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P18754 (RCC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of chromosome condensation
Alternative name(s):
Cell cycle regulatory protein
Chromosome condensation protein 1
Gene names
Name:RCC1
Synonyms:CHC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. Ref.9 Ref.10

Subcellular location

Nucleus. Cytoplasm. Note: Becomes dispersed throughout the cytoplasm during mitosis. Ref.10

Post-translational modification

N-terminal methylation by METTL11A/NTM1 is required for binding double-stranded DNA and stable chromatin association. Di- and trimethylation produce a permanent positive charge on the amino group, which facilitate electrostatic binding to the phosphate groups on DNA, while inhibiting histone-binding. Methylated tail helps retain RCC1 on chromosomes during nucleotide exchange on Ran. Ref.10 Ref.11 Ref.13

Miscellaneous

Patients with Raynaud disease produce antibodies that bind to RCC1.

Sequence similarities

Contains 7 RCC1 repeats.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandDNA-binding
   Molecular functionGuanine-nucleotide releasing factor
   PTMMethylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from mutant phenotype Ref.1. Source: UniProtKB

chromosome segregation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle organization

Inferred from direct assay PubMed 15014043. Source: UniProtKB

regulation of Ran GTPase activity

Inferred from direct assay Ref.7. Source: GOC

regulation of mitosis

Inferred from direct assay PubMed 15014043. Source: UniProtKB

spindle assembly

Inferred from mutant phenotype Ref.10. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcondensed nuclear chromosome

Inferred from direct assay PubMed 15014043. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

nuclear chromatin

Inferred from direct assay PubMed 15014043. Source: UniProtKB

nuclear membrane

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionRan guanyl-nucleotide exchange factor activity

Inferred from direct assay Ref.7. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 2677018. Source: UniProtKB

histone binding

Inferred from direct assay PubMed 11375490. Source: UniProtKB

nucleosomal DNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9PubMed 1961752. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RANP628266EBI-992720,EBI-286642
RANBP3Q9H6Z42EBI-992720,EBI-992681

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P18754-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P18754-2)

Also known as: RCC1-I;

The sequence of this isoform differs from the canonical sequence as follows:
     24-24: K → KDTRAAASRRVPGARSCQGACGPSPPDQKTRP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10 Ref.13
Chain2 – 421420Regulator of chromosome condensation
PRO_0000206628

Regions

Repeat34 – 8451RCC1 1
Repeat85 – 13652RCC1 2
Repeat138 – 18952RCC1 3
Repeat191 – 25767RCC1 4
Repeat258 – 31154RCC1 5
Repeat312 – 36251RCC1 6
Repeat363 – 41654RCC1 7

Amino acid modifications

Modified residue21N,N,N-trimethylserine; alternate Ref.10 Ref.11 Ref.13
Modified residue21N,N-dimethylserine; alternate Ref.10 Ref.11 Ref.13
Modified residue21N-methylserine; alternate Ref.10 Ref.11 Ref.13
Modified residue21Phosphoserine Ref.10
Modified residue111Phosphoserine Ref.8 Ref.14 Ref.16

Natural variations

Alternative sequence241K → KDTRAAASRRVPGARSCQGA CGPSPPDQKTRP in isoform 2.
VSP_041122

Experimental info

Mutagenesis21S → A: Does not abolish N-terminal methylation. Ref.10
Mutagenesis21S → Q: Does not abolish N-terminal methylation. Ref.10
Mutagenesis31P → Q: Abolishes N-terminal methylation. Ref.10
Mutagenesis41K → Q: Abolishes N-terminal methylation. Ref.10 Ref.13
Mutagenesis41K → R: Stongly impairs N-terminal methylation and subcellular localization. Ref.10 Ref.13
Mutagenesis1821D → A: Abolishes interaction with Ran and chromosome localization. Ref.10

Secondary structure

.......................................................................... 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: F6D225AF81928305

FASTA42144,969
        10         20         30         40         50         60 
MSPKRIAKRR SPPADAIPKS KKVKVSHRSH STEPGLVLTL GQGDVGQLGL GENVMERKKP 

        70         80         90        100        110        120 
ALVSIPEDVV QAEAGGMHTV CLSKSGQVYS FGCNDEGALG RDTSVEGSEM VPGKVELQEK 

       130        140        150        160        170        180 
VVQVSAGDSH TAALTDDGRV FLWGSFRDNN GVIGLLEPMK KSMVPVQVQL DVPVVKVASG 

       190        200        210        220        230        240 
NDHLVMLTAD GDLYTLGCGE QGQLGRVPEL FANRGGRQGL ERLLVPKCVM LKSRGSRGHV 

       250        260        270        280        290        300 
RFQDAFCGAY FTFAISHEGH VYGFGLSNYH QLGTPGTESC FIPQNLTSFK NSTKSWVGFS 

       310        320        330        340        350        360 
GGQHHTVCMD SEGKAYSLGR AEYGRLGLGE GAEEKSIPTL ISRLPAVSSV ACGASVGYAV 

       370        380        390        400        410        420 
TKDGRVFAWG MGTNYQLGTG QDEDAWSPVE MMGKQLENRV VLSVSSGGQH TVLLVKDKEQ 


S 

« Hide

Isoform 2 (RCC1-I) [UniParc].

Checksum: A31255E99A01A25F
Show »

FASTA45248,146

References

« Hide 'large scale' references
[1]"Isolation and characterization of the active cDNA of the human cell cycle gene (RCC1) involved in the regulation of onset of chromosome condensation."
Ohtsubo M., Kai R., Furuno N., Sekiguchi T., Sekiguchi M., Hayashida H., Kuma K., Miyata T., Fukushige S., Murotsu T., Matsubara K., Nishimoto T.
Genes Dev. 1:585-593(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Complete nucleotide sequence of the human RCC1 gene involved in coupling between DNA replication and mitosis."
Furuno N., Nakagawa K., Eguchi U., Ohtsubo M., Nishimoto T., Soeda E.
Genomics 11:459-461(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"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] (ISOFORMS 1 AND 2).
Tissue: Eye, Mammary gland, Muscle and Testis.
[5]"Mammalian cells have two functional RCC1 proteins produced by alternative splicing."
Miyabashira J., Sekiguchi T., Nishimoto T.
J. Cell Sci. 107:2203-2208(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-33 (ISOFORM 2), ALTERNATIVE SPLICING.
[6]"A 47-kDa human nuclear protein recognized by antikinetochore autoimmune sera is homologous with the protein encoded by RCC1, a gene implicated in onset of chromosome condensation."
Bischoff F.R., Maier G., Tilz G., Ponstingl H.
Proc. Natl. Acad. Sci. U.S.A. 87:8617-8621(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[7]"Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1."
Bischoff F.R., Ponstingl H.
Nature 354:80-82(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Novel function of beta-arrestin2 in the nucleus of mature spermatozoa."
Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.
J. Cell Sci. 119:3047-3056(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[10]"N-terminal alpha-methylation of RCC1 is necessary for stable chromatin association and normal mitosis."
Chen T., Muratore T.L., Schaner-Tooley C.E., Shabanowitz J., Hunt D.F., Macara I.G.
Nat. Cell Biol. 9:596-603(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE OF INITIATOR METHIONINE, SUBCELLULAR LOCATION, HISTONE-BINDING, INTERACTION WITH RAN, PHOSPHORYLATION AT SER-2, METHYLATION AT SER-2, MUTAGENESIS OF SER-2; PRO-3; LYS-4 AND ASP-182.
[11]"Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1."
Hao Y., Macara I.G.
J. Cell Biol. 182:827-836(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT SER-2.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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 SER-2, MUTAGENESIS OF LYS-4.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The 1.7-A crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller."
Renault L., Nassar N., Vetter I., Becker J., Klebe C., Roth M., Wittinghofer A.
Nature 392:97-101(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-421.
[18]"Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1)."
Renault L., Kuhlmann J., Henkel A., Wittinghofer A.
Cell 105:245-255(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 20-421 IN COMPLEX WITH RAN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12654 mRNA. Translation: CAA31182.1.
X06130 mRNA. Translation: CAA29496.1.
D00591 Genomic DNA. Translation: BAA00469.1.
AF498924 mRNA. Translation: AAM21072.1.
BC007300 mRNA. Translation: AAH07300.1.
BC010067 mRNA. Translation: AAH10067.1.
BC036903 mRNA. Translation: AAH36903.1.
BC069198 mRNA. Translation: AAH69198.1.
S75708 mRNA. Translation: AAB32653.1.
CCDSCCDS323.1. [P18754-1]
CCDS41295.1. [P18754-2]
PIRA26691.
RefSeqNP_001041659.1. NM_001048194.2. [P18754-2]
NP_001041660.1. NM_001048195.2.
NP_001041664.1. NM_001048199.2. [P18754-1]
NP_001260.1. NM_001269.4. [P18754-1]
UniGeneHs.469723.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A12X-ray1.70A/B/C9-421[»]
1I2MX-ray1.76B/D20-421[»]
DisProtDP00691.
ProteinModelPortalP18754.
SMRP18754. Positions 21-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107529. 66 interactions.
DIPDIP-35416N.
IntActP18754. 40 interactions.
MINTMINT-240062.
STRING9606.ENSP00000362937.

PTM databases

PhosphoSiteP18754.

Polymorphism databases

DMDM132170.

Proteomic databases

MaxQBP18754.
PaxDbP18754.
PRIDEP18754.

Protocols and materials databases

DNASU1104.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373831; ENSP00000362937; ENSG00000180198. [P18754-2]
ENST00000373832; ENSP00000362938; ENSG00000180198. [P18754-1]
ENST00000373833; ENSP00000362939; ENSG00000180198. [P18754-1]
ENST00000398958; ENSP00000381931; ENSG00000180198. [P18754-1]
GeneID1104.
KEGGhsa:1104.
UCSCuc001bqa.2. human. [P18754-1]
uc001bqe.2. human. [P18754-2]

Organism-specific databases

CTD1104.
GeneCardsGC01P028834.
HGNCHGNC:1913. RCC1.
HPACAB015413.
HPA027573.
HPA027574.
MIM179710. gene.
neXtProtNX_P18754.
PharmGKBPA26449.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5184.
HOGENOMHOG000234341.
HOVERGENHBG017712.
KOK11493.
OMADDAWSPV.
PhylomeDBP18754.
TreeFamTF101139.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressP18754.
BgeeP18754.
CleanExHS_RCC1.
GenevestigatorP18754.

Family and domain databases

Gene3D2.130.10.30. 1 hit.
InterProIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
[Graphical view]
PfamPF00415. RCC1. 7 hits.
[Graphical view]
PRINTSPR00633. RCCNDNSATION.
SUPFAMSSF50985. SSF50985. 1 hit.
PROSITEPS00625. RCC1_1. 1 hit.
PS00626. RCC1_2. 4 hits.
PS50012. RCC1_3. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP18754.
GeneWikiRCC1.
GenomeRNAi1104.
NextBio4572.
PROP18754.
SOURCESearch...

Entry information

Entry nameRCC1_HUMAN
AccessionPrimary (citable) accession number: P18754
Secondary accession number(s): Q16269, Q6NT97
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM