WW domain-binding protein 11 - Homo sapiens (Human)

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Q9Y2W2 (WBP11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	WBP11
Synonyms:	NPWBP, SIPP1, SNP70

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	641 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Co-localized 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

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing rRNA processing
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW rRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	WW domain binding Inferred from physical interaction Ref.7. Source: UniProtKB single-stranded DNA binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PCBP1	Q15365	2	EBI-714455,EBI-946095

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 641

641

WW domain-binding protein 11

PRO_0000065945

Regions

Region

1 – 45

Required for nuclear import By similarity

Region

217 – 221

Interaction with PP1 By similarity

Region

306 – 310

Interaction with PP1 By similarity

Coiled coil

75 – 133

Potential

Motif

455 – 466

PGR

Compositional bias

140 – 209

Pro-rich

Compositional bias

246 – 297

Asp-rich

Compositional bias

319 – 322

Poly-Lys

Compositional bias

393 – 538

146

Pro-rich

Amino acid modifications

Modified residue

N6-acetyllysine Ref.9

Modified residue

237

Phosphoserine Ref.5 Ref.6

Modified residue

251

Phosphoserine Ref.5

Modified residue

252

Phosphothreonine Ref.5

Modified residue

253

Phosphoserine Ref.5

Modified residue

270

Phosphoserine Ref.5

Modified residue

271

Phosphothreonine Ref.5

Modified residue

274

Phosphoserine Ref.5

Modified residue

276

Phosphothreonine Ref.5

Modified residue

279

Phosphoserine Ref.5

Modified residue

283

Phosphoserine Ref.5

Modified residue

328

Phosphothreonine Ref.6

Modified residue

353

Phosphoserine Ref.5 Ref.6 Ref.8

Modified residue

361

Phosphoserine Ref.5 Ref.6 Ref.8

Modified residue

364

Phosphoserine Ref.5 Ref.6 Ref.8

Experimental info

Mutagenesis

192

R → A: Loss of PQBP1-binding; when associated with A-197 and A-198. Ref.1

Mutagenesis

197

R → A: Loss of PQBP1-binding; when associated with A-192 and A-198. Ref.1

Mutagenesis

198

K → A: Loss of PQBP1-binding; when associated with A-192 and A-197. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Y2W2 [UniParc].

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

FASTA

641

69,998

        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' referencesShow '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: 10593949] [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: 11375989] [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: 15489334] [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: 14640981] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-251; THR-252; SER-253; SER-270; THR-271; SER-274; THR-276; SER-279; SER-283; SER-353; SER-361 AND SER-364, MASS SPECTROMETRY. 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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; THR-328; SER-353; SER-361 AND SER-364, MASS SPECTROMETRY. 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: 19592703] [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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353; SER-361 AND SER-364, MASS SPECTROMETRY. 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13, MASS SPECTROMETRY.
[10]	"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: 21269460] [Abstract] Cited for: 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.
IPI	IPI00170786.
RefSeq	NP_057396.1. NM_016312.2.
UniGene	Hs.655138.
3D structure databases
ProteinModelPortal	Q9Y2W2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y2W2. 15 interactions.
MINT	MINT-112641.
STRING	Q9Y2W2.
PTM databases
PhosphoSite	Q9Y2W2.
Polymorphism databases
DMDM	74735242.
Proteomic databases
PeptideAtlas	Q9Y2W2.
PRIDE	Q9Y2W2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261167; ENSP00000261167; ENSG00000084463.
GeneID	51729.
KEGG	hsa:51729.
UCSC	uc001rci.1. human.
Organism-specific databases
CTD	51729.
GeneCards	GC12M014939.
H-InvDB	HIX0010456.
HGNC	HGNC:16461. WBP11.
HPA	HPA040037.
neXtProt	NX_Q9Y2W2.
PharmGKB	PA38144.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15954.
GeneTree	ENSGT00600000084083.
HOGENOM	HBG278702.
HOVERGEN	HBG056793.
InParanoid	Q9Y2W2.
OMA	GERDNNE.
OrthoDB	EOG480HXK.
PhylomeDB	Q9Y2W2.
Gene expression databases
ArrayExpress	Q9Y2W2.
Bgee	Q9Y2W2.
CleanEx	HS_WBP11.
Genevestigator	Q9Y2W2.
GermOnline	ENSG00000084463. Homo sapiens.
Family and domain databases
InterPro	IPR019007. WW_dom-bd_prot_11. [Graphical view]
KO	K12866.
Pfam	PF09429. Wbp11. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	55792.

Entry information

Entry name

WBP11_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents