ID   RUFY1_HUMAN             Reviewed;         708 AA.
AC   Q96T51; Q59FF3; Q71S93; Q9H6I3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=RUN and FYVE domain-containing protein 1;
DE   AltName: Full=FYVE-finger protein EIP1;
DE   AltName: Full=La-binding protein 1;
DE   AltName: Full=Rab4-interacting protein;
DE   AltName: Full=Zinc finger FYVE domain-containing protein 12;
GN   Name=RUFY1; Synonyms=RABIP4, ZFYVE12;
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), INTERACTION WITH SSB; RAB4 AND
RP   RAB5, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   FUNCTION.
RX   PubMed=14617813; DOI=10.1091/mbc.e03-05-0343;
RA   Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J.,
RA   van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.;
RT   "Rabip4' is an effector of rab5 and rab4 and regulates transport through
RT   early endosomes.";
RL   Mol. Biol. Cell 15:611-624(2004).
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 MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-708 (ISOFORM 1), TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, INTERACTION WITH BMX, PHOSPHORYLATION AT TYR-389 AND
RP   TYR-400, AND MUTAGENESIS OF TYR-389 AND TYR-400.
RX   PubMed=11877430; DOI=10.1074/jbc.m111933200;
RA   Yang J., Kim O., Wu J., Qiu Y.;
RT   "Interaction between tyrosine kinase Etk and a RUN-domain and FYVE-domain
RT   containing protein RUFY1. A possible role of Etk in regulation of vesicle
RT   trafficking.";
RL   J. Biol. Chem. 277:30219-30226(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-708 (ISOFORM 3).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   DOMAIN FYVE-TYPE ZINC-FINGER.
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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620, AND IDENTIFICATION BY
RP   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., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [10]
RP   STRUCTURE BY NMR OF 627-708.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the FYVE domain in zinc finger FYVE domain-
RT   containing protein 12.";
RL   Submitted (OCT-2007) to the PDB data bank.
RN   [11]
RP   VARIANT [LARGE SCALE ANALYSIS] PHE-267.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol
CC       3-phosphate and participates in early endosomal trafficking.
CC       {ECO:0000269|PubMed:14617813}.
CC   -!- SUBUNIT: Interacts with BMX. May interact with SSB. Interacts with RAB4
CC       and RAB5 that have been activated by GTP-binding.
CC       {ECO:0000269|PubMed:11877430, ECO:0000269|PubMed:14617813}.
CC   -!- INTERACTION:
CC       Q96T51; O75928: PIAS2; NbExp=3; IntAct=EBI-3941207, EBI-348555;
CC       Q96T51; Q96DA2: RAB39B; NbExp=4; IntAct=EBI-3941207, EBI-9089467;
CC       Q96T51; Q96QF0: RAB3IP; NbExp=3; IntAct=EBI-3941207, EBI-747844;
CC       Q96T51; Q9BRA2: TXNDC17; NbExp=3; IntAct=EBI-3941207, EBI-1055906;
CC       Q96T51; Q68CQ4: UTP25; NbExp=5; IntAct=EBI-3941207, EBI-747711;
CC       Q96T51-2; P00973-2: OAS1; NbExp=3; IntAct=EBI-12192715, EBI-12081862;
CC       Q96T51-2; Q9H714-3: RUBCNL; NbExp=2; IntAct=EBI-12192715, EBI-9088146;
CC       Q96T51-2; Q96T51-2: RUFY1; NbExp=5; IntAct=EBI-12192715, EBI-12192715;
CC       Q96T51-2; P36406: TRIM23; NbExp=3; IntAct=EBI-12192715, EBI-740098;
CC       Q96T51-2; Q68CQ4: UTP25; NbExp=6; IntAct=EBI-12192715, EBI-747711;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane; Peripheral
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=rabip4';
CC         IsoId=Q96T51-1; Sequence=Displayed;
CC       Name=2; Synonyms=rabip4;
CC         IsoId=Q96T51-2; Sequence=VSP_019785;
CC       Name=3;
CC         IsoId=Q96T51-3; Sequence=VSP_019786, VSP_019787;
CC   -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in lung,
CC       testis, kidney and brain. {ECO:0000269|PubMed:11877430}.
CC   -!- DOMAIN: The FYVE-type zinc finger domain mediates interactions with
CC       phosphatidylinositol 3-phosphate in membranes of early endosomes and
CC       penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched
CC       membranes is substantially increased in acidic conditions.
CC       {ECO:0000269|PubMed:19296456}.
CC   -!- PTM: Phosphorylation on Tyr-389 and/or Tyr-400 is required for
CC       interaction with BMX and endosomal targeting.
CC       {ECO:0000269|PubMed:11877430}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK50771.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB15276.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AF312367; AAQ14554.1; -; mRNA.
DR   EMBL; AK025904; BAB15276.1; ALT_INIT; mRNA.
DR   EMBL; AK075021; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC032571; AAH32571.1; -; mRNA.
DR   EMBL; AF361055; AAK50771.1; ALT_FRAME; mRNA.
DR   EMBL; AB209507; BAD92744.1; -; mRNA.
DR   CCDS; CCDS34312.1; -. [Q96T51-2]
DR   CCDS; CCDS4445.2; -. [Q96T51-1]
DR   RefSeq; NP_001035541.1; NM_001040451.2. [Q96T51-2]
DR   RefSeq; NP_001035542.1; NM_001040452.2. [Q96T51-2]
DR   RefSeq; NP_079434.3; NM_025158.4. [Q96T51-1]
DR   RefSeq; XP_016865384.1; XM_017009895.1.
DR   PDB; 2YQM; NMR; -; A=627-708.
DR   PDB; 2YW8; X-ray; 3.00 A; A=627-708.
DR   PDBsum; 2YQM; -.
DR   PDBsum; 2YW8; -.
DR   AlphaFoldDB; Q96T51; -.
DR   SMR; Q96T51; -.
DR   BioGRID; 123193; 478.
DR   IntAct; Q96T51; 47.
DR   MINT; Q96T51; -.
DR   STRING; 9606.ENSP00000325594; -.
DR   GlyGen; Q96T51; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96T51; -.
DR   MetOSite; Q96T51; -.
DR   PhosphoSitePlus; Q96T51; -.
DR   SwissPalm; Q96T51; -.
DR   BioMuta; RUFY1; -.
DR   DMDM; 110282993; -.
DR   EPD; Q96T51; -.
DR   jPOST; Q96T51; -.
DR   MassIVE; Q96T51; -.
DR   MaxQB; Q96T51; -.
DR   PaxDb; 9606-ENSP00000325594; -.
DR   PeptideAtlas; Q96T51; -.
DR   ProteomicsDB; 78184; -. [Q96T51-1]
DR   ProteomicsDB; 78185; -. [Q96T51-2]
DR   ProteomicsDB; 78186; -. [Q96T51-3]
DR   Pumba; Q96T51; -.
DR   Antibodypedia; 29480; 253 antibodies from 32 providers.
DR   DNASU; 80230; -.
DR   Ensembl; ENST00000319449.9; ENSP00000325594.4; ENSG00000176783.15. [Q96T51-1]
DR   Ensembl; ENST00000393438.6; ENSP00000377087.2; ENSG00000176783.15. [Q96T51-2]
DR   Ensembl; ENST00000437570.6; ENSP00000390025.2; ENSG00000176783.15. [Q96T51-2]
DR   Ensembl; ENST00000639102.1; ENSP00000491803.1; ENSG00000284260.2. [Q96T51-2]
DR   Ensembl; ENST00000639436.1; ENSP00000491925.1; ENSG00000284260.2. [Q96T51-2]
DR   Ensembl; ENST00000639909.2; ENSP00000492748.1; ENSG00000284260.2. [Q96T51-1]
DR   GeneID; 80230; -.
DR   KEGG; hsa:80230; -.
DR   MANE-Select; ENST00000319449.9; ENSP00000325594.4; NM_025158.5; NP_079434.3.
DR   UCSC; uc003mka.3; human. [Q96T51-1]
DR   AGR; HGNC:19760; -.
DR   CTD; 80230; -.
DR   DisGeNET; 80230; -.
DR   GeneCards; RUFY1; -.
DR   HGNC; HGNC:19760; RUFY1.
DR   HPA; ENSG00000176783; Low tissue specificity.
DR   MIM; 610327; gene.
DR   neXtProt; NX_Q96T51; -.
DR   OpenTargets; ENSG00000176783; -.
DR   PharmGKB; PA134944787; -.
DR   VEuPathDB; HostDB:ENSG00000176783; -.
DR   eggNOG; KOG1729; Eukaryota.
DR   eggNOG; KOG4381; Eukaryota.
DR   GeneTree; ENSGT00940000158334; -.
DR   HOGENOM; CLU_014576_3_0_1; -.
DR   InParanoid; Q96T51; -.
DR   OMA; THCKQCK; -.
DR   OrthoDB; 5385125at2759; -.
DR   PhylomeDB; Q96T51; -.
DR   TreeFam; TF323904; -.
DR   PathwayCommons; Q96T51; -.
DR   Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR   SignaLink; Q96T51; -.
DR   SIGNOR; Q96T51; -.
DR   BioGRID-ORCS; 80230; 12 hits in 1153 CRISPR screens.
DR   ChiTaRS; RUFY1; human.
DR   EvolutionaryTrace; Q96T51; -.
DR   GeneWiki; RUFY1; -.
DR   GenomeRNAi; 80230; -.
DR   Pharos; Q96T51; Tbio.
DR   PRO; PR:Q96T51; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q96T51; Protein.
DR   Bgee; ENSG00000176783; Expressed in monocyte and 97 other cell types or tissues.
DR   ExpressionAtlas; Q96T51; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   GO; GO:0030100; P:regulation of endocytosis; IPI:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
DR   CDD; cd15758; FYVE_RUFY1; 1.
DR   CDD; cd17694; RUN_RUFY1; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.58.900; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047331; FYVE_RUFY1.
DR   InterPro; IPR047335; RUFY1-3.
DR   InterPro; IPR004012; Run_dom.
DR   InterPro; IPR037213; Run_dom_sf.
DR   InterPro; IPR047330; RUN_RUFY1.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45956:SF4; RUN AND FYVE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR45956; RUN AND FYVE DOMAIN-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF02759; RUN; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00593; RUN; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF140741; RUN domain-like; 1.
DR   PROSITE; PS50826; RUN; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   Genevisible; Q96T51; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Endocytosis;
KW   Endosome; Lipid-binding; Membrane; Metal-binding; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.
FT   CHAIN           1..708
FT                   /note="RUN and FYVE domain-containing protein 1"
FT                   /id="PRO_0000097530"
FT   DOMAIN          139..271
FT                   /note="RUN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT   ZN_FING         642..700
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..625
FT                   /note="Interaction with RAB4"
FT                   /evidence="ECO:0000250"
FT   COILED          321..374
FT                   /evidence="ECO:0000255"
FT   COILED          405..617
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         648
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         651
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         664
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         667
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         672
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         675
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         692
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         695
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   MOD_RES         389
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:11877430"
FT   MOD_RES         400
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:11877430"
FT   MOD_RES         620
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1..108
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019785"
FT   VAR_SEQ         343..412
FT                   /note="LSAATDRICSLQEEQQQLREQNELIRERSEKSVEITKQDTKVELETYKQTRQ
FT                   GLDEMYSDVWKQLKEEKK -> EERMKGQDKGGLSRGRELAASCPAVSLLDTSCLLLAG
FT                   GGCSALLRLSTAFSCNRPNLLTSRRTAAVKRTK (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_019786"
FT   VAR_SEQ         413..708
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_019787"
FT   VARIANT         267
FT                   /note="C -> F (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035985"
FT   VARIANT         298
FT                   /note="H -> Q (in dbSNP:rs6879322)"
FT                   /id="VAR_051327"
FT   MUTAGEN         389
FT                   /note="Y->F: Abolishes phosphorylation and endosomal
FT                   targeting; when associated with F-400."
FT                   /evidence="ECO:0000269|PubMed:11877430"
FT   MUTAGEN         400
FT                   /note="Y->F: Abolishes phosphorylation and endosomal
FT                   targeting; when associated with F-389."
FT                   /evidence="ECO:0000269|PubMed:11877430"
FT   CONFLICT        519..528
FT                   /note="SHKLQQELGG -> TTSCSRSWAV (in Ref. 1; AAQ14554)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        570
FT                   /note="D -> N (in Ref. 1; AAQ14554)"
FT                   /evidence="ECO:0000305"
FT   TURN            649..651
FT                   /evidence="ECO:0007829|PDB:2YW8"
FT   STRAND          657..659
FT                   /evidence="ECO:0007829|PDB:2YQM"
FT   STRAND          661..663
FT                   /evidence="ECO:0007829|PDB:2YQM"
FT   TURN            665..667
FT                   /evidence="ECO:0007829|PDB:2YW8"
FT   STRAND          670..672
FT                   /evidence="ECO:0007829|PDB:2YQM"
FT   HELIX           674..676
FT                   /evidence="ECO:0007829|PDB:2YW8"
FT   STRAND          678..680
FT                   /evidence="ECO:0007829|PDB:2YW8"
FT   STRAND          683..687
FT                   /evidence="ECO:0007829|PDB:2YQM"
FT   STRAND          689..691
FT                   /evidence="ECO:0007829|PDB:2YW8"
FT   HELIX           693..698
FT                   /evidence="ECO:0007829|PDB:2YW8"
SQ   SEQUENCE   708 AA;  79818 MW;  6697B4BC108AD54F CRC64;
     MADREGGCAA GRGRELEPEL EPGPGPGSAL EPGEEFEIVD RSQLPGPGDL RSATRPRAAE
     GWSAPILTLA RRATGNLSAS CGSALRAAAG LGGGDSGDGT ARAASKCQMM EERANLMHMM
     KLSIKVLLQS ALSLGRSLDA DHAPLQQFFV VMEHCLKHGL KVKKSFIGQN KSFFGPLELV
     EKLCPEASDI ATSVRNLPEL KTAVGRGRAW LYLALMQKKL ADYLKVLIDN KHLLSEFYEP
     EALMMEEEGM VIVGLLVGLN VLDANLCLKG EDLDSQVGVI DFSLYLKDVQ DLDGGKEHER
     ITDVLDQKNY VEELNRHLSC TVGDLQTKID GLEKTNSKLQ EELSAATDRI CSLQEEQQQL
     REQNELIRER SEKSVEITKQ DTKVELETYK QTRQGLDEMY SDVWKQLKEE KKVRLELEKE
     LELQIGMKTE MEIAMKLLEK DTHEKQDTLV ALRQQLEEVK AINLQMFHKA QNAESSLQQK
     NEAITSFEGK TNQVMSSMKQ MEERLQHSER ARQGAEERSH KLQQELGGRI GALQLQLSQL
     HEQCSSLEKE LKSEKEQRQA LQRELQHEKD TSSLLRMELQ QVEGLKKELR ELQDEKAELQ
     KICEEQEQAL QEMGLHLSQS KLKMEDIKEV NQALKGHAWL KDDEATHCRQ CEKEFSISRR
     KHHCRNCGHI FCNTCSSNEL ALPSYPKPVR VCDSCHTLLL QRCSSTAS
//