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Q8TDY2

- RBCC1_HUMAN

UniProt

Q8TDY2 - RBCC1_HUMAN

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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

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 - 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
Complete GO annotation...

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. nuclear membrane Source: HPA
  3. pre-autophagosomal structure membrane Source: UniProtKB
  4. ULK1-ATG13-FIP200 complex Source: UniProtKB
Complete GO annotation...

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

BgeeiQ8TDY2.
CleanExiHS_RB1CC1.
ExpressionAtlasiQ8TDY2. baseline and differential.
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. 45 interactions.
DIPiDIP-45969N.
IntActiQ8TDY2. 39 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.
GeneTreeiENSGT00390000015871.
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

        10         20         30         40         50
MKLYVFLVNT GTTLTFDTEL TVQTVADLKH AIQSKYKIAI QHQVLVVNGG
60 70 80 90 100
ECMAADRRVC TYSAGTDTNP IFLFNKEMIL CDRPPAIPKT TFSTENDMEI
110 120 130 140 150
KVEESLMMPA VFHTVASRTQ LALEMYEVAK KLCSFCEGLV HDEHLQHQGW
160 170 180 190 200
AAIMANLEDC SNSYQKLLFK FESIYSNYLQ SIEDIKLKLT HLGTAVSVMA
210 220 230 240 250
KIPLLECLTR HSYRECLGRL DSLPEHEDSE KAEMKRSTEL VLSPDMPRTT
260 270 280 290 300
NESLLTSFPK SVEHVSPDTA DAESGKEIRE SCQSTVHQQD ETTIDTKDGD
310 320 330 340 350
LPFFNVSLLD WINVQDRPND VESLVRKCFD SMSRLDPRII RPFIAECRQT
360 370 380 390 400
IAKLDNQNMK AIKGLEDRLY ALDQMIASCG RLVNEQKELA QGFLANQKRA
410 420 430 440 450
ENLKDASVLP DLCLSHANQL MIMLQNHRKL LDIKQKCTTA KQELANNLHV
460 470 480 490 500
RLKWCCFVML HADQDGEKLQ ALLRLVIELL ERVKIVEALS TVPQMYCLAV
510 520 530 540 550
VEVVRRKMFI KHYREWAGAL VKDGKRLYEA EKSKRESFGK LFRKSFLRNR
560 570 580 590 600
LFRGLDSWPP SFCTQKPRKF DCELPDISLK DLQFLQSFCP SEVQPFLRVP
610 620 630 640 650
LLCDFEPLHQ HVLALHNLVK AAQSLDEMSQ TITDLLSEQK ASVSQTSPQS
660 670 680 690 700
ASSPRMESTA GITTTTSPRT PPPLTVQDPL CPAVCPLEEL SPDSIDAHTF
710 720 730 740 750
DFETIPHPNI EQTIHQVSLD LDSLAESPES DFMSAVNEFV IEENLSSPNP
760 770 780 790 800
ISDPQSPEMM VESLYSSVIN AIDSRRMQDT NVCGKEDFGD HTSLNVQLER
810 820 830 840 850
CRVVAQDSHF SIQTIKEDLC HFRTFVQKEQ CDFSNSLKCT AVEIRNIIEK
860 870 880 890 900
VKCSLEITLK EKHQKELLSL KNEYEGKLDG LIKETEENEN KIKKLKGELV
910 920 930 940 950
CLEEVLQNKD NEFALVKHEK EAVICLQNEK DQKLLEMENI MHSQNCEIKE
960 970 980 990 1000
LKQSREIVLE DLKKLHVEND EKLQLLRAEL QSLEQSHLKE LEDTLQVRHI
1010 1020 1030 1040 1050
QEFEKVMTDH RVSLEELKKE NQQIINQIQE SHAEIIQEKE KQLQELKLKV
1060 1070 1080 1090 1100
SDLSDTRCKL EVELALKEAE TDEIKILLEE SRAQQKETLK SLLEQETENL
1110 1120 1130 1140 1150
RTEISKLNQK IQDNNENYQV GLAELRTLMT IEKDQCISEL ISRHEEESNI
1160 1170 1180 1190 1200
LKAELNKVTS LHNQAFEIEK NLKEQIIELQ SKLDSELSAL ERQKDEKITQ
1210 1220 1230 1240 1250
QEEKYEAIIQ NLEKDRQKLV SSQEQDREQL IQKLNCEKDE AIQTALKEFK
1260 1270 1280 1290 1300
LEREVVEKEL LEKVKHLENQ IAKSPAIDST RGDSSSLVAE LQEKLQEEKA
1310 1320 1330 1340 1350
KFLEQLEEQE KRKNEEMQNV RTSLIAEQQT NFNTVLTREK MRKENIINDL
1360 1370 1380 1390 1400
SDKLKSTMQQ QERDKDLIES LSEDRARLLE EKKKLEEEVS KLRSSSFVPS
1410 1420 1430 1440 1450
PYVATAPELY GACAPELPGE SDRSAVETAD EGRVDSAMET SMMSVQENIH
1460 1470 1480 1490 1500
MLSEEKQRIM LLERTLQLKE EENKRLNQRL MSQSMSSVSS RHSEKIAIRD
1510 1520 1530 1540 1550
FQVGDLVLII LDERHDNYVL FTVSPTLYFL HSESLPALDL KPGEGASGAS
1560 1570 1580 1590
RRPWVLGKVM EKEYCQAKKA QNRFKVPLGT KFYRVKAVSW NKKV
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. 45 interactions.
DIPi DIP-45969N.
IntActi Q8TDY2. 39 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.
GeneTreei ENSGT00390000015871.
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

Bgeei Q8TDY2.
CleanExi HS_RB1CC1.
ExpressionAtlasi Q8TDY2. baseline and differential.
Genevestigatori Q8TDY2.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 105 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