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Protein

Regulator of chromosome condensation

Gene

RCC1

Organism
Homo sapiens (Human)
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.1 Publication

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • nucleosomal DNA binding Source: UniProtKB
  • Ran guanyl-nucleotide exchange factor activity Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB
  • G1/S transition of mitotic cell cycle Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • mitotic spindle organization Source: UniProtKB
  • regulation of mitotic nuclear division Source: UniProtKB
  • spindle assembly Source: UniProtKB
  • viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000180198-MONOMER.
ReactomeiR-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-180746. Nuclear import of Rev protein.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of chromosome condensation
Alternative name(s):
Cell cycle regulatory protein
Chromosome condensation protein 1
Gene namesi
Name:RCC1
Synonyms:CHC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1913. RCC1.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

  • Note: Becomes dispersed throughout the cytoplasm during mitosis.

GO - Cellular componenti

  • condensed nuclear chromosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • nuclear chromatin Source: UniProtKB
  • nuclear membrane Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2S → A: Does not abolish N-terminal methylation. 1 Publication1
Mutagenesisi2S → Q: Does not abolish N-terminal methylation. 1 Publication1
Mutagenesisi3P → Q: Abolishes N-terminal methylation. 1 Publication1
Mutagenesisi4K → Q: Abolishes N-terminal methylation. 2 Publications1
Mutagenesisi4K → R: Stongly impairs N-terminal methylation and subcellular localization. 2 Publications1
Mutagenesisi182D → A: Abolishes interaction with Ran and chromosome localization. 1 Publication1

Organism-specific databases

DisGeNETi1104.
OpenTargetsiENSG00000180198.
PharmGKBiPA26449.

Polymorphism and mutation databases

BioMutaiRCC1.
DMDMi132170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002066282 – 421Regulator of chromosome condensationAdd BLAST420

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N,N,N-trimethylserine; alternate3 Publications1
Modified residuei2N,N-dimethylserine; alternate3 Publications1
Modified residuei2N-methylserine; alternate3 Publications1
Modified residuei2Phosphoserine1 Publication1
Modified residuei11PhosphoserineCombined sources1

Post-translational modificationi

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 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.3 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiP18754.
PeptideAtlasiP18754.
PRIDEiP18754.
TopDownProteomicsiP18754-1. [P18754-1]

PTM databases

iPTMnetiP18754.
PhosphoSitePlusiP18754.
SwissPalmiP18754.

Expressioni

Gene expression databases

BgeeiENSG00000180198.
CleanExiHS_RCC1.
ExpressionAtlasiP18754. baseline and differential.
GenevisibleiP18754. HS.

Organism-specific databases

HPAiCAB015413.
HPA027573.
HPA027574.

Interactioni

Subunit structurei

Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RANP628266EBI-992720,EBI-286642
RANBP3Q9H6Z42EBI-992720,EBI-992681

GO - Molecular functioni

  • histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107529. 98 interactors.
DIPiDIP-35416N.
IntActiP18754. 59 interactors.
MINTiMINT-240062.

Structurei

Secondary structure

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 42Combined sources8
Beta strandi56 – 63Combined sources8
Beta strandi69 – 74Combined sources6
Beta strandi76 – 83Combined sources8
Beta strandi88 – 92Combined sources5
Helixi108 – 110Combined sources3
Beta strandi121 – 126Combined sources6
Beta strandi128 – 135Combined sources8
Beta strandi140 – 144Combined sources5
Beta strandi146 – 148Combined sources3
Beta strandi151 – 158Combined sources8
Beta strandi162 – 168Combined sources7
Beta strandi174 – 179Combined sources6
Beta strandi181 – 188Combined sources8
Beta strandi193 – 197Combined sources5
Beta strandi205 – 207Combined sources3
Helixi208 – 210Combined sources3
Beta strandi212 – 214Combined sources3
Helixi216 – 219Combined sources4
Helixi220 – 224Combined sources5
Beta strandi242 – 248Combined sources7
Beta strandi251 – 256Combined sources6
Beta strandi261 – 265Combined sources5
Beta strandi280 – 285Combined sources6
Helixi287 – 289Combined sources3
Beta strandi296 – 301Combined sources6
Beta strandi303 – 310Combined sources8
Beta strandi315 – 319Combined sources5
Helixi322 – 324Combined sources3
Beta strandi335 – 340Combined sources6
Beta strandi343 – 352Combined sources10
Beta strandi354 – 361Combined sources8
Beta strandi366 – 370Combined sources5
Beta strandi379 – 381Combined sources3
Beta strandi385 – 390Combined sources6
Turni394 – 398Combined sources5
Beta strandi399 – 406Combined sources8
Beta strandi408 – 417Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A12X-ray1.70A/B/C9-421[»]
1I2MX-ray1.76B/D20-421[»]
5E1BX-ray1.65D/E2-7[»]
5E1DX-ray1.45D/E3-7[»]
5E1MX-ray1.75D/E3-7[»]
5E1OX-ray2.00D/E3-7[»]
5E2AX-ray1.75D/E3-7[»]
5E2BX-ray1.95D/E3-7[»]
DisProtiDP00691.
ProteinModelPortaliP18754.
SMRiP18754.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18754.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati34 – 84RCC1 1Add BLAST51
Repeati85 – 136RCC1 2Add BLAST52
Repeati138 – 189RCC1 3Add BLAST52
Repeati191 – 257RCC1 4Add BLAST67
Repeati258 – 311RCC1 5Add BLAST54
Repeati312 – 362RCC1 6Add BLAST51
Repeati363 – 416RCC1 7Add BLAST54

Sequence similaritiesi

Contains 7 RCC1 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00860000133726.
HOGENOMiHOG000234341.
HOVERGENiHBG017712.
InParanoidiP18754.
KOiK11493.
OMAiVSHRSHN.
OrthoDBiEOG091G05E6.
PhylomeDBiP18754.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P18754-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSPKRIAKRR SPPADAIPKS KKVKVSHRSH STEPGLVLTL GQGDVGQLGL
60 70 80 90 100
GENVMERKKP ALVSIPEDVV QAEAGGMHTV CLSKSGQVYS FGCNDEGALG
110 120 130 140 150
RDTSVEGSEM VPGKVELQEK VVQVSAGDSH TAALTDDGRV FLWGSFRDNN
160 170 180 190 200
GVIGLLEPMK KSMVPVQVQL DVPVVKVASG NDHLVMLTAD GDLYTLGCGE
210 220 230 240 250
QGQLGRVPEL FANRGGRQGL ERLLVPKCVM LKSRGSRGHV RFQDAFCGAY
260 270 280 290 300
FTFAISHEGH VYGFGLSNYH QLGTPGTESC FIPQNLTSFK NSTKSWVGFS
310 320 330 340 350
GGQHHTVCMD SEGKAYSLGR AEYGRLGLGE GAEEKSIPTL ISRLPAVSSV
360 370 380 390 400
ACGASVGYAV TKDGRVFAWG MGTNYQLGTG QDEDAWSPVE MMGKQLENRV
410 420
VLSVSSGGQH TVLLVKDKEQ S
Length:421
Mass (Da):44,969
Last modified:November 1, 1990 - v1
Checksum:iF6D225AF81928305
GO
Isoform 2 (identifier: P18754-2) [UniParc]FASTAAdd to basket
Also known as: RCC1-I

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

Show »
Length:452
Mass (Da):48,146
Checksum:iA31255E99A01A25F
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04112224K → KDTRAAASRRVPGARSCQGA CGPSPPDQKTRP in isoform 2. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS323.1. [P18754-1]
CCDS41295.1. [P18754-2]
PIRiA26691.
RefSeqiNP_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]
UniGeneiHs.469723.

Genome annotation databases

EnsembliENST00000373831; ENSP00000362937; ENSG00000180198. [P18754-2]
ENST00000373832; ENSP00000362938; ENSG00000180198. [P18754-1]
ENST00000373833; ENSP00000362939; ENSG00000180198. [P18754-1]
ENST00000398958; ENSP00000381931; ENSG00000180198. [P18754-1]
GeneIDi1104.
KEGGihsa:1104.
UCSCiuc001bqf.3. human. [P18754-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS323.1. [P18754-1]
CCDS41295.1. [P18754-2]
PIRiA26691.
RefSeqiNP_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]
UniGeneiHs.469723.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A12X-ray1.70A/B/C9-421[»]
1I2MX-ray1.76B/D20-421[»]
5E1BX-ray1.65D/E2-7[»]
5E1DX-ray1.45D/E3-7[»]
5E1MX-ray1.75D/E3-7[»]
5E1OX-ray2.00D/E3-7[»]
5E2AX-ray1.75D/E3-7[»]
5E2BX-ray1.95D/E3-7[»]
DisProtiDP00691.
ProteinModelPortaliP18754.
SMRiP18754.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107529. 98 interactors.
DIPiDIP-35416N.
IntActiP18754. 59 interactors.
MINTiMINT-240062.

PTM databases

iPTMnetiP18754.
PhosphoSitePlusiP18754.
SwissPalmiP18754.

Polymorphism and mutation databases

BioMutaiRCC1.
DMDMi132170.

Proteomic databases

EPDiP18754.
PeptideAtlasiP18754.
PRIDEiP18754.
TopDownProteomicsiP18754-1. [P18754-1]

Protocols and materials databases

DNASUi1104.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373831; ENSP00000362937; ENSG00000180198. [P18754-2]
ENST00000373832; ENSP00000362938; ENSG00000180198. [P18754-1]
ENST00000373833; ENSP00000362939; ENSG00000180198. [P18754-1]
ENST00000398958; ENSP00000381931; ENSG00000180198. [P18754-1]
GeneIDi1104.
KEGGihsa:1104.
UCSCiuc001bqf.3. human. [P18754-1]

Organism-specific databases

CTDi1104.
DisGeNETi1104.
GeneCardsiRCC1.
HGNCiHGNC:1913. RCC1.
HPAiCAB015413.
HPA027573.
HPA027574.
MIMi179710. gene.
neXtProtiNX_P18754.
OpenTargetsiENSG00000180198.
PharmGKBiPA26449.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00860000133726.
HOGENOMiHOG000234341.
HOVERGENiHBG017712.
InParanoidiP18754.
KOiK11493.
OMAiVSHRSHN.
OrthoDBiEOG091G05E6.
PhylomeDBiP18754.
TreeFamiTF101139.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000180198-MONOMER.
ReactomeiR-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-180746. Nuclear import of Rev protein.

Miscellaneous databases

ChiTaRSiRCC1. human.
EvolutionaryTraceiP18754.
GeneWikiiRCC1.
GenomeRNAii1104.
PROiP18754.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000180198.
CleanExiHS_RCC1.
ExpressionAtlasiP18754. baseline and differential.
GenevisibleiP18754. HS.

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...

Entry informationi

Entry nameiRCC1_HUMAN
AccessioniPrimary (citable) accession number: P18754
Secondary accession number(s): Q16269, Q6NT97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 30, 2016
This is version 183 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Patients with Raynaud disease produce antibodies that bind to RCC1.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.