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Protein

RB1-inducible coiled-coil protein 1

Gene

Rb1cc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Implicated in the regulation of RB1 expression. Functions as a DNA-binding transcription factor. Is a potent regulator of the RB1 pathway and a novel mediator that plays a crucial role in muscular differentiation. Expression is, thus, a prerequisite for myogenic differentiation. Inhibits PTK2/FAK1 and PTK2B/PYK2 activity and activation of downstream signaling pathways (By similarity). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of rnf111. Involved in autophagy. Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1. Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) duting S.typhimurium infection and subsequent xenophagy. Autophagy positively regulates repair of DNA damage induced by ionizing radiation and negatively regulates apoptosis. Plays an indispensible role in fetal hematopoiesis and in the regulation of neuronal homeostasis.By similarity10 Publications

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • autophagosome assembly Source: UniProtKB
  • autophagy Source: GO_Central
  • cell cycle Source: UniProtKB-KW
  • heart development Source: MGI
  • liver development Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of cell size Source: MGI
  • positive regulation of JNK cascade Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Autophagy, Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.

Names & Taxonomyi

Protein namesi
Recommended name:
RB1-inducible coiled-coil protein 1
Alternative name(s):
Coiled-coil-forming protein 1
FAK family kinase-interacting protein of 200 kDa
Short name:
FIP200
LaXp180
Gene namesi
Name:Rb1cc1
Synonyms:Cc1, Kiaa0203
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1341850. Rb1cc1.

Subcellular locationi

GO - Cellular componenti

  • ATG1/ULK1 kinase complex Source: UniProtKB
  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB-SubCell
  • nuclear membrane Source: MGI
  • nucleus Source: MGI
  • pre-autophagosomal structure Source: UniProtKB
  • pre-autophagosomal structure membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15881588RB1-inducible coiled-coil protein 1PRO_0000097184Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei222 – 2221PhosphoserineBy similarity
Modified residuei229 – 2291PhosphoserineBy similarity
Modified residuei237 – 2371PhosphoserineCombined sources
Modified residuei238 – 2381PhosphothreonineCombined sources
Modified residuei243 – 2431PhosphoserineCombined sources
Modified residuei253 – 2531PhosphoserineBy similarity
Modified residuei257 – 2571PhosphoserineBy similarity
Modified residuei261 – 2611PhosphoserineCombined sources
Modified residuei623 – 6231PhosphoserineCombined sources
Modified residuei646 – 6461PhosphoserineCombined sources
Modified residuei649 – 6491PhosphoserineCombined sources
Modified residuei652 – 6521PhosphoserineCombined sources
Modified residuei1087 – 10871PhosphoserineCombined sources
Modified residuei1366 – 13661PhosphoserineBy similarity
Modified residuei1478 – 14781PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9ESK9.
MaxQBiQ9ESK9.
PaxDbiQ9ESK9.
PeptideAtlasiQ9ESK9.
PRIDEiQ9ESK9.

PTM databases

iPTMnetiQ9ESK9.
PhosphoSiteiQ9ESK9.

Expressioni

Tissue specificityi

Expressed abundantly in heart and testis, and moderately in kidney, liver and skeletal muscles. Very low expression levels in lung and spleen. Colocalizes with RB1 in various tissues.1 Publication

Developmental stagei

Abundantly expressed from an early stage of the embryo throughout development. Ubiquitously expressed, especially in the musculoskeletal system, heart and neural tissues.1 Publication

Gene expression databases

BgeeiQ9ESK9.
CleanExiMM_RB1CC1.
ExpressionAtlasiQ9ESK9. baseline and differential.
GenevisibleiQ9ESK9. MM.

Interactioni

Subunit structurei

Part of a complex containing ATG13/KIAA0652, ULK1 and RB1CC1. This complex associates with ATG101. Interacts with PTK2/FAK1 and PTK2B/PYK2 (By similarity). Interacts with ATG16L1. Interacts with rnf111, ski ans smad7.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Atg16l1Q8C0J23EBI-647302,EBI-769195

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi198540. 4 interactions.
DIPiDIP-49679N.
IntActiQ9ESK9. 6 interactions.
STRINGi10090.ENSMUSP00000027040.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili858 – 1393536Sequence analysisAdd
BLAST
Coiled coili1440 – 147940Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi565 – 5684Nuclear localization signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi662 – 6654Poly-Thr

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4572. Eukaryota.
ENOG410XSY4. LUCA.
GeneTreeiENSGT00390000015871.
HOGENOMiHOG000154076.
HOVERGENiHBG091209.
InParanoidiQ9ESK9.
KOiK17589.
OMAiTMQQQER.
OrthoDBiEOG7B5WV6.
TreeFamiTF323750.

Family and domain databases

InterProiIPR019460. Autophagy-rel_p11.
[Graphical view]
PfamiPF10377. ATG11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ESK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLYVFLVNT GTTLTFDTEL TVQTVADLKH AIQSKYKIAI QHQVLVVNGG
60 70 80 90 100
ECMAADRRVC TYSAGTDTNP IFLFNKEMIL CDRAPAIPKA TFSTENDMEI
110 120 130 140 150
KVEESLMMPA VFHTVASRTQ LAVEMYDVAK KLCSFCEGLV HDEHLQHQGW
160 170 180 190 200
AAIMANLEDC SNSYQKLLFK FESIYSDYLQ SIEDIKLKLT HLGTAVSVMA
210 220 230 240 250
KIPLLECLTR HSYRECLGRP DSLNEHEGSE KAEMKRSTEL VLSPDMPRTT
260 270 280 290 300
NTSLVTSFHK SMEHVAPDPT GTERGKELRE SCQSTVQQEE ASVDAKDSDL
310 320 330 340 350
PFFNVSLLDW INVQDRPNDV ESLVRKCFDS MSRLDPKIIQ PFMLECHQTI
360 370 380 390 400
AKLDNQNMKA IKGLEDRLYA LDQMIASCSR LVNEQKELAQ GFLANQMRAE
410 420 430 440 450
NLKDASVLPD LCLSHANQLM IMLQNHRKLL DIKQKCTTAK QELANNLHVR
460 470 480 490 500
LKWCCFVMLH ADQDGEKLQA LLRLVIELLE RVRIVEALST VPQMYCLAVV
510 520 530 540 550
EVVRRKMFIK HYREWAGALV KDGKQLYEAE KSKRESFGKL FRKSFLRNRL
560 570 580 590 600
FKGLDSWPSS FCTQKPRKFD CELPDISLKD LQFLQSFCPS EVQPFLRVPL
610 620 630 640 650
LCDFEPLHQH VLALHNLVKA AQSLDEMSQT ITDLLNEQKV STSQASPQSA
660 670 680 690 700
ASPRIESTTG ITTTTSPKTP PPLTVQDTLC PAVCPLEELS PDSIDAHTFD
710 720 730 740 750
FETISHPNTE QPVHQASIDL DSLAESPESD FMSAVNEFVI EENLSSPNPI
760 770 780 790 800
SDPQSPEMMV ESLYSSVINA IDSRRMQDTS TRGNEGFGDR AALHVQLEKC
810 820 830 840 850
RAAAQDSHSS IQTIKDDLCH FRTFVQKEQC DLANYLKCTA VEIRNIIEKV
860 870 880 890 900
KCSLEITLKE KHQQELQSLK IEYECKLDAL VKDSEENVNK ILKLKENLVS
910 920 930 940 950
LEEALQNKDN EFTSIKHEKD AIVCVQQEKD QKLLEMEKIM HTQHCEIKEL
960 970 980 990 1000
KQSREMALED LKKLHDEKIE SLRAEFQCLE QNHLKELEDT LHIRHTQEFE
1010 1020 1030 1040 1050
KVMTDHNMSL EKLKKENQQR IDQMLESHAS TIQEKEQQLQ ELKLKVSDLS
1060 1070 1080 1090 1100
DMRCKLEVEL ALKEAETDEI KILLEESRTQ QKEMLKSLLE QETENLRTEI
1110 1120 1130 1140 1150
SKLNQKIHDN NESYQVGLSE LRALMTIEKD QCISELISRH EEESNILKAE
1160 1170 1180 1190 1200
LDNVTSLHRQ AYEIEKKLKE QIVELQTRLN SELSALEKQK DEKITQQEEK
1210 1220 1230 1240 1250
YEALIQNLEK DKERLVKNHE QDKEHLIQEL NFEKNKAVQT ALDEFKVERE
1260 1270 1280 1290 1300
LVEKELLEKV KHLENQIAKT PAFESAREDS SSLVAELQEK LQEEKAKFLE
1310 1320 1330 1340 1350
QLEEQEKRKN EEMQNVRTSL IAEQQTNFNT VLTREKMRKE NIINDLSDKL
1360 1370 1380 1390 1400
KSTMQQQERD KDLIESLSED RARLLEEKKQ LEEEVSKLRT SSFLSSAPVA
1410 1420 1430 1440 1450
AAPELYGACA PELPGEPERS VMETADEGRL DSAMETSMMS VQENMLSEEK
1460 1470 1480 1490 1500
QRIMLLERTL QLKEEENKRL NQRLMSQSLS SVSSRHSEKI AIRDFQVGDL
1510 1520 1530 1540 1550
VLIILDERHD NYVLFTVSPT LYFLHSESLP ALDLKPGEGA SGASRRPWVL
1560 1570 1580
GKVMEKEYCQ AKKAQNRFKV PLGTKFYRVK AVSWNKKV
Length:1,588
Mass (Da):182,350
Last modified:July 27, 2011 - v3
Checksum:i2D14F1434604C0AF
GO

Sequence cautioni

The sequence BAC30793.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti809 – 8091S → T in BAB16846 (PubMed:12095676).Curated
Sequence conflicti809 – 8091S → T in BAB85610 (PubMed:12095676).Curated
Sequence conflicti981 – 9811Q → E in BAB16846 (PubMed:12095676).Curated
Sequence conflicti981 – 9811Q → E in BAB85610 (PubMed:12095676).Curated
Sequence conflicti1222 – 12221D → A in CAA57761 (PubMed:7724523).Curated
Sequence conflicti1450 – 14512KQ → NE in CAB92238 (PubMed:11207567).Curated
Sequence conflicti1537 – 15393Missing in CAB92238 (PubMed:11207567).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050017 mRNA. Translation: BAB16846.2.
AB070619 mRNA. Translation: BAB85610.1.
AC102781 Genomic DNA. No translation available.
AC139064 Genomic DNA. No translation available.
AK041038 mRNA. Translation: BAC30793.1. Different initiation.
AK159066 mRNA. Translation: BAE34792.1.
X82318 mRNA. Translation: CAA57761.1.
AJ242720 mRNA. Translation: CAB92238.1.
CCDSiCCDS35507.1.
PIRiI48282.
RefSeqiNP_033956.2. NM_009826.4.
UniGeneiMm.293811.

Genome annotation databases

EnsembliENSMUST00000027040; ENSMUSP00000027040; ENSMUSG00000025907.
GeneIDi12421.
KEGGimmu:12421.
UCSCiuc007afr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050017 mRNA. Translation: BAB16846.2.
AB070619 mRNA. Translation: BAB85610.1.
AC102781 Genomic DNA. No translation available.
AC139064 Genomic DNA. No translation available.
AK041038 mRNA. Translation: BAC30793.1. Different initiation.
AK159066 mRNA. Translation: BAE34792.1.
X82318 mRNA. Translation: CAA57761.1.
AJ242720 mRNA. Translation: CAB92238.1.
CCDSiCCDS35507.1.
PIRiI48282.
RefSeqiNP_033956.2. NM_009826.4.
UniGeneiMm.293811.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198540. 4 interactions.
DIPiDIP-49679N.
IntActiQ9ESK9. 6 interactions.
STRINGi10090.ENSMUSP00000027040.

PTM databases

iPTMnetiQ9ESK9.
PhosphoSiteiQ9ESK9.

Proteomic databases

EPDiQ9ESK9.
MaxQBiQ9ESK9.
PaxDbiQ9ESK9.
PeptideAtlasiQ9ESK9.
PRIDEiQ9ESK9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027040; ENSMUSP00000027040; ENSMUSG00000025907.
GeneIDi12421.
KEGGimmu:12421.
UCSCiuc007afr.2. mouse.

Organism-specific databases

CTDi9821.
MGIiMGI:1341850. Rb1cc1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG4572. Eukaryota.
ENOG410XSY4. LUCA.
GeneTreeiENSGT00390000015871.
HOGENOMiHOG000154076.
HOVERGENiHBG091209.
InParanoidiQ9ESK9.
KOiK17589.
OMAiTMQQQER.
OrthoDBiEOG7B5WV6.
TreeFamiTF323750.

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.

Miscellaneous databases

ChiTaRSiRb1cc1. mouse.
PROiQ9ESK9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ESK9.
CleanExiMM_RB1CC1.
ExpressionAtlasiQ9ESK9. baseline and differential.
GenevisibleiQ9ESK9. MM.

Family and domain databases

InterProiIPR019460. Autophagy-rel_p11.
[Graphical view]
PfamiPF10377. ATG11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, characterization and mapping of the mouse and human RB1CC1 genes."
    Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A., Saeki Y., Okabe H.
    Gene 291:29-34(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, COLOCALIZATION WITH RB1, FUNCTION.
    Strain: C57BL/6J.
    Tissue: Skeletal muscle.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-1304 AND 1374-1588.
    Strain: C57BL/6J.
    Tissue: Aorta and Vein.
  4. "Stathmin interaction with a putative kinase and coiled-coil-forming protein domains."
    Maucuer A., Camonis J.H., Sobel A.
    Proc. Natl. Acad. Sci. U.S.A. 92:3100-3104(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1081-1222.
  5. "LaXp180, a mammalian ActA-binding protein, identified with the yeast two-hybrid system co-localizes with intracellular Listeria monocytogenes."
    Pfeuffer T., Goebel W., Laubinger J., Bachmann M., Kuhn M.
    Cell. Microbiol. 2:101-114(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1359-1588.
    Strain: CD-1.
  6. "Expression and regulation of RB1CC1 in developing murine and human tissues."
    Bamba N., Chano T., Taga T., Ohta S., Takeuchi Y., Okabe H.
    Int. J. Mol. Med. 14:583-587(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  7. "Rb1cc1 is critical for myoblast differentiation through Rb1 regulation."
    Watanabe R., Chano T., Inoue H., Isono T., Koiwai O., Okabe H.
    Virchows Arch. 447:643-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy."
    Ganley I.G., Lam du H., Wang J., Ding X., Chen S., Jiang X.
    J. Biol. Chem. 284:12297-12305(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ULK1 AND ATG13, SUBCELLULAR LOCATION.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; THR-238; SER-243; SER-261; SER-623; SER-646; SER-649; SER-652 AND SER-1087, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen and Testis.
  12. "Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration."
    Liang C.C., Wang C., Peng X., Gan B., Guan J.L.
    J. Biol. Chem. 285:3499-3509(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "FIP200, an essential component of mammalian autophagy is indispensible for fetal hematopoiesis."
    Liu F., Guan J.L.
    Autophagy 7:229-230(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "RB1CC1 protein positively regulates transforming growth factor-beta signaling through the modulation of Arkadia E3 ubiquitin ligase activity."
    Koinuma D., Shinozaki M., Nagano Y., Ikushima H., Horiguchi K., Goto K., Chano T., Saitoh M., Imamura T., Miyazono K., Miyazawa K.
    J. Biol. Chem. 286:32502-32512(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RNF111; SKI AND SMAD7.
  15. "The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella."
    Kageyama S., Omori H., Saitoh T., Sone T., Guan J.L., Akira S., Imamoto F., Noda T., Yoshimori T.
    Mol. Biol. Cell 22:2290-2300(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Suppression of autophagy by FIP200 deletion impairs DNA damage repair and increases cell death upon treatments with anticancer agents."
    Bae H., Guan J.L.
    Mol. Cancer Res. 9:1232-1241(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Autophagy induced by calcium phosphate precipitates involves endoplasmic reticulum membranes in autophagosome biogenesis."
    Chen X., Li M., Chen D., Gao W., Guan J.L., Komatsu M., Yin X.M.
    PLoS ONE 7:E52347-E52347(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "FIP200 regulates targeting of Atg16L1 to the isolation membrane."
    Nishimura T., Kaizuka T., Cadwell K., Sahani M.H., Saitoh T., Akira S., Virgin H.W., Mizushima N.
    EMBO Rep. 14:284-291(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATG16L1.

Entry informationi

Entry nameiRBCC1_MOUSE
AccessioniPrimary (citable) accession number: Q9ESK9
Secondary accession number(s): E9QLQ2
, Q3TXX2, Q61384, Q8BRY9, Q9JK14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.