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O75554

- WBP4_HUMAN

UniProt

O75554 - WBP4_HUMAN

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Protein

WW domain-binding protein 4

Gene
WBP4, FBP21, FNBP21
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri11 – 4232Matrin-typeAdd
BLAST

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro
  2. proline-rich region binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. mRNA cis splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiO75554.

Names & Taxonomyi

Protein namesi
Recommended name:
WW domain-binding protein 4
Short name:
WBP-4
Alternative name(s):
Formin-binding protein 21
WW domain-containing-binding protein 4
Gene namesi
Name:WBP4
Synonyms:FBP21, FNBP21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:12739. WBP4.

Subcellular locationi

Nucleus speckle 2 Publications

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB
  2. nucleus Source: HPA
  3. plasma membrane Source: HPA
  4. spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi150 – 1501W → A: Nearly abolishes activation of pre-mRNA splicing. Abolishes interaction with WBP11. 1 Publication
Mutagenesisi191 – 1911W → A: Nearly abolishes activation of pre-mRNA splicing. Abolishes interaction with WBP11. 1 Publication

Organism-specific databases

PharmGKBiPA37350.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376WW domain-binding protein 4PRO_0000076065Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei220 – 2201Phosphoserine2 Publications
Modified residuei262 – 2621Phosphoserine1 Publication
Modified residuei277 – 2771Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75554.
PaxDbiO75554.
PRIDEiO75554.

PTM databases

PhosphoSiteiO75554.

Expressioni

Gene expression databases

ArrayExpressiO75554.
BgeeiO75554.
CleanExiHS_WBP4.
GenevestigatoriO75554.

Organism-specific databases

HPAiHPA038965.

Interactioni

Subunit structurei

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 WBP11.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HTTP428583EBI-7251981,EBI-466029

Protein-protein interaction databases

BioGridi116363. 45 interactions.
IntActiO75554. 2 interactions.
MINTiMINT-127038.
STRINGi9606.ENSP00000368801.

Structurei

Secondary structure

1
376
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi128 – 1303
Turni134 – 1363
Beta strandi140 – 1456
Beta strandi148 – 1514
Beta strandi161 – 1644
Beta strandi168 – 1747
Turni175 – 1773
Beta strandi178 – 1836
Turni184 – 1874
Beta strandi188 – 1925

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK1NMR-A127-163[»]
2JXWNMR-A122-196[»]
ProteinModelPortaliO75554.
SMRiO75554. Positions 122-196.

Miscellaneous databases

EvolutionaryTraceiO75554.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini122 – 15534WW 1Add
BLAST
Domaini163 – 19634WW 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi111 – 12515Lys-richAdd
BLAST

Domaini

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 similaritiesi

Contains 2 WW domains.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5104.
HOGENOMiHOG000067962.
HOVERGENiHBG053152.
InParanoidiO75554.
KOiK13220.
OMAiESHEEVD.
OrthoDBiEOG7H7930.
PhylomeDBiO75554.
TreeFamiTF316671.

Family and domain databases

InterProiIPR001202. WW_dom.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
IPR013085. Znf_U1-C.
[Graphical view]
PfamiPF00397. WW. 2 hits.
PF06220. zf-U1. 1 hit.
[Graphical view]
SMARTiSM00456. WW. 2 hits.
SM00451. ZnF_U1. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 2 hits.
PROSITEiPS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
PS50171. ZF_MATRIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75554-1 [UniParc]FASTAAdd to Basket

« Hide

MADYWKSQPK KFCDYCKCWI ADNRPSVEFH ERGKNHKENV AKRISEIKQK    50
SLDKAKEEEK ASKEFAAMEA AALKAYQEDL KRLGLESEIL EPSITPVTST 100
IPPTSTSNQQ KEKKEKKKRK KDPSKGRWVE GITSEGYHYY YDLISGASQW 150
EKPEGFQGDL KKTAVKTVWV EGLSEDGFTY YYNTETGESR WEKPDDFIPH 200
TSDLPSSKVN ENSLGTLDES KSSDSHSDSD GEQEAEEGGV STETEKPKIK 250
FKEKNKNSDG GSDPETQKEK SIQKQNSLGS NEEKSKTLKK SNPYGEWQEI 300
KQEVESHEEV DLELPSTENE YVSTSEADGG GEPKVVFKEK TVTSLGVMAD 350
GVAPVFKKRR TENGKSRNLR QRGDDQ 376
Length:376
Mass (Da):42,507
Last modified:November 1, 1998 - v1
Checksum:i7A122A29D4325D11
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti113 – 1131K → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_036352

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF071185 mRNA. Translation: AAC34811.1.
AL157877 Genomic DNA. Translation: CAI13223.1.
BC104879 mRNA. Translation: AAI04880.1.
BC108310 mRNA. Translation: AAI08311.1.
CCDSiCCDS9375.1.
RefSeqiNP_009118.1. NM_007187.3.
UniGeneiHs.411300.

Genome annotation databases

EnsembliENST00000379487; ENSP00000368801; ENSG00000120688.
GeneIDi11193.
KEGGihsa:11193.
UCSCiuc001uxt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF071185 mRNA. Translation: AAC34811.1 .
AL157877 Genomic DNA. Translation: CAI13223.1 .
BC104879 mRNA. Translation: AAI04880.1 .
BC108310 mRNA. Translation: AAI08311.1 .
CCDSi CCDS9375.1.
RefSeqi NP_009118.1. NM_007187.3.
UniGenei Hs.411300.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DK1 NMR - A 127-163 [» ]
2JXW NMR - A 122-196 [» ]
ProteinModelPortali O75554.
SMRi O75554. Positions 122-196.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116363. 45 interactions.
IntActi O75554. 2 interactions.
MINTi MINT-127038.
STRINGi 9606.ENSP00000368801.

PTM databases

PhosphoSitei O75554.

Proteomic databases

MaxQBi O75554.
PaxDbi O75554.
PRIDEi O75554.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379487 ; ENSP00000368801 ; ENSG00000120688 .
GeneIDi 11193.
KEGGi hsa:11193.
UCSCi uc001uxt.3. human.

Organism-specific databases

CTDi 11193.
GeneCardsi GC13P041635.
HGNCi HGNC:12739. WBP4.
HPAi HPA038965.
MIMi 604981. gene.
neXtProti NX_O75554.
PharmGKBi PA37350.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5104.
HOGENOMi HOG000067962.
HOVERGENi HBG053152.
InParanoidi O75554.
KOi K13220.
OMAi ESHEEVD.
OrthoDBi EOG7H7930.
PhylomeDBi O75554.
TreeFami TF316671.

Enzyme and pathway databases

SignaLinki O75554.

Miscellaneous databases

EvolutionaryTracei O75554.
GeneWikii WBP4.
GenomeRNAii 11193.
NextBioi 42605.
PROi O75554.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75554.
Bgeei O75554.
CleanExi HS_WBP4.
Genevestigatori O75554.

Family and domain databases

InterProi IPR001202. WW_dom.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
IPR013085. Znf_U1-C.
[Graphical view ]
Pfami PF00397. WW. 2 hits.
PF06220. zf-U1. 1 hit.
[Graphical view ]
SMARTi SM00456. WW. 2 hits.
SM00451. ZnF_U1. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 2 hits.
PROSITEi PS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
PS50171. ZF_MATRIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-113.

Entry informationi

Entry nameiWBP4_HUMAN
AccessioniPrimary (citable) accession number: O75554
Secondary accession number(s): Q32P29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 115 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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