Q8TDY2 (RBCC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1594 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Involved in autophagy. Required for autophagosome formation By similarity. Inhibits PTK2/FAK1 and PTK2B/PYK2 activity and activation of downstream signaling pathways. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
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. Ref.6 Ref.9 Ref.14 Ref.15
Subcellular location	Nucleus. Cytoplasm › cytosol. Preautophagosomal structure By similarity. 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 caution	The sequence BAA13194.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Autophagy Cell cycle Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JNK cascade Inferred from electronic annotation. Source: Compara autophagic vacuole assembly Inferred from electronic annotation. Source: Compara cell cycle Inferred from electronic annotation. Source: UniProtKB-KW heart development Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell size Inferred from electronic annotation. Source: Compara positive regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara regulation of autophagy Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	ULK1-ATG13-FIP200 complex Inferred from physical interaction Ref.15. Source: UniProtKB cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell pre-autophagosomal structure membrane Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATG13	O75143	5	EBI-1047793,EBI-2798775
TBKBP1	A7MCY6	2	EBI-1047793,EBI-359969
ULK1	O75385	4	EBI-1047793,EBI-908831

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1594	1594	RB1-inducible coiled-coil protein 1		PRO_0000097183
Regions
	Coiled coil	859 – 1397	539	Potential
	Coiled coil	1438 – 1485	48	Potential
	Motif	566 – 569	4	Nuclear localization signal Potential
	Compositional bias	663 – 666	4	Poly-Thr
Amino acid modifications
	Modified residue	237	1	Phosphoserine Ref.13
	Modified residue	243	1	Phosphoserine Ref.16
	Modified residue	257	1	Phosphoserine Ref.16
	Modified residue	261	1	Phosphoserine By similarity
	Modified residue	624	1	Phosphoserine Ref.13
	Modified residue	647	1	Phosphoserine Ref.13
	Modified residue	653	1	Phosphoserine Ref.13
	Modified residue	666	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	1543 – 1545	3	Missing in isoform 2.		VSP_040097
	Natural variant	234	1	M → T. Ref.1 Ref.2 Ref.5 Corresponds to variant rs17337252 [ dbSNP | Ensembl ].		VAR_023776
	Natural variant	708	1	P → L. Corresponds to variant rs34016926 [ dbSNP | Ensembl ].		VAR_051309
	Natural variant	1216	1	R → K. Corresponds to variant rs35534432 [ dbSNP | Ensembl ].		VAR_051310
	Natural variant	1314	1	N → K. Corresponds to variant rs34701924 [ dbSNP | Ensembl ].		VAR_051311
	Natural variant	1424	1	S → F. Corresponds to variant rs35342973 [ dbSNP | Ensembl ].		VAR_051312
	Natural variant	1514	1	R → C in a breast cancer sample; somatic mutation. Ref.20		VAR_033031
Experimental info
	Sequence conflict	1136	1	C → R in BAB69690. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 23, 2007. Version 3. Checksum: C9C90A328875016A	FASTA	1,594	183,091
	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
	Isoform 2 [UniParc]. Checksum: DF39499D10C7244E	FASTA	1,591	182,848
	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 KPASGASRRP WVLGKVMEKE 1570 1580 1590 YCQAKKAQNR FKVPLGTKFY RVKAVSWNKK V

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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.
[15]	"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.
[16]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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.
[18]	"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].
[19]	"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].
[20]	"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.
+	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.
IPI	IPI00783392. IPI00794069.
RefSeq	NP_001077086.1. NM_001083617.1. NP_055596.3. NM_014781.4.
UniGene	Hs.196102.
3D structure databases
ProteinModelPortal	Q8TDY2.
SMR	Q8TDY2. Positions 1-67.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8TDY2. 35 interactions.
STRING	9606.ENSP00000025008.
PTM databases
PhosphoSite	Q8TDY2.
Polymorphism databases
DMDM	160359050.
Proteomic databases
PaxDb	Q8TDY2.
PRIDE	Q8TDY2.
Protocols and materials databases
DNASU	9821.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000025008; ENSP00000025008; ENSG00000023287. ENST00000435644; ENSP00000396067; ENSG00000023287. ENST00000539297; ENSP00000445960; ENSG00000023287.
GeneID	9821.
KEGG	hsa:9821.
UCSC	uc003xre.4. human. uc003xrf.4. human.
Organism-specific databases
CTD	9821.
GeneCards	GC08M053584.
H-InvDB	HIX0007503.
HGNC	HGNC:15574. RB1CC1.
HPA	HPA024391. HPA053049.
MIM	606837. gene.
neXtProt	NX_Q8TDY2.
PharmGKB	PA34248.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG280878.
HOGENOM	HOG000154076.
HOVERGEN	HBG091209.
InParanoid	Q8TDY2.
OMA	EQSHLKE.
Gene expression databases
ArrayExpress	Q8TDY2.
Bgee	Q8TDY2.
CleanEx	HS_RB1CC1.
Genevestigator	Q8TDY2.
GermOnline	ENSG00000023287. Homo sapiens.
Family and domain databases
InterPro	IPR019460. Autophagy-rel_p11. [Graphical view]
Pfam	PF10377. ATG11. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RB1CC1. human.
GenomeRNAi	9821.
NextBio	36990.
SOURCE	Search...

Entry information

Entry name

RBCC1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.