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 03-AUG-2022, entry version 149. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project: RT 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 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 role CC in RAN-mediated functions in nuclear import and mitosis. Contributes to CC the generation of high levels of chromosome-associated, GTP-bound RAN, CC which is important for mitotic spindle assembly and normal progress CC through mitosis. Via its role in maintaining high levels of GTP-bound CC RAN in the nucleus, contributes to the release of cargo proteins from CC importins after nuclear import. Involved in the regulation of onset of CC chromosome condensation in the S phase. Binds both to the nucleosomes CC and 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 detected CC in the nucleus upon OR1D2 stimulation. {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 binding CC double-stranded DNA and stable chromatin association. Dimethylation CC produces a permanent positive charge on the amino group, which CC facilitates electrostatic binding to the phosphate groups on DNA, while CC inhibiting histone-binding. Methylated tail helps retain RCC1 on CC chromosomes during nucleotide exchange on Ran. CC {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 AlphaFoldDB; Q8VE37; -. DR SMR; Q8VE37; -. DR BioGRID; 221378; 76. DR IntAct; Q8VE37; 63. DR MINT; Q8VE37; -. DR STRING; 10090.ENSMUSP00000081271; -. DR iPTMnet; Q8VE37; -. DR PhosphoSitePlus; Q8VE37; -. DR SwissPalm; Q8VE37; -. DR EPD; Q8VE37; -. DR MaxQB; Q8VE37; -. DR PaxDb; Q8VE37; -. DR PRIDE; Q8VE37; -. DR ProteomicsDB; 255053; -. DR Antibodypedia; 4212; 439 antibodies from 41 providers. DR DNASU; 100088; -. 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 VEuPathDB; HostDB:ENSMUSG00000028896; -. DR eggNOG; KOG1426; Eukaryota. DR GeneTree; ENSGT00940000155543; -. DR HOGENOM; CLU_005210_6_2_1; -. DR InParanoid; Q8VE37; -. DR OMA; WSWGTND; -. DR PhylomeDB; Q8VE37; -. DR TreeFam; TF101139; -. DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation. DR BioGRID-ORCS; 100088; 27 hits in 77 CRISPR screens. DR ChiTaRS; Rcc1; mouse. DR PRO; PR:Q8VE37; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q8VE37; protein. DR Bgee; ENSMUSG00000028896; Expressed in ectoplacental cone and 236 other tissues. 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: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:0005085; F:guanyl-nucleotide exchange factor activity; IDA: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:0031267; F:small GTPase binding; ISO: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: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; Cytoplasm; DNA-binding; KW Guanine-nucleotide releasing factor; Methylation; Mitosis; Nucleus; KW Phosphoprotein; Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:20668449" FT CHAIN 2..421 FT /note="Regulator of chromosome condensation" FT /id="PRO_0000206630" FT REPEAT 34..84 FT /note="RCC1 1" FT REPEAT 85..136 FT /note="RCC1 2" FT REPEAT 138..189 FT /note="RCC1 3" FT REPEAT 191..257 FT /note="RCC1 4" FT REPEAT 258..311 FT /note="RCC1 5" FT REPEAT 312..362 FT /note="RCC1 6" FT REPEAT 363..416 FT /note="RCC1 7" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 4..24 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:P18754" FT COMPBIAS 7..22 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N,N-dimethylproline; alternate" FT /evidence="ECO:0000269|PubMed:20668449" FT MOD_RES 2 FT /note="N-methylproline; alternate" FT /evidence="ECO:0000269|PubMed:20668449" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P18754" FT CONFLICT 45 FT /note="V -> M (in Ref. 1; BAE29345)" FT /evidence="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 //