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Regulator of chromosome condensation (Chromosome condensation protein 1)

 RCC1_MOUSE              Reviewed;         421 AA.
Q8VE37; Q3UDB6;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
25-APR-2018, entry version 128.
RecName: Full=Regulator of chromosome condensation;
AltName: Full=Chromosome condensation protein 1;
Name=Rcc1; Synonyms=Chc1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT PRO-2.
PubMed=20668449; DOI=10.1038/nature09343;
Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
"NRMT is an alpha-N-methyltransferase that methylates RCC1 and
retinoblastoma protein.";
Nature 466:1125-1128(2010).
-!- FUNCTION: Guanine-nucleotide releasing factor that promotes the
exchange of Ran-bound GDP by GTP, and thereby plays an important
role in RAN-mediated functions in nuclear import and mitosis.
Contributes to the generation of high levels of chromosome-
associated, GTP-bound RAN, which is important for mitotic spindle
assembly and normal progress through mitosis. Via its role in
maintaining high levels of GTP-bound RAN in the nucleus,
contributes to the release of cargo proteins from importins after
nuclear import. Involved in the regulation of onset of chromosome
condensation in the S phase. Binds both to the nucleosomes and
double-stranded DNA. {ECO:0000250|UniProtKB:P18754}.
-!- SUBUNIT: Interacts with RAN. Interacts (via N-terminus and RCC1
repeats) with KPNA4. Interacts with ARRB2; the interaction is
detected in the nucleus upon OR1D2 stimulation.
{ECO:0000250|UniProtKB:P18754}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18754}.
Chromosome {ECO:0000250|UniProtKB:P18754}. Cytoplasm
{ECO:0000250|UniProtKB:P18754}. Note=Predominantly nuclear in
interphase cells. Binds to mitotic chromosomes.
{ECO:0000250|UniProtKB:P18754}.
-!- PTM: N-terminal methylation by METTL11A/NTM1 is required for
binding double-stranded DNA and stable chromatin association.
Dimethylation produces a permanent positive charge on the amino
group, which facilitates electrostatic binding to the phosphate
groups on DNA, while inhibiting histone-binding. Methylated tail
helps retain RCC1 on chromosomes during nucleotide exchange on
Ran. {ECO:0000250|UniProtKB:P18754}.
-----------------------------------------------------------------------
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EMBL; AK150153; BAE29345.1; -; mRNA.
EMBL; BC019807; AAH19807.1; -; mRNA.
CCDS; CCDS18723.1; -.
RefSeq; NP_598639.1; NM_133878.3.
UniGene; Mm.255045; -.
ProteinModelPortal; Q8VE37; -.
SMR; Q8VE37; -.
BioGrid; 221378; 64.
IntAct; Q8VE37; 64.
MINT; Q8VE37; -.
STRING; 10090.ENSMUSP00000030726; -.
iPTMnet; Q8VE37; -.
PhosphoSitePlus; Q8VE37; -.
EPD; Q8VE37; -.
MaxQB; Q8VE37; -.
PaxDb; Q8VE37; -.
PRIDE; Q8VE37; -.
Ensembl; ENSMUST00000084250; ENSMUSP00000081271; ENSMUSG00000028896.
Ensembl; ENSMUST00000105951; ENSMUSP00000101571; ENSMUSG00000028896.
GeneID; 100088; -.
KEGG; mmu:100088; -.
UCSC; uc008vbc.2; mouse.
CTD; 1104; -.
MGI; MGI:1913989; Rcc1.
eggNOG; KOG1426; Eukaryota.
eggNOG; COG5184; LUCA.
GeneTree; ENSGT00910000144029; -.
HOGENOM; HOG000234341; -.
HOVERGEN; HBG017712; -.
InParanoid; Q8VE37; -.
KO; K11493; -.
PhylomeDB; Q8VE37; -.
TreeFam; TF101139; -.
ChiTaRS; Rcc1; mouse.
PRO; PR:Q8VE37; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028896; -.
CleanEx; MM_RCC1; -.
ExpressionAtlas; Q8VE37; baseline and differential.
Genevisible; Q8VE37; MM.
GO; GO:0000794; C:condensed nuclear chromosome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0031965; C:nuclear membrane; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISO:MGI.
GO; GO:0042393; F:histone binding; ISO:MGI.
GO; GO:0031492; F:nucleosomal DNA binding; ISS:UniProtKB.
GO; GO:0031491; F:nucleosome binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0008536; F:Ran GTPase binding; ISO:MGI.
GO; GO:0005087; F:Ran guanyl-nucleotide exchange factor activity; IDA:MGI.
GO; GO:0043199; F:sulfate binding; ISO:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
GO; GO:0051290; P:protein heterotetramerization; ISO:MGI.
GO; GO:0007088; P:regulation of mitotic nuclear division; ISO:MGI.
GO; GO:0051225; P:spindle assembly; ISS:UniProtKB.
Gene3D; 2.130.10.30; -; 1.
InterPro; IPR009091; RCC1/BLIP-II.
InterPro; IPR000408; Reg_chr_condens.
Pfam; PF00415; RCC1; 7.
PRINTS; PR00633; RCCNDNSATION.
SUPFAM; SSF50985; SSF50985; 1.
PROSITE; PS00625; RCC1_1; 1.
PROSITE; PS00626; RCC1_2; 4.
PROSITE; PS50012; RCC1_3; 7.
1: Evidence at protein level;
Cell cycle; Cell division; Chromosome; Complete proteome; Cytoplasm;
DNA-binding; Guanine-nucleotide releasing factor; Methylation;
Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:20668449}.
CHAIN 2 421 Regulator of chromosome condensation.
/FTId=PRO_0000206630.
REPEAT 34 84 RCC1 1.
REPEAT 85 136 RCC1 2.
REPEAT 138 189 RCC1 3.
REPEAT 191 257 RCC1 4.
REPEAT 258 311 RCC1 5.
REPEAT 312 362 RCC1 6.
REPEAT 363 416 RCC1 7.
MOTIF 4 24 Bipartite nuclear localization signal.
{ECO:0000250|UniProtKB:P18754}.
MOD_RES 2 2 N,N-dimethylproline; alternate.
{ECO:0000269|PubMed:20668449}.
MOD_RES 2 2 N-methylproline; alternate.
{ECO:0000269|PubMed:20668449}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:P18754}.
CONFLICT 45 45 V -> M (in Ref. 1; BAE29345).
{ECO:0000305}.
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


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