RCC1_HUMAN
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 03-AUG-2022, entry version 224.
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 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 [23]
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 [24] {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 (via N-terminus and RCC1
CC repeats) with KPNA4 (PubMed:29042532). Interacts with ARRB2; the
CC interaction is detected in the nucleus upon OR1D2 stimulation
CC (PubMed:16820410). {ECO:0000269|PubMed:11336674,
CC ECO:0000269|PubMed:16820410, ECO:0000269|PubMed:17435751,
CC ECO:0000269|PubMed:18762580, ECO:0000269|PubMed:29040603,
CC ECO:0000269|PubMed:29042532}.
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.
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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; CCDS323.1; -. [P18754-1]
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 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 AlphaFoldDB; P18754; -.
DR SMR; P18754; -.
DR BioGRID; 107529; 155.
DR DIP; DIP-35416N; -.
DR IntAct; P18754; 83.
DR MINT; P18754; -.
DR STRING; 9606.ENSP00000362937; -.
DR GlyGen; P18754; 1 site, 1 O-linked glycan (1 site).
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 PeptideAtlas; P18754; -.
DR PRIDE; P18754; -.
DR ProteomicsDB; 53606; -. [P18754-1]
DR ProteomicsDB; 53607; -. [P18754-2]
DR TopDownProteomics; P18754-1; -. [P18754-1]
DR Antibodypedia; 4212; 439 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 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; WSWGTND; -.
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; 779 hits in 1090 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 165 other tissues.
DR ExpressionAtlas; P18754; baseline and differential.
DR Genevisible; P18754; HS.
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:0031965; C:nuclear membrane; IDA:HPA.
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; -; 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 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
