Details for: Rb1cc1
Associated with
Other Information
Genular Protein ID: 3808354100
Symbol: RBCC1_MOUSE
Name: Coiled-coil-forming protein 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 12095676
Title: Isolation, characterization and mapping of the mouse and human RB1CC1 genes.
PubMed ID: 12095676
PubMed ID: 19468303
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
PubMed ID: 19468303
PubMed ID: 16141072
Title: The transcriptional landscape of the mammalian genome.
PubMed ID: 16141072
PubMed ID: 7724523
Title: Stathmin interaction with a putative kinase and coiled-coil-forming protein domains.
PubMed ID: 7724523
PubMed ID: 11207567
Title: LaXp180, a mammalian ActA-binding protein, identified with the yeast two-hybrid system co-localizes with intracellular Listeria monocytogenes.
PubMed ID: 11207567
PubMed ID: 15375585
Title: Expression and regulation of RB1CC1 in developing murine and human tissues.
PubMed ID: 15375585
PubMed ID: 15968549
Title: Rb1cc1 is critical for myoblast differentiation through Rb1 regulation.
PubMed ID: 15968549
PubMed ID: 16452087
Title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.
PubMed ID: 16452087
PubMed ID: 17242355
Title: Large-scale phosphorylation analysis of mouse liver.
PubMed ID: 17242355
PubMed ID: 19258318
Title: ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy.
PubMed ID: 19258318
PubMed ID: 21183079
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
PubMed ID: 21183079
PubMed ID: 19940130
Title: Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration.
PubMed ID: 19940130
PubMed ID: 21088496
Title: FIP200, an essential component of mammalian autophagy is indispensible for fetal hematopoiesis.
PubMed ID: 21088496
PubMed ID: 21795712
Title: RB1CC1 protein positively regulates transforming growth factor-beta signaling through the modulation of Arkadia E3 ubiquitin ligase activity.
PubMed ID: 21795712
PubMed ID: 21525242
Title: The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella.
PubMed ID: 21525242
PubMed ID: 21807966
Title: Suppression of autophagy by FIP200 deletion impairs DNA damage repair and increases cell death upon treatments with anticancer agents.
PubMed ID: 21807966
PubMed ID: 23285000
Title: Autophagy induced by calcium phosphate precipitates involves endoplasmic reticulum membranes in autophagosome biogenesis.
PubMed ID: 23285000
PubMed ID: 23392225
Title: FIP200 regulates targeting of Atg16L1 to the isolation membrane.
PubMed ID: 23392225
DOI: 10.1038/embor.2013.6
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: 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
Sequence Information:
- Length: 1588
- Mass: 182350
- Checksum: 2D14F1434604C0AF
- Sequence:
MKLYVFLVNT GTTLTFDTEL TVQTVADLKH AIQSKYKIAI QHQVLVVNGG ECMAADRRVC TYSAGTDTNP IFLFNKEMIL CDRAPAIPKA TFSTENDMEI KVEESLMMPA VFHTVASRTQ LAVEMYDVAK KLCSFCEGLV HDEHLQHQGW AAIMANLEDC SNSYQKLLFK FESIYSDYLQ SIEDIKLKLT HLGTAVSVMA KIPLLECLTR HSYRECLGRP DSLNEHEGSE KAEMKRSTEL VLSPDMPRTT NTSLVTSFHK SMEHVAPDPT GTERGKELRE SCQSTVQQEE ASVDAKDSDL PFFNVSLLDW INVQDRPNDV ESLVRKCFDS MSRLDPKIIQ PFMLECHQTI AKLDNQNMKA IKGLEDRLYA LDQMIASCSR LVNEQKELAQ GFLANQMRAE NLKDASVLPD LCLSHANQLM IMLQNHRKLL DIKQKCTTAK QELANNLHVR LKWCCFVMLH ADQDGEKLQA LLRLVIELLE RVRIVEALST VPQMYCLAVV EVVRRKMFIK HYREWAGALV KDGKQLYEAE KSKRESFGKL FRKSFLRNRL FKGLDSWPSS FCTQKPRKFD CELPDISLKD LQFLQSFCPS EVQPFLRVPL LCDFEPLHQH VLALHNLVKA AQSLDEMSQT ITDLLNEQKV STSQASPQSA ASPRIESTTG ITTTTSPKTP PPLTVQDTLC PAVCPLEELS PDSIDAHTFD FETISHPNTE QPVHQASIDL DSLAESPESD FMSAVNEFVI EENLSSPNPI SDPQSPEMMV ESLYSSVINA IDSRRMQDTS TRGNEGFGDR AALHVQLEKC RAAAQDSHSS IQTIKDDLCH FRTFVQKEQC DLANYLKCTA VEIRNIIEKV KCSLEITLKE KHQQELQSLK IEYECKLDAL VKDSEENVNK ILKLKENLVS LEEALQNKDN EFTSIKHEKD AIVCVQQEKD QKLLEMEKIM HTQHCEIKEL KQSREMALED LKKLHDEKIE SLRAEFQCLE QNHLKELEDT LHIRHTQEFE KVMTDHNMSL EKLKKENQQR IDQMLESHAS TIQEKEQQLQ ELKLKVSDLS DMRCKLEVEL ALKEAETDEI KILLEESRTQ QKEMLKSLLE QETENLRTEI SKLNQKIHDN NESYQVGLSE LRALMTIEKD QCISELISRH EEESNILKAE LDNVTSLHRQ AYEIEKKLKE QIVELQTRLN SELSALEKQK DEKITQQEEK YEALIQNLEK DKERLVKNHE QDKEHLIQEL NFEKNKAVQT ALDEFKVERE LVEKELLEKV KHLENQIAKT PAFESAREDS SSLVAELQEK LQEEKAKFLE QLEEQEKRKN EEMQNVRTSL IAEQQTNFNT VLTREKMRKE NIINDLSDKL KSTMQQQERD KDLIESLSED RARLLEEKKQ LEEEVSKLRT SSFLSSAPVA AAPELYGACA PELPGEPERS VMETADEGRL DSAMETSMMS VQENMLSEEK QRIMLLERTL QLKEEENKRL NQRLMSQSLS SVSSRHSEKI AIRDFQVGDL VLIILDERHD NYVLFTVSPT LYFLHSESLP ALDLKPGEGA SGASRRPWVL GKVMEKEYCQ AKKAQNRFKV PLGTKFYRVK AVSWNKKV
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.