Details for: RB1CC1
Associated with
Other Information
Genular Protein ID: 3695733870
Symbol: RBCC1_HUMAN
Name: FAK family kinase-interacting protein of 200 kDa
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 11850849
Title: Identification of RB1CC1, a novel human gene that can induce RB1 in various human cells.
PubMed ID: 11850849
PubMed ID: 9039502
Title: 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.
PubMed ID: 9039502
PubMed ID: 16421571
Title: DNA sequence and analysis of human chromosome 8.
PubMed ID: 16421571
DOI: 10.1038/nature04406
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 10769033
Title: Suppression of Pyk2 kinase and cellular activities by FIP200.
PubMed ID: 10769033
PubMed ID: 12163359
Title: Preferential expression of RB1-inducible coiled-coil 1 in terminal differentiated musculoskeletal cells.
PubMed ID: 12163359
PubMed ID: 12095676
Title: Isolation, characterization and mapping of the mouse and human RB1CC1 genes.
PubMed ID: 12095676
PubMed ID: 12221124
Title: Regulation of focal adhesion kinase by a novel protein inhibitor FIP200.
PubMed ID: 12221124
PubMed ID: 12068296
Title: Truncating mutations of RB1CC1 in human breast cancer.
PubMed ID: 12068296
DOI: 10.1038/ng911
PubMed ID: 14533007
Title: RB1CC1 suppresses cell cycle progression through RB1 expression in human neoplastic cells.
PubMed ID: 14533007
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19597335
Title: Atg101, a novel mammalian autophagy protein interacting with Atg13.
PubMed ID: 19597335
PubMed ID: 19211835
Title: Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy.
PubMed ID: 19211835
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21775823
Title: p53 inhibits autophagy by interacting with the human ortholog of yeast Atg17, RB1CC1/FIP200.
PubMed ID: 21775823
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23043107
Title: ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs.
PubMed ID: 23043107
PubMed ID: 23392225
Title: FIP200 regulates targeting of Atg16L1 to the isolation membrane.
PubMed ID: 23392225
DOI: 10.1038/embor.2013.6
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 24954904
Title: WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and pathogen clearance by recruiting Atg12-5-16L1.
PubMed ID: 24954904
PubMed ID: 23289756
Title: The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy.
PubMed ID: 23289756
PubMed ID: 23262492
Title: Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-dependent and -independent autophagy.
PubMed ID: 23262492
DOI: 10.1038/nsmb.2475
PubMed ID: 27334615
Title: The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy.
PubMed ID: 27334615
PubMed ID: 28890335
Title: The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates SERCA Activity to Control ER-Isolation Membrane Contacts for Autophagosome Formation.
PubMed ID: 28890335
PubMed ID: 28561066
Title: WIPI3 and WIPI4 beta-propellers are scaffolds for LKB1-AMPK-TSC signalling circuits in the control of autophagy.
PubMed ID: 28561066
DOI: 10.1038/ncomms15637
PubMed ID: 31806350
Title: The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.
PubMed ID: 31806350
PubMed ID: 33226137
Title: Receptor-mediated clustering of FIP200 bypasses the role of LC3 lipidation in autophagy.
PubMed ID: 33226137
PubMed ID: 34471133
Title: Reconstitution defines the roles of p62, NBR1 and TAX1BP1 in ubiquitin condensate formation and autophagy initiation.
PubMed ID: 34471133
PubMed ID: 33124732
Title: FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts.
PubMed ID: 33124732
PubMed ID: 17224074
Title: Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas.
PubMed ID: 17224074
DOI: 10.1186/bcr1637
Sequence Information:
- Length: 1594
- Mass: 183091
- Checksum: C9C90A328875016A
- Sequence:
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
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.