RBCC1_HUMAN
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 03-AUG-2022, entry version 166.
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 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). {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 -!- 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 -!- 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};
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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 PDBsum; 6DCE; -.
DR PDBsum; 6GMA; -.
DR PDBsum; 7CZG; -.
DR PDBsum; 7CZM; -.
DR PDBsum; 7D0E; -.
DR PDBsum; 7EA2; -.
DR PDBsum; 7EAA; -.
DR AlphaFoldDB; Q8TDY2; -.
DR SMR; Q8TDY2; -.
DR BioGRID; 115160; 327.
DR ComplexPortal; CPX-373; ULK1-ATG13-RB1CC1-ATG101 autophagy initiation complex.
DR CORUM; Q8TDY2; -.
DR DIP; DIP-45969N; -.
DR IntAct; Q8TDY2; 91.
DR MINT; Q8TDY2; -.
DR STRING; 9606.ENSP00000025008; -.
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; Q8TDY2; -.
DR PeptideAtlas; Q8TDY2; -.
DR PRIDE; Q8TDY2; -.
DR ProteomicsDB; 74368; -. [Q8TDY2-1]
DR ProteomicsDB; 74369; -. [Q8TDY2-2]
DR Antibodypedia; 24432; 331 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 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; AQDSKVH; -.
DR OrthoDB; 91906at2759; -.
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; 108 hits in 1094 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 216 other tissues.
DR ExpressionAtlas; Q8TDY2; baseline and differential.
DR Genevisible; Q8TDY2; HS.
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:0019898; C:extrinsic component of membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IDA:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISS:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA: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; IEA:Ensembl.
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:0046777; P:protein autophosphorylation; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:1903059; P:regulation of protein lipidation; IDA:ComplexPortal.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR InterPro; IPR040040; ATG11.
DR InterPro; IPR019460; Atg11_C.
DR InterPro; IPR045326; ATG17-like_dom.
DR PANTHER; PTHR13222; PTHR13222; 1.
DR Pfam; PF10377; ATG11; 1.
DR Pfam; PF04108; ATG17_like; 1.
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 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 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
