ID RCC1_HUMAN Reviewed; 421 AA. AC P18754; Q16269; Q6NT97; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 27-MAR-2024, entry version 233. DE RecName: Full=Regulator of chromosome condensation; DE AltName: Full=Cell cycle regulatory protein; DE AltName: Full=Chromosome condensation protein 1; GN Name=RCC1; Synonyms=CHC1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RX PubMed=3678831; DOI=10.1101/gad.1.6.585; RA Ohtsubo M., Kai R., Furuno N., Sekiguchi T., Sekiguchi M., Hayashida H., RA Kuma K., Miyata T., Fukushige S., Murotsu T., Matsubara K., Nishimoto T.; RT "Isolation and characterization of the active cDNA of the human cell cycle RT gene (RCC1) involved in the regulation of onset of chromosome RT condensation."; RL Genes Dev. 1:585-593(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1769659; DOI=10.1016/0888-7543(91)90156-9; RA Furuno N., Nakagawa K., Eguchi U., Ohtsubo M., Nishimoto T., Soeda E.; RT "Complete nucleotide sequence of the human RCC1 gene involved in coupling RT between DNA replication and mitosis."; RL Genomics 11:459-461(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Eye, Mammary gland, Muscle, and Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-33 (ISOFORM 2), AND ALTERNATIVE SPLICING. RX PubMed=7983178; DOI=10.1242/jcs.107.8.2203; RA Miyabashira J., Sekiguchi T., Nishimoto T.; RT "Mammalian cells have two functional RCC1 proteins produced by alternative RT splicing."; RL J. Cell Sci. 107:2203-2208(1994). RN [6] RP PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION. RX PubMed=2236072; DOI=10.1073/pnas.87.21.8617; RA Bischoff F.R., Maier G., Tilz G., Ponstingl H.; RT "A 47-kDa human nuclear protein recognized by antikinetochore autoimmune RT sera is homologous with the protein encoded by RCC1, a gene implicated in RT onset of chromosome condensation."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8617-8621(1990). RN [7] RP FUNCTION. RX PubMed=1944575; DOI=10.1038/354080a0; RA Bischoff F.R., Ponstingl H.; RT "Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RT RCC1."; RL Nature 354:80-82(1991). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-182. RX PubMed=12194828; DOI=10.1016/s0960-9822(02)01076-x; RA Moore W., Zhang C., Clarke P.R.; RT "Targeting of RCC1 to chromosomes is required for proper mitotic spindle RT assembly in human cells."; RL Curr. Biol. 12:1442-1447(2002). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP INTERACTION WITH ARRB2, AND SUBCELLULAR LOCATION. RX PubMed=16820410; DOI=10.1242/jcs.03046; RA Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.; RT "Novel function of beta-arrestin2 in the nucleus of mature spermatozoa."; RL J. Cell Sci. 119:3047-3056(2006). RN [11] RP CLEAVAGE OF INITIATOR METHIONINE, SUBCELLULAR LOCATION, FUNCTION, RP HISTONE-BINDING, INTERACTION WITH RAN, PHOSPHORYLATION AT SER-2, RP METHYLATION AT SER-2, AND MUTAGENESIS OF SER-2; PRO-3; LYS-4 AND ASP-182. RX PubMed=17435751; DOI=10.1038/ncb1572; RA Chen T., Muratore T.L., Schaner-Tooley C.E., Shabanowitz J., Hunt D.F., RA Macara I.G.; RT "N-terminal alpha-methylation of RCC1 is necessary for stable chromatin RT association and normal mitosis."; RL Nat. Cell Biol. 9:596-603(2007). RN [12] RP METHYLATION AT SER-2, FUNCTION, INTERACTION WITH RAN, AND SUBCELLULAR RP LOCATION. RX PubMed=18762580; DOI=10.1083/jcb.200803110; RA Hao Y., Macara I.G.; RT "Regulation of chromatin binding by a conformational switch in the tail of RT the Ran exchange factor RCC1."; RL J. Cell Biol. 182:827-836(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT SER-2, MUTAGENESIS OF RP LYS-4, FUNCTION, AND SUBCELLULAR LOCATION. 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). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP FUNCTION. RX PubMed=22215983; DOI=10.1371/journal.pbio.1001225; RA Halpin D., Kalab P., Wang J., Weis K., Heald R.; RT "Mitotic spindle assembly around RCC1-coated beads in Xenopus egg RT extracts."; RL PLoS Biol. 9:E1001225-E1001225(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP INTERACTION WITH RAN. RX PubMed=29040603; DOI=10.1093/jmcb/mjx045; RA Bao X., Liu H., Liu X., Ruan K., Zhang Y., Zhang Z., Hu Q., Liu Y., RA Akram S., Zhang J., Gong Q., Wang W., Yuan X., Li J., Zhao L., Dou Z., RA Tian R., Yao X., Wu J., Shi Y.; RT "Mitosis-specific acetylation tunes Ran effector binding for chromosome RT segregation."; RL J. Mol. Cell Biol. 10:18-32(2018). RN [22] RP INTERACTION WITH KPNA3. RX PubMed=34564892; DOI=10.1002/ana.26228; RA Schob C., Hempel M., Safka Brozkova D., Jiang H., Kim S.Y., Batzir N.A., RA Orenstein N., Bierhals T., Johannsen J., Uhrova Meszarosova A., Chae J.H., RA Seeman P., Woidy M., Fang F., Kubisch C., Kindler S., Denecke J.; RT "Dominant KPNA3 Mutations Cause Infantile-Onset Hereditary Spastic RT Paraplegia."; RL Ann. Neurol. 90:738-750(2021). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-421. RX PubMed=9510255; DOI=10.1038/32204; RA Renault L., Nassar N., Vetter I., Becker J., Klebe C., Roth M., RA Wittinghofer A.; RT "The 1.7-A crystal structure of the regulator of chromosome condensation RT (RCC1) reveals a seven-bladed propeller."; RL Nature 392:97-101(1998). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 20-421 IN COMPLEX WITH RAN, AND RP FUNCTION. RX PubMed=11336674; DOI=10.1016/s0092-8674(01)00315-4; RA Renault L., Kuhlmann J., Henkel A., Wittinghofer A.; RT "Structural basis for guanine nucleotide exchange on Ran by the regulator RT of chromosome condensation (RCC1)."; RL Cell 105:245-255(2001). RN [25] {ECO:0007744|PDB:5TBK} RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) IN COMPLEX WITH KPNA4, AND RP MUTAGENESIS OF ARG-9; SER-11 AND LYS-21. RX PubMed=29042532; DOI=10.1038/s41467-017-01057-7; RA Sankhala R.S., Lokareddy R.K., Begum S., Pumroy R.A., Gillilan R.E., RA Cingolani G.; RT "Three-dimensional context rather than NLS amino acid sequence determines RT importin alpha subtype specificity for RCC1."; RL Nat. Commun. 8:979-979(2017). 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 CC (PubMed:1944575, PubMed:17435751, PubMed:20668449, PubMed:22215983, CC PubMed:11336674). Contributes to the generation of high levels of CC chromosome-associated, GTP-bound RAN, which is important for mitotic CC spindle assembly and normal progress through mitosis (PubMed:12194828, CC PubMed:17435751, PubMed:22215983). Via its role in maintaining high CC levels of GTP-bound RAN in the nucleus, contributes to the release of CC cargo proteins from importins after nuclear import (PubMed:22215983). CC Involved in the regulation of onset of chromosome condensation in the S CC phase (PubMed:3678831). Binds both to the nucleosomes and double- CC stranded DNA (PubMed:17435751, PubMed:18762580). CC {ECO:0000269|PubMed:11336674, ECO:0000269|PubMed:12194828, CC ECO:0000269|PubMed:17435751, ECO:0000269|PubMed:18762580, CC ECO:0000269|PubMed:1944575, ECO:0000269|PubMed:20668449, CC ECO:0000269|PubMed:22215983, ECO:0000269|PubMed:3678831}. CC -!- SUBUNIT: Interacts with RAN (PubMed:17435751, PubMed:18762580, CC PubMed:29040603, PubMed:11336674). Interacts with KPNA3 CC (PubMed:34564892). Interacts (via N-terminus and RCC1 repeats) with CC KPNA4 (PubMed:29042532). Interacts with ARRB2; the interaction is CC detected in the nucleus upon OR1D2 stimulation (PubMed:16820410). CC {ECO:0000269|PubMed:11336674, ECO:0000269|PubMed:16820410, CC ECO:0000269|PubMed:17435751, ECO:0000269|PubMed:18762580, CC ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:29042532, CC ECO:0000269|PubMed:34564892}. CC -!- INTERACTION: CC P18754; Q9BV86: NTMT1; NbExp=4; IntAct=EBI-992720, EBI-373016; CC P18754; P62826: RAN; NbExp=15; IntAct=EBI-992720, EBI-286642; CC P18754; Q9H6Z4: RANBP3; NbExp=2; IntAct=EBI-992720, EBI-992681; CC P18754; P02281; Xeno; NbExp=2; IntAct=EBI-992720, EBI-1251201; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12194828, CC ECO:0000269|PubMed:16820410, ECO:0000269|PubMed:17435751, CC ECO:0000269|PubMed:2236072}. Chromosome {ECO:0000269|PubMed:12194828, CC ECO:0000269|PubMed:17435751, ECO:0000269|PubMed:18762580, CC ECO:0000269|PubMed:20668449}. Cytoplasm {ECO:0000269|PubMed:12194828, CC ECO:0000269|PubMed:17435751, ECO:0000269|PubMed:20668449}. CC Note=Predominantly nuclear in interphase cells (PubMed:12194828). Binds CC to mitotic chromosomes (PubMed:12194828, PubMed:17435751, CC PubMed:20668449). {ECO:0000269|PubMed:12194828, CC ECO:0000269|PubMed:17435751, ECO:0000269|PubMed:20668449}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P18754-1; Sequence=Displayed; CC Name=2; Synonyms=RCC1-I; CC IsoId=P18754-2; Sequence=VSP_041122; CC -!- PTM: N-terminal methylation by METTL11A/NTM1 is required for binding CC double-stranded DNA and stable chromatin association. Di- and CC trimethylation produce a permanent positive charge on the amino group, CC which facilitates electrostatic binding to the phosphate groups on DNA, CC while inhibiting histone-binding. Methylated tail helps retain RCC1 on CC chromosomes during nucleotide exchange on Ran. CC {ECO:0000269|PubMed:17435751, ECO:0000269|PubMed:18762580, CC ECO:0000269|PubMed:20668449}. CC -!- MISCELLANEOUS: Patients with Raynaud disease produce antibodies that CC bind to RCC1. 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; X12654; CAA31182.1; -; mRNA. DR EMBL; X06130; CAA29496.1; -; mRNA. DR EMBL; D00591; BAA00469.1; -; Genomic_DNA. DR EMBL; AF498924; AAM21072.1; -; mRNA. DR EMBL; BC007300; AAH07300.1; -; mRNA. DR EMBL; BC010067; AAH10067.1; -; mRNA. DR EMBL; BC036903; AAH36903.1; -; mRNA. DR EMBL; BC069198; AAH69198.1; -; mRNA. DR EMBL; S75708; AAB32653.1; -; mRNA. DR CCDS; CCDS41295.1; -. [P18754-2] DR PIR; A26691; A26691. DR RefSeq; NP_001041659.1; NM_001048194.2. [P18754-2] DR RefSeq; NP_001041660.1; NM_001048195.2. DR RefSeq; NP_001041664.1; NM_001048199.2. [P18754-1] DR RefSeq; NP_001260.1; NM_001269.4. [P18754-1] DR PDB; 1A12; X-ray; 1.70 A; A/B/C=9-421. DR PDB; 1I2M; X-ray; 1.76 A; B/D=20-421. DR PDB; 5E1B; X-ray; 1.65 A; D/E=2-7. DR PDB; 5E1D; X-ray; 1.45 A; D/E=3-7. DR PDB; 5E1M; X-ray; 1.75 A; D/E=3-7. DR PDB; 5E1O; X-ray; 2.00 A; D/E=3-7. DR PDB; 5E2A; X-ray; 1.75 A; D/E=3-7. DR PDB; 5E2B; X-ray; 1.95 A; D/E=3-7. DR PDB; 5TBK; X-ray; 3.45 A; I/J/K/L/M/N/O/P=1-421. DR PDB; 6DUB; X-ray; 1.20 A; E/F=3-7. DR PDB; 8UX1; EM; 2.50 A; L=2-421. DR PDBsum; 1A12; -. DR PDBsum; 1I2M; -. DR PDBsum; 5E1B; -. DR PDBsum; 5E1D; -. DR PDBsum; 5E1M; -. DR PDBsum; 5E1O; -. DR PDBsum; 5E2A; -. DR PDBsum; 5E2B; -. DR PDBsum; 5TBK; -. DR PDBsum; 6DUB; -. DR PDBsum; 8UX1; -. DR AlphaFoldDB; P18754; -. DR EMDB; EMD-42685; -. DR SMR; P18754; -. DR BioGRID; 107529; 193. DR DIP; DIP-35416N; -. DR IntAct; P18754; 85. DR MINT; P18754; -. DR STRING; 9606.ENSP00000497402; -. DR GlyCosmos; P18754; 1 site, 1 glycan. DR GlyGen; P18754; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P18754; -. DR MetOSite; P18754; -. DR PhosphoSitePlus; P18754; -. DR SwissPalm; P18754; -. DR BioMuta; RCC1; -. DR DMDM; 132170; -. DR EPD; P18754; -. DR jPOST; P18754; -. DR MassIVE; P18754; -. DR MaxQB; P18754; -. DR PaxDb; 9606-ENSP00000362937; -. DR PeptideAtlas; P18754; -. DR ProteomicsDB; 53606; -. [P18754-1] DR ProteomicsDB; 53607; -. [P18754-2] DR Pumba; P18754; -. DR TopDownProteomics; P18754-1; -. [P18754-1] DR Antibodypedia; 4212; 509 antibodies from 41 providers. DR DNASU; 1104; -. DR Ensembl; ENST00000373831.7; ENSP00000362937.3; ENSG00000180198.17. [P18754-2] DR Ensembl; ENST00000373832.5; ENSP00000362938.1; ENSG00000180198.17. [P18754-1] DR Ensembl; ENST00000373833.10; ENSP00000362939.5; ENSG00000180198.17. [P18754-1] DR Ensembl; ENST00000398958.6; ENSP00000381931.2; ENSG00000180198.17. [P18754-1] DR Ensembl; ENST00000649185.1; ENSP00000497402.1; ENSG00000180198.17. [P18754-2] DR Ensembl; ENST00000683442.1; ENSP00000508074.1; ENSG00000180198.17. [P18754-1] DR GeneID; 1104; -. DR KEGG; hsa:1104; -. DR MANE-Select; ENST00000683442.1; ENSP00000508074.1; NM_001381865.2; NP_001368794.1. DR UCSC; uc001bqf.3; human. [P18754-1] DR AGR; HGNC:1913; -. DR CTD; 1104; -. DR DisGeNET; 1104; -. DR GeneCards; RCC1; -. DR HGNC; HGNC:1913; RCC1. DR HPA; ENSG00000180198; Low tissue specificity. DR MIM; 179710; gene. DR neXtProt; NX_P18754; -. DR OpenTargets; ENSG00000180198; -. DR PharmGKB; PA26449; -. DR VEuPathDB; HostDB:ENSG00000180198; -. DR eggNOG; KOG1426; Eukaryota. DR GeneTree; ENSGT00940000155543; -. DR HOGENOM; CLU_005210_6_2_1; -. DR InParanoid; P18754; -. DR OMA; IFVWGTG; -. DR OrthoDB; 5940at2759; -. DR PhylomeDB; P18754; -. DR TreeFam; TF101139; -. DR PathwayCommons; P18754; -. DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA. DR Reactome; R-HSA-180746; Nuclear import of Rev protein. DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation. DR SignaLink; P18754; -. DR SIGNOR; P18754; -. DR BioGRID-ORCS; 1104; 811 hits in 1178 CRISPR screens. DR ChiTaRS; RCC1; human. DR EvolutionaryTrace; P18754; -. DR GeneWiki; RCC1; -. DR GenomeRNAi; 1104; -. DR Pharos; P18754; Tbio. DR PRO; PR:P18754; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P18754; Protein. DR Bgee; ENSG00000180198; Expressed in right testis and 167 other cell types or tissues. DR ExpressionAtlas; P18754; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0005694; C:chromosome; TAS:Reactome. DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB. DR GO; GO:0031491; F:nucleosome binding; IMP:CAFA. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA. DR GO; GO:0031267; F:small GTPase binding; IDA:CAFA. DR GO; GO:0043199; F:sulfate binding; IDA:CAFA. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; TAS:Reactome. DR GO; GO:0007052; P:mitotic spindle organization; IDA:UniProtKB. DR GO; GO:0007088; P:regulation of mitotic nuclear division; IDA:UniProtKB. DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB. DR GO; GO:0016032; P:viral process; TAS:Reactome. DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1. DR InterPro; IPR009091; RCC1/BLIP-II. DR InterPro; IPR000408; Reg_chr_condens. DR PANTHER; PTHR45982; REGULATOR OF CHROMOSOME CONDENSATION; 1. DR PANTHER; PTHR45982:SF11; REGULATOR OF CHROMOSOME CONDENSATION; 1. DR Pfam; PF00415; RCC1; 7. DR PRINTS; PR00633; RCCNDNSATION. DR SUPFAM; SSF50985; RCC1/BLIP-II; 1. DR PROSITE; PS00625; RCC1_1; 1. DR PROSITE; PS00626; RCC1_2; 4. DR PROSITE; PS50012; RCC1_3; 7. DR Genevisible; P18754; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Chromosome; KW Cytoplasm; Direct protein sequencing; 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:17435751, FT ECO:0000269|PubMed:20668449" FT CHAIN 2..421 FT /note="Regulator of chromosome condensation" FT /id="PRO_0000206628" 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:0000305|PubMed:29042532" FT COMPBIAS 8..22 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N,N,N-trimethylserine; alternate" FT /evidence="ECO:0000269|PubMed:17435751, FT ECO:0000269|PubMed:18762580, ECO:0000269|PubMed:20668449" FT MOD_RES 2 FT /note="N,N-dimethylserine; alternate" FT /evidence="ECO:0000269|PubMed:17435751, FT ECO:0000269|PubMed:18762580, ECO:0000269|PubMed:20668449" FT MOD_RES 2 FT /note="N-methylserine; alternate" FT /evidence="ECO:0000269|PubMed:17435751, FT ECO:0000269|PubMed:18762580, ECO:0000269|PubMed:20668449" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17435751" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 24 FT /note="K -> KDTRAAASRRVPGARSCQGACGPSPPDQKTRP (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7983178" FT /id="VSP_041122" FT MUTAGEN 2 FT /note="S->A: Does not abolish N-terminal methylation." FT /evidence="ECO:0000269|PubMed:17435751" FT MUTAGEN 2 FT /note="S->Q: Does not abolish N-terminal methylation." FT /evidence="ECO:0000269|PubMed:17435751" FT MUTAGEN 3 FT /note="P->Q: Abolishes N-terminal methylation." FT /evidence="ECO:0000269|PubMed:17435751" FT MUTAGEN 4 FT /note="K->Q: Abolishes N-terminal methylation." FT /evidence="ECO:0000269|PubMed:17435751, FT ECO:0000269|PubMed:20668449" FT MUTAGEN 4 FT /note="K->R: Strongly impairs N-terminal methylation and FT subcellular localization." FT /evidence="ECO:0000269|PubMed:17435751, FT ECO:0000269|PubMed:20668449" FT MUTAGEN 9 FT /note="R->A: Decreases KPNA4 binding. Strongly decreases FT KPNA4 binding; when associated with A-21." FT /evidence="ECO:0000269|PubMed:29042532" FT MUTAGEN 11 FT /note="S->E: Phosphomimetic mutant. Decreases KPNA4 binding FT by about 10%." FT /evidence="ECO:0000269|PubMed:29042532" FT MUTAGEN 21 FT /note="K->A: Decreases KPNA4 binding. Strongly decreases FT KPNA4 binding; when associated with A-9." FT /evidence="ECO:0000269|PubMed:29042532" FT MUTAGEN 182 FT /note="D->A: Abolishes interaction with Ran and impairs FT chromosome localization." FT /evidence="ECO:0000269|PubMed:12194828, FT ECO:0000269|PubMed:17435751" FT STRAND 35..42 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 56..63 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 69..74 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 76..83 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:1A12" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 128..135 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 140..144 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 151..158 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 162..168 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 174..179 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 181..188 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 193..197 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:1I2M" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:1A12" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:1A12" FT HELIX 220..224 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 242..248 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 251..256 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 261..265 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 280..285 FT /evidence="ECO:0007829|PDB:1A12" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 296..301 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 303..310 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 315..319 FT /evidence="ECO:0007829|PDB:1A12" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 328..331 FT /evidence="ECO:0007829|PDB:5TBK" FT STRAND 335..340 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 343..352 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 354..361 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 366..370 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 385..390 FT /evidence="ECO:0007829|PDB:1A12" FT TURN 394..398 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 399..406 FT /evidence="ECO:0007829|PDB:1A12" FT STRAND 408..417 FT /evidence="ECO:0007829|PDB:1A12" SQ SEQUENCE 421 AA; 44969 MW; F6D225AF81928305 CRC64; MSPKRIAKRR SPPADAIPKS KKVKVSHRSH STEPGLVLTL GQGDVGQLGL GENVMERKKP ALVSIPEDVV QAEAGGMHTV CLSKSGQVYS FGCNDEGALG RDTSVEGSEM VPGKVELQEK VVQVSAGDSH TAALTDDGRV FLWGSFRDNN GVIGLLEPMK KSMVPVQVQL DVPVVKVASG NDHLVMLTAD GDLYTLGCGE QGQLGRVPEL FANRGGRQGL ERLLVPKCVM LKSRGSRGHV RFQDAFCGAY FTFAISHEGH VYGFGLSNYH QLGTPGTESC FIPQNLTSFK NSTKSWVGFS GGQHHTVCMD SEGKAYSLGR AEYGRLGLGE GAEEKSIPTL ISRLPAVSSV ACGASVGYAV TKDGRVFAWG MGTNYQLGTG QDEDAWSPVE MMGKQLENRV VLSVSSGGQH TVLLVKDKEQ S //