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O75554 (WBP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 4

Short name=WBP-4
Alternative name(s):
Formin-binding protein 21
WW domain-containing-binding protein 4
Gene names
Name:WBP4
Synonyms:FBP21, FNBP21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes pre-mRNA splicing. A spliceosome-associated protein; may play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex. Ref.1 Ref.7

Subunit structure

Associated with U2 snRNPs. Binds splicing factors SNRPB, SNRPC and SF1. Interacts via the WW domains with the Pro-rich domains of KHDRBS1/SAM68 By similarity. Interacts via the WW domains with the Pro-rich domains of WBP11. Ref.1 Ref.7

Subcellular location

Nucleus speckle Ref.1 Ref.7.

Domain

The WW domain recognizes the proline, glycine and methionine-rich (PGM) motif present in the splicing factors, as well as the Arg/Gly-rich-flanked Pro-rich domains found in several WW domain-binding proteins By similarity.

Sequence similarities

Contains 1 matrin-type zinc finger.

Contains 2 WW domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HTTP428583EBI-7251981,EBI-466029

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376WW domain-binding protein 4
PRO_0000076065

Regions

Domain122 – 15534WW 1
Domain163 – 19634WW 2
Zinc finger11 – 4232Matrin-type
Compositional bias111 – 12515Lys-rich

Amino acid modifications

Modified residue2201Phosphoserine Ref.4 Ref.5
Modified residue2621Phosphoserine Ref.5
Modified residue2771Phosphoserine Ref.5

Natural variations

Natural variant1131K → R in a breast cancer sample; somatic mutation. Ref.8
VAR_036352

Experimental info

Mutagenesis1501W → A: Nearly abolishes activation of pre-mRNA splicing. Abolishes interaction with WBP11. Ref.7
Mutagenesis1911W → A: Nearly abolishes activation of pre-mRNA splicing. Abolishes interaction with WBP11. Ref.7

Secondary structure

................. 376
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75554 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 7A122A29D4325D11

FASTA37642,507
        10         20         30         40         50         60 
MADYWKSQPK KFCDYCKCWI ADNRPSVEFH ERGKNHKENV AKRISEIKQK SLDKAKEEEK 

        70         80         90        100        110        120 
ASKEFAAMEA AALKAYQEDL KRLGLESEIL EPSITPVTST IPPTSTSNQQ KEKKEKKKRK 

       130        140        150        160        170        180 
KDPSKGRWVE GITSEGYHYY YDLISGASQW EKPEGFQGDL KKTAVKTVWV EGLSEDGFTY 

       190        200        210        220        230        240 
YYNTETGESR WEKPDDFIPH TSDLPSSKVN ENSLGTLDES KSSDSHSDSD GEQEAEEGGV 

       250        260        270        280        290        300 
STETEKPKIK FKEKNKNSDG GSDPETQKEK SIQKQNSLGS NEEKSKTLKK SNPYGEWQEI 

       310        320        330        340        350        360 
KQEVESHEEV DLELPSTENE YVSTSEADGG GEPKVVFKEK TVTSLGVMAD GVAPVFKKRR 

       370 
TENGKSRNLR QRGDDQ 

« Hide

References

« Hide 'large scale' references
[1]"WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif."
Bedford M.T., Reed R., Leder P.
Proc. Natl. Acad. Sci. U.S.A. 95:10602-10607(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNRPB; SNRPC; SF1 AND U2.
[2]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Brain and Testis.
[4]"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-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"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-220; SER-262 AND SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Solution structure of WW domain in WW domain binding protein 4 (WBP-4)."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 124-164.
[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: STRUCTURE BY NMR OF 122-196, FUNCTION, MUTAGENESIS OF TRP-150 AND TRP-191, SUBCELLULAR LOCATION, INTERACTION WITH WBP11.
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-113.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF071185 mRNA. Translation: AAC34811.1.
AL157877 Genomic DNA. Translation: CAI13223.1.
BC104879 mRNA. Translation: AAI04880.1.
BC108310 mRNA. Translation: AAI08311.1.
RefSeqNP_009118.1. NM_007187.3.
UniGeneHs.411300.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK1NMR-A127-163[»]
2JXWNMR-A122-196[»]
ProteinModelPortalO75554.
SMRO75554. Positions 9-48, 122-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116363. 45 interactions.
IntActO75554. 2 interactions.
MINTMINT-127038.
STRING9606.ENSP00000368801.

PTM databases

PhosphoSiteO75554.

Proteomic databases

PaxDbO75554.
PRIDEO75554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379487; ENSP00000368801; ENSG00000120688.
GeneID11193.
KEGGhsa:11193.
UCSCuc001uxt.3. human.

Organism-specific databases

CTD11193.
GeneCardsGC13P041635.
HGNCHGNC:12739. WBP4.
HPAHPA038965.
MIM604981. gene.
neXtProtNX_O75554.
PharmGKBPA37350.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5104.
HOGENOMHOG000067962.
HOVERGENHBG053152.
InParanoidO75554.
KOK13220.
OMAESHEEVD.
OrthoDBEOG7H7930.
PhylomeDBO75554.
TreeFamTF316671.

Enzyme and pathway databases

SignaLinkO75554.

Gene expression databases

ArrayExpressO75554.
BgeeO75554.
CleanExHS_WBP4.
GenevestigatorO75554.

Family and domain databases

InterProIPR001202. WW_dom.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
IPR013085. Znf_U1-C.
[Graphical view]
PfamPF00397. WW. 2 hits.
PF06220. zf-U1. 1 hit.
[Graphical view]
SMARTSM00456. WW. 2 hits.
SM00451. ZnF_U1. 1 hit.
[Graphical view]
SUPFAMSSF51045. SSF51045. 2 hits.
PROSITEPS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
PS50171. ZF_MATRIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75554.
GeneWikiWBP4.
GenomeRNAi11193.
NextBio42605.
PROO75554.
SOURCESearch...

Entry information

Entry nameWBP4_HUMAN
AccessionPrimary (citable) accession number: O75554
Secondary accession number(s): Q32P29
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 112 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM