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Q8TDY2 (RBCC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RB1-inducible coiled-coil protein 1
Alternative name(s):
FAK family kinase-interacting protein of 200 kDa
Short name=FIP200
Gene names
Name:RB1CC1
Synonyms:KIAA0203, RBICC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1594 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.20 Ref.25

Subunit structure

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. Ref.6 Ref.9 Ref.15 Ref.16 Ref.20 Ref.22 Ref.24 Ref.25

Subcellular location

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. Ref.1 Ref.6

Tissue specificity

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. Ref.1 Ref.7

Developmental stage

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. Ref.7

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.

Sequence similarities

Belongs to the ATG17 family.

Sequence caution

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

Ontologies

Keywords
   Biological processAutophagy
Cell cycle
Transcription
Transcription regulation
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from electronic annotation. Source: Ensembl

autophagic vacuole assembly

Inferred from electronic annotation. Source: Ensembl

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

heart development

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell size

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentULK1-ATG13-FIP200 complex

Inferred from physical interaction Ref.16. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from direct assay. Source: HPA

pre-autophagosomal structure membrane

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TDY2-1)

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.
Isoform 2 (identifier: Q8TDY2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1543-1545: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15941594RB1-inducible coiled-coil protein 1
PRO_0000097183

Regions

Coiled coil859 – 1397539 Potential
Coiled coil1438 – 148548 Potential
Motif566 – 5694Nuclear localization signal Potential
Compositional bias663 – 6664Poly-Thr

Amino acid modifications

Modified residue2371Phosphoserine Ref.13
Modified residue2431Phosphoserine Ref.17
Modified residue2571Phosphoserine Ref.17
Modified residue6241Phosphoserine Ref.13
Modified residue6471Phosphoserine Ref.13
Modified residue6531Phosphoserine Ref.13

Natural variations

Alternative sequence1543 – 15453Missing in isoform 2.
VSP_040097
Natural variant2341M → T. Ref.1 Ref.2 Ref.5
Corresponds to variant rs17337252 [ dbSNP | Ensembl ].
VAR_023776
Natural variant7081P → L.
Corresponds to variant rs34016926 [ dbSNP | Ensembl ].
VAR_051309
Natural variant12161R → K.
Corresponds to variant rs35534432 [ dbSNP | Ensembl ].
VAR_051310
Natural variant13141N → K.
Corresponds to variant rs34701924 [ dbSNP | Ensembl ].
VAR_051311
Natural variant14241S → F.
Corresponds to variant rs35342973 [ dbSNP | Ensembl ].
VAR_051312
Natural variant15141R → C in a breast cancer sample; somatic mutation. Ref.23
VAR_033031

Experimental info

Sequence conflict11361C → R in BAB69690. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 23, 2007. Version 3.
Checksum: C9C90A328875016A

FASTA1,594183,091
        10         20         30         40         50         60 
MKLYVFLVNT GTTLTFDTEL TVQTVADLKH AIQSKYKIAI QHQVLVVNGG ECMAADRRVC 

        70         80         90        100        110        120 
TYSAGTDTNP IFLFNKEMIL CDRPPAIPKT TFSTENDMEI KVEESLMMPA VFHTVASRTQ 

       130        140        150        160        170        180 
LALEMYEVAK KLCSFCEGLV HDEHLQHQGW AAIMANLEDC SNSYQKLLFK FESIYSNYLQ 

       190        200        210        220        230        240 
SIEDIKLKLT HLGTAVSVMA KIPLLECLTR HSYRECLGRL DSLPEHEDSE KAEMKRSTEL 

       250        260        270        280        290        300 
VLSPDMPRTT NESLLTSFPK SVEHVSPDTA DAESGKEIRE SCQSTVHQQD ETTIDTKDGD 

       310        320        330        340        350        360 
LPFFNVSLLD WINVQDRPND VESLVRKCFD SMSRLDPRII RPFIAECRQT IAKLDNQNMK 

       370        380        390        400        410        420 
AIKGLEDRLY ALDQMIASCG RLVNEQKELA QGFLANQKRA ENLKDASVLP DLCLSHANQL 

       430        440        450        460        470        480 
MIMLQNHRKL LDIKQKCTTA KQELANNLHV RLKWCCFVML HADQDGEKLQ ALLRLVIELL 

       490        500        510        520        530        540 
ERVKIVEALS TVPQMYCLAV VEVVRRKMFI KHYREWAGAL VKDGKRLYEA EKSKRESFGK 

       550        560        570        580        590        600 
LFRKSFLRNR LFRGLDSWPP SFCTQKPRKF DCELPDISLK DLQFLQSFCP SEVQPFLRVP 

       610        620        630        640        650        660 
LLCDFEPLHQ HVLALHNLVK AAQSLDEMSQ TITDLLSEQK ASVSQTSPQS ASSPRMESTA 

       670        680        690        700        710        720 
GITTTTSPRT PPPLTVQDPL CPAVCPLEEL SPDSIDAHTF DFETIPHPNI EQTIHQVSLD 

       730        740        750        760        770        780 
LDSLAESPES DFMSAVNEFV IEENLSSPNP ISDPQSPEMM VESLYSSVIN AIDSRRMQDT 

       790        800        810        820        830        840 
NVCGKEDFGD HTSLNVQLER CRVVAQDSHF SIQTIKEDLC HFRTFVQKEQ CDFSNSLKCT 

       850        860        870        880        890        900 
AVEIRNIIEK VKCSLEITLK EKHQKELLSL KNEYEGKLDG LIKETEENEN KIKKLKGELV 

       910        920        930        940        950        960 
CLEEVLQNKD NEFALVKHEK EAVICLQNEK DQKLLEMENI MHSQNCEIKE LKQSREIVLE 

       970        980        990       1000       1010       1020 
DLKKLHVEND EKLQLLRAEL QSLEQSHLKE LEDTLQVRHI QEFEKVMTDH RVSLEELKKE 

      1030       1040       1050       1060       1070       1080 
NQQIINQIQE SHAEIIQEKE KQLQELKLKV SDLSDTRCKL EVELALKEAE TDEIKILLEE 

      1090       1100       1110       1120       1130       1140 
SRAQQKETLK SLLEQETENL RTEISKLNQK IQDNNENYQV GLAELRTLMT IEKDQCISEL 

      1150       1160       1170       1180       1190       1200 
ISRHEEESNI LKAELNKVTS LHNQAFEIEK NLKEQIIELQ SKLDSELSAL ERQKDEKITQ 

      1210       1220       1230       1240       1250       1260 
QEEKYEAIIQ NLEKDRQKLV SSQEQDREQL IQKLNCEKDE AIQTALKEFK LEREVVEKEL 

      1270       1280       1290       1300       1310       1320 
LEKVKHLENQ IAKSPAIDST RGDSSSLVAE LQEKLQEEKA KFLEQLEEQE KRKNEEMQNV 

      1330       1340       1350       1360       1370       1380 
RTSLIAEQQT NFNTVLTREK MRKENIINDL SDKLKSTMQQ QERDKDLIES LSEDRARLLE 

      1390       1400       1410       1420       1430       1440 
EKKKLEEEVS KLRSSSFVPS PYVATAPELY GACAPELPGE SDRSAVETAD EGRVDSAMET 

      1450       1460       1470       1480       1490       1500 
SMMSVQENIH MLSEEKQRIM LLERTLQLKE EENKRLNQRL MSQSMSSVSS RHSEKIAIRD 

      1510       1520       1530       1540       1550       1560 
FQVGDLVLII LDERHDNYVL FTVSPTLYFL HSESLPALDL KPGEGASGAS RRPWVLGKVM 

      1570       1580       1590 
EKEYCQAKKA QNRFKVPLGT KFYRVKAVSW NKKV 

« Hide

Isoform 2 [UniParc].

Checksum: DF39499D10C7244E
Show »

FASTA1,591182,848

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001077086.1. NM_001083617.1.
NP_055596.3. NM_014781.4.
UniGeneHs.196102.

3D structure databases

ProteinModelPortalQ8TDY2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115160. 41 interactions.
DIPDIP-45969N.
IntActQ8TDY2. 38 interactions.
MINTMINT-5003383.
STRING9606.ENSP00000025008.

PTM databases

PhosphoSiteQ8TDY2.

Polymorphism databases

DMDM160359050.

Proteomic databases

PaxDbQ8TDY2.
PRIDEQ8TDY2.

Protocols and materials databases

DNASU9821.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000025008; ENSP00000025008; ENSG00000023287. [Q8TDY2-1]
ENST00000435644; ENSP00000396067; ENSG00000023287. [Q8TDY2-2]
ENST00000539297; ENSP00000445960; ENSG00000023287. [Q8TDY2-2]
GeneID9821.
KEGGhsa:9821.
UCSCuc003xre.4. human. [Q8TDY2-1]
uc003xrf.4. human. [Q8TDY2-2]

Organism-specific databases

CTD9821.
GeneCardsGC08M053584.
H-InvDBHIX0007503.
HGNCHGNC:15574. RB1CC1.
HPAHPA024391.
HPA053049.
MIM606837. gene.
neXtProtNX_Q8TDY2.
PharmGKBPA34248.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG280878.
HOGENOMHOG000154076.
HOVERGENHBG091209.
InParanoidQ8TDY2.
KOK17589.
OMATMQQQER.
OrthoDBEOG7B5WV6.
PhylomeDBQ8TDY2.
TreeFamTF323750.

Gene expression databases

ArrayExpressQ8TDY2.
BgeeQ8TDY2.
CleanExHS_RB1CC1.
GenevestigatorQ8TDY2.

Family and domain databases

InterProIPR019460. Autophagy-rel_p11.
[Graphical view]
PfamPF10377. ATG11. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRB1CC1. human.
GeneWikiRB1CC1.
GenomeRNAi9821.
NextBio36990.
PROQ8TDY2.
SOURCESearch...

Entry information

Entry nameRBCC1_HUMAN
AccessionPrimary (citable) accession number: Q8TDY2
Secondary accession number(s): Q86YR4, Q8WVU9, Q92601
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM