RCC1_MOUSE
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}.
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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
