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Q9Y2W2

- WBP11_HUMAN

UniProt

Q9Y2W2 - WBP11_HUMAN

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Protein

WW domain-binding protein 11

Gene

WBP11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Activates pre-mRNA splicing. May inhibit PP1 phosphatase activity.3 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein phosphatase type 1 regulator activity Source: Ensembl
  3. single-stranded DNA binding Source: ProtInc
  4. WW domain binding Source: UniProtKB

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. RNA splicing Source: UniProtKB-KW
  3. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, rRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
WW domain-binding protein 11
Short name:
WBP-11
Alternative name(s):
Npw38-binding protein
Short name:
NpwBP
SH3 domain-binding protein SNP70
Splicing factor that interacts with PQBP-1 and PP1
Gene namesi
Name:WBP11
Synonyms:NPWBP, SIPP1, SNP70
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:16461. WBP11.

Subcellular locationi

Nucleus. Cytoplasm
Note: Predominantly located in the nucleus with granular heterogeneous distribution. Excluded from nucleoli in interphase cells, distributed throughout cytoplasm in dividing cells. Colocalized with SC35 and U2B in the nucleus. In the cytoplasm, associates with the intermediate filament protein vimentin.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nuclear speck Source: Ensembl
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi192 – 1921R → A: Loss of PQBP1-binding; when associated with A-197 and A-198. 1 Publication
Mutagenesisi197 – 1971R → A: Loss of PQBP1-binding; when associated with A-192 and A-198. 1 Publication
Mutagenesisi198 – 1981K → A: Loss of PQBP1-binding; when associated with A-192 and A-197. 1 Publication

Organism-specific databases

PharmGKBiPA38144.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 641641WW domain-binding protein 11PRO_0000065945Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131N6-acetyllysine1 Publication
Modified residuei181 – 1811Phosphoserine1 Publication
Modified residuei237 – 2371Phosphoserine3 Publications
Modified residuei279 – 2791Phosphoserine2 Publications
Modified residuei283 – 2831Phosphoserine2 Publications
Modified residuei353 – 3531Phosphoserine2 Publications
Modified residuei361 – 3611Phosphoserine2 Publications
Modified residuei364 – 3641Phosphoserine2 Publications
Modified residuei565 – 5651N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y2W2.
PaxDbiQ9Y2W2.
PeptideAtlasiQ9Y2W2.
PRIDEiQ9Y2W2.

PTM databases

PhosphoSiteiQ9Y2W2.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in the heart, pancreas, kidney skeletal muscle, placenta and brain (at protein level). Weakly expressed in liver and lung.1 Publication

Gene expression databases

BgeeiQ9Y2W2.
CleanExiHS_WBP11.
ExpressionAtlasiQ9Y2W2. baseline and differential.
GenevestigatoriQ9Y2W2.

Organism-specific databases

HPAiHPA040037.
HPA046403.
HPA049126.

Interactioni

Subunit structurei

Interacts with PPP1CA, PPP1CB and PPP1CC (By similarity). Interacts via the PGR motif with PQBP1 in the nucleus. Interacts with the WW domains of WBP4.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB83EBI-714455,EBI-6927928From a different organism.
PCBP1Q153652EBI-714455,EBI-946095

Protein-protein interaction databases

BioGridi119702. 27 interactions.
IntActiQ9Y2W2. 21 interactions.
MINTiMINT-112641.
STRINGi9606.ENSP00000261167.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2W2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4545Required for nuclear importBy similarityAdd
BLAST
Regioni217 – 2215Interaction with PP1By similarity
Regioni306 – 3105Interaction with PP1By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili75 – 13359Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi455 – 46612PGRAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi140 – 20970Pro-richAdd
BLAST
Compositional biasi246 – 29752Asp-richAdd
BLAST
Compositional biasi319 – 3224Poly-Lys
Compositional biasi393 – 538146Pro-richAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG264066.
GeneTreeiENSGT00730000111015.
HOGENOMiHOG000154840.
HOVERGENiHBG056793.
InParanoidiQ9Y2W2.
KOiK12866.
OMAiRGHDDDM.
OrthoDBiEOG7RNK1J.
PhylomeDBiQ9Y2W2.
TreeFamiTF323226.

Family and domain databases

InterProiIPR019007. WW_dom-bd_prot_11.
[Graphical view]
PfamiPF09429. Wbp11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y2W2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRRSTSSTK SGKFMNPTDQ ARKEARKREL KKNKKQRMMV RAAVLKMKDP
60 70 80 90 100
KQIIRDMEKL DEMEFNPVQQ PQLNEKVLKD KRKKLRETFE RILRLYEKEN
110 120 130 140 150
PDIYKELRKL EVEYEQKRAQ LSQYFDAVKN AQHVEVESIP LPDMPHAPSN
160 170 180 190 200
ILIQDIPLPG AQPPSILKKT SAYGPPTRAV SILPLLGHGV PRLPPGRKPP
210 220 230 240 250
GPPPGPPPPQ VVQMYGRKVG FALDLPPRRR DEDMLYSPEL AQRGHDDDVS
260 270 280 290 300
STSEDDGYPE DMDQDKHDDS TDDSDTDKSD GESDGDEFVH RDNGERDNNE
310 320 330 340 350
EKKSGLSVRF ADMPGKSRKK KKNMKELTPL QAMMLRMAGQ EIPEEGREVE
360 370 380 390 400
EFSEDDDEDD SDDSEAEKQS QKQHKEESHS DGTSTASSQQ QAPPQSVPPS
410 420 430 440 450
QIQAPPMPGP PPLGPPPAPP LRPPGPPTGL PPGPPPGAPP FLRPPGMPGL
460 470 480 490 500
RGPLPRLLPP GPPPGRPPGP PPGPPPGLPP GPPPRGPPPR LPPPAPPGIP
510 520 530 540 550
PPRPGMMRPP LVPPLGPAPP GLFPPAPLPN PGVLSAPPNL IQRPKADDTS
560 570 580 590 600
AATIEKKATA TISAKPQITN PKAEITRFVP TALRVRRENK GATAAPQRKS
610 620 630 640
EDDSAVPLAK AAPKSGPSVP VSVQTKDDVY EAFMKEMEGL L
Length:641
Mass (Da):69,998
Last modified:November 1, 1999 - v1
Checksum:iC94F9687D132CE77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029309 mRNA. Translation: BAA88410.1.
AF118023 mRNA. Translation: AAD30425.1.
BC001621 mRNA. Translation: AAH01621.1.
BC016441 mRNA. Translation: AAH16441.2.
BC023532 mRNA. Translation: AAH23532.1.
CCDSiCCDS8666.1.
RefSeqiNP_057396.1. NM_016312.2.
UniGeneiHs.655138.

Genome annotation databases

EnsembliENST00000261167; ENSP00000261167; ENSG00000084463.
GeneIDi51729.
KEGGihsa:51729.
UCSCiuc001rci.3. human.

Polymorphism databases

DMDMi74735242.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029309 mRNA. Translation: BAA88410.1 .
AF118023 mRNA. Translation: AAD30425.1 .
BC001621 mRNA. Translation: AAH01621.1 .
BC016441 mRNA. Translation: AAH16441.2 .
BC023532 mRNA. Translation: AAH23532.1 .
CCDSi CCDS8666.1.
RefSeqi NP_057396.1. NM_016312.2.
UniGenei Hs.655138.

3D structure databases

ProteinModelPortali Q9Y2W2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119702. 27 interactions.
IntActi Q9Y2W2. 21 interactions.
MINTi MINT-112641.
STRINGi 9606.ENSP00000261167.

PTM databases

PhosphoSitei Q9Y2W2.

Polymorphism databases

DMDMi 74735242.

Proteomic databases

MaxQBi Q9Y2W2.
PaxDbi Q9Y2W2.
PeptideAtlasi Q9Y2W2.
PRIDEi Q9Y2W2.

Protocols and materials databases

DNASUi 51729.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261167 ; ENSP00000261167 ; ENSG00000084463 .
GeneIDi 51729.
KEGGi hsa:51729.
UCSCi uc001rci.3. human.

Organism-specific databases

CTDi 51729.
GeneCardsi GC12M014939.
HGNCi HGNC:16461. WBP11.
HPAi HPA040037.
HPA046403.
HPA049126.
neXtProti NX_Q9Y2W2.
PharmGKBi PA38144.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG264066.
GeneTreei ENSGT00730000111015.
HOGENOMi HOG000154840.
HOVERGENi HBG056793.
InParanoidi Q9Y2W2.
KOi K12866.
OMAi RGHDDDM.
OrthoDBi EOG7RNK1J.
PhylomeDBi Q9Y2W2.
TreeFami TF323226.

Miscellaneous databases

ChiTaRSi WBP11. human.
GeneWikii WBP11.
GenomeRNAii 51729.
NextBioi 55792.
PROi Q9Y2W2.

Gene expression databases

Bgeei Q9Y2W2.
CleanExi HS_WBP11.
ExpressionAtlasi Q9Y2W2. baseline and differential.
Genevestigatori Q9Y2W2.

Family and domain databases

InterProi IPR019007. WW_dom-bd_prot_11.
[Graphical view ]
Pfami PF09429. Wbp11. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Association of two nuclear proteins, Npw38 and NpwBP, via the interaction between the WW domain and a novel proline-rich motif containing glycine and arginine."
    Komuro A., Saeki M., Kato S.
    J. Biol. Chem. 274:36513-36519(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-25, FUNCTION, INTERACTION WITH PQBP1, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-192; ARG-197 AND LYS-198.
  2. "A nuclear SH3 domain-binding protein that colocalizes with mRNA splicing factors and intermediate filament-containing perinuclear networks."
    Craggs G., Finan P.M., Lawson D., Wingfield J., Perera T., Gadher S., Totty N.F., Kellie S.
    J. Biol. Chem. 276:30552-30560(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye, Muscle and Placenta.
  4. "SIPP1, a novel pre-mRNA splicing factor and interactor of protein phosphatase-1."
    Llorian M., Beullens M., Andres I., Ortiz J.M., Bollen M.
    Biochem. J. 378:229-238(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Structure and function of the two tandem WW domains of the pre-mRNA splicing factor FBP21 (formin-binding protein 21)."
    Huang X., Beullens M., Zhang J., Zhou Y., Nicolaescu E., Lesage B., Hu Q., Wu J., Bollen M., Shi Y.
    J. Biol. Chem. 284:25375-25387(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WBP4.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-353; SER-361 AND SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1 affects its binding activity and deregulates pre-mRNA splicing."
    Tapia V.E., Nicolaescu E., McDonald C.B., Musi V., Oka T., Inayoshi Y., Satteson A.C., Mazack V., Humbert J., Gaffney C.J., Beullens M., Schwartz C.E., Landgraf C., Volkmer R., Pastore A., Farooq A., Bollen M., Sudol M.
    J. Biol. Chem. 285:19391-19401(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PQBP1.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-279; SER-283; SER-353; SER-361 AND SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiWBP11_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2W2
Secondary accession number(s): Q96AY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM

External Data

Dasty 3