ID WBP2_HUMAN Reviewed; 261 AA.
AC Q969T9; B4DFG2; O95638;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 177.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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 its
RT polyproline containing ligands.";
RL J. Biol. Chem. 272:17070-17077(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
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 cloning of
RT ligand targets.";
RL J. Biol. Chem. 272:14611-14616(1997).
RN [6]
RP FUNCTION, INTERACTION WITH ESR1 AND UBE3A, MUTAGENESIS OF 248-PRO--TYR-252,
RP AND DOMAIN.
RX PubMed=16772533; DOI=10.1210/me.2005-0533;
RA Dhananjayan S.C., Ramamoorthy S., Khan O.Y., Ismail A., Sun J.,
RA Slingerland J., O'Malley B.W., Nawaz Z.;
RT "WW domain binding protein-2, an E6-associated protein interacting protein,
RT acts as a coactivator of estrogen and progesterone receptors.";
RL Mol. Endocrinol. 20:2343-2354(2006).
RN [7]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-192 AND TYR-231,
RP MUTAGENESIS OF TYR-25; TYR-51; TYR-55; TYR-75; TYR-143; TYR-145; TYR-153;
RP TYR-164; TYR-170; TYR-172; TYR-180; TYR-192; TYR-200; TYR-231; TYR-232;
RP TYR-252 AND TYR-253, AND INTERACTION WITH ESR1.
RX PubMed=21642474; DOI=10.1096/fj.10-169136;
RA Lim S.K., Orhant-Prioux M., Toy W., Tan K.Y., Lim Y.P.;
RT "Tyrosine phosphorylation of transcriptional coactivator WW-domain binding
RT protein 2 regulates estrogen receptor alpha function in breast cancer via
RT the Wnt pathway.";
RL FASEB J. 25:3004-3018(2011).
RN [9]
RP INVOLVEMENT IN DFNB107, AND VARIANTS DFNB107 THR-160; LEU-163 AND VAL-224.
RX PubMed=26881968; DOI=10.15252/emmm.201505523;
RA Buniello A., Ingham N.J., Lewis M.A., Huma A.C., Martinez-Vega R.,
RA Varela-Nieto I., Vizcay-Barrena G., Fleck R.A., Houston O., Bardhan T.,
RA Johnson S.L., White J.K., Yuan H., Marcotti W., Steel K.P.;
RT "Wbp2 is required for normal glutamatergic synapses in the cochlea and is
RT crucial for hearing.";
RL EMBO Mol. Med. 8:191-207(2016).
CC -!- FUNCTION: Acts as a transcriptional coactivator of estrogen and
CC progesterone receptors (ESR1 and PGR) upon hormone activation
CC (PubMed:16772533). In presence of estrogen, binds to ESR1-responsive
CC promoters (PubMed:16772533). Required for YAP1 coactivation function on
CC PGR activity (PubMed:16772533). Synergizes with WBP2 in enhancing PGR
CC activity (PubMed:16772533). Modulates expression of post-synaptic
CC scaffolding proteins via regulation of ESR1, ESR2 and PGR (By
CC similarity). {ECO:0000250|UniProtKB:P97765,
CC ECO:0000269|PubMed:16772533}.
CC -!- SUBUNIT: Binds to the WW domain of YAP1, WWP1 and WWP2. Interacts with
CC NEDD4 (By similarity). Interacts with ESR1 and UBE3A (PubMed:16772533,
CC PubMed:21642474). {ECO:0000250|UniProtKB:P97765,
CC ECO:0000269|PubMed:16772533, ECO:0000269|PubMed:21642474}.
CC -!- INTERACTION:
CC Q969T9; O95817: BAG3; NbExp=4; IntAct=EBI-727055, EBI-747185;
CC Q969T9; Q99832: CCT7; NbExp=3; IntAct=EBI-727055, EBI-357046;
CC Q969T9; O95208-2: EPN2; NbExp=3; IntAct=EBI-727055, EBI-12135243;
CC Q969T9; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-727055, EBI-748420;
CC Q969T9; O00214-2: LGALS8; NbExp=3; IntAct=EBI-727055, EBI-12069522;
CC Q969T9; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-727055, EBI-10194128;
CC Q969T9; Q99717: SMAD5; NbExp=3; IntAct=EBI-727055, EBI-6391136;
CC Q969T9; Q969T4: UBE2E3; NbExp=3; IntAct=EBI-727055, EBI-348496;
CC Q969T9; Q9GZV5: WWTR1; NbExp=6; IntAct=EBI-727055, EBI-747743;
CC Q969T9; P46937: YAP1; NbExp=7; IntAct=EBI-727055, EBI-1044059;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21642474}. Nucleus
CC {ECO:0000269|PubMed:21642474}. Note=Translocates from cytoplasm to
CC nucleus when phosphorylated. {ECO:0000269|PubMed:21642474}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q969T9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969T9-2; Sequence=VSP_059233;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The PPxY motif 1 mediates interaction with NEDD4 (By
CC similarity). The PPxY motif 2 is required for the coactivation function
CC (PubMed:16772533). {ECO:0000250|UniProtKB:P97765,
CC ECO:0000269|PubMed:16772533}.
CC -!- PTM: Phosphorylated in repsonse to EGF as well as estrogen and
CC progesterone hormones (PubMed:21642474). Tyr-192 and Tyr-231 are
CC phosphorylated by YES and SRC inducing nuclear translocation
CC (PubMed:21642474). {ECO:0000269|PubMed:21642474}.
CC -!- DISEASE: Deafness, autosomal recessive, 107 (DFNB107) [MIM:617639]: A
CC form of non-syndromic sensorineural hearing loss. Sensorineural
CC deafness results from damage to the neural receptors of the inner ear,
CC the nerve pathways to the brain, or the area of the brain that receives
CC sound information. {ECO:0000269|PubMed:26881968}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10951.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U79458; AAD10951.1; ALT_INIT; mRNA.
DR EMBL; AK294082; BAG57423.1; -; mRNA.
DR EMBL; AC087289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007452; AAH07452.1; -; mRNA.
DR EMBL; BC010616; AAH10616.1; -; mRNA.
DR CCDS; CCDS11731.1; -. [Q969T9-1]
DR CCDS; CCDS82206.1; -. [Q969T9-2]
DR RefSeq; NP_001317428.1; NM_001330499.1. [Q969T9-2]
DR RefSeq; NP_001335099.1; NM_001348170.1. [Q969T9-1]
DR RefSeq; NP_036610.2; NM_012478.3. [Q969T9-1]
DR AlphaFoldDB; Q969T9; -.
DR BioGRID; 117102; 82.
DR DIP; DIP-42509N; -.
DR IntAct; Q969T9; 23.
DR MINT; Q969T9; -.
DR STRING; 9606.ENSP00000467579; -.
DR iPTMnet; Q969T9; -.
DR MetOSite; Q969T9; -.
DR PhosphoSitePlus; Q969T9; -.
DR BioMuta; WBP2; -.
DR DMDM; 25091539; -.
DR OGP; Q969T9; -.
DR EPD; Q969T9; -.
DR jPOST; Q969T9; -.
DR MassIVE; Q969T9; -.
DR MaxQB; Q969T9; -.
DR PaxDb; 9606-ENSP00000467579; -.
DR PeptideAtlas; Q969T9; -.
DR ProteomicsDB; 4034; -.
DR ProteomicsDB; 75845; -.
DR Pumba; Q969T9; -.
DR Antibodypedia; 32285; 177 antibodies from 26 providers.
DR DNASU; 23558; -.
DR Ensembl; ENST00000254806.8; ENSP00000254806.3; ENSG00000132471.12. [Q969T9-1]
DR Ensembl; ENST00000433525.6; ENSP00000415251.2; ENSG00000132471.12. [Q969T9-2]
DR Ensembl; ENST00000591399.5; ENSP00000467579.1; ENSG00000132471.12. [Q969T9-1]
DR GeneID; 23558; -.
DR KEGG; hsa:23558; -.
DR MANE-Select; ENST00000254806.8; ENSP00000254806.3; NM_012478.4; NP_036610.2.
DR UCSC; uc002jps.3; human. [Q969T9-1]
DR UCSC; uc010wsm.3; human.
DR AGR; HGNC:12738; -.
DR DisGeNET; 23558; -.
DR GeneCards; WBP2; -.
DR HGNC; HGNC:12738; WBP2.
DR HPA; ENSG00000132471; Low tissue specificity.
DR MalaCards; WBP2; -.
DR MIM; 606962; gene.
DR MIM; 617639; phenotype.
DR neXtProt; NX_Q969T9; -.
DR OpenTargets; ENSG00000132471; -.
DR Orphanet; 90636; Rare autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA37349; -.
DR VEuPathDB; HostDB:ENSG00000132471; -.
DR eggNOG; KOG3294; Eukaryota.
DR GeneTree; ENSGT00530000063718; -.
DR InParanoid; Q969T9; -.
DR OMA; ANGMYPQ; -.
DR OrthoDB; 759742at2759; -.
DR PhylomeDB; Q969T9; -.
DR TreeFam; TF314141; -.
DR PathwayCommons; Q969T9; -.
DR SignaLink; Q969T9; -.
DR SIGNOR; Q969T9; -.
DR BioGRID-ORCS; 23558; 14 hits in 1149 CRISPR screens.
DR ChiTaRS; WBP2; human.
DR GeneWiki; WBP2; -.
DR GenomeRNAi; 23558; -.
DR Pharos; Q969T9; Tbio.
DR PRO; PR:Q969T9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q969T9; Protein.
DR Bgee; ENSG00000132471; Expressed in right frontal lobe and 207 other cell types or tissues.
DR ExpressionAtlas; Q969T9; baseline and differential.
DR Genevisible; Q969T9; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IMP:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IMP:UniProtKB.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR GO; GO:0032570; P:response to progesterone; IDA:UniProtKB.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IMP:UniProtKB.
DR CDD; cd13214; PH-GRAM_WBP2; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR044852; WBP2-like.
DR PANTHER; PTHR31606; WW DOMAIN BINDING PROTEIN 2, ISOFORM E; 1.
DR PANTHER; PTHR31606:SF4; WW DOMAIN-BINDING PROTEIN 2; 1.
DR Pfam; PF02893; GRAM; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Deafness; Disease variant;
KW Non-syndromic deafness; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..261
FT /note="WW domain-binding protein 2"
FT /id="PRO_0000065950"
FT DOMAIN 1..84
FT /note="GRAM"
FT REGION 196..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 196..200
FT /note="PPxY motif 1"
FT MOTIF 248..252
FT /note="PPxY motif 2"
FT COMPBIAS 196..213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 192
FT /note="Phosphotyrosine; by YES and SRC"
FT /evidence="ECO:0000269|PubMed:21642474"
FT MOD_RES 231
FT /note="Phosphotyrosine; by YES and SRC"
FT /evidence="ECO:0000269|PubMed:21642474"
FT VAR_SEQ 133..177
FT /note="Missing (in isoform 2)"
FT /id="VSP_059233"
FT VARIANT 160
FT /note="A -> T (in DFNB107; dbSNP:rs202022024)"
FT /evidence="ECO:0000269|PubMed:26881968"
FT /id="VAR_079500"
FT VARIANT 163
FT /note="M -> L (in DFNB107; uncertain significance;
FT dbSNP:rs1555604710)"
FT /evidence="ECO:0000269|PubMed:26881968"
FT /id="VAR_079501"
FT VARIANT 224
FT /note="A -> V (in DFNB107; uncertain significance;
FT dbSNP:rs1555604549)"
FT /evidence="ECO:0000269|PubMed:26881968"
FT /id="VAR_079502"
FT MUTAGEN 25
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 51
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 55
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 75
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 143
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 145
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 153
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 164
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 170
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 172
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 180
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 192
FT /note="Y->F: Strongly decreases phosphorylation induced by
FT EGF. Abolishes phosphorylation in response to EGF, estrogen
FT and progesterone; when associated with F-231."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 200
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 231
FT /note="Y->F: Strongly decreases phosphorylation induced by
FT EGF. Abolishes phosphorylation in response to EGF, estrogen
FT and progesterone; when associated with F-231."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 232
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 248..252
FT /note="PPPPY->AAAPA: Loss of coactivator activity in
FT presence of estrogen."
FT /evidence="ECO:0000269|PubMed:16772533"
FT MUTAGEN 252
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
FT MUTAGEN 253
FT /note="Y->F: No effect on phosphorylation induced by EGF."
FT /evidence="ECO:0000269|PubMed:21642474"
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
//
