Q9Y2W2 (WBP11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 nuclear speck Inferred from electronic annotation. Source: Compara nucleus Traceable author statement Ref.1. Source: ProtInc
Molecular_function	protein phosphatase type 1 regulator activity Inferred from electronic annotation. Source: Compara single-stranded DNA binding Traceable author statement Ref.1. 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	45	Required for nuclear import By similarity
	Region	217 – 221	5	Interaction with PP1 By similarity
	Region	306 – 310	5	Interaction with PP1 By similarity
	Coiled coil	75 – 133	59	Potential
	Motif	455 – 466	12	PGR
	Compositional bias	140 – 209	70	Pro-rich
	Compositional bias	246 – 297	52	Asp-rich
	Compositional bias	319 – 322	4	Poly-Lys
	Compositional bias	393 – 538	146	Pro-rich
Amino acid modifications
	Modified residue	13	1	N6-acetyllysine Ref.9
	Modified residue	181	1	Phosphoserine Ref.8
	Modified residue	237	1	Phosphoserine Ref.6 Ref.10 Ref.12
	Modified residue	279	1	Phosphoserine Ref.5 Ref.12
	Modified residue	283	1	Phosphoserine Ref.5 Ref.12
	Modified residue	353	1	Phosphoserine Ref.8 Ref.12
	Modified residue	361	1	Phosphoserine Ref.8 Ref.12
	Modified residue	364	1	Phosphoserine Ref.8 Ref.12
Experimental info
	Mutagenesis	192	1	R → A: Loss of PQBP1-binding; when associated with A-197 and A-198. Ref.1
	Mutagenesis	197	1	R → A: Loss of PQBP1-binding; when associated with A-192 and A-198. Ref.1
	Mutagenesis	198	1	K → A: Loss of PQBP1-binding; when associated with A-192 and A-197. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2W2 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: C94F9687D132CE77	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

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] [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, 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, 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] [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, 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.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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. 16 interactions.
MINT	MINT-112641.
STRING	9606.ENSP00000261167.
PTM databases
PhosphoSite	Q9Y2W2.
Polymorphism databases
DMDM	74735242.
Proteomic databases
PaxDb	Q9Y2W2.
PeptideAtlas	Q9Y2W2.
PRIDE	Q9Y2W2.
Protocols and materials databases
DNASU	51729.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261167; ENSP00000261167; ENSG00000084463.
GeneID	51729.
KEGG	hsa:51729.
UCSC	uc001rci.3. human.
Organism-specific databases
CTD	51729.
GeneCards	GC12M014939.
HGNC	HGNC:16461. WBP11.
HPA	HPA040037.
neXtProt	NX_Q9Y2W2.
PharmGKB	PA38144.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG264066.
HOGENOM	HOG000154840.
HOVERGEN	HBG056793.
InParanoid	Q9Y2W2.
KO	K12866.
OMA	DMSSTSE.
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]
Pfam	PF09429. Wbp11. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	WBP11. human.
GenomeRNAi	51729.
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:	April 3, 2013
This is version 97 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.