ID RBCC1_HUMAN Reviewed; 1594 AA. AC Q8TDY2; Q86YR4; Q8WVU9; Q92601; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 3. DT 27-MAR-2024, entry version 175. DE RecName: Full=RB1-inducible coiled-coil protein 1 {ECO:0000305}; DE AltName: Full=FAK family kinase-interacting protein of 200 kDa; DE Short=FIP200 {ECO:0000303|PubMed:28890335}; GN Name=RB1CC1 {ECO:0000312|HGNC:HGNC:15574}; Synonyms=KIAA0203, RBICC; 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), VARIANT THR-234, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, INDUCTION, AND INDUCTION OF RB1 EXPRESSION. RC TISSUE=Osteosarcoma; RX PubMed=11850849; DOI=10.1038/sj.onc.1205178; RA Chano T., Ikegawa S., Kontani K., Okabe H., Baldini N., Saeki Y.; RT "Identification of RB1CC1, a novel human gene that can induce RB1 in RT various human cells."; RL Oncogene 21:1295-1298(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-234. RC TISSUE=Myeloid; 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 [3] 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-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-234. RC TISSUE=Uterus; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1377-1594, FUNCTION, SUBCELLULAR LOCATION, RP AND INTERACTION WITH PTK2/FAK1 AND PTK2B/PYK2. RX PubMed=10769033; DOI=10.1083/jcb.149.2.423; RA Ueda H., Abbi S., Zheng C., Guan J.-L.; RT "Suppression of Pyk2 kinase and cellular activities by FIP200."; RL J. Cell Biol. 149:423-430(2000). RN [7] RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION. RX PubMed=12163359; DOI=10.1016/s0002-9440(10)64190-9; RA Chano T., Saeki Y., Serra M., Matsumoto K., Okabe H.; RT "Preferential expression of RB1-inducible coiled-coil 1 in terminal RT differentiated musculoskeletal cells."; RL Am. J. Pathol. 161:359-364(2002). RN [8] RP CHARACTERIZATION, AND FUNCTION. RX PubMed=12095676; DOI=10.1016/s0378-1119(02)00585-1; RA Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A., Saeki Y., RA Okabe H.; RT "Isolation, characterization and mapping of the mouse and human RB1CC1 RT genes."; RL Gene 291:29-34(2002). RN [9] RP FUNCTION, AND INTERACTION WITH PTK2/FAK1. RX PubMed=12221124; DOI=10.1091/mbc.e02-05-0295; RA Abbi S., Ueda H., Zheng C., Cooper L.A., Zhao J., Christopher R., RA Guan J.L.; RT "Regulation of focal adhesion kinase by a novel protein inhibitor FIP200."; RL Mol. Biol. Cell 13:3178-3191(2002). RN [10] RP INVOLVEMENT IN BREAST CANCER. RX PubMed=12068296; DOI=10.1038/ng911; RA Chano T., Kontani K., Teramoto K., Okabe H., Ikegawa S.; RT "Truncating mutations of RB1CC1 in human breast cancer."; RL Nat. Genet. 31:285-288(2002). RN [11] RP FUNCTION. RX PubMed=14533007; RA Kontani K., Chano T., Ozaki Y., Tezuka N., Sawai S., Fujino S., Saeki Y., RA Okabe H.; RT "RB1CC1 suppresses cell cycle progression through RB1 expression in human RT neoplastic cells."; RL Int. J. Mol. Med. 12:767-769(2003). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-624; SER-647 AND RP SER-653, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP SUBUNIT. RX PubMed=19597335; DOI=10.4161/auto.5.7.9296; RA Hosokawa N., Sasaki T., Iemura S.I., Natsume T., Hara T., Mizushima N.; RT "Atg101, a novel mammalian autophagy protein interacting with Atg13."; RL Autophagy 5:973-979(2009). RN [16] RP INTERACTION WITH ULK1 AND ATG13. RX PubMed=19211835; DOI=10.1091/mbc.e08-12-1248; RA Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y., RA Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N., RA Mizushima N.; RT "Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex RT required for autophagy."; RL Mol. Biol. Cell 20:1981-1991(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-257, AND RP IDENTIFICATION BY 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 [18] RP IDENTIFICATION 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] 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 [20] RP FUNCTION, AND INTERACTION WITH TP53. RX PubMed=21775823; DOI=10.4161/cc.10.16.16868; RA Morselli E., Shen S., Ruckenstuhl C., Bauer M.A., Marino G., Galluzzi L., RA Criollo A., Michaud M., Maiuri M.C., Chano T., Madeo F., Kroemer G.; RT "p53 inhibits autophagy by interacting with the human ortholog of yeast RT Atg17, RB1CC1/FIP200."; RL Cell Cycle 10:2763-2769(2011). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP INTERACTION WITH GABARAP AND GABARAPL1. RX PubMed=23043107; DOI=10.1074/jbc.m112.378109; RA Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B., RA Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.; RT "ATG8 family proteins act as scaffolds for assembly of the ULK complex: RT sequence requirements for LC3-interacting region (LIR) motifs."; RL J. Biol. Chem. 287:39275-39290(2012). RN [23] RP FUNCTION, AND INTERACTION WITH ATG16L1. RX PubMed=23392225; DOI=10.1038/embor.2013.6; RA Nishimura T., Kaizuka T., Cadwell K., Sahani M.H., Saitoh T., Akira S., RA Virgin H.W., Mizushima N.; RT "FIP200 regulates targeting of Atg16L1 to the isolation membrane."; RL EMBO Rep. 14:284-291(2013). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-229; SER-237; RP SER-243; SER-253; SER-257; SER-266; SER-647; SER-652; SER-1222; SER-1370 RP AND SER-1484, 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). RN [25] 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., 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 [26] RP INTERACTION WITH ATG16L1. RX PubMed=24954904; DOI=10.1016/j.molcel.2014.05.021; RA Dooley H.C., Razi M., Polson H.E., Girardin S.E., Wilson M.I., Tooze S.A.; RT "WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and RT pathogen clearance by recruiting Atg12-5-16L1."; RL Mol. Cell 55:238-252(2014). RN [27] RP INTERACTION WITH COP1. RX PubMed=23289756; DOI=10.1186/1471-2091-14-1; RA Kobayashi S., Yoneda-Kato N., Itahara N., Yoshida A., Kato J.Y.; RT "The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian RT autophagy."; RL BMC Biochem. 14:1-1(2013). RN [28] RP INTERACTION WITH ATG16L1. RX PubMed=23262492; DOI=10.1038/nsmb.2475; RA Gammoh N., Florey O., Overholtzer M., Jiang X.; RT "Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex- RT dependent and -independent autophagy."; RL Nat. Struct. Mol. Biol. 20:144-149(2013). RN [29] RP INTERACTION WITH C9ORF72. RX PubMed=27334615; DOI=10.15252/embj.201694401; RA Webster C.P., Smith E.F., Bauer C.S., Moller A., Hautbergue G.M., RA Ferraiuolo L., Myszczynska M.A., Higginbottom A., Walsh M.J., RA Whitworth A.J., Kaspar B.K., Meyer K., Shaw P.J., Grierson A.J., RA De Vos K.J.; RT "The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate RT initiation of autophagy."; RL EMBO J. 35:1656-1676(2016). RN [30] RP INTERACTION WITH WIPI2 AND ATG16L1, AND SUBCELLULAR LOCATION. RX PubMed=28890335; DOI=10.1016/j.molcel.2017.08.005; RA Zhao Y.G., Chen Y., Miao G., Zhao H., Qu W., Li D., Wang Z., Liu N., Li L., RA Chen S., Liu P., Feng D., Zhang H.; RT "The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates SERCA Activity RT to Control ER-Isolation Membrane Contacts for Autophagosome Formation."; RL Mol. Cell 67:974.e6-989.e6(2017). RN [31] RP INTERACTION WITH WDR45B, AND SUBCELLULAR LOCATION. RX PubMed=28561066; DOI=10.1038/ncomms15637; RA Bakula D., Mueller A.J., Zuleger T., Takacs Z., Franz-Wachtel M., RA Thost A.K., Brigger D., Tschan M.P., Frickey T., Robenek H., Macek B., RA Proikas-Cezanne T.; RT "WIPI3 and WIPI4 beta-propellers are scaffolds for LKB1-AMPK-TSC signalling RT circuits in the control of autophagy."; RL Nat. Commun. 8:15637-15637(2017). RN [32] RP INTERACTION WITH ATG13. RX PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035; RA Miao G., Zhang Y., Chen D., Zhang H.; RT "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy RT by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1."; RL Mol. Cell 0:0-0(2019). RN [33] RP INTERACTION WITH TAX1BP1. RX PubMed=33226137; DOI=10.15252/embj.2020104948; RA Ohnstad A.E., Delgado J.M., North B.J., Nasa I., Kettenbach A.N., RA Schultz S.W., Shoemaker C.J.; RT "Receptor-mediated clustering of FIP200 bypasses the role of LC3 lipidation RT in autophagy."; RL EMBO J. 39:e104948-e104948(2020). RN [34] RP INTERACTION WITH TAX1BP1. RX PubMed=34471133; DOI=10.1038/s41467-021-25572-w; RA Turco E., Savova A., Gere F., Ferrari L., Romanov J., Schuschnig M., RA Martens S.; RT "Reconstitution defines the roles of p62, NBR1 and TAX1BP1 in ubiquitin RT condensate formation and autophagy initiation."; RL Nat. Commun. 12:5212-5212(2021). RN [35] RP INTERACTION WITH MOSPD2; VAPA AND VAPB, FFAT MOTIF, PHOSPHORYLATION AT RP SER-734, AND DOMAIN. RX PubMed=33124732; DOI=10.15252/embj.2019104369; RA Di Mattia T., Martinet A., Ikhlef S., McEwen A.G., Nomine Y., Wendling C., RA Poussin-Courmontagne P., Voilquin L., Eberling P., Ruffenach F., RA Cavarelli J., Slee J., Levine T.P., Drin G., Tomasetto C., Alpy F.; RT "FFAT motif phosphorylation controls formation and lipid transfer function RT of inter-organelle contacts."; RL EMBO J. 39:e104369-e104369(2020). RN [36] RP VARIANT CYS-1514. RX PubMed=17224074; DOI=10.1186/bcr1637; RA Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., RA Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., RA Boerresen-Dale A.-L.; RT "Somatic sequence alterations in twenty-one genes selected by expression RT profile analysis of breast carcinomas."; RL Breast Cancer Res. 9:R5-R5(2007). CC -!- FUNCTION: Involved in autophagy (PubMed:21775823). Regulates early CC events but also late events of autophagosome formation through direct CC interaction with Atg16L1 (PubMed:23392225). Required for the formation CC of the autophagosome-like double-membrane structure that surrounds the CC Salmonella-containing vacuole (SCV) during S.typhimurium infection and CC subsequent xenophagy (By similarity). Involved in repair of DNA damage CC caused by ionizing radiation, which subsequently improves cell survival CC by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and CC PTK2B/PYK2 kinase activity, affecting their downstream signaling CC pathways (PubMed:10769033, PubMed:12221124). Plays a role as a CC modulator of TGF-beta-signaling by restricting substrate specificity of CC RNF111 (By similarity). Functions as a DNA-binding transcription factor CC (PubMed:12095676). Is a potent regulator of the RB1 pathway through CC induction of RB1 expression (PubMed:14533007). Plays a crucial role in CC muscular differentiation (PubMed:12163359). Plays an indispensable role CC in fetal hematopoiesis and in the regulation of neuronal homeostasis CC (By similarity). {ECO:0000250|UniProtKB:Q9ESK9, CC ECO:0000269|PubMed:10769033, ECO:0000269|PubMed:12095676, CC ECO:0000269|PubMed:12163359, ECO:0000269|PubMed:12221124, CC ECO:0000269|PubMed:14533007, ECO:0000269|PubMed:21775823, CC ECO:0000269|PubMed:23392225}. CC -!- SUBUNIT: Part of a complex consisting of ATG13/KIAA0652, ULK1 and CC RB1CC1 (PubMed:19597335, PubMed:19211835). This complex associates with CC ATG101 (PubMed:19597335, PubMed:19211835). Interacts with PTK2/FAK1 and CC PTK2B/PYK2 (PubMed:10769033, PubMed:12221124). Interacts with GABARAP CC and GABARAPL1 (PubMed:23043107). Interacts with ATG16L1; the CC interaction is required for ULK1 complex-dependent autophagy CC (PubMed:24954904, PubMed:23262492, PubMed:23392225, PubMed:28890335). CC Interacts with RNF111, SKI and SMAD7 (By similarity). Interacts with CC COP1 in the cytoplasm of proliferating cells in response to UV CC stimulation (PubMed:23289756). Interacts with TP53 (PubMed:21775823). CC Interacts with C9orf72 (PubMed:27334615). Interacts with WDR45B CC (PubMed:28561066). Interacts with ATG13; this interaction is increased CC in the absence of TMEM39A (PubMed:31806350). Interacts with WIPI2 CC (PubMed:28890335). Interacts with TAX1BP1 (PubMed:33226137, CC PubMed:34471133). Interacts (via phosphorylated FFAT motif) with CC MOSPD2, VAPA and VAPB (PubMed:33124732). {ECO:0000250|UniProtKB:Q9ESK9, CC ECO:0000269|PubMed:10769033, ECO:0000269|PubMed:12221124, CC ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19597335, CC ECO:0000269|PubMed:21775823, ECO:0000269|PubMed:23043107, CC ECO:0000269|PubMed:23262492, ECO:0000269|PubMed:23289756, CC ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:24954904, CC ECO:0000269|PubMed:27334615, ECO:0000269|PubMed:28561066, CC ECO:0000269|PubMed:28890335, ECO:0000269|PubMed:31806350, CC ECO:0000269|PubMed:33124732, ECO:0000269|PubMed:33226137, CC ECO:0000269|PubMed:34471133}. CC -!- INTERACTION: CC Q8TDY2; Q9BSB4: ATG101; NbExp=7; IntAct=EBI-1047793, EBI-2946739; CC Q8TDY2; O75143: ATG13; NbExp=10; IntAct=EBI-1047793, EBI-2798775; CC Q8TDY2; Q676U5: ATG16L1; NbExp=6; IntAct=EBI-1047793, EBI-535909; CC Q8TDY2; Q9H1Y0: ATG5; NbExp=3; IntAct=EBI-1047793, EBI-1047414; CC Q8TDY2; Q96LT7-1: C9orf72; NbExp=7; IntAct=EBI-1047793, EBI-16693635; CC Q8TDY2; Q96LT7-2: C9orf72; NbExp=6; IntAct=EBI-1047793, EBI-16693673; CC Q8TDY2; A7MCY6: TBKBP1; NbExp=2; IntAct=EBI-1047793, EBI-359969; CC Q8TDY2; O75385: ULK1; NbExp=11; IntAct=EBI-1047793, EBI-908831; CC Q8TDY2; Q8C0J2-3: Atg16l1; Xeno; NbExp=6; IntAct=EBI-1047793, EBI-16029274; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11850849}. Cytoplasm CC {ECO:0000269|PubMed:10769033}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q9ESK9}. Preautophagosomal structure CC {ECO:0000269|PubMed:28561066}. Lysosome {ECO:0000269|PubMed:28561066}. CC Note=Under starvation conditions, is localized to puncate structures CC primarily representing the isolation membrane that sequesters a portion CC of the cytoplasm resulting in the formation of an autophagosome. CC {ECO:0000269|PubMed:28561066, ECO:0000269|PubMed:28890335}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8TDY2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TDY2-2; Sequence=VSP_040097; CC -!- TISSUE SPECIFICITY: Expression levels correlated closely with those of CC RB1 in cancer cell lines as well as in various normal human tissues. CC Abundantly expressed in human musculoskeletal and cultured osteosarcoma CC cells. {ECO:0000269|PubMed:11850849, ECO:0000269|PubMed:12163359}. CC -!- DEVELOPMENTAL STAGE: Expression was difficult to detect in immature CC proliferating chondroblasts or myogenic cells in embryos, but became CC obvious and prominent concomitantly with the maturation of osteocytes, CC chondrocytes, and skeletal muscle cells. Expression in these CC musculoskeletal cells increased with RB1 expression, which is linked to CC the terminal differentiation of many tissues and cells. The CC introduction of the wild-type protein decreased the formation of CC macroscopic colonies in a cell growth assay. CC {ECO:0000269|PubMed:12163359}. CC -!- DOMAIN: The FFAT motif is involved in the interaction with MOSPD2, VAPA CC and VAPB and its phosphorylation regulates these interactions. CC {ECO:0000269|PubMed:33124732}. CC -!- PTM: Phosphorylation at Ser-734 of the FFAT motif activates interaction CC with MOSPD2, VAPA and VAPB. {ECO:0000269|PubMed:33124732}. CC -!- MISCELLANEOUS: Probably involved in the tumorigenesis of breast cancer. CC RB1CC1 is frequently mutated in breast cancer and shows characteristics CC of a classical tumor suppressor gene. CC -!- SIMILARITY: Belongs to the ATG17 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA13194.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AB059622; BAB69690.1; -; mRNA. DR EMBL; D86958; BAA13194.2; ALT_INIT; mRNA. DR EMBL; AC090814; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC113139; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC017556; AAH17556.1; -; mRNA. DR EMBL; AY173931; AAO17545.1; -; mRNA. DR CCDS; CCDS34892.1; -. [Q8TDY2-1] DR CCDS; CCDS47856.1; -. [Q8TDY2-2] DR RefSeq; NP_001077086.1; NM_001083617.1. [Q8TDY2-2] DR RefSeq; NP_055596.3; NM_014781.4. [Q8TDY2-1] DR RefSeq; XP_011515945.1; XM_011517643.2. [Q8TDY2-1] DR RefSeq; XP_016869596.1; XM_017014107.1. [Q8TDY2-2] DR PDB; 6DCE; X-ray; 1.56 A; A=1494-1594. DR PDB; 6GMA; X-ray; 3.20 A; A/B/C/D/E/F=1458-1594. DR PDB; 7CZG; X-ray; 1.80 A; A/B/C/D=1490-1594. DR PDB; 7CZM; X-ray; 2.00 A; A/B=1490-1594. DR PDB; 7D0E; X-ray; 1.40 A; A=1490-1594. DR PDB; 7EA2; X-ray; 2.14 A; A/B=1490-1594. DR PDB; 7EAA; X-ray; 2.60 A; C/D=1286-1395. DR PDB; 8SOI; EM; 4.20 A; A/B=1-600. DR PDB; 8SQZ; EM; 5.85 A; A/B=1-640. DR PDB; 8SRM; EM; 4.46 A; A/B=1-640. DR PDB; 8SRQ; EM; 6.20 A; A/B=1-600. DR PDBsum; 6DCE; -. DR PDBsum; 6GMA; -. DR PDBsum; 7CZG; -. DR PDBsum; 7CZM; -. DR PDBsum; 7D0E; -. DR PDBsum; 7EA2; -. DR PDBsum; 7EAA; -. DR PDBsum; 8SOI; -. DR PDBsum; 8SQZ; -. DR PDBsum; 8SRM; -. DR PDBsum; 8SRQ; -. DR AlphaFoldDB; Q8TDY2; -. DR EMDB; EMD-40658; -. DR EMDB; EMD-40715; -. DR EMDB; EMD-40735; -. DR EMDB; EMD-40738; -. DR SMR; Q8TDY2; -. DR BioGRID; 115160; 353. DR ComplexPortal; CPX-373; ULK1-ATG13-RB1CC1-ATG101 autophagy initiation complex. DR CORUM; Q8TDY2; -. DR DIP; DIP-45969N; -. DR IntAct; Q8TDY2; 92. DR MINT; Q8TDY2; -. DR STRING; 9606.ENSP00000025008; -. DR GlyGen; Q8TDY2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8TDY2; -. DR MetOSite; Q8TDY2; -. DR PhosphoSitePlus; Q8TDY2; -. DR BioMuta; RB1CC1; -. DR DMDM; 160359050; -. DR EPD; Q8TDY2; -. DR jPOST; Q8TDY2; -. DR MassIVE; Q8TDY2; -. DR MaxQB; Q8TDY2; -. DR PaxDb; 9606-ENSP00000025008; -. DR PeptideAtlas; Q8TDY2; -. DR ProteomicsDB; 74368; -. [Q8TDY2-1] DR ProteomicsDB; 74369; -. [Q8TDY2-2] DR Pumba; Q8TDY2; -. DR Antibodypedia; 24432; 360 antibodies from 30 providers. DR DNASU; 9821; -. DR Ensembl; ENST00000025008.10; ENSP00000025008.5; ENSG00000023287.13. [Q8TDY2-1] DR Ensembl; ENST00000435644.6; ENSP00000396067.2; ENSG00000023287.13. [Q8TDY2-2] DR GeneID; 9821; -. DR KEGG; hsa:9821; -. DR MANE-Select; ENST00000025008.10; ENSP00000025008.5; NM_014781.5; NP_055596.3. DR UCSC; uc003xre.5; human. [Q8TDY2-1] DR AGR; HGNC:15574; -. DR CTD; 9821; -. DR DisGeNET; 9821; -. DR GeneCards; RB1CC1; -. DR HGNC; HGNC:15574; RB1CC1. DR HPA; ENSG00000023287; Low tissue specificity. DR MalaCards; RB1CC1; -. DR MIM; 606837; gene. DR neXtProt; NX_Q8TDY2; -. DR OpenTargets; ENSG00000023287; -. DR PharmGKB; PA34248; -. DR VEuPathDB; HostDB:ENSG00000023287; -. DR eggNOG; KOG4572; Eukaryota. DR GeneTree; ENSGT00390000015871; -. DR HOGENOM; CLU_003711_0_0_1; -. DR InParanoid; Q8TDY2; -. DR OMA; RWIMYVE; -. DR OrthoDB; 2878794at2759; -. DR PhylomeDB; Q8TDY2; -. DR TreeFam; TF323750; -. DR PathwayCommons; Q8TDY2; -. DR Reactome; R-HSA-1632852; Macroautophagy. DR SignaLink; Q8TDY2; -. DR SIGNOR; Q8TDY2; -. DR BioGRID-ORCS; 9821; 113 hits in 1171 CRISPR screens. DR ChiTaRS; RB1CC1; human. DR GeneWiki; RB1CC1; -. DR GenomeRNAi; 9821; -. DR Pharos; Q8TDY2; Tbio. DR PRO; PR:Q8TDY2; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q8TDY2; Protein. DR Bgee; ENSG00000023287; Expressed in buccal mucosa cell and 218 other cell types or tissues. DR ExpressionAtlas; Q8TDY2; baseline and differential. DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IPI:UniProtKB. DR GO; GO:0000421; C:autophagosome membrane; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0000407; C:phagophore assembly site; IDA:UniProtKB. DR GO; GO:0034045; C:phagophore assembly site membrane; ISS:UniProtKB. DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; IDA:UniProt. DR GO; GO:0043495; F:protein-membrane adaptor activity; IDA:UniProt. DR GO; GO:0000045; P:autophagosome assembly; IDA:UniProtKB. DR GO; GO:0006914; P:autophagy; ISS:GO_Central. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0061723; P:glycophagy; IBA:GO_Central. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:ComplexPortal. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central. DR GO; GO:0010508; P:positive regulation of autophagy; ISO:ComplexPortal. DR GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl. DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central. DR GO; GO:1903059; P:regulation of protein lipidation; IDA:ComplexPortal. DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central. DR CDD; cd17060; Ubl_RB1CC1; 1. DR InterPro; IPR040040; ATG11. DR InterPro; IPR019460; Atg11_C. DR PANTHER; PTHR13222; RB1-INDUCIBLE COILED-COIL; 1. DR PANTHER; PTHR13222:SF1; RB1-INDUCIBLE COILED-COIL PROTEIN 1; 1. DR Pfam; PF10377; ATG11; 1. DR Genevisible; Q8TDY2; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Autophagy; Cell cycle; Coiled coil; KW Cytoplasm; Lysosome; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Tumor suppressor. FT CHAIN 1..1594 FT /note="RB1-inducible coiled-coil protein 1" FT /id="PRO_0000097183" FT REGION 638..673 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 859..1397 FT /evidence="ECO:0000255" FT COILED 1438..1485 FT /evidence="ECO:0000255" FT MOTIF 566..569 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 731..737 FT /note="FFAT" FT /evidence="ECO:0000269|PubMed:33124732" FT COMPBIAS 638..671 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 222 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 237 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 238 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9ESK9" FT MOD_RES 243 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 253 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 257 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 261 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9ESK9" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 624 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 647 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 650 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9ESK9" FT MOD_RES 652 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 653 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 734 FT /note="Phosphoserine" FT /evidence="ECO:0000305|PubMed:33124732" FT MOD_RES 1091 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9ESK9" FT MOD_RES 1222 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1370 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1484 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1543..1545 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9039502" FT /id="VSP_040097" FT VARIANT 234 FT /note="M -> T (in dbSNP:rs17337252)" FT /evidence="ECO:0000269|PubMed:11850849, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9039502" FT /id="VAR_023776" FT VARIANT 708 FT /note="P -> L (in dbSNP:rs34016926)" FT /id="VAR_051309" FT VARIANT 1216 FT /note="R -> K (in dbSNP:rs35534432)" FT /id="VAR_051310" FT VARIANT 1314 FT /note="N -> K (in dbSNP:rs34701924)" FT /id="VAR_051311" FT VARIANT 1424 FT /note="S -> F (in dbSNP:rs35342973)" FT /id="VAR_051312" FT VARIANT 1514 FT /note="R -> C (in a breast cancer sample; somatic mutation; FT dbSNP:rs113117391)" FT /evidence="ECO:0000269|PubMed:17224074" FT /id="VAR_033031" FT CONFLICT 1136 FT /note="C -> R (in Ref. 1; BAB69690)" FT /evidence="ECO:0000305" FT HELIX 1286..1393 FT /evidence="ECO:0007829|PDB:7EAA" FT HELIX 1458..1486 FT /evidence="ECO:0007829|PDB:6GMA" FT STRAND 1495..1497 FT /evidence="ECO:0007829|PDB:7EA2" FT STRAND 1506..1512 FT /evidence="ECO:0007829|PDB:7D0E" FT TURN 1513..1516 FT /evidence="ECO:0007829|PDB:7D0E" FT STRAND 1517..1520 FT /evidence="ECO:0007829|PDB:7D0E" FT STRAND 1523..1526 FT /evidence="ECO:0007829|PDB:7D0E" FT STRAND 1528..1530 FT /evidence="ECO:0007829|PDB:7D0E" FT HELIX 1532..1534 FT /evidence="ECO:0007829|PDB:7D0E" FT HELIX 1536..1538 FT /evidence="ECO:0007829|PDB:7D0E" FT STRAND 1554..1567 FT /evidence="ECO:0007829|PDB:7D0E" FT STRAND 1569..1571 FT /evidence="ECO:0007829|PDB:7D0E" FT STRAND 1581..1589 FT /evidence="ECO:0007829|PDB:7D0E" SQ SEQUENCE 1594 AA; 183091 MW; C9C90A328875016A CRC64; MKLYVFLVNT GTTLTFDTEL TVQTVADLKH AIQSKYKIAI QHQVLVVNGG ECMAADRRVC TYSAGTDTNP IFLFNKEMIL CDRPPAIPKT TFSTENDMEI KVEESLMMPA VFHTVASRTQ LALEMYEVAK KLCSFCEGLV HDEHLQHQGW AAIMANLEDC SNSYQKLLFK FESIYSNYLQ SIEDIKLKLT HLGTAVSVMA KIPLLECLTR HSYRECLGRL DSLPEHEDSE KAEMKRSTEL VLSPDMPRTT NESLLTSFPK SVEHVSPDTA DAESGKEIRE SCQSTVHQQD ETTIDTKDGD LPFFNVSLLD WINVQDRPND VESLVRKCFD SMSRLDPRII RPFIAECRQT IAKLDNQNMK AIKGLEDRLY ALDQMIASCG RLVNEQKELA QGFLANQKRA ENLKDASVLP DLCLSHANQL MIMLQNHRKL LDIKQKCTTA KQELANNLHV RLKWCCFVML HADQDGEKLQ ALLRLVIELL ERVKIVEALS TVPQMYCLAV VEVVRRKMFI KHYREWAGAL VKDGKRLYEA EKSKRESFGK LFRKSFLRNR LFRGLDSWPP SFCTQKPRKF DCELPDISLK DLQFLQSFCP SEVQPFLRVP LLCDFEPLHQ HVLALHNLVK AAQSLDEMSQ TITDLLSEQK ASVSQTSPQS ASSPRMESTA GITTTTSPRT PPPLTVQDPL CPAVCPLEEL SPDSIDAHTF DFETIPHPNI EQTIHQVSLD LDSLAESPES DFMSAVNEFV IEENLSSPNP ISDPQSPEMM VESLYSSVIN AIDSRRMQDT NVCGKEDFGD HTSLNVQLER CRVVAQDSHF SIQTIKEDLC HFRTFVQKEQ CDFSNSLKCT AVEIRNIIEK VKCSLEITLK EKHQKELLSL KNEYEGKLDG LIKETEENEN KIKKLKGELV CLEEVLQNKD NEFALVKHEK EAVICLQNEK DQKLLEMENI MHSQNCEIKE LKQSREIVLE DLKKLHVEND EKLQLLRAEL QSLEQSHLKE LEDTLQVRHI QEFEKVMTDH RVSLEELKKE NQQIINQIQE SHAEIIQEKE KQLQELKLKV SDLSDTRCKL EVELALKEAE TDEIKILLEE SRAQQKETLK SLLEQETENL RTEISKLNQK IQDNNENYQV GLAELRTLMT IEKDQCISEL ISRHEEESNI LKAELNKVTS LHNQAFEIEK NLKEQIIELQ SKLDSELSAL ERQKDEKITQ QEEKYEAIIQ NLEKDRQKLV SSQEQDREQL IQKLNCEKDE AIQTALKEFK LEREVVEKEL LEKVKHLENQ IAKSPAIDST RGDSSSLVAE LQEKLQEEKA KFLEQLEEQE KRKNEEMQNV RTSLIAEQQT NFNTVLTREK MRKENIINDL SDKLKSTMQQ QERDKDLIES LSEDRARLLE EKKKLEEEVS KLRSSSFVPS PYVATAPELY GACAPELPGE SDRSAVETAD EGRVDSAMET SMMSVQENIH MLSEEKQRIM LLERTLQLKE EENKRLNQRL MSQSMSSVSS RHSEKIAIRD FQVGDLVLII LDERHDNYVL FTVSPTLYFL HSESLPALDL KPGEGASGAS RRPWVLGKVM EKEYCQAKKA QNRFKVPLGT KFYRVKAVSW NKKV //