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Identification
HMDB Protein ID HMDBP08535
Secondary Accession Numbers
  • 14247
Name Regulator of chromosome condensation
Synonyms
  1. Cell cycle regulatory protein
  2. Chromosome condensation protein 1
Gene Name RCC1
Protein Type Unknown
Biological Properties
General Function Involved in histone binding
Specific Function Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP. Involved in the regulation of onset of chromosome condensation in the S phase. Binds both to the nucleosomes and double-stranded DNA. RCC1-Ran complex (together with other proteins) acts as a component of a signal transmission pathway that detects unreplicated DNA. Plays a key role in nucleo- cytoplasmic transport, mitosis and nuclear-envelope assembly
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Nucleus
  2. Cytoplasm
Gene Properties
Chromosome Location Chromosome:1
Locus 1p36.1
SNPs RCC1
Gene Sequence
>1266 bp
ATGTCACCCAAGCGCATAGCTAAAAGAAGGTCCCCCCCAGCAGATGCCATCCCCAAAAGC
AAGAAGGTGAAGGTCTCACACAGGTCCCACAGCACAGAACCCGGCTTGGTGCTGACACTA
GGCCAGGGCGACGTGGGCCAGCTGGGGCTGGGTGAGAATGTGATGGAGAGGAAGAAGCCG
GCCCTGGTATCCATTCCGGAGGATGTTGTGCAGGCTGAGGCTGGGGGCATGCACACCGTG
TGTCTAAGCAAAAGTGGCCAGGTCTATTCCTTCGGCTGCAATGATGAGGGTGCCCTGGGA
AGGGACACATCAGTGGAGGGCTCGGAGATGGTCCCTGGGAAAGTGGAGCTGCAAGAGAAG
GTGGTACAGGTGTCAGCAGGAGACAGTCACACAGCAGCCCTCACCGATGATGGCCGTGTC
TTCCTCTGGGGCTCCTTCCGGGACAATAACGGTGTGATTGGACTGTTGGAGCCCATGAAG
AAGAGCATGGTGCCTGTGCAGGTGCAGCTGGATGTGCCTGTGGTAAAGGTGGCCTCAGGA
AACGACCACTTGGTGATGCTGACAGCTGATGGTGACCTCTACACCTTGGGCTGCGGGGAA
CAGGGCCAGCTAGGCCGTGTGCCTGAGTTATTTGCCAACCGTGGTGGCCGGCAAGGCCTC
GAACGACTCCTGGTCCCCAAGTGTGTGATGCTGAAATCCAGGGGAAGCCGGGGCCACGTG
AGATTCCAGGATGCCTTTTGTGGTGCCTATTTCACCTTTGCCATCTCCCATGAGGGCCAC
GTGTACGGCTTCGGCCTCTCCAACTACCATCAGCTTGGAACTCCGGGCACAGAATCTTGC
TTCATACCCCAGAACCTAACATCCTTCAAGAATTCCACCAAGTCCTGGGTGGGCTTCTCT
GGTGGCCAGCACCATACAGTCTGCATGGATTCGGAAGGAAAAGCATACAGCCTGGGCCGG
GCTGAGTATGGGCGGCTGGGCCTTGGAGAGGGTGCTGAGGAGAAGAGCATACCCACCCTC
ATCTCCAGGCTGCCTGCTGTCTCCTCGGTGGCTTGTGGGGCCTCTGTGGGGTATGCTGTG
ACCAAGGATGGTCGTGTTTTCGCCTGGGGCATGGGCACCAACTACCAGCTGGGCACAGGG
CAGGATGAGGACGCCTGGAGCCCTGTGGAGATGATGGGCAAACAGCTGGAGAACCGTGTG
GTCTTATCTGTGTCCAGCGGGGGCCAGCATACAGTCTTATTAGTCAAGGACAAAGAACAG
AGCTGA
Protein Properties
Number of Residues 421
Molecular Weight 44968.9
Theoretical pI 7.57
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Regulator of chromosome condensation
MSPKRIAKRRSPPADAIPKSKKVKVSHRSHSTEPGLVLTLGQGDVGQLGLGENVMERKKP
ALVSIPEDVVQAEAGGMHTVCLSKSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEK
VVQVSAGDSHTAALTDDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASG
NDHLVMLTADGDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHV
RFQDAFCGAYFTFAISHEGHVYGFGLSNYHQLGTPGTESCFIPQNLTSFKNSTKSWVGFS
GGQHHTVCMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPAVSSVACGASVGYAV
TKDGRVFAWGMGTNYQLGTGQDEDAWSPVEMMGKQLENRVVLSVSSGGQHTVLLVKDKEQ
S
GenBank ID Protein 20379024
UniProtKB/Swiss-Prot ID P18754
UniProtKB/Swiss-Prot Entry Name RCC1_HUMAN
PDB IDs
GenBank Gene ID AF498924
GeneCard ID RCC1
GenAtlas ID RCC1
HGNC ID HGNC:1913
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  5. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  7. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  8. Neuhaus EM, Mashukova A, Barbour J, Wolters D, Hatt H: Novel function of beta-arrestin2 in the nucleus of mature spermatozoa. J Cell Sci. 2006 Aug 1;119(Pt 15):3047-56. Epub 2006 Jul 4. [PubMed:16820410 ]
  9. Ohtsubo M, Kai R, Furuno N, Sekiguchi T, Sekiguchi M, Hayashida H, Kuma K, Miyata T, Fukushige S, Murotsu T, et al.: Isolation and characterization of the active cDNA of the human cell cycle gene (RCC1) involved in the regulation of onset of chromosome condensation. Genes Dev. 1987 Aug;1(6):585-93. [PubMed:3678831 ]
  10. Furuno N, Nakagawa K, Eguchi U, Ohtsubo M, Nishimoto T, Soeda E: Complete nucleotide sequence of the human RCC1 gene involved in coupling between DNA replication and mitosis. Genomics. 1991 Oct;11(2):459-61. [PubMed:1769659 ]
  11. Bischoff FR, Maier G, Tilz G, Ponstingl H: A 47-kDa human nuclear protein recognized by antikinetochore autoimmune sera is homologous with the protein encoded by RCC1, a gene implicated in onset of chromosome condensation. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8617-21. [PubMed:2236072 ]
  12. Bischoff FR, Ponstingl H: Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1. Nature. 1991 Nov 7;354(6348):80-2. [PubMed:1944575 ]
  13. Chen T, Muratore TL, Schaner-Tooley CE, Shabanowitz J, Hunt DF, Macara IG: N-terminal alpha-methylation of RCC1 is necessary for stable chromatin association and normal mitosis. Nat Cell Biol. 2007 May;9(5):596-603. Epub 2007 Apr 15. [PubMed:17435751 ]
  14. Hao Y, Macara IG: Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1. J Cell Biol. 2008 Sep 8;182(5):827-36. doi: 10.1083/jcb.200803110. Epub 2008 Sep 1. [PubMed:18762580 ]
  15. Tooley CE, Petkowski JJ, Muratore-Schroeder TL, Balsbaugh JL, Shabanowitz J, Sabat M, Minor W, Hunt DF, Macara IG: NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein. Nature. 2010 Aug 26;466(7310):1125-8. doi: 10.1038/nature09343. [PubMed:20668449 ]
  16. Renault L, Nassar N, Vetter I, Becker J, Klebe C, Roth M, Wittinghofer A: The 1.7 A crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. Nature. 1998 Mar 5;392(6671):97-101. [PubMed:9510255 ]