Q969T9 B4DFG2 O95638 WBP2_HUMAN WW domain-binding protein 2 WBP-2 WBP2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Characterization of the WW domain of human Yes-associated protein and its polyproline containing ligands. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) INTERACTION WITH YAP1 Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain Placenta Identification of novel human WW domain-containing proteins by cloning of ligand targets. INTERACTION WITH WWP1 AND WWP2 WW domain binding protein-2, an E6-associated protein interacting protein, acts as a coactivator of estrogen and progesterone receptors. FUNCTION INTERACTION WITH ESR1 AND UBE3A MUTAGENESIS OF 248-PRO--TYR-252 DOMAIN Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Tyrosine phosphorylation of transcriptional coactivator WW-domain binding protein 2 regulates estrogen receptor alpha function in breast cancer via the Wnt pathway. FUNCTION SUBCELLULAR LOCATION PHOSPHORYLATION AT TYR-192 AND TYR-231 MUTAGENESIS OF TYR-25; TYR-51; TYR-55; TYR-75; TYR-143; TYR-145; TYR-153; TYR-164; TYR-170; TYR-172; TYR-180; TYR-192; TYR-200; TYR-231; TYR-232; TYR-252 AND TYR-253 INTERACTION WITH ESR1 Wbp2 is required for normal glutamatergic synapses in the cochlea and is crucial for hearing. INVOLVEMENT IN DFNB107 VARIANTS DFNB107 THR-160; LEU-163 AND VAL-224 Acts as a transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation (PubMed:16772533). In presence of estrogen, binds to ESR1-responsive promoters (PubMed:16772533). Synergizes with YAP1 to enhance PGR activity (PubMed:16772533). Modulates expression of post-synaptic scaffolding proteins via regulation of ESR1, ESR2 and PGR (By similarity). Binds to the WW domain of YAP1, WWP1 and WWP2 (PubMed:9169421, PubMed:9202023). Interacts with NEDD4 (By similarity). Interacts with ESR1 and UBE3A (PubMed:16772533, PubMed:21642474). Q969T9 O95817 false 4 Q969T9 Q99832 false 3 Q969T9 O95208-2 false 3 Q969T9 Q9NSC5 false 3 Q969T9 O00214-2 false 3 Q969T9 Q1RN33 false 3 Q969T9 Q99717 false 3 Q969T9 Q969T4 false 3 Q969T9 Q9GZV5 false 6 Q969T9 P46937 false 7 Cytoplasm Nucleus Translocates from cytoplasm to nucleus when phosphorylated. Q969T9-1 1 Q969T9-2 2 Ubiquitous. The PPxY motif 1 mediates interaction with NEDD4 (By similarity). The PPxY motif 2 is required for the coactivation function (PubMed:16772533). Phosphorylated in repsonse to EGF as well as estrogen and progesterone hormones (PubMed:21642474). Tyr-192 and Tyr-231 are phosphorylated by YES and SRC inducing nuclear translocation (PubMed:21642474). Deafness, autosomal recessive, 107 DFNB107 A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. The disease is caused by variants affecting the gene represented in this entry. Extended N-terminus. Alternative splicing Cytoplasm Deafness Disease variant Non-syndromic deafness Nucleus Phosphoprotein Proteomics identification Reference proteome Repeat A T M L A V Y F Y F Y F Y F Y F Y F Y F Y F Y F Y F Y F Y F Y F Y F Y F PPPPY AAAPA Y F Y F MALNKNHSEGGGVIVNNTESILMSYDHVELTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLSKGKDAMQSFMMPFYLMKDCEIKQPVFGANYIKGTVKAEAGGGWEGSASYKLTFTAGGAIEFGQRMLQVASQASRGEVPSGAYGYSYMPSGAYVYPPPVANGMYPCPPGYPYPPPPPEFYPGPPMMDGAMGYVQPPPPPYPGPMEPPVSGPDVPSTPAAEAKAAEAAASAYYNPGNPHNVYMPTSQPPPPPYYPPEDKKTQ Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License