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RB1-inducible coiled-coil protein 1 (FAK family kinase-interacting protein of 200 kDa) (FIP200)

 RBCC1_HUMAN             Reviewed;        1594 AA.
Q8TDY2; Q86YR4; Q8WVU9; Q92601;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 3.
27-SEP-2017, entry version 131.
RecName: Full=RB1-inducible coiled-coil protein 1;
AltName: Full=FAK family kinase-interacting protein of 200 kDa;
Short=FIP200;
Name=RB1CC1; Synonyms=KIAA0203, RBICC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-234, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, INDUCTION, AND INDUCTION OF RB1
EXPRESSION.
TISSUE=Osteosarcoma;
PubMed=11850849; DOI=10.1038/sj.onc.1205178;
Chano T., Ikegawa S., Kontani K., Okabe H., Baldini N., Saeki Y.;
"Identification of RB1CC1, a novel human gene that can induce RB1 in
various human cells.";
Oncogene 21:1295-1298(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
THR-234.
TISSUE=Myeloid;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[3]
SEQUENCE REVISION.
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-234.
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1377-1594, FUNCTION, SUBCELLULAR
LOCATION, AND INTERACTION WITH PTK2/FAK1 AND PTK2B/PYK2.
PubMed=10769033; DOI=10.1083/jcb.149.2.423;
Ueda H., Abbi S., Zheng C., Guan J.-L.;
"Suppression of Pyk2 kinase and cellular activities by FIP200.";
J. Cell Biol. 149:423-430(2000).
[7]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION.
PubMed=12163359; DOI=10.1016/S0002-9440(10)64190-9;
Chano T., Saeki Y., Serra M., Matsumoto K., Okabe H.;
"Preferential expression of RB1-inducible coiled-coil 1 in terminal
differentiated musculoskeletal cells.";
Am. J. Pathol. 161:359-364(2002).
[8]
CHARACTERIZATION, AND FUNCTION.
PubMed=12095676; DOI=10.1016/S0378-1119(02)00585-1;
Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A.,
Saeki Y., Okabe H.;
"Isolation, characterization and mapping of the mouse and human RB1CC1
genes.";
Gene 291:29-34(2002).
[9]
FUNCTION, AND INTERACTION WITH PTK2/FAK1.
PubMed=12221124; DOI=10.1091/mbc.E02-05-0295;
Abbi S., Ueda H., Zheng C., Cooper L.A., Zhao J., Christopher R.,
Guan J.L.;
"Regulation of focal adhesion kinase by a novel protein inhibitor
FIP200.";
Mol. Biol. Cell 13:3178-3191(2002).
[10]
INVOLVEMENT IN BREAST CANCER.
PubMed=12068296; DOI=10.1038/ng911;
Chano T., Kontani K., Teramoto K., Okabe H., Ikegawa S.;
"Truncating mutations of RB1CC1 in human breast cancer.";
Nat. Genet. 31:285-288(2002).
[11]
FUNCTION.
PubMed=14533007;
Kontani K., Chano T., Ozaki Y., Tezuka N., Sawai S., Fujino S.,
Saeki Y., Okabe H.;
"RB1CC1 suppresses cell cycle progression through RB1 expression in
human neoplastic cells.";
Int. J. Mol. Med. 12:767-769(2003).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-624; SER-647
AND SER-653, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
SUBUNIT.
PubMed=19597335; DOI=10.4161/auto.5.7.9296;
Hosokawa N., Sasaki T., Iemura S.I., Natsume T., Hara T.,
Mizushima N.;
"Atg101, a novel mammalian autophagy protein interacting with Atg13.";
Autophagy 5:973-979(2009).
[16]
INTERACTION WITH ULK1 AND ATG13.
PubMed=19211835; DOI=10.1091/mbc.E08-12-1248;
Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y.,
Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N.,
Mizushima N.;
"Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
complex required for autophagy.";
Mol. Biol. Cell 20:1981-1991(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-257, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=21775823; DOI=10.4161/cc.10.16.16868;
Morselli E., Shen S., Ruckenstuhl C., Bauer M.A., Marino G.,
Galluzzi L., Criollo A., Michaud M., Maiuri M.C., Chano T., Madeo F.,
Kroemer G.;
"p53 inhibits autophagy by interacting with the human ortholog of
yeast Atg17, RB1CC1/FIP200.";
Cell Cycle 10:2763-2769(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
INTERACTION WITH GABARAP AND GABARAPL1.
PubMed=23043107; DOI=10.1074/jbc.M112.378109;
Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B.,
Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.;
"ATG8 family proteins act as scaffolds for assembly of the ULK
complex: sequence requirements for LC3-interacting region (LIR)
motifs.";
J. Biol. Chem. 287:39275-39290(2012).
[23]
FUNCTION, AND INTERACTION WITH ATG16L1.
PubMed=23392225; DOI=10.1038/embor.2013.6;
Nishimura T., Kaizuka T., Cadwell K., Sahani M.H., Saitoh T.,
Akira S., Virgin H.W., Mizushima N.;
"FIP200 regulates targeting of Atg16L1 to the isolation membrane.";
EMBO Rep. 14:284-291(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-229; SER-237;
SER-243; SER-253; SER-257; SER-266; SER-647; SER-652; SER-1222;
SER-1370 AND SER-1484, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
INTERACTION WITH ATG16L1.
PubMed=24954904; DOI=10.1016/j.molcel.2014.05.021;
Dooley H.C., Razi M., Polson H.E., Girardin S.E., Wilson M.I.,
Tooze S.A.;
"WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and
pathogen clearance by recruiting Atg12-5-16L1.";
Mol. Cell 55:238-252(2014).
[27]
VARIANT CYS-1514.
PubMed=17224074; DOI=10.1186/bcr1637;
Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A.,
Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S.,
Kristensen V., Perou C.M., Boerresen-Dale A.-L.;
"Somatic sequence alterations in twenty-one genes selected by
expression profile analysis of breast carcinomas.";
Breast Cancer Res. 9:R5-R5(2007).
[28]
INTERACTION WITH RFWD2.
PubMed=23289756; DOI=10.1186/1471-2091-14-1;
Kobayashi S., Yoneda-Kato N., Itahara N., Yoshida A., Kato J.Y.;
"The COP1 E3-ligase interacts with FIP200, a key regulator of
mammalian autophagy.";
BMC Biochem. 14:1-1(2013).
[29]
INTERACTION WITH ATG16L1.
PubMed=23262492; DOI=10.1038/nsmb.2475;
Gammoh N., Florey O., Overholtzer M., Jiang X.;
"Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-
dependent and -independent autophagy.";
Nat. Struct. Mol. Biol. 20:144-149(2013).
-!- FUNCTION: Involved in autophagy (PubMed:21775823). Regulates early
events but also late events of autophagosome formation through
direct interaction with Atg16L1 (PubMed:23392225). Required for
the formation of the autophagosome-like double-membrane structure
that surrounds the Salmonella-containing vacuole (SCV) during
S.typhimurium infection and subsequent xenophagy (By similarity).
Involved in repair of DNA damage caused by ionizing radiation,
which subsequently improves cell survival by decreasing apoptosis
(By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase
activity, affecting their downstream signaling pathways
(PubMed:10769033, PubMed:12221124). Plays a role as a modulator of
TGF-beta-signaling by restricting substrate specificity of RNF111
(By similarity). Functions as a DNA-binding transcription factor
(PubMed:12095676). Is a potent regulator of the RB1 pathway
through induction of RB1 expression (PubMed:14533007). Plays a
crucial role in muscular differentiation (PubMed:12163359). Plays
an indispensable role in fetal hematopoiesis and in the regulation
of neuronal homeostasis (By similarity).
{ECO:0000250|UniProtKB:Q9ESK9, ECO:0000269|PubMed:10769033,
ECO:0000269|PubMed:12095676, ECO:0000269|PubMed:12163359,
ECO:0000269|PubMed:12221124, ECO:0000269|PubMed:14533007,
ECO:0000269|PubMed:21775823, ECO:0000269|PubMed:23392225}.
-!- SUBUNIT: Part of a complex consisting of ATG13/KIAA0652, ULK1 and
RB1CC1 (PubMed:19597335, PubMed:19211835). This complex associates
with ATG101 (PubMed:19597335, PubMed:19211835). Interacts with
PTK2/FAK1 and PTK2B/PYK2 (PubMed:10769033, PubMed:12221124).
Interacts with GABARAP and GABARAPL1 (PubMed:23043107). Interacts
with ATG16L1; the interaction is required for ULK1 complex-
dependent autophagy (PubMed:24954904, PubMed:23262492,
PubMed:23392225). Interacts with RNF111, SKI and SMAD7 (By
similarity). Interacts with RFWD2 in the cytoplasm of
proliferating cells in response to UV stimulation
(PubMed:23289756). Interacts with TP53 (PubMed:21775823).
{ECO:0000250|UniProtKB:Q9ESK9, ECO:0000269|PubMed:10769033,
ECO:0000269|PubMed:12221124, ECO:0000269|PubMed:19211835,
ECO:0000269|PubMed:19597335, ECO:0000269|PubMed:21775823,
ECO:0000269|PubMed:23043107, ECO:0000269|PubMed:23262492,
ECO:0000269|PubMed:23289756, ECO:0000269|PubMed:23392225,
ECO:0000269|PubMed:24954904}.
-!- INTERACTION:
Q9BSB4:ATG101; NbExp=7; IntAct=EBI-1047793, EBI-2946739;
O75143:ATG13; NbExp=9; IntAct=EBI-1047793, EBI-2798775;
Q676U5:ATG16L1; NbExp=5; IntAct=EBI-1047793, EBI-535909;
A7MCY6:TBKBP1; NbExp=2; IntAct=EBI-1047793, EBI-359969;
O75385:ULK1; NbExp=7; IntAct=EBI-1047793, EBI-908831;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11850849}.
Cytoplasm {ECO:0000269|PubMed:10769033}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q9ESK9}. Preautophagosomal structure
{ECO:0000250|UniProtKB:Q9ESK9}. Note=Under starvation conditions,
is localized to puncate structures primarily representing the
isolation membrane that sequesters a portion of the cytoplasm
resulting in the formation of an autophagosome.
{ECO:0000250|UniProtKB:Q9ESK9}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8TDY2-1; Sequence=Displayed;
Name=2;
IsoId=Q8TDY2-2; Sequence=VSP_040097;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expression levels correlated closely with
those of RB1 in cancer cell lines as well as in various normal
human tissues. Abundantly expressed in human musculoskeletal and
cultured osteosarcoma cells. {ECO:0000269|PubMed:11850849,
ECO:0000269|PubMed:12163359}.
-!- DEVELOPMENTAL STAGE: Expression was difficult to detect in
immature proliferating chondroblasts or myogenic cells in embryos,
but became obvious and prominent concomitantly with the maturation
of osteocytes, chondrocytes, and skeletal muscle cells. Expression
in these musculoskeletal cells increased with RB1 expression,
which is linked to the terminal differentiation of many tissues
and cells. The introduction of the wild-type protein decreased the
formation of macroscopic colonies in a cell growth assay.
{ECO:0000269|PubMed:12163359}.
-!- MISCELLANEOUS: Probably involved in the tumorigenesis of breast
cancer. RB1CC1 is frequently mutated in breast cancer and shows
characteristics of a classical tumor suppressor gene.
-!- SIMILARITY: Belongs to the ATG17 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA13194.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB059622; BAB69690.1; -; mRNA.
EMBL; D86958; BAA13194.2; ALT_INIT; mRNA.
EMBL; AC090814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC113139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017556; AAH17556.1; -; mRNA.
EMBL; AY173931; AAO17545.1; -; mRNA.
CCDS; CCDS34892.1; -. [Q8TDY2-1]
CCDS; CCDS47856.1; -. [Q8TDY2-2]
RefSeq; NP_001077086.1; NM_001083617.1. [Q8TDY2-2]
RefSeq; NP_055596.3; NM_014781.4. [Q8TDY2-1]
RefSeq; XP_011515945.1; XM_011517643.2. [Q8TDY2-1]
RefSeq; XP_016869596.1; XM_017014107.1. [Q8TDY2-2]
UniGene; Hs.196102; -.
ProteinModelPortal; Q8TDY2; -.
SMR; Q8TDY2; -.
BioGrid; 115160; 87.
CORUM; Q8TDY2; -.
DIP; DIP-45969N; -.
IntAct; Q8TDY2; 78.
MINT; MINT-5003383; -.
STRING; 9606.ENSP00000025008; -.
iPTMnet; Q8TDY2; -.
PhosphoSitePlus; Q8TDY2; -.
BioMuta; RB1CC1; -.
DMDM; 160359050; -.
EPD; Q8TDY2; -.
MaxQB; Q8TDY2; -.
PaxDb; Q8TDY2; -.
PeptideAtlas; Q8TDY2; -.
PRIDE; Q8TDY2; -.
DNASU; 9821; -.
Ensembl; ENST00000025008; ENSP00000025008; ENSG00000023287. [Q8TDY2-1]
Ensembl; ENST00000435644; ENSP00000396067; ENSG00000023287. [Q8TDY2-2]
GeneID; 9821; -.
KEGG; hsa:9821; -.
UCSC; uc003xre.5; human. [Q8TDY2-1]
CTD; 9821; -.
DisGeNET; 9821; -.
EuPathDB; HostDB:ENSG00000023287.12; -.
GeneCards; RB1CC1; -.
H-InvDB; HIX0007503; -.
HGNC; HGNC:15574; RB1CC1.
HPA; HPA024391; -.
HPA; HPA053049; -.
MalaCards; RB1CC1; -.
MIM; 606837; gene.
neXtProt; NX_Q8TDY2; -.
OpenTargets; ENSG00000023287; -.
PharmGKB; PA34248; -.
eggNOG; KOG4572; Eukaryota.
eggNOG; ENOG410XSY4; LUCA.
GeneTree; ENSGT00390000015871; -.
HOGENOM; HOG000154076; -.
HOVERGEN; HBG091209; -.
InParanoid; Q8TDY2; -.
KO; K17589; -.
OMA; AECRQTI; -.
OrthoDB; EOG091G0PNM; -.
PhylomeDB; Q8TDY2; -.
TreeFam; TF323750; -.
Reactome; R-HSA-1632852; Macroautophagy.
SIGNOR; Q8TDY2; -.
ChiTaRS; RB1CC1; human.
GeneWiki; RB1CC1; -.
GenomeRNAi; 9821; -.
PRO; PR:Q8TDY2; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000023287; -.
CleanEx; HS_RB1CC1; -.
ExpressionAtlas; Q8TDY2; baseline and differential.
Genevisible; Q8TDY2; HS.
GO; GO:1990316; C:ATG1/ULK1 kinase complex; IPI:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0034045; C:pre-autophagosomal structure membrane; ISS:UniProtKB.
GO; GO:0032947; F:protein complex scaffold activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
GO; GO:0006914; P:autophagy; ISS:GO_Central.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0061723; P:glycophagy; IBA:GO_Central.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0030242; P:pexophagy; IBA:GO_Central.
GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR019460; Autophagy-rel_p11.
Pfam; PF10377; ATG11; 1.
1: Evidence at protein level;
Alternative splicing; Autophagy; Cell cycle; Coiled coil;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Tumor suppressor.
CHAIN 1 1594 RB1-inducible coiled-coil protein 1.
/FTId=PRO_0000097183.
COILED 859 1397 {ECO:0000255}.
COILED 1438 1485 {ECO:0000255}.
MOTIF 566 569 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 663 666 Poly-Thr.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 238 238 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ESK9}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ESK9}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 624 624 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 647 647 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ESK9}.
MOD_RES 652 652 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1091 1091 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ESK9}.
MOD_RES 1222 1222 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1370 1370 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1484 1484 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1543 1545 Missing (in isoform 2).
{ECO:0000303|PubMed:9039502}.
/FTId=VSP_040097.
VARIANT 234 234 M -> T (in dbSNP:rs17337252).
{ECO:0000269|PubMed:11850849,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9039502}.
/FTId=VAR_023776.
VARIANT 708 708 P -> L (in dbSNP:rs34016926).
/FTId=VAR_051309.
VARIANT 1216 1216 R -> K (in dbSNP:rs35534432).
/FTId=VAR_051310.
VARIANT 1314 1314 N -> K (in dbSNP:rs34701924).
/FTId=VAR_051311.
VARIANT 1424 1424 S -> F (in dbSNP:rs35342973).
/FTId=VAR_051312.
VARIANT 1514 1514 R -> C (in a breast cancer sample;
somatic mutation; dbSNP:rs113117391).
{ECO:0000269|PubMed:17224074}.
/FTId=VAR_033031.
CONFLICT 1136 1136 C -> R (in Ref. 1; BAB69690).
{ECO:0000305}.
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


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