Full text data of WBP2
WBP2
[Confidence: low (only semi-automatic identification from reviews)]
WW domain-binding protein 2; WBP-2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
WW domain-binding protein 2; WBP-2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q969T9
ID WBP2_HUMAN Reviewed; 261 AA.
AC Q969T9; O95638;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=WW domain-binding protein 2;
DE Short=WBP-2;
GN Name=WBP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH YAP1.
RX PubMed=9202023; DOI=10.1074/jbc.272.27.17070;
RA Chen H.I., Einbond A., Kwak S.-J., Linn H., Koepf E., Peterson S.,
RA Kelly J.W., Sudol M.;
RT "Characterization of the WW domain of human Yes-associated protein and
RT its polyproline containing ligands.";
RL J. Biol. Chem. 272:17070-17077(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH WWP1 AND WWP2.
RX PubMed=9169421; DOI=10.1074/jbc.272.23.14611;
RA Pirozzi G., McConnell S.J., Uveges A.J., Carter J.M., Sparks A.B.,
RA Kay B.K., Fowlkes D.M.;
RT "Identification of novel human WW domain-containing proteins by
RT cloning of ligand targets.";
RL J. Biol. Chem. 272:14611-14616(1997).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- SUBUNIT: Binds to the WW domain of YAP1, WWP1 and WWP2. Interacts
CC with NEDD4 (By similarity).
CC -!- INTERACTION:
CC Q9GZV5:WWTR1; NbExp=6; IntAct=EBI-727055, EBI-747743;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The WW-binding 1 motif mediates interaction with NEDD4 (By
CC similarity).
CC -!- SIMILARITY: Contains 1 GRAM domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10951.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U79458; AAD10951.1; ALT_INIT; mRNA.
DR EMBL; BC007452; AAH07452.1; -; mRNA.
DR EMBL; BC010616; AAH10616.1; -; mRNA.
DR RefSeq; NP_036610.2; NM_012478.3.
DR UniGene; Hs.514489; -.
DR ProteinModelPortal; Q969T9; -.
DR SMR; Q969T9; 13-81.
DR IntAct; Q969T9; 7.
DR MINT; MINT-1431535; -.
DR STRING; 9606.ENSP00000254806; -.
DR PhosphoSite; Q969T9; -.
DR DMDM; 25091539; -.
DR OGP; Q969T9; -.
DR PaxDb; Q969T9; -.
DR PRIDE; Q969T9; -.
DR DNASU; 23558; -.
DR Ensembl; ENST00000254806; ENSP00000254806; ENSG00000132471.
DR Ensembl; ENST00000591399; ENSP00000467579; ENSG00000132471.
DR GeneID; 23558; -.
DR KEGG; hsa:23558; -.
DR UCSC; uc002jps.3; human.
DR CTD; 23558; -.
DR GeneCards; GC17M073841; -.
DR HGNC; HGNC:12738; WBP2.
DR MIM; 606962; gene.
DR neXtProt; NX_Q969T9; -.
DR PharmGKB; PA37349; -.
DR eggNOG; NOG291070; -.
DR HOGENOM; HOG000231103; -.
DR HOVERGEN; HBG027489; -.
DR InParanoid; Q969T9; -.
DR OMA; YMPTNQP; -.
DR OrthoDB; EOG73805Q; -.
DR PhylomeDB; Q969T9; -.
DR ChiTaRS; WBP2; human.
DR GeneWiki; WBP2; -.
DR GenomeRNAi; 23558; -.
DR NextBio; 46134; -.
DR PRO; PR:Q969T9; -.
DR ArrayExpress; Q969T9; -.
DR Bgee; Q969T9; -.
DR CleanEx; HS_WBP2; -.
DR Genevestigator; Q969T9; -.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR018826; WW-domain-binding.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF10349; WWbp; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Reference proteome; Repeat.
FT CHAIN 1 261 WW domain-binding protein 2.
FT /FTId=PRO_0000065950.
FT DOMAIN 1 84 GRAM.
FT MOTIF 196 200 WW-binding 1.
FT MOTIF 248 252 WW-binding 2.
FT COMPBIAS 146 255 Pro-rich.
SQ SEQUENCE 261 AA; 28087 MW; 8043727A03E67C82 CRC64;
MALNKNHSEG GGVIVNNTES ILMSYDHVEL TFNDMKNVPE AFKGTKKGTV YLTPYRVIFL
SKGKDAMQSF MMPFYLMKDC EIKQPVFGAN YIKGTVKAEA GGGWEGSASY KLTFTAGGAI
EFGQRMLQVA SQASRGEVPS GAYGYSYMPS GAYVYPPPVA NGMYPCPPGY PYPPPPPEFY
PGPPMMDGAM GYVQPPPPPY PGPMEPPVSG PDVPSTPAAE AKAAEAAASA YYNPGNPHNV
YMPTSQPPPP PYYPPEDKKT Q
//
ID WBP2_HUMAN Reviewed; 261 AA.
AC Q969T9; O95638;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=WW domain-binding protein 2;
DE Short=WBP-2;
GN Name=WBP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH YAP1.
RX PubMed=9202023; DOI=10.1074/jbc.272.27.17070;
RA Chen H.I., Einbond A., Kwak S.-J., Linn H., Koepf E., Peterson S.,
RA Kelly J.W., Sudol M.;
RT "Characterization of the WW domain of human Yes-associated protein and
RT its polyproline containing ligands.";
RL J. Biol. Chem. 272:17070-17077(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH WWP1 AND WWP2.
RX PubMed=9169421; DOI=10.1074/jbc.272.23.14611;
RA Pirozzi G., McConnell S.J., Uveges A.J., Carter J.M., Sparks A.B.,
RA Kay B.K., Fowlkes D.M.;
RT "Identification of novel human WW domain-containing proteins by
RT cloning of ligand targets.";
RL J. Biol. Chem. 272:14611-14616(1997).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- SUBUNIT: Binds to the WW domain of YAP1, WWP1 and WWP2. Interacts
CC with NEDD4 (By similarity).
CC -!- INTERACTION:
CC Q9GZV5:WWTR1; NbExp=6; IntAct=EBI-727055, EBI-747743;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The WW-binding 1 motif mediates interaction with NEDD4 (By
CC similarity).
CC -!- SIMILARITY: Contains 1 GRAM domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10951.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U79458; AAD10951.1; ALT_INIT; mRNA.
DR EMBL; BC007452; AAH07452.1; -; mRNA.
DR EMBL; BC010616; AAH10616.1; -; mRNA.
DR RefSeq; NP_036610.2; NM_012478.3.
DR UniGene; Hs.514489; -.
DR ProteinModelPortal; Q969T9; -.
DR SMR; Q969T9; 13-81.
DR IntAct; Q969T9; 7.
DR MINT; MINT-1431535; -.
DR STRING; 9606.ENSP00000254806; -.
DR PhosphoSite; Q969T9; -.
DR DMDM; 25091539; -.
DR OGP; Q969T9; -.
DR PaxDb; Q969T9; -.
DR PRIDE; Q969T9; -.
DR DNASU; 23558; -.
DR Ensembl; ENST00000254806; ENSP00000254806; ENSG00000132471.
DR Ensembl; ENST00000591399; ENSP00000467579; ENSG00000132471.
DR GeneID; 23558; -.
DR KEGG; hsa:23558; -.
DR UCSC; uc002jps.3; human.
DR CTD; 23558; -.
DR GeneCards; GC17M073841; -.
DR HGNC; HGNC:12738; WBP2.
DR MIM; 606962; gene.
DR neXtProt; NX_Q969T9; -.
DR PharmGKB; PA37349; -.
DR eggNOG; NOG291070; -.
DR HOGENOM; HOG000231103; -.
DR HOVERGEN; HBG027489; -.
DR InParanoid; Q969T9; -.
DR OMA; YMPTNQP; -.
DR OrthoDB; EOG73805Q; -.
DR PhylomeDB; Q969T9; -.
DR ChiTaRS; WBP2; human.
DR GeneWiki; WBP2; -.
DR GenomeRNAi; 23558; -.
DR NextBio; 46134; -.
DR PRO; PR:Q969T9; -.
DR ArrayExpress; Q969T9; -.
DR Bgee; Q969T9; -.
DR CleanEx; HS_WBP2; -.
DR Genevestigator; Q969T9; -.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR018826; WW-domain-binding.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF10349; WWbp; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Reference proteome; Repeat.
FT CHAIN 1 261 WW domain-binding protein 2.
FT /FTId=PRO_0000065950.
FT DOMAIN 1 84 GRAM.
FT MOTIF 196 200 WW-binding 1.
FT MOTIF 248 252 WW-binding 2.
FT COMPBIAS 146 255 Pro-rich.
SQ SEQUENCE 261 AA; 28087 MW; 8043727A03E67C82 CRC64;
MALNKNHSEG GGVIVNNTES ILMSYDHVEL TFNDMKNVPE AFKGTKKGTV YLTPYRVIFL
SKGKDAMQSF MMPFYLMKDC EIKQPVFGAN YIKGTVKAEA GGGWEGSASY KLTFTAGGAI
EFGQRMLQVA SQASRGEVPS GAYGYSYMPS GAYVYPPPVA NGMYPCPPGY PYPPPPPEFY
PGPPMMDGAM GYVQPPPPPY PGPMEPPVSG PDVPSTPAAE AKAAEAAASA YYNPGNPHNV
YMPTSQPPPP PYYPPEDKKT Q
//
MIM
606962
*RECORD*
*FIELD* NO
606962
*FIELD* TI
*606962 WW DOMAIN-BINDING PROTEIN 2; WBP2
*FIELD* TX
DESCRIPTION
The globular WW domain is composed of 38 to 40 semiconserved amino acids
read moreshared by proteins of diverse functions including structural,
regulatory, and signaling proteins. The domain is involved in mediating
protein-protein interactions through the binding of polyproline ligands.
Thus, its function is similar to that of the Src homology-3 (SH3)
domain.
CLONING
Using a functional screen of a mouse cDNA expression library, Chen and
Sudol (1995) cloned 2 ligands, which they designated Wbp1 (606961) and
Wpb2, that bound to the WW domain of human Yes kinase-associated protein
(YAP; 606608). Sequence comparison showed no homology between the 2
proteins except in a short proline-rich region containing the invariant
residues PPPPY, which the authors designated the PY motif. Wbp1 contains
a single PY motif, whereas Wbp2 contains 2 in the forward orientation
and 1 in the reverse orientation. A structural similarity between the WW
and SH3 domains is a hydrophobic core of conserved aromatic residues
surrounded by beta loops containing charged amino acids. Northern blot
analysis of multiple human tissues detected Northern blot analysis of
multiple human tissues revealed ubiquitous expression of a 2.0-kb WBP2
transcript. Using the partial mouse cDNA as probe, Chen et al. (1997)
cloned WBP2 from a human lung fibroblast cDNA library. The cDNA encodes
a deduced 268-amino acid protein that shares 94% sequence identity with
the mouse protein.
GENE FUNCTION
Since Wbp1 contains only a single PY motif, Chen and Sudol (1995) used
this as a model protein to characterize interaction between the PY and
WW domains. By mutagenesis followed by Western ligand blot analysis,
they established that all residues of the PY motif engage in binding the
WW domain, and that P2, P3, and Y5 are crucial but not entirely
sufficient for optimal binding. Chen et al. (1997) confirmed and refined
the consensus PY motif as XPPXW.
MAPPING
By FISH, Chen et al. (1997) mapped the WBP2 gene to chromosome 17q25.
*FIELD* RF
1. Chen, H. I.; Einbond, A.; Kwak, S.-J.; Linn, H.; Koepf, E.; Peterson,
S.; Kelly, J. W.; Sudol, M.: Characterization of the WW domain of
human Yes-associated protein and its polyproline containing ligands. J.
Biol. Chem. 272: 17070-17077, 1997.
2. Chen, H. I.; Sudol, M.: The WW domain of Yes-associated protein
binds a proline-rich ligand that differs from the consensus established
for Src homology 3-binding modules. Proc. Nat. Acad. Sci. 92: 7819-7823,
1995.
*FIELD* CD
Patricia A. Hartz: 5/22/2002
*FIELD* ED
alopez: 11/04/2003
carol: 5/22/2002
*RECORD*
*FIELD* NO
606962
*FIELD* TI
*606962 WW DOMAIN-BINDING PROTEIN 2; WBP2
*FIELD* TX
DESCRIPTION
The globular WW domain is composed of 38 to 40 semiconserved amino acids
read moreshared by proteins of diverse functions including structural,
regulatory, and signaling proteins. The domain is involved in mediating
protein-protein interactions through the binding of polyproline ligands.
Thus, its function is similar to that of the Src homology-3 (SH3)
domain.
CLONING
Using a functional screen of a mouse cDNA expression library, Chen and
Sudol (1995) cloned 2 ligands, which they designated Wbp1 (606961) and
Wpb2, that bound to the WW domain of human Yes kinase-associated protein
(YAP; 606608). Sequence comparison showed no homology between the 2
proteins except in a short proline-rich region containing the invariant
residues PPPPY, which the authors designated the PY motif. Wbp1 contains
a single PY motif, whereas Wbp2 contains 2 in the forward orientation
and 1 in the reverse orientation. A structural similarity between the WW
and SH3 domains is a hydrophobic core of conserved aromatic residues
surrounded by beta loops containing charged amino acids. Northern blot
analysis of multiple human tissues detected Northern blot analysis of
multiple human tissues revealed ubiquitous expression of a 2.0-kb WBP2
transcript. Using the partial mouse cDNA as probe, Chen et al. (1997)
cloned WBP2 from a human lung fibroblast cDNA library. The cDNA encodes
a deduced 268-amino acid protein that shares 94% sequence identity with
the mouse protein.
GENE FUNCTION
Since Wbp1 contains only a single PY motif, Chen and Sudol (1995) used
this as a model protein to characterize interaction between the PY and
WW domains. By mutagenesis followed by Western ligand blot analysis,
they established that all residues of the PY motif engage in binding the
WW domain, and that P2, P3, and Y5 are crucial but not entirely
sufficient for optimal binding. Chen et al. (1997) confirmed and refined
the consensus PY motif as XPPXW.
MAPPING
By FISH, Chen et al. (1997) mapped the WBP2 gene to chromosome 17q25.
*FIELD* RF
1. Chen, H. I.; Einbond, A.; Kwak, S.-J.; Linn, H.; Koepf, E.; Peterson,
S.; Kelly, J. W.; Sudol, M.: Characterization of the WW domain of
human Yes-associated protein and its polyproline containing ligands. J.
Biol. Chem. 272: 17070-17077, 1997.
2. Chen, H. I.; Sudol, M.: The WW domain of Yes-associated protein
binds a proline-rich ligand that differs from the consensus established
for Src homology 3-binding modules. Proc. Nat. Acad. Sci. 92: 7819-7823,
1995.
*FIELD* CD
Patricia A. Hartz: 5/22/2002
*FIELD* ED
alopez: 11/04/2003
carol: 5/22/2002