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Q8TDY2

- RBCC1_HUMAN

UniProt

Q8TDY2 - RBCC1_HUMAN

Protein

RB1-inducible coiled-coil protein 1

Gene

RB1CC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 3 (23 Oct 2007)
      Previous versions | rss
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    Functioni

    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 similarity. Implicated in the regulation of RB1 expression. Functions as a DNA-binding transcription factor. Is a potent regulator of the RB1 pathway and a 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 similarity7 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. autophagic vacuole assembly Source: Ensembl
    2. cell cycle Source: UniProtKB-KW
    3. heart development Source: Ensembl
    4. JNK cascade Source: Ensembl
    5. liver development Source: Ensembl
    6. negative regulation of apoptotic process Source: Ensembl
    7. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    8. positive regulation of cell size Source: Ensembl
    9. positive regulation of protein phosphorylation Source: Ensembl
    10. regulation of autophagy Source: UniProtKB
    11. regulation of transcription, DNA-templated Source: UniProtKB-KW
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Autophagy, Cell cycle, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RB1-inducible coiled-coil protein 1
    Alternative name(s):
    FAK family kinase-interacting protein of 200 kDa
    Short name:
    FIP200
    Gene namesi
    Name:RB1CC1
    Synonyms:KIAA0203, RBICC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:15574. RB1CC1.

    Subcellular locationi

    Nucleus. Cytoplasmcytosol. Preautophagosomal structure membrane; Peripheral membrane protein
    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.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB-SubCell
    3. nuclear membrane Source: HPA
    4. pre-autophagosomal structure membrane Source: UniProtKB
    5. ULK1-ATG13-FIP200 complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA34248.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15941594RB1-inducible coiled-coil protein 1PRO_0000097183Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei237 – 2371Phosphoserine1 Publication
    Modified residuei243 – 2431Phosphoserine1 Publication
    Modified residuei257 – 2571Phosphoserine1 Publication
    Modified residuei624 – 6241Phosphoserine1 Publication
    Modified residuei647 – 6471Phosphoserine1 Publication
    Modified residuei653 – 6531Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8TDY2.
    PaxDbiQ8TDY2.
    PRIDEiQ8TDY2.

    PTM databases

    PhosphoSiteiQ8TDY2.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Developmental stagei

    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.1 Publication

    Gene expression databases

    ArrayExpressiQ8TDY2.
    BgeeiQ8TDY2.
    CleanExiHS_RB1CC1.
    GenevestigatoriQ8TDY2.

    Organism-specific databases

    HPAiHPA024391.
    HPA053049.

    Interactioni

    Subunit structurei

    Part of a complex consisting of ATG13/KIAA0652, ULK1 and RB1CC1. This complex associates with ATG101. Interacts with PTK2/FAK1 and PTK2B/PYK2. Interactcs with ATG16L1, GABARAP and GABARAPL1. Interacts with RFWD2 in the cytoplasm of proliferating cells in response to UV stimulation.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATG13O751438EBI-1047793,EBI-2798775
    ATG16L1Q676U55EBI-1047793,EBI-535909
    TBKBP1A7MCY62EBI-1047793,EBI-359969
    ULK1O753857EBI-1047793,EBI-908831

    Protein-protein interaction databases

    BioGridi115160. 42 interactions.
    DIPiDIP-45969N.
    IntActiQ8TDY2. 38 interactions.
    MINTiMINT-5003383.
    STRINGi9606.ENSP00000025008.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TDY2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili859 – 1397539Sequence AnalysisAdd
    BLAST
    Coiled coili1438 – 148548Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi566 – 5694Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi663 – 6664Poly-Thr

    Sequence similaritiesi

    Belongs to the ATG17 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG280878.
    HOGENOMiHOG000154076.
    HOVERGENiHBG091209.
    InParanoidiQ8TDY2.
    KOiK17589.
    OMAiEQSHLKE.
    OrthoDBiEOG7B5WV6.
    PhylomeDBiQ8TDY2.
    TreeFamiTF323750.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8TDY2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKLYVFLVNT GTTLTFDTEL TVQTVADLKH AIQSKYKIAI QHQVLVVNGG     50
    ECMAADRRVC TYSAGTDTNP IFLFNKEMIL CDRPPAIPKT TFSTENDMEI 100
    KVEESLMMPA VFHTVASRTQ LALEMYEVAK KLCSFCEGLV HDEHLQHQGW 150
    AAIMANLEDC SNSYQKLLFK FESIYSNYLQ SIEDIKLKLT HLGTAVSVMA 200
    KIPLLECLTR HSYRECLGRL DSLPEHEDSE KAEMKRSTEL VLSPDMPRTT 250
    NESLLTSFPK SVEHVSPDTA DAESGKEIRE SCQSTVHQQD ETTIDTKDGD 300
    LPFFNVSLLD WINVQDRPND VESLVRKCFD SMSRLDPRII RPFIAECRQT 350
    IAKLDNQNMK AIKGLEDRLY ALDQMIASCG RLVNEQKELA QGFLANQKRA 400
    ENLKDASVLP DLCLSHANQL MIMLQNHRKL LDIKQKCTTA KQELANNLHV 450
    RLKWCCFVML HADQDGEKLQ ALLRLVIELL ERVKIVEALS TVPQMYCLAV 500
    VEVVRRKMFI KHYREWAGAL VKDGKRLYEA EKSKRESFGK LFRKSFLRNR 550
    LFRGLDSWPP SFCTQKPRKF DCELPDISLK DLQFLQSFCP SEVQPFLRVP 600
    LLCDFEPLHQ HVLALHNLVK AAQSLDEMSQ TITDLLSEQK ASVSQTSPQS 650
    ASSPRMESTA GITTTTSPRT PPPLTVQDPL CPAVCPLEEL SPDSIDAHTF 700
    DFETIPHPNI EQTIHQVSLD LDSLAESPES DFMSAVNEFV IEENLSSPNP 750
    ISDPQSPEMM VESLYSSVIN AIDSRRMQDT NVCGKEDFGD HTSLNVQLER 800
    CRVVAQDSHF SIQTIKEDLC HFRTFVQKEQ CDFSNSLKCT AVEIRNIIEK 850
    VKCSLEITLK EKHQKELLSL KNEYEGKLDG LIKETEENEN KIKKLKGELV 900
    CLEEVLQNKD NEFALVKHEK EAVICLQNEK DQKLLEMENI MHSQNCEIKE 950
    LKQSREIVLE DLKKLHVEND EKLQLLRAEL QSLEQSHLKE LEDTLQVRHI 1000
    QEFEKVMTDH RVSLEELKKE NQQIINQIQE SHAEIIQEKE KQLQELKLKV 1050
    SDLSDTRCKL EVELALKEAE TDEIKILLEE SRAQQKETLK SLLEQETENL 1100
    RTEISKLNQK IQDNNENYQV GLAELRTLMT IEKDQCISEL ISRHEEESNI 1150
    LKAELNKVTS LHNQAFEIEK NLKEQIIELQ SKLDSELSAL ERQKDEKITQ 1200
    QEEKYEAIIQ NLEKDRQKLV SSQEQDREQL IQKLNCEKDE AIQTALKEFK 1250
    LEREVVEKEL LEKVKHLENQ IAKSPAIDST RGDSSSLVAE LQEKLQEEKA 1300
    KFLEQLEEQE KRKNEEMQNV RTSLIAEQQT NFNTVLTREK MRKENIINDL 1350
    SDKLKSTMQQ QERDKDLIES LSEDRARLLE EKKKLEEEVS KLRSSSFVPS 1400
    PYVATAPELY GACAPELPGE SDRSAVETAD EGRVDSAMET SMMSVQENIH 1450
    MLSEEKQRIM LLERTLQLKE EENKRLNQRL MSQSMSSVSS RHSEKIAIRD 1500
    FQVGDLVLII LDERHDNYVL FTVSPTLYFL HSESLPALDL KPGEGASGAS 1550
    RRPWVLGKVM EKEYCQAKKA QNRFKVPLGT KFYRVKAVSW NKKV 1594
    Length:1,594
    Mass (Da):183,091
    Last modified:October 23, 2007 - v3
    Checksum:iC9C90A328875016A
    GO
    Isoform 2 (identifier: Q8TDY2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1543-1545: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,591
    Mass (Da):182,848
    Checksum:iDF39499D10C7244E
    GO

    Sequence cautioni

    The sequence BAA13194.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1136 – 11361C → R in BAB69690. (PubMed:11850849)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti234 – 2341M → T.3 Publications
    Corresponds to variant rs17337252 [ dbSNP | Ensembl ].
    VAR_023776
    Natural varianti708 – 7081P → L.
    Corresponds to variant rs34016926 [ dbSNP | Ensembl ].
    VAR_051309
    Natural varianti1216 – 12161R → K.
    Corresponds to variant rs35534432 [ dbSNP | Ensembl ].
    VAR_051310
    Natural varianti1314 – 13141N → K.
    Corresponds to variant rs34701924 [ dbSNP | Ensembl ].
    VAR_051311
    Natural varianti1424 – 14241S → F.
    Corresponds to variant rs35342973 [ dbSNP | Ensembl ].
    VAR_051312
    Natural varianti1514 – 15141R → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_033031

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1543 – 15453Missing in isoform 2. 1 PublicationVSP_040097

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB059622 mRNA. Translation: BAB69690.1.
    D86958 mRNA. Translation: BAA13194.2. Different initiation.
    AC090814 Genomic DNA. No translation available.
    AC113139 Genomic DNA. No translation available.
    BC017556 mRNA. Translation: AAH17556.1.
    AY173931 mRNA. Translation: AAO17545.1.
    CCDSiCCDS34892.1. [Q8TDY2-1]
    CCDS47856.1. [Q8TDY2-2]
    RefSeqiNP_001077086.1. NM_001083617.1. [Q8TDY2-2]
    NP_055596.3. NM_014781.4. [Q8TDY2-1]
    XP_006716554.1. XM_006716491.1. [Q8TDY2-2]
    UniGeneiHs.196102.

    Genome annotation databases

    EnsembliENST00000025008; ENSP00000025008; ENSG00000023287. [Q8TDY2-1]
    ENST00000435644; ENSP00000396067; ENSG00000023287. [Q8TDY2-2]
    GeneIDi9821.
    KEGGihsa:9821.
    UCSCiuc003xre.4. human. [Q8TDY2-1]
    uc003xrf.4. human. [Q8TDY2-2]

    Polymorphism databases

    DMDMi160359050.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB059622 mRNA. Translation: BAB69690.1 .
    D86958 mRNA. Translation: BAA13194.2 . Different initiation.
    AC090814 Genomic DNA. No translation available.
    AC113139 Genomic DNA. No translation available.
    BC017556 mRNA. Translation: AAH17556.1 .
    AY173931 mRNA. Translation: AAO17545.1 .
    CCDSi CCDS34892.1. [Q8TDY2-1 ]
    CCDS47856.1. [Q8TDY2-2 ]
    RefSeqi NP_001077086.1. NM_001083617.1. [Q8TDY2-2 ]
    NP_055596.3. NM_014781.4. [Q8TDY2-1 ]
    XP_006716554.1. XM_006716491.1. [Q8TDY2-2 ]
    UniGenei Hs.196102.

    3D structure databases

    ProteinModelPortali Q8TDY2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115160. 42 interactions.
    DIPi DIP-45969N.
    IntActi Q8TDY2. 38 interactions.
    MINTi MINT-5003383.
    STRINGi 9606.ENSP00000025008.

    PTM databases

    PhosphoSitei Q8TDY2.

    Polymorphism databases

    DMDMi 160359050.

    Proteomic databases

    MaxQBi Q8TDY2.
    PaxDbi Q8TDY2.
    PRIDEi Q8TDY2.

    Protocols and materials databases

    DNASUi 9821.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000025008 ; ENSP00000025008 ; ENSG00000023287 . [Q8TDY2-1 ]
    ENST00000435644 ; ENSP00000396067 ; ENSG00000023287 . [Q8TDY2-2 ]
    GeneIDi 9821.
    KEGGi hsa:9821.
    UCSCi uc003xre.4. human. [Q8TDY2-1 ]
    uc003xrf.4. human. [Q8TDY2-2 ]

    Organism-specific databases

    CTDi 9821.
    GeneCardsi GC08M053584.
    H-InvDB HIX0007503.
    HGNCi HGNC:15574. RB1CC1.
    HPAi HPA024391.
    HPA053049.
    MIMi 606837. gene.
    neXtProti NX_Q8TDY2.
    PharmGKBi PA34248.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG280878.
    HOGENOMi HOG000154076.
    HOVERGENi HBG091209.
    InParanoidi Q8TDY2.
    KOi K17589.
    OMAi EQSHLKE.
    OrthoDBi EOG7B5WV6.
    PhylomeDBi Q8TDY2.
    TreeFami TF323750.

    Miscellaneous databases

    ChiTaRSi RB1CC1. human.
    GeneWikii RB1CC1.
    GenomeRNAii 9821.
    NextBioi 36990.
    PROi Q8TDY2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TDY2.
    Bgeei Q8TDY2.
    CleanExi HS_RB1CC1.
    Genevestigatori Q8TDY2.

    Family and domain databases

    InterProi IPR019460. Autophagy-rel_p11.
    [Graphical view ]
    Pfami PF10377. ATG11. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of RB1CC1, a novel human gene that can induce RB1 in various human cells."
      Chano T., Ikegawa S., Kontani K., Okabe H., Baldini N., Saeki Y.
      Oncogene 21:1295-1298(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-234, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, INDUCTION OF RB1 EXPRESSION.
      Tissue: Osteosarcoma.
    2. "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."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-234.
      Tissue: Myeloid.
    3. 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
      Cited for: SEQUENCE REVISION.
    4. "DNA sequence and analysis of human chromosome 8."
      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.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-234.
      Tissue: Uterus.
    6. "Suppression of Pyk2 kinase and cellular activities by FIP200."
      Ueda H., Abbi S., Zheng C., Guan J.-L.
      J. Cell Biol. 149:423-430(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1377-1594, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK1 AND PTK2B/PYK2.
    7. "Preferential expression of RB1-inducible coiled-coil 1 in terminal differentiated musculoskeletal cells."
      Chano T., Saeki Y., Serra M., Matsumoto K., Okabe H.
      Am. J. Pathol. 161:359-364(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION.
    8. "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: CHARACTERIZATION, FUNCTION.
    9. "Regulation of focal adhesion kinase by a novel protein inhibitor FIP200."
      Abbi S., Ueda H., Zheng C., Cooper L.A., Zhao J., Christopher R., Guan J.L.
      Mol. Biol. Cell 13:3178-3191(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTK2/FAK1.
    10. "Truncating mutations of RB1CC1 in human breast cancer."
      Chano T., Kontani K., Teramoto K., Okabe H., Ikegawa S.
      Nat. Genet. 31:285-288(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN BREAST CANCER.
    11. "RB1CC1 suppresses cell cycle progression through RB1 expression in human neoplastic cells."
      Kontani K., Chano T., Ozaki Y., Tezuka N., Sawai S., Fujino S., Saeki Y., Okabe H.
      Int. J. Mol. Med. 12:767-769(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-624; SER-647 AND SER-653, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Atg101, a novel mammalian autophagy protein interacting with Atg13."
      Hosokawa N., Sasaki T., Iemura S.I., Natsume T., Hara T., Mizushima N.
      Autophagy 5:973-979(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    16. "Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy."
      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.
      Mol. Biol. Cell 20:1981-1991(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ULK1 AND ATG13.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "p53 inhibits autophagy by interacting with the human ortholog of yeast Atg17, RB1CC1/FIP200."
      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.
      Cell Cycle 10:2763-2769(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs."
      Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B., Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.
      J. Biol. Chem. 287:39275-39290(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GABARAP AND GABARAPL1.
    23. "Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas."
      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.
      Breast Cancer Res. 9:R5-R5(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CYS-1514.
    24. "The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy."
      Kobayashi S., Yoneda-Kato N., Itahara N., Yoshida A., Kato J.Y.
      BMC Biochem. 14:1-1(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RFWD2.
    25. "Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-dependent and -independent autophagy."
      Gammoh N., Florey O., Overholtzer M., Jiang X.
      Nat. Struct. Mol. Biol. 20:144-149(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ATG16L1.

    Entry informationi

    Entry nameiRBCC1_HUMAN
    AccessioniPrimary (citable) accession number: Q8TDY2
    Secondary accession number(s): Q86YR4, Q8WVU9, Q92601
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 104 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3