; -.
DR jPOST; Q5PQQ2; -.
DR PaxDb; Q5PQQ2; -.
DR PRIDE; Q5PQQ2; -.
DR Ensembl; ENSRNOT00000007402; ENSRNOP00000007402; ENSRNOG00000005505.
DR GeneID; 297695; -.
DR KEGG; rno:297695; -.
DR UCSC; RGD:1307911; rat.
DR CTD; 51729; -.
DR RGD; 1307911; Wbp11.
DR eggNOG; KOG4672; Eukaryota.
DR GeneTree; ENSGT01050000245768; -.
DR HOGENOM; CLU_028337_1_0_1; -.
DR InParanoid; Q5PQQ2; -.
DR OMA; NKEPPGV; -.
DR OrthoDB; 1304995at2759; -.
DR PhylomeDB; Q5PQQ2; -.
DR TreeFam; TF323226; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q5PQQ2; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000005505; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q5PQQ2; baseline and differential.
DR Genevisible; Q5PQQ2; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISO:RGD.
DR GO; GO:0050699; F:WW domain binding; ISO:RGD.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; ISO:RGD.
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_0000065947"
FT REGION 1..45
FT /note="Required for nuclear import"
FT /evidence="ECO:0000250"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..221
FT /note="Interaction with PP1"
FT /evidence="ECO:0000250"
FT REGION 236..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..310
FT /note="Interaction with PP1"
FT /evidence="ECO:0000250"
FT REGION 588..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W2"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W2"
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:0000250|UniProtKB:Q923D5"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 565
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q923D5"
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"
SQ SEQUENCE 641 AA; 69996 MW; 3DD194767F149CD6 CRC64;
MGRRSTSSTK SGKFMNPTDQ ARKEARKREL KKNKKQRMMV RAAVLKMKDP KQIIRDMEKL
DEMEFNPVQQ PQLNEKVLKD KRKKLRETFE RILRLYEKEN PDIYKELRKL EVEYEQKRAQ
LSQYFDAVKN AQHVEVESIP LPDMPHAPSN ILIQDIPLPG AQPPSILKKT SAYGPPTRAV
SILPLLGHGV PRLPPGRKPP GPPPGPPPPQ VLQMYGRKVG FALDLPPRRR DEDMLYSPEL
AQRGHDDDMS STSEDDGYPE DMDQDKHDDS TEDSDTDRSD AESDGDEFGH RDDSERDNTE
EKKSGLSVRF ADMPGKSRKK KKNMKELTPL QAMMLRMAGQ EIPEEGREVE EFSEEEDDDD
SEDSEAEKPS QKQHKEDSHA DGSSAASSQQ QAPPQAVPPS QIQAPPMPGP PPLGPPPAPP
LRPPGPPTGL PPGPPPGAPP FLRPPGMPGI RGPLPRLLPP GPPPGRPPGP PPGPPPGLPP
GPPPRGPPPR LPPPAPPGIP PPRPGMMRPP LVPPLGPAPP GLFPPAPLPN PGVLSAPPSL
IQRPKADDAS AATIEKKATA TISAKPQITN PKAEVTRFVP TALRVRRENK GATAVPQRRS
EEDSAVPVAK AAPRSGPSVP VSVQTKDDVY EAFMKEMEGL L
