P18754 · RCC1_HUMAN
- ProteinRegulator of chromosome condensation
- GeneRCC1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids421 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 (PubMed:11336674, PubMed:17435751, PubMed:1944575, PubMed:20668449, PubMed:22215983, PubMed:29042532).
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 (PubMed:12194828, PubMed:17435751, PubMed:22215983).
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 (PubMed:22215983).
Involved in the regulation of onset of chromosome condensation in the S phase (PubMed:3678831).
Binds both to the nucleosomes and double-stranded DNA (PubMed:17435751, PubMed:18762580).
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 (PubMed:12194828, PubMed:17435751, PubMed:22215983).
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 (PubMed:22215983).
Involved in the regulation of onset of chromosome condensation in the S phase (PubMed:3678831).
Binds both to the nucleosomes and double-stranded DNA (PubMed:17435751, PubMed:18762580).
Miscellaneous
Patients with Raynaud disease produce antibodies that bind to RCC1.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | chromosome | |
Cellular Component | condensed nuclear chromosome | |
Cellular Component | cytoplasm | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | protein-containing complex | |
Molecular Function | chromatin binding | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Molecular Function | histone binding | |
Molecular Function | nucleosomal DNA binding | |
Molecular Function | nucleosome binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | small GTPase binding | |
Molecular Function | sulfate binding | |
Biological Process | cell division | |
Biological Process | chromosome segregation | |
Biological Process | G1/S transition of mitotic cell cycle | |
Biological Process | mitotic nuclear membrane reassembly | |
Biological Process | mitotic spindle organization | |
Biological Process | regulation of mitotic nuclear division | |
Biological Process | spindle assembly | |
Biological Process | viral process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRegulator of chromosome condensation
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP18754
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | Does not abolish N-terminal methylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 2 | Does not abolish N-terminal methylation. | ||||
Sequence: S → Q | ||||||
Mutagenesis | 3 | Abolishes N-terminal methylation. | ||||
Sequence: P → Q | ||||||
Mutagenesis | 4 | Abolishes N-terminal methylation. | ||||
Sequence: K → Q | ||||||
Mutagenesis | 4 | Strongly impairs N-terminal methylation and subcellular localization. | ||||
Sequence: K → R | ||||||
Mutagenesis | 9 | Decreases KPNA4 binding. Strongly decreases KPNA4 binding; when associated with A-21. | ||||
Sequence: R → A | ||||||
Mutagenesis | 11 | Phosphomimetic mutant. Decreases KPNA4 binding by about 10%. | ||||
Sequence: S → E | ||||||
Mutagenesis | 21 | Decreases KPNA4 binding. Strongly decreases KPNA4 binding; when associated with A-9. | ||||
Sequence: K → A | ||||||
Mutagenesis | 182 | Abolishes interaction with Ran and impairs chromosome localization. | ||||
Sequence: D → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 431 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N,N,N-trimethylserine; alternate | ||||
Sequence: S | |||||||
Modified residue | 2 | UniProt | N,N-dimethylserine; alternate | ||||
Sequence: S | |||||||
Modified residue | 2 | UniProt | N-methylserine; alternate | ||||
Sequence: S | |||||||
Modified residue | 2 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000206628 | 2-421 | UniProt | Regulator of chromosome condensation | |||
Sequence: SPKRIAKRRSPPADAIPKSKKVKVSHRSHSTEPGLVLTLGQGDVGQLGLGENVMERKKPALVSIPEDVVQAEAGGMHTVCLSKSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTDDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASGNDHLVMLTADGDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHVRFQDAFCGAYFTFAISHEGHVYGFGLSNYHQLGTPGTESCFIPQNLTSFKNSTKSWVGFSGGQHHTVCMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPAVSSVACGASVGYAVTKDGRVFAWGMGTNYQLGTGQDEDAWSPVEMMGKQLENRVVLSVSSGGQHTVLLVKDKEQS | |||||||
Modified residue | 11 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 104 | PRIDE | Phosphoserine | ||||
Sequence: S |
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 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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with RAN (PubMed:11336674, PubMed:17435751, PubMed:18762580, PubMed:29040603).
Interacts with KPNA3 (PubMed:34564892).
Interacts (via N-terminus and RCC1 repeats) with KPNA4 (PubMed:29042532).
Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation (PubMed:16820410).
Interacts with KPNA3 (PubMed:34564892).
Interacts (via N-terminus and RCC1 repeats) with KPNA4 (PubMed:29042532).
Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation (PubMed:16820410).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P18754 | NTMT1 Q9BV86 | 4 | EBI-992720, EBI-373016 | |
XENO | P18754 | P02281 | 2 | EBI-992720, EBI-1251201 | |
BINARY | P18754 | RAN P62826 | 19 | EBI-992720, EBI-286642 | |
BINARY | P18754 | RANBP3 Q9H6Z4 | 2 | EBI-992720, EBI-992681 | |
BINARY | P18754 | XPO1 O14980 | 2 | EBI-992720, EBI-355867 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-36 | Disordered | ||||
Sequence: MSPKRIAKRRSPPADAIPKSKKVKVSHRSHSTEPGL | ||||||
Motif | 4-24 | Bipartite nuclear localization signal | ||||
Sequence: KRIAKRRSPPADAIPKSKKVK | ||||||
Compositional bias | 8-22 | Basic and acidic residues | ||||
Sequence: KRRSPPADAIPKSKK | ||||||
Repeat | 34-84 | RCC1 1 | ||||
Sequence: PGLVLTLGQGDVGQLGLGENVMERKKPALVSIPEDVVQAEAGGMHTVCLSK | ||||||
Repeat | 85-136 | RCC1 2 | ||||
Sequence: SGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTD | ||||||
Repeat | 138-189 | RCC1 3 | ||||
Sequence: GRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASGNDHLVMLTA | ||||||
Repeat | 191-257 | RCC1 4 | ||||
Sequence: GDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHVRFQDAFCGAYFTFAISH | ||||||
Repeat | 258-311 | RCC1 5 | ||||
Sequence: EGHVYGFGLSNYHQLGTPGTESCFIPQNLTSFKNSTKSWVGFSGGQHHTVCMDS | ||||||
Repeat | 312-362 | RCC1 6 | ||||
Sequence: EGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPAVSSVACGASVGYAVTK | ||||||
Repeat | 363-416 | RCC1 7 | ||||
Sequence: DGRVFAWGMGTNYQLGTGQDEDAWSPVEMMGKQLENRVVLSVSSGGQHTVLLVK |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
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.
- Name1
- Length421
- Mass (Da)44,969
- Last updated1990-11-01 v1
- ChecksumF6D225AF81928305
P18754-2
- Name2
- SynonymsRCC1-I
- Differences from canonical
- 24-24: K → KDTRAAASRRVPGARSCQGACGPSPPDQKTRP
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 8-22 | Basic and acidic residues | ||||
Sequence: KRRSPPADAIPKSKK | ||||||
Alternative sequence | VSP_041122 | 24 | in isoform 2 | |||
Sequence: K → KDTRAAASRRVPGARSCQGACGPSPPDQKTRP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X12654 EMBL· GenBank· DDBJ | CAA31182.1 EMBL· GenBank· DDBJ | mRNA | ||
X06130 EMBL· GenBank· DDBJ | CAA29496.1 EMBL· GenBank· DDBJ | mRNA | ||
D00591 EMBL· GenBank· DDBJ | BAA00469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF498924 EMBL· GenBank· DDBJ | AAM21072.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007300 EMBL· GenBank· DDBJ | AAH07300.1 EMBL· GenBank· DDBJ | mRNA | ||
BC010067 EMBL· GenBank· DDBJ | AAH10067.1 EMBL· GenBank· DDBJ | mRNA | ||
BC036903 EMBL· GenBank· DDBJ | AAH36903.1 EMBL· GenBank· DDBJ | mRNA | ||
BC069198 EMBL· GenBank· DDBJ | AAH69198.1 EMBL· GenBank· DDBJ | mRNA | ||
S75708 EMBL· GenBank· DDBJ | AAB32653.1 EMBL· GenBank· DDBJ | mRNA |