ID EEA1_HUMAN Reviewed; 1411 AA. AC Q15075; Q14221; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 09-DEC-2015, entry version 138. DE RecName: Full=Early endosome antigen 1; DE AltName: Full=Endosome-associated protein p162; DE AltName: Full=Zinc finger FYVE domain-containing protein 2; GN Name=EEA1; Synonyms=ZFYVE2; 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, AND VARIANT GLN-810. RC TISSUE=Cervix carcinoma; RX PubMed=7768953; DOI=10.1074/jbc.270.22.13503; RA Mu F.-T., Callaghan J.M., Steele-Mortimer O., Stenmark H., RA Parton R.G., Campbell P.L., McCluskey J., Yeo J.-P., Tock E.P.C., RA Toh B.-H.; RT "EEA1, an early endosome-associated protein. EEA1 is a conserved RT alpha-helical peripheral membrane protein flanked by cysteine RT 'fingers' and contains a calmodulin-binding IQ motif."; RL J. Biol. Chem. 270:13503-13511(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-810. RA Seelig H.P.; RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP PROTEIN SEQUENCE OF 996-1011 AND 1319-1332, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [5] RP INTERACTION WITH RAB5A. RX PubMed=9697774; DOI=10.1038/28879; RA Simonsen A., Lippe R., Christoforidis S., Gaullier J.-M., Brech A., RA Callaghan J.M., Toh B.-H., Murphy C., Zerial M., Stenmark H.; RT "EEA1 links PI(3)K function to Rab5 regulation of endosome fusion."; RL Nature 394:494-498(1998). RN [6] RP INTERACTION WITH RAB5A AND RAB5B. RX PubMed=10491193; DOI=10.1046/j.1432-1327.1999.00743.x; RA Callaghan J.M., Nixon S., Bucci C., Toh B.-H., Stenmark H.; RT "Direct interaction of EEA1 with Rab5b."; RL Eur. J. Biochem. 265:361-366(1999). RN [7] RP INTERACTION WITH STX6, AND SUBCELLULAR LOCATION. RX PubMed=10506127; DOI=10.1074/jbc.274.41.28857; RA Simonsen A., Gaullier J.-M., D'Arrigo A., Stenmark H.; RT "The Rab5 effector EEA1 interacts directly with syntaxin-6."; RL J. Biol. Chem. 274:28857-28860(1999). RN [8] RP MUTAGENESIS OF ASP-1352; ASN-1357; 1367-VAL-THR-1368; ARG-1375 AND RP ARG-1400, HOMODIMERIZATION, AND INTERACTION WITH PHOSPHATIDYLINOSITOL RP 3-PHOSPHATE. RX PubMed=10394369; DOI=10.1016/S1097-2765(01)80013-7; RA Kutateladze T.G., Ogburn K.D., Watson W.T., de Beer T., Emr S.D., RA Burd C.G., Overduin M.; RT "Phosphatidylinositol 3-phosphate recognition by the FYVE domain."; RL Mol. Cell 3:805-811(1999). RN [9] RP MUTAGENESIS OF TRP-1349; CYS-1358; PHE-1365; ARG-1370; ARG-1371; RP HIS-1372; HIS-1373; CYS-1374; ARG-1375; CYS-1377; GLY-1378; CYS-1385; RP ARG-1400 AND CYS-1405, SUBCELLULAR LOCATION, AND INTERACTION WITH RP PHOSPHATIDYLINOSITOL 3-PHOSPHATE. RX PubMed=10807926; DOI=10.1074/jbc.M906554199; RA Gaullier J.-M., Roenning E., Gillooly D.J., Stenmark H.; RT "Interaction of the EEA1 FYVE finger with phosphatidylinositol 3- RT phosphate and early endosomes. Role of conserved residues."; RL J. Biol. Chem. 275:24595-24600(2000). RN [10] RP INTERACTION WITH RAB22A. RX PubMed=11870209; RA Kauppi M., Simonsen A., Bremnes B., Vieira A., Callaghan J.M., RA Stenmark H., Olkkonen V.M.; RT "The small GTPase Rab22 interacts with EEA1 and controls endosomal RT membrane trafficking."; RL J. Cell Sci. 115:899-911(2002). RN [11] RP MUTAGENESIS OF GLU-39; PHE-41; ILE-42; PRO-44; MET-47 AND TYR-60, RP HOMODIMERIZATION, AND INTERACTION WITH RAB5C. RX PubMed=12493736; DOI=10.1074/jbc.M211514200; RA Merithew E., Stone C., Eathiraj S., Lambright D.G.; RT "Determinants of Rab5 interaction with the N-terminus of early RT endosome antigen 1."; RL J. Biol. Chem. 278:8494-8500(2003). RN [12] RP INTERACTION WITH ERBB2. RX PubMed=16314522; DOI=10.1128/MCB.25.24.11005-11018.2005; RA Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G., RA Wang S.C., Hung M.C.; RT "Endosomal transport of ErbB-2: mechanism for nuclear entry of the RT cell surface receptor."; RL Mol. Cell. Biol. 25:11005-11018(2005). RN [13] RP SUBCELLULAR LOCATION, AND INTERACTION WITH RAB31. RX PubMed=19725050; DOI=10.1002/jcp.21911; RA Ng E.L., Ng J.J., Liang F., Tang B.L.; RT "Rab22B is expressed in the CNS astroglia lineage and plays a role in RT epidermal growth factor receptor trafficking in A431 cells."; RL J. Cell. Physiol. 221:716-728(2009). RN [14] RP DOMAIN FYVE-TYPE ZINC-FINGER, AND MUTAGENESIS OF HIS-1372 AND RP HIS-1373. RX PubMed=19296456; DOI=10.1002/prot.22392; RA He J., Vora M., Haney R.M., Filonov G.S., Musselman C.A., Burd C.G., RA Kutateladze A.G., Verkhusha V.V., Stahelin R.V., Kutateladze T.G.; RT "Membrane insertion of the FYVE domain is modulated by pH."; RL Proteins 76:852-860(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] 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). RN [17] RP INTERACTION WITH PLEKHF2, AND SUBCELLULAR LOCATION. RX PubMed=22816767; DOI=10.1111/j.1600-0854.2012.01400.x; RA Pedersen N.M., Raiborg C., Brech A., Skarpen E., Roxrud I., RA Platta H.W., Liestol K., Stenmark H.; RT "The PtdIns3P-binding protein Phafin 2 mediates epidermal growth RT factor receptor degradation by promoting endosome fusion."; RL Traffic 13:1547-1563(2012). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1289-1411 IN COMPLEX WITH RP PHOSPHATIDYLINOSITOL 3-PHOSPHATE, AND HOMODIMERIZATION. RX PubMed=11741531; DOI=10.1016/S1097-2765(01)00385-9; RA Dumas J.J., Merithew E., Sudharshan E., Rajamani D., Hayes S., RA Lawe D., Corvera S., Lambright D.G.; RT "Multivalent endosome targeting by homodimeric EEA1."; RL Mol. Cell 8:947-958(2001). RN [20] RP STRUCTURE BY NMR OF 1346-1410 ALONE AND IN COMPLEX WITH RP PHOSPHATIDYLINOSITOL 3-PHOSPHATE. RX PubMed=11230696; DOI=10.1126/science.291.5509.1793; RA Kutateladze T.G., Overduin M.; RT "Structural mechanism of endosome docking by the FYVE domain."; RL Science 291:1793-1796(2001). CC -!- FUNCTION: Binds phospholipid vesicles containing CC phosphatidylinositol 3-phosphate and participates in endosomal CC trafficking. CC -!- SUBUNIT: Homodimer. Binds STX6. Binds RAB5A, RAB5B, RAB5C and CC RAB22A that have been activated by GTP-binding. Interacts with CC RAB31. Interacts with ERBB2. May interact with PLEKHF2. CC {ECO:0000269|PubMed:10394369, ECO:0000269|PubMed:10491193, CC ECO:0000269|PubMed:10506127, ECO:0000269|PubMed:10807926, CC ECO:0000269|PubMed:11230696, ECO:0000269|PubMed:11741531, CC ECO:0000269|PubMed:11870209, ECO:0000269|PubMed:12493736, CC ECO:0000269|PubMed:16314522, ECO:0000269|PubMed:19725050, CC ECO:0000269|PubMed:22816767, ECO:0000269|PubMed:9697774}. CC -!- INTERACTION: CC P04626:ERBB2; NbExp=5; IntAct=EBI-298113, EBI-641062; CC Q9UL26:RAB22A; NbExp=3; IntAct=EBI-298113, EBI-399456; CC P20339:RAB5A; NbExp=4; IntAct=EBI-298113, EBI-399437; CC P61020:RAB5B; NbExp=3; IntAct=EBI-298113, EBI-399401; CC Q5K651:SAMD9; NbExp=2; IntAct=EBI-298113, EBI-2814750; CC Q69Z37:Samd9l (xeno); NbExp=2; IntAct=EBI-298113, EBI-8784283; CC Q63635:Stx6 (xeno); NbExp=4; IntAct=EBI-298113, EBI-398854; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane; CC Peripheral membrane protein. CC -!- DOMAIN: The FYVE-type zinc finger domain mediates interactions CC with phosphatidylinositol 3-phosphate in membranes of early CC endosomes and penetrates bilayers. The FYVE domain insertion into CC PtdIns(3)P-enriched membranes is substantially increased in acidic CC conditions. {ECO:0000269|PubMed:19296456}. CC -!- MISCELLANEOUS: Antibodies against EEA1 are found in sera from CC patients with subacute cutaneous lupus erythematosus and other CC autoimmune diseases. CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00042}. CC -!- SIMILARITY: Contains 1 FYVE-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00091}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L40157; AAA79121.1; -; mRNA. DR EMBL; X78998; CAA55632.1; -; mRNA. DR EMBL; AC016136; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC021646; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026111; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS31874.1; -. DR PIR; A57013; A57013. DR RefSeq; NP_003557.2; NM_003566.3. DR UniGene; Hs.567367; -. DR PDB; 1HYI; NMR; -; A=1347-1411. DR PDB; 1HYJ; NMR; -; A=1347-1411. DR PDB; 1JOC; X-ray; 2.20 A; A/B=1287-1324, A/B=1326-1411. DR PDB; 3MJH; X-ray; 2.03 A; B/D=36-69. DR PDBsum; 1HYI; -. DR PDBsum; 1HYJ; -. DR PDBsum; 1JOC; -. DR PDBsum; 3MJH; -. DR ProteinModelPortal; Q15075; -. DR SMR; Q15075; 36-69, 1289-1411. DR BioGrid; 113999; 31. DR IntAct; Q15075; 48. DR MINT; MINT-5004646; -. DR STRING; 9606.ENSP00000317955; -. DR PhosphoSite; Q15075; -. DR BioMuta; EEA1; -. DR DMDM; 229462866; -. DR MaxQB; Q15075; -. DR PaxDb; Q15075; -. DR PRIDE; Q15075; -. DR DNASU; 8411; -. DR Ensembl; ENST00000322349; ENSP00000317955; ENSG00000102189. DR GeneID; 8411; -. DR KEGG; hsa:8411; -. DR UCSC; uc001tck.3; human. DR CTD; 8411; -. DR GeneCards; EEA1; -. DR HGNC; HGNC:3185; EEA1. DR HPA; CAB005861; -. DR HPA; CAB018782; -. DR HPA; HPA038158; -. DR HPA; HPA038159; -. DR MIM; 605070; gene. DR neXtProt; NX_Q15075; -. DR PharmGKB; PA27621; -. DR eggNOG; ENOG410IFA7; Eukaryota. DR eggNOG; ENOG4111F3Q; LUCA. DR GeneTree; ENSGT00730000110715; -. DR HOGENOM; HOG000112329; -. DR HOVERGEN; HBG039440; -. DR InParanoid; Q15075; -. DR KO; K12478; -. DR OMA; NANSEAT; -. DR OrthoDB; EOG754HNM; -. DR PhylomeDB; Q15075; -. DR TreeFam; TF329698; -. DR Reactome; R-HSA-168138; Toll Like Receptor 9 (TLR9) Cascade. DR ChiTaRS; EEA1; human. DR EvolutionaryTrace; Q15075; -. DR GeneWiki; EEA1; -. DR GenomeRNAi; 8411; -. DR NextBio; 31490; -. DR PMAP-CutDB; Q15075; -. DR PRO; PR:Q15075; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; Q15075; -. DR CleanEx; HS_EEA1; -. DR ExpressionAtlas; Q15075; baseline and differential. DR Genevisible; Q15075; HS. DR GO; GO:0044308; C:axonal spine; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005969; C:serine-pyruvate aminotransferase complex; IEA:Ensembl. DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB. DR GO; GO:0005516; F:calmodulin binding; NAS:UniProtKB. DR GO; GO:0030742; F:GTP-dependent protein binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB. DR GO; GO:0045022; P:early endosome to late endosome transport; NAS:UniProtKB. DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB. DR GO; GO:0016189; P:synaptic vesicle to endosome fusion; TAS:UniProtKB. DR GO; GO:0006906; P:vesicle fusion; IMP:UniProtKB. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR015880; Znf_C2H2-like. DR InterPro; IPR000306; Znf_FYVE. DR InterPro; IPR017455; Znf_FYVE-rel. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF01363; FYVE; 1. DR SMART; SM00064; FYVE; 1. DR SMART; SM00355; ZnF_C2H2; 1. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS50178; ZF_FYVE; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Complete proteome; Cytoplasm; KW Direct protein sequencing; Endosome; Membrane; Metal-binding; KW Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 1411 Early endosome antigen 1. FT /FTId=PRO_0000098706. FT ZN_FING 41 64 C2H2-type. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 1352 1410 FYVE-type. {ECO:0000255|PROSITE- FT ProRule:PRU00091}. FT COILED 74 1348 {ECO:0000255}. FT COMPBIAS 397 758 Gln/Glu/Lys-rich. FT COMPBIAS 937 1032 Gln/Glu/Lys-rich. FT COMPBIAS 1093 1231 Glu/Lys-rich. FT MOD_RES 70 70 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT VARIANT 810 810 K -> Q (in dbSNP:rs10745623). FT {ECO:0000269|PubMed:7768953, FT ECO:0000269|Ref.2}. FT /FTId=VAR_052980. FT MUTAGEN 39 39 E->A: Strongly reduces interaction with FT RAB5C. {ECO:0000269|PubMed:12493736}. FT MUTAGEN 41 41 F->A: Strongly reduces interaction with FT RAB5C. {ECO:0000269|PubMed:12493736}. FT MUTAGEN 42 42 I->A: Strongly reduces interaction with FT RAB5C. {ECO:0000269|PubMed:12493736}. FT MUTAGEN 44 44 P->A: Strongly reduces interaction with FT RAB5C. {ECO:0000269|PubMed:12493736}. FT MUTAGEN 47 47 M->A: Strongly reduces interaction with FT RAB5C. {ECO:0000269|PubMed:12493736}. FT MUTAGEN 60 60 Y->A: Strongly reduces interaction with FT RAB5C. {ECO:0000269|PubMed:12493736}. FT MUTAGEN 1349 1349 W->A: Reduces phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10807926}. FT MUTAGEN 1352 1352 D->V: Reduces phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10394369}. FT MUTAGEN 1357 1357 N->D: Reduces phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10394369}. FT MUTAGEN 1358 1358 C->S: Abolishes phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10807926}. FT MUTAGEN 1365 1365 F->A: Strongly reduces FT phosphatidylinositol 3-phosphate binding FT and endosomal location. FT {ECO:0000269|PubMed:10807926}. FT MUTAGEN 1367 1368 VT->EE,GG: Abolishes phosphatidylinositol FT 3-phosphate binding and endosomal FT location. {ECO:0000269|PubMed:10394369}. FT MUTAGEN 1370 1370 R->A: Abolishes endosomal location. FT {ECO:0000269|PubMed:10807926}. FT MUTAGEN 1371 1371 R->A: Abolishes phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10807926}. FT MUTAGEN 1372 1372 H->A: Abolishes endosomal location. FT Abolishes pH sensitivity of the FYVE-type FT zinc finger domain; when associated with FT A-1373. {ECO:0000269|PubMed:10807926, FT ECO:0000269|PubMed:19296456}. FT MUTAGEN 1373 1373 H->A: Abolishes phosphatidylinositol 3- FT phosphate binding and endosomal location. FT Abolishes pH sensitivity of the FYVE-type FT zinc finger domain; when associated with FT A-1372. {ECO:0000269|PubMed:10807926, FT ECO:0000269|PubMed:19296456}. FT MUTAGEN 1374 1374 C->A: Abolishes phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10807926}. FT MUTAGEN 1375 1375 R->G: Abolishes phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10394369, FT ECO:0000269|PubMed:10807926}. FT MUTAGEN 1377 1377 C->A: Abolishes phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10807926}. FT MUTAGEN 1378 1378 G->A: Abolishes phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10807926}. FT MUTAGEN 1385 1385 C->A: Abolishes phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10807926}. FT MUTAGEN 1400 1400 R->G: Strongly reduces FT phosphatidylinositol 3-phosphate binding FT and abolishes endosomal location. FT {ECO:0000269|PubMed:10394369, FT ECO:0000269|PubMed:10807926}. FT MUTAGEN 1405 1405 C->S: Abolishes phosphatidylinositol 3- FT phosphate binding and endosomal location. FT {ECO:0000269|PubMed:10807926}. FT CONFLICT 255 255 C -> S (in Ref. 1; AAA79121). FT {ECO:0000305}. FT CONFLICT 258 259 LQ -> FE (in Ref. 1; AAA79121). FT {ECO:0000305}. FT CONFLICT 277 277 A -> S (in Ref. 1; AAA79121). FT {ECO:0000305}. FT CONFLICT 284 284 A -> R (in Ref. 1; AAA79121). FT {ECO:0000305}. FT CONFLICT 520 520 D -> E (in Ref. 1; AAA79121). FT {ECO:0000305}. FT CONFLICT 575 576 EQ -> DE (in Ref. 1; AAA79121). FT {ECO:0000305}. FT CONFLICT 583 584 KL -> NV (in Ref. 1; AAA79121). FT {ECO:0000305}. FT CONFLICT 680 680 Q -> H (in Ref. 1; AAA79121). FT {ECO:0000305}. FT CONFLICT 1325 1325 Missing (in Ref. 1; AAA79121). FT {ECO:0000305}. FT STRAND 38 42 {ECO:0000244|PDB:3MJH}. FT TURN 44 46 {ECO:0000244|PDB:3MJH}. FT STRAND 49 52 {ECO:0000244|PDB:3MJH}. FT HELIX 53 63 {ECO:0000244|PDB:3MJH}. FT STRAND 65 67 {ECO:0000244|PDB:3MJH}. FT HELIX 1290 1324 {ECO:0000244|PDB:1JOC}. FT HELIX 1326 1346 {ECO:0000244|PDB:1JOC}. FT HELIX 1352 1354 {ECO:0000244|PDB:1JOC}. FT TURN 1359 1361 {ECO:0000244|PDB:1JOC}. FT STRAND 1367 1369 {ECO:0000244|PDB:1JOC}. FT STRAND 1371 1373 {ECO:0000244|PDB:1HYI}. FT TURN 1375 1377 {ECO:0000244|PDB:1JOC}. FT STRAND 1380 1382 {ECO:0000244|PDB:1HYI}. FT HELIX 1383 1385 {ECO:0000244|PDB:1JOC}. FT STRAND 1388 1390 {ECO:0000244|PDB:1JOC}. FT TURN 1393 1396 {ECO:0000244|PDB:1HYI}. FT STRAND 1399 1401 {ECO:0000244|PDB:1JOC}. FT HELIX 1403 1408 {ECO:0000244|PDB:1JOC}. SQ SEQUENCE 1411 AA; 162466 MW; 51BA418F561E3411 CRC64; MLRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL GSADELFKHY EAVHDAGNDS GHGGESNLAL KRDDVTLLRQ EVQDLQASLK EEKWYSEELK KELEKYQGLQ QQEAKPDGLV TDSSAELQSL EQQLEEAQTE NFNIKQMKDL FEQKAAQLAT EIADIKSKYD EERSLREAAE QKVTRLTEEL NKEATVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM TLERERESEK LKDECKKLQS QYASSEATIS QLRSELAKGP QEVAVYVQEL QKLKSSVNEL TQKNQTLTEN LLKKEQDYTK LEEKHNEESV SKKNIQATLH QKDLDCQQLQ SRLSASETSL HRIHVELSEK GEATQKLKEE LSEVETKYQH LKAEFKQLQQ QREEKEQHGL QLQSEINQLH SKLLETERQL GEAHGRLKEQ RQLSSEKLMD KEQQVADLQL KLSRLEEQLK EKVTNSTELQ HQLDKTKQQH QEQQALQQST TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKSKENIS LLEKEREDLY AKIQAGEGET AVLNQLQEKN HTLQEQVTQL TEKLKNQSES HKQAQENLHD QVQEQKAHLR AAQDRVLSLE TSVNELNSQL NESKEKVSQL DIQIKAKTEL LLSAEAAKTA QRADLQNHLD TAQNALQDKQ QELNKITTQL DQVTAKLQDK QEHCSQLESH LKEYKEKYLS LEQKTEELEG QIKKLEADSL EVKASKEQAL QDLQQQRQLN TDLELRATEL SKQLEMEKEI VSSTRLDLQK KSEALESIKQ KLTKQEEEKK ILKQDFETLS QETKIQHEEL NNRIQTTVTE LQKVKMEKEA LMTELSTVKD KLSKVSDSLK NSKSEFEKEN QKGKAAILDL EKTCKELKHQ LQVQMENTLK EQKELKKSLE KEKEASHQLK LELNSMQEQL IQAQNTLKQN EKEEQQLQGN INELKQSSEQ KKKQIEALQG ELKIAVLQKT ELENKLQQQL TQAAQELAAE KEKISVLQNN YEKSQETFKQ LQSDFYGRES ELLATRQDLK SVEEKLSLAQ EDLISNRNQI GNQNKLIQEL KTAKATLEQD SAKKEQQLQE RCKALQDIQK EKSLKEKELV NEKSKLAEIE EIKCRQEKEI TKLNEELKSH KLESIKEITN LKDAKQLLIQ QKLELQGKAD SLKAAVEQEK RNQQILKDQV KKEEEELKKE FIEKEAKLHS EIKEKEVGMK KHEENEAKLT MQITALNENL GTVKKEWQSS QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL KGEGEIEKLQ TKVLELQRKL DNTTAAVQEL GRENQSLQIK HTQALNRKWA EDNEVQNCMA CGKGFSVTVR RHHCRQCGNI FCAECSAKNA LTPSSKKPVR VCDACFNDLQ G //