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 08-MAY-2019, entry version 136. 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; Myomorpha; 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, and thereby plays an important CC role in RAN-mediated functions in nuclear import and mitosis. CC Contributes to the generation of high levels of chromosome- CC associated, GTP-bound RAN, which is important for mitotic spindle CC assembly and normal progress through mitosis. Via its role in CC maintaining high levels of GTP-bound RAN in the nucleus, CC contributes to the release of cargo proteins from importins after CC nuclear import. Involved in the regulation of onset of chromosome CC condensation in the S phase. Binds both to the nucleosomes and CC double-stranded DNA. {ECO:0000250|UniProtKB:P18754}. CC -!- SUBUNIT: Interacts with RAN. Interacts (via N-terminus and RCC1 CC repeats) with KPNA4. Interacts with ARRB2; the interaction is CC detected in the nucleus upon OR1D2 stimulation. CC {ECO:0000250|UniProtKB:P18754}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18754}. CC Chromosome {ECO:0000250|UniProtKB:P18754}. Cytoplasm CC {ECO:0000250|UniProtKB:P18754}. Note=Predominantly nuclear in CC interphase cells. Binds to mitotic chromosomes. CC {ECO:0000250|UniProtKB:P18754}. 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 CC Ran. {ECO:0000250|UniProtKB:P18754}. 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 SMR; Q8VE37; -. DR BioGrid; 221378; 64. DR IntAct; Q8VE37; 64. DR MINT; Q8VE37; -. DR STRING; 10090.ENSMUSP00000081271; -. DR iPTMnet; Q8VE37; -. DR PhosphoSitePlus; Q8VE37; -. DR SwissPalm; Q8VE37; -. DR EPD; Q8VE37; -. DR jPOST; 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; ENSGT00940000155543; -. DR HOGENOM; HOG000234341; -. DR InParanoid; Q8VE37; -. DR KO; K11493; -. DR OMA; EGTVCCS; -. DR OrthoDB; 1062377at2759; -. DR PhylomeDB; Q8VE37; -. DR TreeFam; TF101139; -. DR ChiTaRS; Rcc1; mouse. DR PRO; PR:Q8VE37; -. DR Proteomes; UP000000589; Chromosome 4. DR Bgee; ENSMUSG00000028896; Expressed in 252 organ(s), highest expression level in testis. DR ExpressionAtlas; Q8VE37; baseline and differential. DR Genevisible; Q8VE37; MM. DR GO; GO:0000785; C:chromatin; ISO:MGI. 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:0032991; C:protein-containing complex; ISO:MGI. 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:0031491; F:nucleosome binding; ISO:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0008536; F:Ran GTPase binding; ISO:MGI. DR GO; GO:0005087; F:Ran guanyl-nucleotide exchange factor activity; IDA:MGI. DR GO; GO:0043199; F:sulfate binding; ISO: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:0007052; P:mitotic spindle organization; ISO:MGI. DR GO; GO:0051290; P:protein heterotetramerization; 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; Chromosome; Complete proteome; Cytoplasm; KW DNA-binding; Guanine-nucleotide releasing factor; Methylation; KW Mitosis; Nucleus; 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 MOTIF 4 24 Bipartite nuclear localization signal. FT {ECO:0000250|UniProtKB:P18754}. 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 //