O75554 (WBP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	WBP4
Synonyms:	FBP21, FNBP21

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	376 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA cis splicing, via spliceosome Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	nuclear speck Inferred from direct assay Ref.7. Source: UniProtKB plasma membrane Inferred from direct assay. Source: HPA spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	nucleic acid binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 376

376

WW domain-binding protein 4

PRO_0000076065

Regions

Domain

122 – 155

34

WW 1

Domain

163 – 196

34

WW 2

Zinc finger

11 – 42

32

Matrin-type

Compositional bias

111 – 125

15

Lys-rich

Amino acid modifications

Modified residue

220

1

Phosphoserine Ref.4 Ref.5

Modified residue

262

1

Phosphoserine Ref.5

Modified residue

277

1

Phosphoserine Ref.5

Natural variations

Natural variant

113

1

K → R in a breast cancer sample; somatic mutation. Ref.8

VAR_036352

Experimental info

Mutagenesis

150

1

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

Mutagenesis

191

1

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

Secondary structure

1

.

.

.

.

.

.

.

.

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.

.

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.

.

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.

.

376

Helix Strand Turn

Details...

Beta strand

128 – 130

3

Turn

134 – 136

3

Beta strand

140 – 145

6

Beta strand

148 – 151

4

Beta strand

161 – 164

4

Beta strand

168 – 174

7

Turn

175 – 177

3

Beta strand

178 – 183

6

Turn

184 – 187

4

Beta strand

188 – 192

5

Sequences

	Sequence		Length	Mass (Da)
	O75554 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 7A122A29D4325D11	FASTA	376	42,507
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. , 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.

IPI

IPI00026957.

RefSeq

NP_009118.1. NM_007187.3.

UniGene

Hs.411300.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DK1	NMR	-	A	127-163	[»]
2JXW	NMR	-	A	122-196	[»]

ProteinModelPortal

O75554.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-127038.

STRING

9606.ENSP00000368801.

PTM databases

PhosphoSite

O75554.

Proteomic databases

PaxDb

O75554.

PRIDE

O75554.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379487; ENSP00000368801; ENSG00000120688.

GeneID

11193.

KEGG

hsa:11193.

UCSC

uc001uxt.3. human.

Organism-specific databases

CTD

11193.

GeneCards

GC13P041635.

HGNC

HGNC:12739. WBP4.

HPA

HPA038965.

MIM

604981. gene.

neXtProt

NX_O75554.

PharmGKB

PA37350.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5104.

HOGENOM

HOG000067962.

HOVERGEN

HBG053152.

InParanoid

O75554.

KO

K13220.

OMA

HEEVDLE.

OrthoDB

EOG4R7VBT.

PhylomeDB

O75554.

Gene expression databases

ArrayExpress

O75554.

Bgee

O75554.

CleanEx

HS_WBP4.

Genevestigator

O75554.

GermOnline

ENSG00000120688. Homo sapiens.

Family and domain databases

InterPro

IPR001202. WW_dom.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
IPR013085. Znf_U1-C.
[Graphical view]

Pfam

PF00397. WW. 2 hits.
PF06220. zf-U1. 1 hit.
[Graphical view]

SMART

SM00456. WW. 2 hits.
SM00451. ZnF_U1. 1 hit.
[Graphical view]

SUPFAM

SSF51045. WW_Rsp5_WWP. 2 hits.

PROSITE

PS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
PS50171. ZF_MATRIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O75554.

GenomeRNAi

11193.

NextBio

42605.

SOURCE

Search...

Entry information

Entry name

WBP4_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 104 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.