ID RCC1_MOUSE Reviewed; 421 AA. AC Q8VE37; Q3UDB6; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 11-MAY-2016, entry version 115. DE RecName: Full=Regulator of chromosome condensation; DE AltName: Full=Chromosome condensation protein 1; GN Name=Rcc1; Synonyms=Chc1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [4] RP CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT PRO-2. RX PubMed=20668449; DOI=10.1038/nature09343; RA Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L., RA Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.; RT "NRMT is an alpha-N-methyltransferase that methylates RCC1 and RT retinoblastoma protein."; RL Nature 466:1125-1128(2010). CC -!- FUNCTION: Guanine-nucleotide releasing factor that promotes the CC exchange of Ran-bound GDP by GTP. Involved in the regulation of CC onset of chromosome condensation in the S phase. Binds both to the CC nucleosomes and double-stranded DNA. RCC1-Ran complex (together CC with other proteins) acts as a component of a signal transmission CC pathway that detects unreplicated DNA. Plays a key role in nucleo- CC cytoplasmic transport, mitosis and nuclear-envelope assembly (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm CC {ECO:0000250}. Note=Becomes dispersed throughout the cytoplasm CC during mitosis. {ECO:0000250}. CC -!- PTM: N-terminal methylation by METTL11A/NTM1 is required for CC binding double-stranded DNA and stable chromatin association. CC Dimethylation produces a permanent positive charge on the amino CC group, which facilitates electrostatic binding to the phosphate CC groups on DNA, while inhibiting histone-binding. Methylated tail CC helps retain RCC1 on chromosomes during nucleotide exchange on Ran CC (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Contains 7 RCC1 repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00235}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK150153; BAE29345.1; -; mRNA. DR EMBL; BC019807; AAH19807.1; -; mRNA. DR CCDS; CCDS18723.1; -. DR RefSeq; NP_598639.1; NM_133878.3. DR UniGene; Mm.255045; -. DR ProteinModelPortal; Q8VE37; -. DR SMR; Q8VE37; 21-421. DR BioGrid; 221378; 63. DR IntAct; Q8VE37; 64. DR MINT; MINT-2568412; -. DR STRING; 10090.ENSMUSP00000030726; -. DR iPTMnet; Q8VE37; -. DR PhosphoSite; Q8VE37; -. DR EPD; Q8VE37; -. DR MaxQB; Q8VE37; -. DR PaxDb; Q8VE37; -. DR PRIDE; Q8VE37; -. DR Ensembl; ENSMUST00000084250; ENSMUSP00000081271; ENSMUSG00000028896. DR Ensembl; ENSMUST00000105951; ENSMUSP00000101571; ENSMUSG00000028896. DR GeneID; 100088; -. DR KEGG; mmu:100088; -. DR UCSC; uc008vbc.2; mouse. DR CTD; 1104; -. DR MGI; MGI:1913989; Rcc1. DR eggNOG; KOG1426; Eukaryota. DR eggNOG; COG5184; LUCA. DR GeneTree; ENSGT00840000129719; -. DR HOGENOM; HOG000234341; -. DR HOVERGEN; HBG017712; -. DR InParanoid; Q8VE37; -. DR KO; K11493; -. DR OrthoDB; EOG7HQN8F; -. DR PhylomeDB; Q8VE37; -. DR TreeFam; TF101139; -. DR ChiTaRS; Rcc1; mouse. DR NextBio; 354253; -. DR PRO; PR:Q8VE37; -. DR Proteomes; UP000000589; Chromosome 4. DR Bgee; Q8VE37; -. DR CleanEx; MM_RCC1; -. DR ExpressionAtlas; Q8VE37; baseline and differential. DR Genevisible; Q8VE37; MM. DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0000790; C:nuclear chromatin; ISO:MGI. DR GO; GO:0031965; C:nuclear membrane; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISO:MGI. DR GO; GO:0042393; F:histone binding; ISO:MGI. DR GO; GO:0031492; F:nucleosomal DNA binding; ISS:UniProtKB. DR GO; GO:0005087; F:Ran guanyl-nucleotide exchange factor activity; IDA:MGI. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI. DR GO; GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW. DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI. DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI. DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISO:MGI. DR GO; GO:0051225; P:spindle assembly; ISS:UniProtKB. DR Gene3D; 2.130.10.30; -; 1. DR InterPro; IPR009091; RCC1/BLIP-II. DR InterPro; IPR000408; Reg_chr_condens. DR Pfam; PF00415; RCC1; 7. DR PRINTS; PR00633; RCCNDNSATION. DR SUPFAM; SSF50985; SSF50985; 1. DR PROSITE; PS00625; RCC1_1; 1. DR PROSITE; PS00626; RCC1_2; 4. DR PROSITE; PS50012; RCC1_3; 7. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Complete proteome; Cytoplasm; DNA-binding; KW Guanine-nucleotide releasing factor; Methylation; Mitosis; Nucleus; KW Phosphoprotein; Reference proteome; Repeat. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:20668449}. FT CHAIN 2 421 Regulator of chromosome condensation. FT /FTId=PRO_0000206630. FT REPEAT 34 84 RCC1 1. FT REPEAT 85 136 RCC1 2. FT REPEAT 138 189 RCC1 3. FT REPEAT 191 257 RCC1 4. FT REPEAT 258 311 RCC1 5. FT REPEAT 312 362 RCC1 6. FT REPEAT 363 416 RCC1 7. FT MOD_RES 2 2 N,N-dimethylproline; alternate. FT {ECO:0000269|PubMed:20668449}. FT MOD_RES 2 2 N-methylproline; alternate. FT {ECO:0000269|PubMed:20668449}. FT MOD_RES 11 11 Phosphoserine. FT {ECO:0000250|UniProtKB:P18754}. FT CONFLICT 45 45 V -> M (in Ref. 1; BAE29345). FT {ECO:0000305}. SQ SEQUENCE 421 AA; 44931 MW; ACE5019E50E1E9DC CRC64; MPPKRIAKRR SPPEDAIPKS KKVKVSHRSH NTEPGLVLTL GQGDVGQLGL GESVLERKKP ALVPLLQDVV QAEAGGMHTV CLSQSGQVYS FGCNDEGALG RDTSVEGSEM VPGKVELQEK VVQVSAGDSH TAALTEDGRV FLWGSFRDNN GVIGLLEPMK KSMVPVQVQL DAPVVKVASG NDHLVMLTND GDLYTLGCGE QGQLGRVPEL FANRGGRQGL GRLLVPRCVL LKSRGTRGRV RFQDAFCGAY FTFAISREGH VYGFGLSNYH QLGTPGTGSC FIPQNLTSFK NSTKSWVGFS GGQHHTVCMD SEGKAYSLGR AEYGRLGLGE GAEEKSIPTL ISRLPVVSSV ACGASVGYAV SKDGRVFAWG MGTNYQLGTG QDEDAWSPVE MTGKQLENRV VLTVSSGGQH TVLLVKDQAQ S //