RUBIC_HUMAN
ID RUBIC_HUMAN Reviewed; 972 AA.
AC Q92622; Q96CK5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Run domain Beclin-1-interacting and cysteine-rich domain-containing protein {ECO:0000312|HGNC:HGNC:28991};
DE Short=Rubicon;
DE AltName: Full=Beclin-1 associated RUN domain containing protein;
DE Short=Baron;
GN Name=RUBCN {ECO:0000312|HGNC:HGNC:28991}; Synonyms=KIAA0226;
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 2).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP SEQUENCE REVISION.
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-228 (ISOFORM 1).
RC TISSUE=Thymus;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 239-972.
RC TISSUE=Kidney;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-671, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-266 AND SER-528, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [8]
RP FUNCTION, INTERACTION WITH BECN1; PIK3C3; PIK3R4 AND UVRAG, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19270696; DOI=10.1038/ncb1846;
RA Matsunaga K., Saitoh T., Tabata K., Omori H., Satoh T., Kurotori N.,
RA Maejima I., Shirahama-Noda K., Ichimura T., Isobe T., Akira S., Noda T.,
RA Yoshimori T.;
RT "Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate
RT autophagy at different stages.";
RL Nat. Cell Biol. 11:385-396(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP INVOLVEMENT IN SCAR15.
RX PubMed=20826435; DOI=10.1093/brain/awq181;
RA Assoum M., Salih M.A., Drouot N., H'Mida-Ben Brahim D., Lagier-Tourenne C.,
RA AlDrees A., Elmalik S.A., Ahmed T.S., Seidahmed M.Z., Kabiraj M.M.,
RA Koenig M.;
RT "Rundataxin, a novel protein with RUN and diacylglycerol binding domains,
RT is mutant in a new recessive ataxia.";
RL Brain 133:2439-2447(2010).
RN [11]
RP INTERACTION WITH RAB7 AND PI3K COMPLEX, AND MUTAGENESIS OF CYS-912;
RP CYS-915; HIS-920 AND CYS-923.
RX PubMed=20943950; DOI=10.1091/mbc.e10-06-0495;
RA Tabata K., Matsunaga K., Sakane A., Sasaki T., Noda T., Yoshimori T.;
RT "Rubicon and PLEKHM1 negatively regulate the endocytic/autophagic pathway
RT via a novel Rab7-binding domain.";
RL Mol. Biol. Cell 21:4162-4172(2010).
RN [12]
RP FUNCTION, INTERACTION WITH UVRAG AND RAB7A, AND SUBCELLULAR LOCATION.
RX PubMed=20974968; DOI=10.1073/pnas.1010554107;
RA Sun Q., Westphal W., Wong K.N., Tan I., Zhong Q.;
RT "Rubicon controls endosome maturation as a Rab7 effector.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19338-19343(2010).
RN [13]
RP SUBUNIT, AND FUNCTION.
RX PubMed=21062745; DOI=10.1074/jbc.m110.126425;
RA Sun Q., Zhang J., Fan W., Wong K.N., Ding X., Chen S., Zhong Q.;
RT "The RUN domain of rubicon is important for hVps34 binding, lipid kinase
RT inhibition, and autophagy suppression.";
RL J. Biol. Chem. 286:185-191(2011).
RN [14]
RP FUNCTION, AND INTERACTION WITH BECN1; CYBA; CYBB AND NOX4.
RX PubMed=22423966; DOI=10.1016/j.chom.2012.01.018;
RA Yang C.S., Lee J.S., Rodgers M., Min C.K., Lee J.Y., Kim H.J., Lee K.H.,
RA Kim C.J., Oh B., Zandi E., Yue Z., Kramnik I., Liang C., Jung J.U.;
RT "Autophagy protein Rubicon mediates phagocytic NADPH oxidase activation in
RT response to microbial infection or TLR stimulation.";
RL Cell Host Microbe 11:264-276(2012).
RN [15]
RP FUNCTION, INTERACTION WITH CARD9 AND YWHAB, AND MUTAGENESIS OF SER-248.
RX PubMed=22423967; DOI=10.1016/j.chom.2012.01.019;
RA Yang C.S., Rodgers M., Min C.K., Lee J.S., Kingeter L., Lee J.Y., Jong A.,
RA Kramnik I., Lin X., Jung J.U.;
RT "The autophagy regulator Rubicon is a feedback inhibitor of CARD9-mediated
RT host innate immunity.";
RL Cell Host Microbe 11:277-289(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-248; SER-266;
RP SER-388 AND SER-562, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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: Inhibits PIK3C3 activity; under basal conditions negatively
CC regulates PI3K complex II (PI3KC3-C2) function in autophagy. Negatively
CC regulates endosome maturation and degradative endocytic trafficking and
CC impairs autophagosome maturation process. Can sequester UVRAG from
CC association with a class C Vps complex (possibly the HOPS complex) and
CC negatively regulates Rab7 activation (PubMed:20974968,
CC PubMed:21062745). {ECO:0000269|PubMed:20974968,
CC ECO:0000269|PubMed:21062745}.
CC -!- FUNCTION: Involved in regulation of pathogen-specific host defense of
CC activated macrophages. Following bacterial infection promotes NADH
CC oxidase activity by association with CYBA thereby affecting TLR2
CC signaling and probably other TLR-NOX pathways. Stabilizes the CYBA:CYBB
CC NADPH oxidase heterodimer, increases its association with TLR2 and its
CC phagosome trafficking to induce antimicrobial burst of ROS and
CC production of inflammatory cytokines (PubMed:22423966). Following
CC fungal or viral infection (implicating CLEC7A (dectin-1)-mediated
CC myeloid cell activation or DDX58/RIG-I-dependent sensing of RNA
CC viruses) negatively regulates pro-inflammatory cytokine production by
CC association with CARD9 and sequestering it from signaling complexes
CC (PubMed:22423967). {ECO:0000269|PubMed:22423966,
CC ECO:0000269|PubMed:22423967}.
CC -!- SUBUNIT: Associates with PI3K (PI3KC3/PI3K-III/class III
CC phosphatidylinositol 3-kinase) complex II (PI3KC3-C2) in which the core
CC composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4
CC and BECN1 is associated with UVRAG; in the complex interacts directly
CC with PI3KC3 and UVRAG (PubMed:19270696, PubMed:21062745). Interacts
CC with Rab7 (RAB7A or RAB7B) (GTP-bound form); Rab7 and UVRAG compete for
CC RUBCN binding; can interact simultaneously with Rab7 and the PI3K
CC complex (PubMed:20943950, PubMed:20974968, PubMed:21062745). Interacts
CC with CYBA and CYBB; indicative for the association with the CYBA:CYBB
CC NADPH oxidase heterodimer. Interacts with NOX4 and probably associates
CC with the CYBA:NOX4 complex (PubMed:22423966). Interacts with YWHAB and
CC CARD9 in a competitive and stimulation-dependent manner; RUBCN
CC exchanges interaction from YWHAB to CARD9 upon stimulation with beta-
CC 1,3-glucan (PubMed:22423967). {ECO:0000269|PubMed:19270696,
CC ECO:0000269|PubMed:20943950, ECO:0000269|PubMed:20974968,
CC ECO:0000269|PubMed:21062745, ECO:0000269|PubMed:22423966,
CC ECO:0000269|PubMed:22423967}.
CC -!- INTERACTION:
CC Q92622; X5D778: ANKRD11; NbExp=3; IntAct=EBI-2952709, EBI-17183751;
CC Q92622; Q14457: BECN1; NbExp=15; IntAct=EBI-2952709, EBI-949378;
CC Q92622; O95696: BRD1; NbExp=3; IntAct=EBI-2952709, EBI-714754;
CC Q92622; Q13895: BYSL; NbExp=3; IntAct=EBI-2952709, EBI-358049;
CC Q92622; Q92785: DPF2; NbExp=3; IntAct=EBI-2952709, EBI-359932;
CC Q92622; P00533: EGFR; NbExp=3; IntAct=EBI-2952709, EBI-297353;
CC Q92622; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-2952709, EBI-744099;
CC Q92622; Q3B820: FAM161A; NbExp=3; IntAct=EBI-2952709, EBI-719941;
CC Q92622; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-2952709, EBI-10175124;
CC Q92622; O95995: GAS8; NbExp=3; IntAct=EBI-2952709, EBI-1052570;
CC Q92622; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-2952709, EBI-744782;
CC Q92622; Q8NEB9: PIK3C3; NbExp=7; IntAct=EBI-2952709, EBI-1056470;
CC Q92622; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-2952709, EBI-11955057;
CC Q92622; Q9P2Y5: UVRAG; NbExp=9; IntAct=EBI-2952709, EBI-2952704;
CC Q92622; Q14119: VEZF1; NbExp=3; IntAct=EBI-2952709, EBI-11980193;
CC Q92622; P15622-3: ZNF250; NbExp=3; IntAct=EBI-2952709, EBI-10177272;
CC Q92622; Q5T619: ZNF648; NbExp=3; IntAct=EBI-2952709, EBI-11985915;
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:19270696}.
CC Lysosome {ECO:0000269|PubMed:19270696}. Early endosome
CC {ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:20974968}.
CC Note=Predominantly located in late endosomes/lysosomes, only partially
CC detected in early endosome and not at all in the Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92622-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92622-2; Sequence=VSP_039160, VSP_039161;
CC Name=3;
CC IsoId=Q92622-3; Sequence=VSP_039471, VSP_039472, VSP_039473;
CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 15 (SCAR15)
CC [MIM:615705]: A form of spinocerebellar ataxia, a clinically and
CC genetically heterogeneous group of cerebellar disorders. Patients show
CC progressive incoordination of gait and often poor coordination of
CC hands, speech and eye movements, due to degeneration of the cerebellum
CC with variable involvement of the brainstem and spinal cord. SCAR15
CC patients manifest cerebellar ataxia in early childhood and delayed
CC motor development with delayed walking. Additional features include
CC dysarthria, upper limb involvement, abnormal eye movements, and
CC hyporeflexia. {ECO:0000269|PubMed:20826435}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13215.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86979; BAA13215.3; ALT_INIT; mRNA.
DR EMBL; AC024560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX437131; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC014173; AAH14173.2; -; mRNA.
DR CCDS; CCDS43195.1; -. [Q92622-1]
DR CCDS; CCDS46987.1; -. [Q92622-2]
DR RefSeq; NP_001139114.1; NM_001145642.4. [Q92622-2]
DR RefSeq; NP_055502.1; NM_014687.3. [Q92622-1]
DR PDB; 6WCW; X-ray; 2.80 A; A=699-949.
DR PDBsum; 6WCW; -.
DR AlphaFoldDB; Q92622; -.
DR SMR; Q92622; -.
DR BioGRID; 115062; 58.
DR IntAct; Q92622; 23.
DR STRING; 9606.ENSP00000296343; -.
DR iPTMnet; Q92622; -.
DR PhosphoSitePlus; Q92622; -.
DR BioMuta; RUBCN; -.
DR DMDM; 296439479; -.
DR EPD; Q92622; -.
DR jPOST; Q92622; -.
DR MassIVE; Q92622; -.
DR MaxQB; Q92622; -.
DR PaxDb; Q92622; -.
DR PeptideAtlas; Q92622; -.
DR PRIDE; Q92622; -.
DR ProteomicsDB; 75375; -. [Q92622-1]
DR ProteomicsDB; 75376; -. [Q92622-2]
DR ProteomicsDB; 75377; -. [Q92622-3]
DR Antibodypedia; 54002; 217 antibodies from 27 providers.
DR DNASU; 9711; -.
DR Ensembl; ENST00000273582.9; ENSP00000273582.5; ENSG00000145016.16. [Q92622-2]
DR Ensembl; ENST00000296343.10; ENSP00000296343.5; ENSG00000145016.16. [Q92622-1]
DR GeneID; 9711; -.
DR KEGG; hsa:9711; -.
DR MANE-Select; ENST00000296343.10; ENSP00000296343.5; NM_014687.4; NP_055502.1.
DR UCSC; uc003fyc.3; human. [Q92622-1]
DR CTD; 9711; -.
DR DisGeNET; 9711; -.
DR GeneCards; RUBCN; -.
DR HGNC; HGNC:28991; RUBCN.
DR HPA; ENSG00000145016; Tissue enhanced (brain).
DR MalaCards; RUBCN; -.
DR MIM; 613516; gene.
DR MIM; 615705; phenotype.
DR neXtProt; NX_Q92622; -.
DR OpenTargets; ENSG00000145016; -.
DR Orphanet; 404499; Autosomal recessive cerebellar ataxia-epilepsy-intellectual disability syndrome due to RUBCN deficiency.
DR PharmGKB; PA134887849; -.
DR VEuPathDB; HostDB:ENSG00000145016; -.
DR eggNOG; KOG1829; Eukaryota.
DR eggNOG; KOG4381; Eukaryota.
DR GeneTree; ENSGT00940000160658; -.
DR InParanoid; Q92622; -.
DR OMA; EQVKCNR; -.
DR PhylomeDB; Q92622; -.
DR TreeFam; TF317067; -.
DR PathwayCommons; Q92622; -.
DR SignaLink; Q92622; -.
DR SIGNOR; Q92622; -.
DR BioGRID-ORCS; 9711; 23 hits in 1069 CRISPR screens.
DR ChiTaRS; RUBCN; human.
DR GenomeRNAi; 9711; -.
DR Pharos; Q92622; Tbio.
DR PRO; PR:Q92622; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q92622; protein.
DR Bgee; ENSG00000145016; Expressed in sural nerve and 196 other tissues.
DR ExpressionAtlas; Q92622; baseline and differential.
DR Genevisible; Q92622; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0071985; P:multivesicular body sorting pathway; TAS:ParkinsonsUK-UCL.
DR GO; GO:1901097; P:negative regulation of autophagosome maturation; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0045806; P:negative regulation of endocytosis; IMP:UniProtKB.
DR GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.900; -; 1.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR025258; Zf-RING_9.
DR Pfam; PF02759; RUN; 1.
DR Pfam; PF13901; zf-RING_9; 1.
DR SMART; SM01175; DUF4206; 1.
DR SMART; SM00593; RUN; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR PROSITE; PS50826; RUN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autophagy; Endocytosis; Endosome;
KW Immunity; Lysosome; Neurodegeneration; Phagocytosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..972
FT /note="Run domain Beclin-1-interacting and cysteine-rich
FT domain-containing protein"
FT /id="PRO_0000050736"
FT DOMAIN 48..189
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..180
FT /note="Interaction with PIK3C3"
FT /evidence="ECO:0000269|PubMed:19270696,
FT ECO:0000269|PubMed:21062745"
FT REGION 204..447
FT /note="Interaction with YWHAB"
FT /evidence="ECO:0000269|PubMed:22423967"
FT REGION 233..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..600
FT /note="Interaction with UVRAG"
FT /evidence="ECO:0000269|PubMed:21062745"
FT REGION 307..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..557
FT /note="Interaction with BECN1"
FT /evidence="ECO:0000269|PubMed:22423966"
FT REGION 562..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..625
FT /note="Interaction with CYBA"
FT /evidence="ECO:0000269|PubMed:22423966"
FT REGION 672..760
FT /note="Interaction with CARD9"
FT /evidence="ECO:0000269|PubMed:22423967"
FT REGION 721..972
FT /note="Interaction with Rab7"
FT /evidence="ECO:0000269|PubMed:20943950"
FT COMPBIAS 233..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U62"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9039502"
FT /id="VSP_039160"
FT VAR_SEQ 420
FT /note="P -> PGGPRNITIIVEDPIA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9039502"
FT /id="VSP_039161"
FT VAR_SEQ 596
FT /note="D -> DGSEGSNLTHISKNGLSVSLASMFSD (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039471"
FT VAR_SEQ 883..896
FT /note="LCQAKGFICEFCQN -> VRKSHCSMQLSPCF (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039472"
FT VAR_SEQ 897..972
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039473"
FT MUTAGEN 248
FT /note="S->A: Disrupts interaction with YWHAB."
FT /evidence="ECO:0000269|PubMed:22423967"
FT MUTAGEN 912
FT /note="C->G: Disrupts interaction with Rab7, translocation
FT to cytoplasm; when associated with G-915, L-920 and G-923."
FT /evidence="ECO:0000269|PubMed:20943950"
FT MUTAGEN 915
FT /note="C->G: Disrupts interaction with Rab7, translocation
FT to cytoplasm; when associated with G-912, L-920 and G-923."
FT /evidence="ECO:0000269|PubMed:20943950"
FT MUTAGEN 920
FT /note="H->L: Disrupts interaction with Rab7, translocation
FT to cytoplasm; when associated with G-912,G-915 and G-923."
FT /evidence="ECO:0000269|PubMed:20943950"
FT MUTAGEN 923
FT /note="C->G: Disrupts interaction with Rab7, translocation
FT to cytoplasm; when associated with G-912, G-915 and L-920."
FT /evidence="ECO:0000269|PubMed:20943950"
FT HELIX 708..716
FT /evidence="ECO:0007829|PDB:6WCW"
FT TURN 717..719
FT /evidence="ECO:0007829|PDB:6WCW"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 730..735
FT /evidence="ECO:0007829|PDB:6WCW"
FT TURN 740..742
FT /evidence="ECO:0007829|PDB:6WCW"
FT STRAND 744..746
FT /evidence="ECO:0007829|PDB:6WCW"
FT TURN 748..750
FT /evidence="ECO:0007829|PDB:6WCW"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 759..763
FT /evidence="ECO:0007829|PDB:6WCW"
FT STRAND 771..773
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 775..783
FT /evidence="ECO:0007829|PDB:6WCW"
FT TURN 784..786
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 792..795
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 799..802
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 804..823
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 830..835
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 841..845
FT /evidence="ECO:0007829|PDB:6WCW"
FT STRAND 847..850
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 852..859
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 863..880
FT /evidence="ECO:0007829|PDB:6WCW"
FT TURN 882..884
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 885..887
FT /evidence="ECO:0007829|PDB:6WCW"
FT TURN 892..894
FT /evidence="ECO:0007829|PDB:6WCW"
FT TURN 906..908
FT /evidence="ECO:0007829|PDB:6WCW"
FT STRAND 909..911
FT /evidence="ECO:0007829|PDB:6WCW"
FT STRAND 913..915
FT /evidence="ECO:0007829|PDB:6WCW"
FT STRAND 918..920
FT /evidence="ECO:0007829|PDB:6WCW"
FT TURN 921..923
FT /evidence="ECO:0007829|PDB:6WCW"
FT STRAND 924..927
FT /evidence="ECO:0007829|PDB:6WCW"
FT HELIX 930..942
FT /evidence="ECO:0007829|PDB:6WCW"
SQ SEQUENCE 972 AA; 108622 MW; 4B76166F29F5AF97 CRC64;
MRPEGAGMEL GGGEERLPEE SRREHWQLLG NLKTTVEGLV STNSPNVWSK YGGLERLCRD
MQSILYHGLI RDQACRRQTD YWQFVKDIRW LSPHSALHVE KFISVHENDQ SSADGASERA
VAELWLQHSL QYHCLSAQLR PLLGDRQYIR KFYTDAAFLL SDAHVTAMLQ CLEAVEQNNP
RLLAQIDASM FARKHESPLL VTKSQSLTAL PSSTYTPPNS YAQHSYFGSF SSLHQSVPNN
GSERRSTSFP LSGPPRKPQE SRGHVSPAED QTIQAPPVSV SALARDSPLT PNEMSSSTLT
SPIEASWVSS QNDSPGDASE GPEYLAIGNL DPRGRTASCQ SHSSNAESSS SNLFSSSSSQ
KPDSAASSLG DQEGGGESQL SSVLRRSSFS EGQTLTVTSG AKKSHIRSHS DTSIASRGAP
ESCNDKAKLR GPLPYSGQSS EVSTPSSLYM EYEGGRYLCS GEGMFRRPSE GQSLISYLSE
QDFGSCADLE KENAHFSISE SLIAAIELMK CNMMSQCLEE EEVEEEDSDR EIQELKQKIR
LRRQQIRTKN LLPMYQEAEH GSFRVTSSSS QFSSRDSAQL SDSGSADEVD EFEIQDADIR
RNTASSSKSF VSSQSFSHCF LHSTSAEAVA MGLLKQFEGM QLPAASELEW LVPEHDAPQK
LLPIPDSLPI SPDDGQHADI YKLRIRVRGN LEWAPPRPQI IFNVHPAPTR KIAVAKQNYR
CAGCGIRTDP DYIKRLRYCE YLGKYFCQCC HENAQMAIPS RVLRKWDFSK YYVSNFSKDL
LIKIWNDPLF NVQDINSALY RKVKLLNQVR LLRVQLCHMK NMFKTCRLAK ELLDSFDTVP
GHLTEDLHLY SLNDLTATRK GELGPRLAEL TRAGATHVER CMLCQAKGFI CEFCQNEDDI
IFPFELHKCR TCEECKACYH KACFKSGSCP RCERLQARRE ALARQSLESY LSDYEEEPAE
ALALEAAVLE AT
