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Protein

Regulator of chromosome condensation

Gene

Rcc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP. Involved in the regulation of onset of chromosome condensation in the S phase. Binds both to the nucleosomes and double-stranded DNA. RCC1-Ran complex (together with other proteins) acts as a component of a signal transmission pathway that detects unreplicated DNA. Plays a key role in nucleo-cytoplasmic transport, mitosis and nuclear-envelope assembly (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of chromosome condensation
Alternative name(s):
Chromosome condensation protein 1
Gene namesi
Name:Rcc1
Synonyms:Chc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1913989. Rcc1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Becomes dispersed throughout the cytoplasm during mitosis.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 421420Regulator of chromosome condensationPRO_0000206630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N,N-dimethylproline; alternate1 Publication
Modified residuei2 – 21N-methylproline; alternate1 Publication
Modified residuei11 – 111PhosphoserineBy similarity

Post-translational modificationi

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 (By similarity).By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ8VE37.
MaxQBiQ8VE37.
PaxDbiQ8VE37.
PRIDEiQ8VE37.

PTM databases

iPTMnetiQ8VE37.
PhosphoSiteiQ8VE37.

Expressioni

Gene expression databases

BgeeiQ8VE37.
CleanExiMM_RCC1.
ExpressionAtlasiQ8VE37. baseline and differential.
GenevisibleiQ8VE37. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi221378. 64 interactions.
IntActiQ8VE37. 64 interactions.
MINTiMINT-2568412.
STRINGi10090.ENSMUSP00000030726.

Structurei

3D structure databases

ProteinModelPortaliQ8VE37.
SMRiQ8VE37. Positions 21-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati34 – 8451RCC1 1Add
BLAST
Repeati85 – 13652RCC1 2Add
BLAST
Repeati138 – 18952RCC1 3Add
BLAST
Repeati191 – 25767RCC1 4Add
BLAST
Repeati258 – 31154RCC1 5Add
BLAST
Repeati312 – 36251RCC1 6Add
BLAST
Repeati363 – 41654RCC1 7Add
BLAST

Sequence similaritiesi

Contains 7 RCC1 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1426. Eukaryota.
COG5184. LUCA.
GeneTreeiENSGT00840000129719.
HOGENOMiHOG000234341.
HOVERGENiHBG017712.
InParanoidiQ8VE37.
KOiK11493.
OrthoDBiEOG7HQN8F.
PhylomeDBiQ8VE37.
TreeFamiTF101139.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
[Graphical view]
PfamiPF00415. RCC1. 7 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SUPFAMiSSF50985. SSF50985. 1 hit.
PROSITEiPS00625. RCC1_1. 1 hit.
PS00626. RCC1_2. 4 hits.
PS50012. RCC1_3. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8VE37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPKRIAKRR SPPEDAIPKS KKVKVSHRSH NTEPGLVLTL GQGDVGQLGL
60 70 80 90 100
GESVLERKKP ALVPLLQDVV QAEAGGMHTV CLSQSGQVYS FGCNDEGALG
110 120 130 140 150
RDTSVEGSEM VPGKVELQEK VVQVSAGDSH TAALTEDGRV FLWGSFRDNN
160 170 180 190 200
GVIGLLEPMK KSMVPVQVQL DAPVVKVASG NDHLVMLTND GDLYTLGCGE
210 220 230 240 250
QGQLGRVPEL FANRGGRQGL GRLLVPRCVL LKSRGTRGRV RFQDAFCGAY
260 270 280 290 300
FTFAISREGH VYGFGLSNYH QLGTPGTGSC FIPQNLTSFK NSTKSWVGFS
310 320 330 340 350
GGQHHTVCMD SEGKAYSLGR AEYGRLGLGE GAEEKSIPTL ISRLPVVSSV
360 370 380 390 400
ACGASVGYAV SKDGRVFAWG MGTNYQLGTG QDEDAWSPVE MTGKQLENRV
410 420
VLTVSSGGQH TVLLVKDQAQ S
Length:421
Mass (Da):44,931
Last modified:March 1, 2002 - v1
Checksum:iACE5019E50E1E9DC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451V → M in BAE29345 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK150153 mRNA. Translation: BAE29345.1.
BC019807 mRNA. Translation: AAH19807.1.
CCDSiCCDS18723.1.
RefSeqiNP_598639.1. NM_133878.3.
UniGeneiMm.255045.

Genome annotation databases

EnsembliENSMUST00000084250; ENSMUSP00000081271; ENSMUSG00000028896.
ENSMUST00000105951; ENSMUSP00000101571; ENSMUSG00000028896.
GeneIDi100088.
KEGGimmu:100088.
UCSCiuc008vbc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK150153 mRNA. Translation: BAE29345.1.
BC019807 mRNA. Translation: AAH19807.1.
CCDSiCCDS18723.1.
RefSeqiNP_598639.1. NM_133878.3.
UniGeneiMm.255045.

3D structure databases

ProteinModelPortaliQ8VE37.
SMRiQ8VE37. Positions 21-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221378. 64 interactions.
IntActiQ8VE37. 64 interactions.
MINTiMINT-2568412.
STRINGi10090.ENSMUSP00000030726.

PTM databases

iPTMnetiQ8VE37.
PhosphoSiteiQ8VE37.

Proteomic databases

EPDiQ8VE37.
MaxQBiQ8VE37.
PaxDbiQ8VE37.
PRIDEiQ8VE37.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084250; ENSMUSP00000081271; ENSMUSG00000028896.
ENSMUST00000105951; ENSMUSP00000101571; ENSMUSG00000028896.
GeneIDi100088.
KEGGimmu:100088.
UCSCiuc008vbc.2. mouse.

Organism-specific databases

CTDi1104.
MGIiMGI:1913989. Rcc1.

Phylogenomic databases

eggNOGiKOG1426. Eukaryota.
COG5184. LUCA.
GeneTreeiENSGT00840000129719.
HOGENOMiHOG000234341.
HOVERGENiHBG017712.
InParanoidiQ8VE37.
KOiK11493.
OrthoDBiEOG7HQN8F.
PhylomeDBiQ8VE37.
TreeFamiTF101139.

Miscellaneous databases

ChiTaRSiRcc1. mouse.
PROiQ8VE37.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VE37.
CleanExiMM_RCC1.
ExpressionAtlasiQ8VE37. baseline and differential.
GenevisibleiQ8VE37. MM.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
[Graphical view]
PfamiPF00415. RCC1. 7 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SUPFAMiSSF50985. SSF50985. 1 hit.
PROSITEiPS00625. RCC1_1. 1 hit.
PS00626. RCC1_2. 4 hits.
PS50012. RCC1_3. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.
  4. "NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein."
    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.
    Nature 466:1125-1128(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT PRO-2.

Entry informationi

Entry nameiRCC1_MOUSE
AccessioniPrimary (citable) accession number: Q8VE37
Secondary accession number(s): Q3UDB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.