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Q9Y2W2 (WBP11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:WBP11
Synonyms:NPWBP, SIPP1, SNP70
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activates pre-mRNA splicing. May inhibit PP1 phosphatase activity. Ref.1 Ref.2 Ref.4

Subunit structure

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. Ref.1 Ref.7

Subcellular location

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. Ref.1 Ref.4

Tissue specificity

Ubiquitous. Highly expressed in the heart, pancreas, kidney skeletal muscle, placenta and brain (at protein level). Weakly expressed in liver and lung. Ref.2

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB83EBI-714455,EBI-6927928From a different organism.
PCBP1Q153652EBI-714455,EBI-946095

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 641641WW domain-binding protein 11
PRO_0000065945

Regions

Region1 – 4545Required for nuclear import By similarity
Region217 – 2215Interaction with PP1 By similarity
Region306 – 3105Interaction with PP1 By similarity
Coiled coil75 – 13359 Potential
Motif455 – 46612PGR
Compositional bias140 – 20970Pro-rich
Compositional bias246 – 29752Asp-rich
Compositional bias319 – 3224Poly-Lys
Compositional bias393 – 538146Pro-rich

Amino acid modifications

Modified residue131N6-acetyllysine Ref.9
Modified residue1811Phosphoserine Ref.8
Modified residue2371Phosphoserine Ref.6 Ref.10 Ref.12
Modified residue2791Phosphoserine Ref.5 Ref.12
Modified residue2831Phosphoserine Ref.5 Ref.12
Modified residue3531Phosphoserine Ref.8 Ref.12
Modified residue3611Phosphoserine Ref.8 Ref.12
Modified residue3641Phosphoserine Ref.8 Ref.12
Modified residue5651N6-acetyllysine By similarity

Experimental info

Mutagenesis1921R → A: Loss of PQBP1-binding; when associated with A-197 and A-198. Ref.1
Mutagenesis1971R → A: Loss of PQBP1-binding; when associated with A-192 and A-198. Ref.1
Mutagenesis1981K → A: Loss of PQBP1-binding; when associated with A-192 and A-197. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Y2W2 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: C94F9687D132CE77

FASTA64169,998
        10         20         30         40         50         60 
MGRRSTSSTK SGKFMNPTDQ ARKEARKREL KKNKKQRMMV RAAVLKMKDP KQIIRDMEKL 

        70         80         90        100        110        120 
DEMEFNPVQQ PQLNEKVLKD KRKKLRETFE RILRLYEKEN PDIYKELRKL EVEYEQKRAQ 

       130        140        150        160        170        180 
LSQYFDAVKN AQHVEVESIP LPDMPHAPSN ILIQDIPLPG AQPPSILKKT SAYGPPTRAV 

       190        200        210        220        230        240 
SILPLLGHGV PRLPPGRKPP GPPPGPPPPQ VVQMYGRKVG FALDLPPRRR DEDMLYSPEL 

       250        260        270        280        290        300 
AQRGHDDDVS STSEDDGYPE DMDQDKHDDS TDDSDTDKSD GESDGDEFVH RDNGERDNNE 

       310        320        330        340        350        360 
EKKSGLSVRF ADMPGKSRKK KKNMKELTPL QAMMLRMAGQ EIPEEGREVE EFSEDDDEDD 

       370        380        390        400        410        420 
SDDSEAEKQS QKQHKEESHS DGTSTASSQQ QAPPQSVPPS QIQAPPMPGP PPLGPPPAPP 

       430        440        450        460        470        480 
LRPPGPPTGL PPGPPPGAPP FLRPPGMPGL RGPLPRLLPP GPPPGRPPGP PPGPPPGLPP 

       490        500        510        520        530        540 
GPPPRGPPPR LPPPAPPGIP PPRPGMMRPP LVPPLGPAPP GLFPPAPLPN PGVLSAPPNL 

       550        560        570        580        590        600 
IQRPKADDTS AATIEKKATA TISAKPQITN PKAEITRFVP TALRVRRENK GATAAPQRKS 

       610        620        630        640 
EDDSAVPLAK AAPKSGPSVP VSVQTKDDVY EAFMKEMEGL L 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"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.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8666.1.
RefSeqNP_057396.1. NM_016312.2.
UniGeneHs.655138.

3D structure databases

ProteinModelPortalQ9Y2W2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119702. 27 interactions.
IntActQ9Y2W2. 21 interactions.
MINTMINT-112641.
STRING9606.ENSP00000261167.

PTM databases

PhosphoSiteQ9Y2W2.

Polymorphism databases

DMDM74735242.

Proteomic databases

MaxQBQ9Y2W2.
PaxDbQ9Y2W2.
PeptideAtlasQ9Y2W2.
PRIDEQ9Y2W2.

Protocols and materials databases

DNASU51729.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261167; ENSP00000261167; ENSG00000084463.
GeneID51729.
KEGGhsa:51729.
UCSCuc001rci.3. human.

Organism-specific databases

CTD51729.
GeneCardsGC12M014939.
HGNCHGNC:16461. WBP11.
HPAHPA040037.
HPA046403.
HPA049126.
neXtProtNX_Q9Y2W2.
PharmGKBPA38144.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264066.
HOGENOMHOG000154840.
HOVERGENHBG056793.
InParanoidQ9Y2W2.
KOK12866.
OMARGHDDDM.
OrthoDBEOG7RNK1J.
PhylomeDBQ9Y2W2.
TreeFamTF323226.

Gene expression databases

ArrayExpressQ9Y2W2.
BgeeQ9Y2W2.
CleanExHS_WBP11.
GenevestigatorQ9Y2W2.

Family and domain databases

InterProIPR019007. WW_dom-bd_prot_11.
[Graphical view]
PfamPF09429. Wbp11. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWBP11. human.
GeneWikiWBP11.
GenomeRNAi51729.
NextBio55792.
PROQ9Y2W2.

Entry information

Entry nameWBP11_HUMAN
AccessionPrimary (citable) accession number: Q9Y2W2
Secondary accession number(s): Q96AY8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 12

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