NFIP2_HUMAN
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 03-AUG-2022, entry version 159.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., 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., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., 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., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., 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., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA 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., 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 [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 from
RT 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 project:
RT 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 homeostasis
RT by a ubiquitin-dependent mechanism involving Ndfips and 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 NDFIP
RT proteins.";
RL EMBO Rep. 10:501-507(2009).
RN [9]
RP FUNCTION, INTERACTION WITH LYN; NDFIP1; NEDD4; PTEN AND SRC, SUBCELLULAR
RP LOCATION, TOPOLOGY, PHOSPHORYLATION AT TYR-151; TYR-167; TYR-171 AND
RP TYR-177, AND MUTAGENESIS OF 149-PRO--TYR-151; TYR-167; 175-PRO--TYR-177 AND
RP 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 ubiquitin
RT 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 result, may
CC control many cellular processes. Recruits ITCH, NEDD4 and SMURF2 to
CC endosomal membranes. Negatively regulates KCNH2 potassium channel
CC activity by decreasing its cell-surface expression and interfering with
CC channel maturation through recruitment of NEDD4L to the Golgi apparatus
CC and multivesicular body where it mediates KCNH2 degradation
CC (PubMed:26363003). May modulate EGFR signaling. Together with NDFIP1,
CC limits the cytokine signaling and expansion of effector Th2 T-cells by
CC promoting 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 domain-
CC containing E3 ubiquitin-protein ligases, including NEDD4
CC (PubMed:12796489). Interacts with NEDD4L (PubMed:26363003). Interacts
CC with PTEN. When phosphorylated at Tyr-167, interacts with SRC and LYN
CC SH2 domain. May thus act as a scaffold that recruits SRC to NDFIP1,
CC enhancing NDFIP1 phosphorylation. Interacts with SLC11A2/DMT1
CC (PubMed:18776082). May interact with phosphorylated EGFR. Interacts
CC with KCNH2 (PubMed:26363003). {ECO:0000250,
CC ECO:0000269|PubMed:12796489, ECO:0000269|PubMed:18776082,
CC ECO:0000269|PubMed:20534535, ECO:0000269|PubMed:26363003}.
CC -!- INTERACTION:
CC Q9NV92; Q16637: SMN2; NbExp=3; IntAct=EBI-2933200, EBI-395421;
CC Q9NV92; P07919: UQCRH; NbExp=3; IntAct=EBI-2933200, EBI-1224427;
CC Q9NV92; P46937: YAP1; NbExp=2; IntAct=EBI-2933200, EBI-1044059;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:18776082};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18776082}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:12796489,
CC ECO:0000269|PubMed:26363003}. Endosome, multivesicular body membrane
CC {ECO:0000269|PubMed:26363003}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, heart, skeletal muscle,
CC kidney, liver and placenta. {ECO:0000269|PubMed:12796489}.
CC -!- INDUCTION: By T-cell activation. {ECO:0000269|PubMed:12796489}.
CC -!- DOMAIN: The PPxY motifs are required for E3 ubiquitin-protein ligase
CC activation and for ubiquitination.
CC -!- PTM: Ubiquitinated by NEDD4 and ITCH. Also ubiquitinated by NEDD4L.
CC Ubiquitination by NEDD4 or NEDD4L does not affect turnover (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Undergoes transient tyrosine-phosphorylation following EGF
CC stimulation, most probably catalyzed by SRC. Phosphorylation on Tyr-
CC 151, Tyr-171 and Tyr-177 are dependent on the phosphorylation on Tyr-
CC 167. Also phosphorylated by LYN and FYN. {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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355603; -; NOT_ANNOTATED_CDS; 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 AlphaFoldDB; Q9NV92; -.
DR BioGRID; 120074; 60.
DR IntAct; Q9NV92; 14.
DR STRING; 9606.ENSP00000480798; -.
DR GlyGen; Q9NV92; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NV92; -.
DR PhosphoSitePlus; Q9NV92; -.
DR BioMuta; NDFIP2; -.
DR DMDM; 73921209; -.
DR EPD; Q9NV92; -.
DR jPOST; Q9NV92; -.
DR MassIVE; Q9NV92; -.
DR MaxQB; Q9NV92; -.
DR PaxDb; Q9NV92; -.
DR PeptideAtlas; Q9NV92; -.
DR PRIDE; Q9NV92; -.
DR ProteomicsDB; 82762; -.
DR Antibodypedia; 1950; 59 antibodies from 19 providers.
DR DNASU; 54602; -.
DR Ensembl; ENST00000218652.12; ENSP00000218652.7; ENSG00000102471.15.
DR Ensembl; ENST00000612570.4; ENSP00000480798.1; ENSG00000102471.15.
DR GeneID; 54602; -.
DR KEGG; hsa:54602; -.
DR MANE-Select; ENST00000218652.12; ENSP00000218652.7; NM_019080.3; NP_061953.2.
DR UCSC; uc001vlf.4; human.
DR CTD; 54602; -.
DR DisGeNET; 54602; -.
DR GeneCards; NDFIP2; -.
DR HGNC; HGNC:18537; NDFIP2.
DR HPA; ENSG00000102471; Low tissue specificity.
DR MIM; 610041; gene.
DR neXtProt; NX_Q9NV92; -.
DR OpenTargets; ENSG00000102471; -.
DR PharmGKB; PA134953250; -.
DR VEuPathDB; HostDB:ENSG00000102471; -.
DR eggNOG; KOG4812; Eukaryota.
DR GeneTree; ENSGT00390000012721; -.
DR HOGENOM; CLU_074980_0_0_1; -.
DR InParanoid; Q9NV92; -.
DR OMA; NMTENMA; -.
DR OrthoDB; 1495850at2759; -.
DR PhylomeDB; Q9NV92; -.
DR TreeFam; TF324911; -.
DR PathwayCommons; Q9NV92; -.
DR SignaLink; Q9NV92; -.
DR SIGNOR; Q9NV92; -.
DR BioGRID-ORCS; 54602; 19 hits in 1087 CRISPR screens.
DR ChiTaRS; NDFIP2; human.
DR GeneWiki; NDFIP2; -.
DR GenomeRNAi; 54602; -.
DR Pharos; Q9NV92; Tbio.
DR PRO; PR:Q9NV92; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9NV92; protein.
DR Bgee; ENSG00000102471; Expressed in secondary oocyte and 184 other tissues.
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:0050699; F:WW domain binding; IPI:BHF-UCL.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
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; HMP:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0007034; P:vacuolar transport; IEA:InterPro.
DR InterPro; IPR019325; NEDD4/Bsd2.
DR PANTHER; PTHR13396; PTHR13396; 1.
PE 1: Evidence at protein level;
KW Endosome; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..336
FT /note="NEDD4 family-interacting protein 2"
FT /id="PRO_0000096794"
FT TOPO_DOM 1..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..336
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..151
FT /note="Interaction with NEDD4"
FT /evidence="ECO:0000250"
FT MOTIF 148..151
FT /note="PPxY motif 1"
FT MOTIF 174..177
FT /note="PPxY motif 2"
FT MOTIF 184..186
FT /note="PPxY motif 3"
FT COMPBIAS 80..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 186
FT /note="Not phosphorylated by SRC"
FT MOD_RES 151
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:20534535"
FT MOD_RES 167
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:20534535"
FT MOD_RES 171
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:20534535"
FT MOD_RES 177
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:20534535"
FT VARIANT 124
FT /note="P -> S (in dbSNP:rs55887763)"
FT /id="VAR_061687"
FT VARIANT 136
FT /note="A -> V (in dbSNP:rs11549502)"
FT /evidence="ECO:0000269|PubMed:10574461,
FT ECO:0000269|PubMed:12761501, ECO:0000269|PubMed:15489334"
FT /id="VAR_023414"
FT MUTAGEN 150..151
FT /note="PY->AG: Loss of E3 ubiquitin-protein ligase
FT activation; when associated with 175-P--G-177 AND 184-P--G-
FT 186. Greatly decreases NEDD4-binding; when associated with
FT 175-P--G-177 and 184-P--G-186. No effect on PTEN-binding;
FT when associated with 175-P--G-177 AND 184-P--G-186."
FT MUTAGEN 167
FT /note="Y->F: Loss of NDFIP2 phosphorylation by SRC."
FT /evidence="ECO:0000269|PubMed:20534535"
FT MUTAGEN 176..177
FT /note="PY->AG: Loss of E3 ubiquitin-protein ligase
FT activation; when associated with 149-P--G-151 AND 184-P--G-
FT 186. Greatly decreases NEDD4-binding; when associated with
FT 149-P-G-151 AND 184-P--G-186. No effect on PTEN-binding;
FT when associated with 149-P--G-151 AND 184-P--G-186."
FT MUTAGEN 185..186
FT /note="TY->AG: Loss of E3 ubiquitin-protein ligase
FT activation; when associated with 149-P--G-151 AND 175-P--G-
FT 177. Greatly decreases NEDD4-binding; when associated with
FT 149-P--G-151 AND 175-P--G-177. No effect on PTEN-binding;
FT when associated 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
