LST2_HUMAN
ID LST2_HUMAN Reviewed; 887 AA.
AC Q9HCC9; B2RP83; B3KX50; B7Z1Q7; B7Z2G9; B7Z2M2; B7ZB19; E9PB54; E9PB64;
AC E9PG77; Q7Z6J3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Lateral signaling target protein 2 homolog;
DE Short=hLst2;
DE AltName: Full=Zinc finger FYVE domain-containing protein 28;
GN Name=ZFYVE28; Synonyms=KIAA1643, LST2;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-672.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5), AND
RP VARIANTS ASN-603 AND PRO-672.
RC TISSUE=Brain, Cerebellum, and Thymus;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 6; 7 AND 8), AND
RP VARIANT PRO-672.
RC TISSUE=Leiomyosarcoma, Ovary, and Pancreas;
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 FUNCTION, SUBCELLULAR LOCATION, DOMAIN FYVE-TYPE ZINC-FINGER, INTERACTION
RP WITH TRIM3, PHOSPHORYLATION AT SER-586 AND THR-870, UBIQUITINATION AT
RP LYS-87, AND MUTAGENESIS OF LYS-87 AND CYS-823.
RX PubMed=19460345; DOI=10.1016/j.devcel.2009.03.015;
RA Mosesson Y., Chetrit D., Schley L., Berghoff J., Ziv T., Carvalho S.,
RA Milanezi F., Admon A., Schmitt F., Ehrlich M., Yarden Y.;
RT "Monoubiquitinylation regulates endosomal localization of Lst2, a negative
RT regulator of EGF receptor signaling.";
RL Dev. Cell 16:687-698(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334 AND THR-516, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR)
CC signaling. Acts by promoting EGFR degradation in endosomes when not
CC monoubiquitinated. {ECO:0000269|PubMed:19460345}.
CC -!- SUBUNIT: Interacts with TRIM3. {ECO:0000269|PubMed:19460345}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19460345}.
CC Early endosome membrane {ECO:0000269|PubMed:19460345}. Note=Localizes
CC to early endosome membrane in absence of Lys-87 monoubiquitination.
CC Localizes to cytosol when monoubiquitinated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q9HCC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCC9-2; Sequence=VSP_037616;
CC Name=3;
CC IsoId=Q9HCC9-3; Sequence=VSP_037615;
CC Name=4;
CC IsoId=Q9HCC9-4; Sequence=VSP_037615, VSP_037616;
CC Name=5;
CC IsoId=Q9HCC9-5; Sequence=VSP_037614;
CC Name=6;
CC IsoId=Q9HCC9-6; Sequence=VSP_045805, VSP_045806;
CC Name=7;
CC IsoId=Q9HCC9-7; Sequence=VSP_046092, VSP_046093, VSP_046094;
CC Name=8;
CC IsoId=Q9HCC9-8; Sequence=VSP_037615, VSP_046379;
CC -!- DOMAIN: The FYVE-type zinc finger mediates the interaction with
CC phosphatidylinositol 3-phosphate (PI3P) and localization to early
CC endosome membranes when not monoubiquitinated at Lys-87.
CC {ECO:0000269|PubMed:19460345}.
CC -!- PTM: Monoubiquitination at Lys-87 prevents binding to
CC phosphatidylinositol 3-phosphate (PI3P) and localization to early
CC endosome membranes.
CC -!- SIMILARITY: Belongs to the lst-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53664.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB13469.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB046863; BAB13469.1; ALT_INIT; mRNA.
DR EMBL; AK126692; BAG54362.1; -; mRNA.
DR EMBL; AK293775; BAH11593.1; -; mRNA.
DR EMBL; AK294710; BAH11855.1; -; mRNA.
DR EMBL; AK294874; BAH11908.1; -; mRNA.
DR EMBL; AK316484; BAH14855.1; -; mRNA.
DR EMBL; AL158068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032605; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC035793; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC053664; AAH53664.1; ALT_INIT; mRNA.
DR EMBL; BC137309; AAI37310.1; -; mRNA.
DR EMBL; BC137310; AAI37311.1; -; mRNA.
DR CCDS; CCDS33942.1; -. [Q9HCC9-1]
DR CCDS; CCDS54708.1; -. [Q9HCC9-3]
DR CCDS; CCDS54709.1; -. [Q9HCC9-8]
DR CCDS; CCDS54710.1; -. [Q9HCC9-7]
DR CCDS; CCDS54711.1; -. [Q9HCC9-2]
DR CCDS; CCDS54712.1; -. [Q9HCC9-6]
DR RefSeq; NP_001166127.1; NM_001172656.1. [Q9HCC9-2]
DR RefSeq; NP_001166128.1; NM_001172657.1. [Q9HCC9-6]
DR RefSeq; NP_001166129.1; NM_001172658.1. [Q9HCC9-7]
DR RefSeq; NP_001166130.1; NM_001172659.1. [Q9HCC9-3]
DR RefSeq; NP_001166131.1; NM_001172660.1. [Q9HCC9-8]
DR RefSeq; NP_066023.2; NM_020972.2. [Q9HCC9-1]
DR RefSeq; XP_016863994.1; XM_017008505.1. [Q9HCC9-5]
DR AlphaFoldDB; Q9HCC9; -.
DR SMR; Q9HCC9; -.
DR BioGRID; 121752; 8.
DR IntAct; Q9HCC9; 1.
DR STRING; 9606.ENSP00000290974; -.
DR iPTMnet; Q9HCC9; -.
DR PhosphoSitePlus; Q9HCC9; -.
DR BioMuta; ZFYVE28; -.
DR DMDM; 251757462; -.
DR EPD; Q9HCC9; -.
DR jPOST; Q9HCC9; -.
DR MassIVE; Q9HCC9; -.
DR PaxDb; Q9HCC9; -.
DR PeptideAtlas; Q9HCC9; -.
DR PRIDE; Q9HCC9; -.
DR ProteomicsDB; 19146; -.
DR ProteomicsDB; 19155; -.
DR ProteomicsDB; 20260; -.
DR ProteomicsDB; 81671; -. [Q9HCC9-1]
DR ProteomicsDB; 81672; -. [Q9HCC9-2]
DR ProteomicsDB; 81673; -. [Q9HCC9-3]
DR ProteomicsDB; 81674; -. [Q9HCC9-4]
DR ProteomicsDB; 81675; -. [Q9HCC9-5]
DR Antibodypedia; 22351; 93 antibodies from 20 providers.
DR DNASU; 57732; -.
DR Ensembl; ENST00000290974.7; ENSP00000290974.3; ENSG00000159733.14. [Q9HCC9-1]
DR Ensembl; ENST00000503000.1; ENSP00000423694.1; ENSG00000159733.14. [Q9HCC9-6]
DR Ensembl; ENST00000509171.5; ENSP00000422638.1; ENSG00000159733.14. [Q9HCC9-7]
DR Ensembl; ENST00000511071.5; ENSP00000425706.1; ENSG00000159733.14. [Q9HCC9-2]
DR Ensembl; ENST00000515169.5; ENSP00000425766.1; ENSG00000159733.14. [Q9HCC9-8]
DR Ensembl; ENST00000515312.5; ENSP00000426299.1; ENSG00000159733.14. [Q9HCC9-3]
DR GeneID; 57732; -.
DR KEGG; hsa:57732; -.
DR MANE-Select; ENST00000290974.7; ENSP00000290974.3; NM_020972.3; NP_066023.2.
DR UCSC; uc003gex.3; human. [Q9HCC9-1]
DR CTD; 57732; -.
DR DisGeNET; 57732; -.
DR GeneCards; ZFYVE28; -.
DR HGNC; HGNC:29334; ZFYVE28.
DR HPA; ENSG00000159733; Tissue enriched (brain).
DR MIM; 614176; gene.
DR neXtProt; NX_Q9HCC9; -.
DR OpenTargets; ENSG00000159733; -.
DR PharmGKB; PA134904138; -.
DR VEuPathDB; HostDB:ENSG00000159733; -.
DR eggNOG; KOG1819; Eukaryota.
DR GeneTree; ENSGT00940000157217; -.
DR HOGENOM; CLU_007360_1_0_1; -.
DR InParanoid; Q9HCC9; -.
DR OMA; PELGYDR; -.
DR OrthoDB; 451347at2759; -.
DR PhylomeDB; Q9HCC9; -.
DR TreeFam; TF320752; -.
DR PathwayCommons; Q9HCC9; -.
DR SignaLink; Q9HCC9; -.
DR BioGRID-ORCS; 57732; 11 hits in 1082 CRISPR screens.
DR ChiTaRS; ZFYVE28; human.
DR GenomeRNAi; 57732; -.
DR Pharos; Q9HCC9; Tbio.
DR PRO; PR:Q9HCC9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9HCC9; protein.
DR Bgee; ENSG00000159733; Expressed in right hemisphere of cerebellum and 127 other tissues.
DR ExpressionAtlas; Q9HCC9; baseline and differential.
DR Genevisible; Q9HCC9; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IMP:UniProtKB.
DR CDD; cd15731; FYVE_LST2; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR043269; FYVE_LST2.
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 SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endosome; Isopeptide bond; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..887
FT /note="Lateral signaling target protein 2 homolog"
FT /id="PRO_0000098722"
FT ZN_FING 817..879
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 308..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 826
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 839
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 842
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 847
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 850
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 869
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 872
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 586
FT /note="Phosphoserine; by MAP2K"
FT /evidence="ECO:0000269|PubMed:19460345"
FT MOD_RES 870
FT /note="Phosphothreonine; by MAP2K"
FT /evidence="ECO:0000269|PubMed:19460345"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19460345"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037614"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 3, isoform 4 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037615"
FT VAR_SEQ 14..60
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046092"
FT VAR_SEQ 204..234
FT /note="RALDFGYLTQDMIDDYEPALMFSIPRLAIVC -> S (in isoform 2
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037616"
FT VAR_SEQ 205..219
FT /note="ALDFGYLTQDMIDDY -> NGKGVLKFMWNCNGP (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046093"
FT VAR_SEQ 220..887
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046094"
FT VAR_SEQ 234..887
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046379"
FT VAR_SEQ 235..287
FT /note="GLVVYADGPLNLDRKVEDMSELFRPFHTLLRKIRDLLQTLTEEELHTLERNL
FT C -> PLLPAHPRTRAGATAHVACRMVAGSSSGALTHPPVSKQGVISALLRPLPELPP
FT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045805"
FT VAR_SEQ 288..887
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045806"
FT VARIANT 603
FT /note="S -> N (in dbSNP:rs17768776)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_052988"
FT VARIANT 672
FT /note="S -> P (in dbSNP:rs661301)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_052989"
FT MUTAGEN 87
FT /note="K->R: Abolishes monoubiquitination and promotes
FT localization to early endosomes."
FT /evidence="ECO:0000269|PubMed:19460345"
FT MUTAGEN 823
FT /note="C->A: Abolishes binding to phosphatidylinositol 3-
FT phosphate (PI3P)."
FT /evidence="ECO:0000269|PubMed:19460345"
FT CONFLICT 157
FT /note="M -> I (in Ref. 2; BAG54362)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="L -> P (in Ref. 2; BAH14855)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="M -> I (in Ref. 2; BAH11855)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="E -> G (in Ref. 2; BAG54362)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="E -> D (in Ref. 2; BAH14855)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="A -> G (in Ref. 2; BAG54362)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="A -> P (in Ref. 2; BAH11855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 887 AA; 96490 MW; EAF3A26A50FF26F5 CRC64;
MMNRFRKWLY KPKRSDPQLL ARFYYADEEL NQVAAELDSL DGRKDPQRCT LLVSQFRSCQ
DNVLNIINQI MDECIPQDRA PRDFCVKFPE EIRHDNLAGQ LWFGAECLAA GSIIMNRELE
SMAMRPLAKE LTRSLEDVRG ALRDQALRDL NTYTEKMREA LRHFDVLFAE FELSYVSAMV
PVKSPREYYV QQEVIVLFCE TVERALDFGY LTQDMIDDYE PALMFSIPRL AIVCGLVVYA
DGPLNLDRKV EDMSELFRPF HTLLRKIRDL LQTLTEEELH TLERNLCISQ DVEFPIRADV
QGPAALAPAL SAPLPPEGPL SAKAKDPDAE LACSMQYDDQ ELEQLSRMVH RAGDEMSSLL
SPPIACQSPA HRPGAEGSPG GEASPGRPRL RSGSDEEERV FFMDDVEGTA EALARPESPA
GPFGWAGSTW ADPQEKGQGG PGGAAGISLP ASEKEEDLSN NNLEAEGTDG ASLAGTSSCS
CLDSRLHLDG WEVGADDAET AEMIAHRTGG MKLSATVIFN PKSPTSLDSA VATQEAASEP
VAEGMDGGPH KLSTGATNCL LHSCVCCGSC GDSREDVVER LREKCSPGGV IGASYAAGLA
KASDRAPERQ EEAPPPSEDA SNGREPKAPT SDKCLPHTSG SQVDTASGLQ GEAGVAGQQE
PEARELHAGS PSAHEAPQAL SGSSSSTAGS CSSDKMGPEA APAATHAAPQ ATREKIRSRF
HGSHDLIHRL FVCISGVADQ LQTNYASDLR SILKTLFEVM ATKPETDDKE KLRKVTQTLR
SAALEDCALC QETLSSSELA AKTRDGDFED PPEWVPDEAC GFCTACKAPF TVIRRKHHCR
SCGKIFCSRC SSHSAPLPRY GQVKPVRVCT HCYMFHVTPF YSDKAGL
