MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=NEDD4 family-interacting protein 2; AltName: Full=NEDD4 WW domain-binding protein 5A; AltName: Full=Putative MAPK-activating protein PM04/PM05/PM06/PM07; AltName: Full=Putative NF-kappa-B-activating protein 413; |
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| MyHits synonyms | NFIP2_HUMAN , Q9NV92 , Q7Z2H3 , Q7Z428 , Q8TAR3 , Q9ULQ5 , A7E386C12886321E |
 Legends: 1, SITE Not phosphorylated by SRC; 2, Phosphotyrosine; by SRC. {ECO:0000269|PubMed:20534535}; 3, VARIANT P -> S (in dbSNP:rs55887763); 4, VARIANT A -> V (in dbSNP:rs11549502). {ECO:0000269|PubMed:10574461, ECO:0000269|PubMed:12761501, ECO:0000269|PubMed:15489334}; 5, MUTAGEN Y->F: Loss of NDFIP2 phosphorylation by SRC. {ECO:0000269|PubMed:20534535}; 6, TRANSMEM Helical. {ECO:0000255}; 7, TOPO_DOM Extracellular. {ECO:0000255}; 8, TOPO_DOM Cytoplasmic. {ECO:0000255}; 9, REGION Interaction with NEDD4. {ECO:0000250}; 10, MOTIF WW-binding 1; 11, MOTIF WW-binding 2; 12, MOTIF WW-binding 3; 13, MUTAGEN PY->AG: Loss of E3 ubiquitin-protein ligase activation; when associated with 175-P--G-177 AND 184-P--G-186. Greatly decreases NEDD4-binding; when associated with 175-P--G-177 and 184-P--G-186. No effect on PTEN-binding; when associated with 175-P--G-177 AND 184-P--G-186; 14, MUTAGEN PY->AG: Loss of E3 ubiquitin-protein ligase activation; when associated with 149-P--G-151 AND 184-P--G-186. Greatly decreases NEDD4-binding; when associated with 149-P-G-151 AND 184-P--G-186. No effect on PTEN-binding; when associated with 149-P--G-151 AND 184-P--G-186; 15, MUTAGEN TY->AG: Loss of E3 ubiquitin-protein ligase activation; when associated with 149-P--G-151 AND 175-P--G-177. Greatly decreases NEDD4-binding; when associated with 149-P--G-151 AND 175-P--G-177. No effect on PTEN-binding; when associated with 149-P--G-151 AND 175-P--G-177.
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ID NFIP2_HUMAN Reviewed; 336 AA.
AC Q9NV92; Q7Z2H3; Q7Z428; Q8TAR3; Q9ULQ5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 10-MAY-2017, entry version 127.
DE RecName: Full=NEDD4 family-interacting protein 2;
DE AltName: Full=NEDD4 WW domain-binding protein 5A;
DE AltName: Full=Putative MAPK-activating protein PM04/PM05/PM06/PM07;
DE AltName: Full=Putative NF-kappa-B-activating protein 413;
GN Name=NDFIP2; Synonyms=KIAA1165, N4WBP5A;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, AND INTERACTION WITH NEDD4.
RC TISSUE=T-cell;
RX PubMed=12796489; DOI=10.1074/jbc.M304723200;
RA Cristillo A.D., Nie L., Macri M.J., Bierer B.E.;
RT "Cloning and characterization of N4WBP5A, an inducible, cyclosporine-
RT sensitive, Nedd4-binding protein in human T lymphocytes.";
RL J. Biol. Chem. 278:34587-34597(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], FUNCTION, AND VARIANT VAL-136.
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-336.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 53-336, AND VARIANT VAL-136.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis
RT from size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-336, AND VARIANT VAL-136.
RC TISSUE=Bone marrow, and Muscle;
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SLC11A2 AND WWP2.
RX PubMed=18776082; DOI=10.1182/blood-2008-04-150953;
RA Foot N.J., Dalton H.E., Shearwin-Whyatt L.M., Dorstyn L., Tan S.S.,
RA Yang B., Kumar S.;
RT "Regulation of the divalent metal ion transporter DMT1 and iron
RT homeostasis by a ubiquitin-dependent mechanism involving Ndfips and
RT WWP2.";
RL Blood 112:4268-4275(2008).
RN [8]
RP FUNCTION, AND UBIQUITINATION.
RX PubMed=19343052; DOI=10.1038/embor.2009.30;
RA Mund T., Pelham H.R.;
RT "Control of the activity of WW-HECT domain E3 ubiquitin ligases by
RT NDFIP proteins.";
RL EMBO Rep. 10:501-507(2009).
RN [9]
RP FUNCTION, INTERACTION WITH LYN; NDFIP1; NEDD4; PTEN AND SRC,
RP SUBCELLULAR LOCATION, TOPOLOGY, PHOSPHORYLATION AT TYR-151; TYR-167;
RP TYR-171 AND TYR-177, AND MUTAGENESIS OF 149-PRO--TYR-151; TYR-167;
RP 175-PRO--TYR-177 AND 184-PRO--TYR-186.
RX PubMed=20534535; DOI=10.1073/pnas.0911714107;
RA Mund T., Pelham H.R.;
RT "Regulation of PTEN/Akt and MAP kinase signaling pathways by the
RT ubiquitin ligase activators Ndfip1 and Ndfip2.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11429-11434(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KCNH2 AND NEDD4L.
RX PubMed=26363003; DOI=10.1042/BJ20141282;
RA Kang Y., Guo J., Yang T., Li W., Zhang S.;
RT "Regulation of the human ether-a-go-go-related gene (hERG) potassium
RT channel by Nedd4 family interacting proteins (Ndfips).";
RL Biochem. J. 472:71-82(2015).
CC -!- FUNCTION: Activates HECT domain-containing E3 ubiquitin-protein
CC ligases, including ITCH, NEDD4, NEDD4L, SMURF2, WWP1 and WWP2, and
CC consequently modulates the stability of their targets. As a
CC result, may control many cellular processes. Recruits ITCH, NEDD4
CC and SMURF2 to endosomal membranes. Negatively regulates KCNH2
CC potassium channel activity by decreasing its cell-surface
CC expression and interfering with channel maturation through
CC recruitment of NEDD4L to the Golgi apparatus and multivesicular
CC body where it mediates KCNH2 degradation (PubMed:26363003). May
CC modulate EGFR signaling. Together with NDFIP1, limits the cytokine
CC signaling and expansion of effector Th2 T-cells by promoting
CC degradation of JAK1, probably by ITCH- and NEDD4L-mediated
CC ubiquitination (By similarity). {ECO:0000250|UniProtKB:Q91ZP6,
CC ECO:0000269|PubMed:12761501, ECO:0000269|PubMed:19343052,
CC ECO:0000269|PubMed:20534535, ECO:0000269|PubMed:26363003}.
CC -!- SUBUNIT: Forms heterodimers with NDFIP1. Interacts with HECT
CC domain-containing E3 ubiquitin-protein ligases, including NEDD4
CC (PubMed:12796489). Interacts with NEDD4L (PubMed:26363003).
CC Interacts with PTEN. When phosphorylated at Tyr-167, interacts
CC with SRC and LYN SH2 domain. May thus act as a scaffold that
CC recruits SRC to NDFIP1, enhancing NDFIP1 phosphorylation.
CC Interacts with SLC11A2/DMT1 (PubMed:18776082). May interact with
CC phosphorylated EGFR. Interacts with KCNH2 (PubMed:26363003).
CC {ECO:0000250, ECO:0000269|PubMed:12796489,
CC ECO:0000269|PubMed:18776082, ECO:0000269|PubMed:20534535,
CC ECO:0000269|PubMed:26363003}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000269|PubMed:18776082}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18776082}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:12796489, ECO:0000269|PubMed:26363003}.
CC Endosome, multivesicular body membrane
CC {ECO:0000269|PubMed:26363003}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, heart, skeletal
CC muscle, kidney, liver and placenta. {ECO:0000269|PubMed:12796489}.
CC -!- INDUCTION: By T-cell activation. {ECO:0000269|PubMed:12796489}.
CC -!- DOMAIN: The PY/WW-binding motifs are required for E3 ubiquitin-
CC protein ligase activation and for ubiquitination.
CC -!- PTM: Ubiquitinated by NEDD4 and ITCH. Also ubiquitinated by
CC NEDD4L. Ubiquitination by NEDD4 or NEDD4L does not affect turnover
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Undergoes transient tyrosine-phosphorylation following EGF
CC stimulation, most probably catalyzed by SRC. Phosphorylation on
CC Tyr-151, Tyr-171 and Tyr-177 are dependent on the phosphorylation
CC on Tyr-167. Also phosphorylated by LYN and FYN.
CC {ECO:0000269|PubMed:20534535}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21988.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH26126.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91863.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB097019; BAC77372.1; -; mRNA.
DR EMBL; AB097028; BAC77381.1; -; mRNA.
DR EMBL; AB097029; BAC77382.1; -; mRNA.
DR EMBL; AB097030; BAC77383.1; -; mRNA.
DR EMBL; AB097031; BAC77384.1; -; mRNA.
DR EMBL; AL136442; CAH71782.1; -; Genomic_DNA.
DR EMBL; AL355603; CAH71782.1; JOINED; Genomic_DNA.
DR EMBL; AL355603; CAH73355.1; -; Genomic_DNA.
DR EMBL; AL136442; CAH73355.1; JOINED; Genomic_DNA.
DR EMBL; AK001723; BAA91863.1; ALT_INIT; mRNA.
DR EMBL; AB032991; BAA86479.1; -; mRNA.
DR EMBL; BC021988; AAH21988.1; ALT_INIT; mRNA.
DR EMBL; BC026126; AAH26126.1; ALT_INIT; mRNA.
DR CCDS; CCDS31998.1; -.
DR RefSeq; NP_061953.2; NM_019080.2.
DR UniGene; Hs.525093; -.
DR ProteinModelPortal; Q9NV92; -.
DR BioGrid; 120074; 17.
DR IntAct; Q9NV92; 3.
DR STRING; 9606.ENSP00000218652; -.
DR iPTMnet; Q9NV92; -.
DR PhosphoSitePlus; Q9NV92; -.
DR BioMuta; NDFIP2; -.
DR DMDM; 73921209; -.
DR EPD; Q9NV92; -.
DR MaxQB; Q9NV92; -.
DR PaxDb; Q9NV92; -.
DR PeptideAtlas; Q9NV92; -.
DR PRIDE; Q9NV92; -.
DR Ensembl; ENST00000218652; ENSP00000218652; ENSG00000102471.
DR Ensembl; ENST00000612570; ENSP00000480798; ENSG00000102471.
DR GeneID; 54602; -.
DR KEGG; hsa:54602; -.
DR UCSC; uc001vlf.4; human.
DR CTD; 54602; -.
DR DisGeNET; 54602; -.
DR GeneCards; NDFIP2; -.
DR HGNC; HGNC:18537; NDFIP2.
DR HPA; HPA009160; -.
DR MIM; 610041; gene.
DR neXtProt; NX_Q9NV92; -.
DR OpenTargets; ENSG00000102471; -.
DR PharmGKB; PA134953250; -.
DR eggNOG; KOG4812; Eukaryota.
DR eggNOG; ENOG4111M6U; LUCA.
DR GeneTree; ENSGT00390000012721; -.
DR HOGENOM; HOG000038752; -.
DR HOVERGEN; HBG057103; -.
DR InParanoid; Q9NV92; -.
DR OMA; SPPPYCS; -.
DR OrthoDB; EOG091G0IMV; -.
DR PhylomeDB; Q9NV92; -.
DR TreeFam; TF324911; -.
DR ChiTaRS; NDFIP2; human.
DR GeneWiki; NDFIP2; -.
DR GenomeRNAi; 54602; -.
DR PRO; PR:Q9NV92; -.
DR Proteomes; UP000005640; Chromosome 13.
DR Bgee; ENSG00000102471; -.
DR CleanEx; HS_NDFIP2; -.
DR ExpressionAtlas; Q9NV92; baseline and differential.
DR Genevisible; Q9NV92; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
DR GO; GO:0050699; F:WW domain binding; IPI:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0051224; P:negative regulation of protein transport; IMP:UniProtKB.
DR GO; GO:0032410; P:negative regulation of transporter activity; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Complete proteome; Endosome; Golgi apparatus; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1 336 NEDD4 family-interacting protein 2.
FT /FTId=PRO_0000096794.
FT TOPO_DOM 1 231 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 232 252 Helical. {ECO:0000255}.
FT TOPO_DOM 253 257 Extracellular. {ECO:0000255}.
FT TRANSMEM 258 278 Helical. {ECO:0000255}.
FT TOPO_DOM 279 287 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 288 308 Helical. {ECO:0000255}.
FT TOPO_DOM 309 336 Extracellular. {ECO:0000255}.
FT REGION 148 151 Interaction with NEDD4. {ECO:0000250}.
FT MOTIF 149 151 WW-binding 1.
FT MOTIF 175 177 WW-binding 2.
FT MOTIF 184 186 WW-binding 3.
FT SITE 186 186 Not phosphorylated by SRC.
FT MOD_RES 151 151 Phosphotyrosine; by SRC.
FT {ECO:0000269|PubMed:20534535}.
FT MOD_RES 167 167 Phosphotyrosine; by SRC.
FT {ECO:0000269|PubMed:20534535}.
FT MOD_RES 171 171 Phosphotyrosine; by SRC.
FT {ECO:0000269|PubMed:20534535}.
FT MOD_RES 177 177 Phosphotyrosine; by SRC.
FT {ECO:0000269|PubMed:20534535}.
FT VARIANT 124 124 P -> S (in dbSNP:rs55887763).
FT /FTId=VAR_061687.
FT VARIANT 136 136 A -> V (in dbSNP:rs11549502).
FT {ECO:0000269|PubMed:10574461,
FT ECO:0000269|PubMed:12761501,
FT ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_023414.
FT MUTAGEN 150 151 PY->AG: Loss of E3 ubiquitin-protein
FT ligase activation; when associated with
FT 175-P--G-177 AND 184-P--G-186. Greatly
FT decreases NEDD4-binding; when associated
FT with 175-P--G-177 and 184-P--G-186. No
FT effect on PTEN-binding; when associated
FT with 175-P--G-177 AND 184-P--G-186.
FT MUTAGEN 167 167 Y->F: Loss of NDFIP2 phosphorylation by
FT SRC. {ECO:0000269|PubMed:20534535}.
FT MUTAGEN 176 177 PY->AG: Loss of E3 ubiquitin-protein
FT ligase activation; when associated with
FT 149-P--G-151 AND 184-P--G-186. Greatly
FT decreases NEDD4-binding; when associated
FT with 149-P-G-151 AND 184-P--G-186. No
FT effect on PTEN-binding; when associated
FT with 149-P--G-151 AND 184-P--G-186.
FT MUTAGEN 185 186 TY->AG: Loss of E3 ubiquitin-protein
FT ligase activation; when associated with
FT 149-P--G-151 AND 175-P--G-177. Greatly
FT decreases NEDD4-binding; when associated
FT with 149-P--G-151 AND 175-P--G-177. No
FT effect on PTEN-binding; when associated
FT with 149-P--G-151 AND 175-P--G-177.
SQ SEQUENCE 336 AA; 36390 MW; A7E386C12886321E CRC64;
MARRRSQRVC ASGPSMLNSA RGAPELLRGT ATNAEVSAAA AGATGSEELP PGDRGCRNGG
GRGPAATTSS TGVAVGAEHG EDSLSRKPDP EPGRMDHHQP GTGRYQVLLN EEDNSESSAI
EQPPTSNPAP QIVQAASSAP ALETDSSPPP YSSITVEVPT TSDTEVYGEF YPVPPPYSVA
TSLPTYDEAE KAKAAAMAAA AAETSQRIQE EECPPRDDFS DADQLRVGND GIFMLAFFMA
FIFNWLGFCL SFCITNTIAG RYGAICGFGL SLIKWILIVR FSDYFTGYFN GQYWLWWIFL
VLGLLLFFRG FVNYLKVRNM SESMAAAHRT RYFFLL
//
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