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Protein Page:
RCC1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RCC1 a guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP for GTP. Localised generation of Ran-GTP by RCC1 on chromatin is critical for nucleocytoplasmic transport, mitotic spindle assembly and nuclear envelope formation. 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. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: GEFs, Ras; GEFs; Cell cycle regulation
Chromosomal Location of Human Ortholog: 1p36.1
Cellular Component: nucleoplasm; nuclear membrane; condensed nuclear chromosome; cytoplasm; nuclear chromatin; nucleolus; nucleus
Molecular Function: protein binding; nucleosomal DNA binding; Ran guanyl-nucleotide exchange factor activity; histone binding; chromatin binding
Biological Process: mitosis; mitotic spindle organization and biogenesis; viral reproduction; regulation of mitosis; spindle assembly; positive regulation of Ran GTPase activity; chromosome segregation; G1/S transition of mitotic cell cycle
Reference #:  P18754 (UniProtKB)
Alt. Names/Synonyms: Cell cycle regulatory protein; CHC1; chromosome condensation 1; Chromosome condensation protein 1; guanine nucleotide-releasing protein; RCC1; RCC1-I; Regulator of chromosome condensation; regulator of chromosome condensation 1
Gene Symbols: RCC1
Molecular weight: 44,969 Da
Basal Isoelectric point: 7.18  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RCC1

Protein Structure Not Found.


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Sites Implicated In
cell growth, altered: S11‑p
cytoskeletal reorganization: S11‑p
intracellular localization: S11‑p
molecular association, regulation: S11‑p, S20‑p, S26‑p, S29‑p, T32‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
1 0 S2-p ______MsPKRIAKR
3 40 S11-p KRIAKRRsPPADAIP
1 0 S20-p PADAIPKsKKVKVsH
0 2 - gap
1 0 S26-p KsKKVKVsHRsHStE
1 0 S29-p KVKVsHRsHStEPGL
1 0 T32-p VsHRsHStEPGLVLT
0 1 S85-p HTVCLSKsGQVysFG
0 1 Y89-p LSKsGQVysFGCNDE
0 2 S90-p SKsGQVysFGCNDEG
0 2 S104-p GALGRDTsVEGSEMV
0 1 K114-ub GSEMVPGkVELQEKV
0 1 K160-ub IGLLEPMkksMVPVQ
0 1 K161-ub GLLEPMkksMVPVQV
0 1 S162-p LLEPMkksMVPVQVQ
0 3 R214 VPELFANRGGRQGLE
1 0 T274-p SNYHQLGtPGTESCF
0 1 T306-p FSGGQHHtVCMDsEG
0 1 S311-p HHtVCMDsEGKAYSL
0 2 K335-ub LGEGAEEksIPtLIS
0 1 S336-p GEGAEEksIPtLISR
0 1 T339-p AEEksIPtLISRLPA
1 0 S387-p GQDEDAWsPVEMMGK
0 1 S403-p LENRVVLsVssGGQH
0 1 S405-p NRVVLsVssGGQHtV
0 1 S406-p RVVLsVssGGQHtVL
0 1 T411-p VssGGQHtVLLVKDK
4210 : Phospho-RCC1 (Ser11) Antibody
5500 : Phospho-RCC1 (Ser11) (D18B5) Rabbit mAb
  RCC1 iso2  
S2 ______MSPKRIAKR
S11-p KRIAKRRsPPADAIP
S20 PADAIPKSKKVKDTR
S47-p CQGACGPsPPDQKTR
S57 DQKTRPVSHRSHSTE
S60 TRPVSHRSHSTEPGL
T63 VSHRSHSTEPGLVLT
S116 HTVCLSKSGQVYSFG
Y120 LSKSGQVYSFGCNDE
S121 SKSGQVYSFGCNDEG
S135 GALGRDTSVEGSEMV
K145 GSEMVPGKVELQEKV
K191 IGLLEPMKKSMVPVQ
K192 GLLEPMKKSMVPVQV
S193 LLEPMKKSMVPVQVQ
R245 VPELFANRGGRQGLE
T305 SNYHQLGTPGTESCF
T337 FSGGQHHTVCMDSEG
S342 HHTVCMDSEGKAYSL
K366 LGEGAEEKSIPTLIS
S367 GEGAEEKSIPTLISR
T370 AEEKSIPTLISRLPA
S418 GQDEDAWSPVEMMGK
S434 LENRVVLSVSSGGQH
S436 NRVVLSVSSGGQHTV
S437 RVVLSVSSGGQHTVL
T442 VSSGGQHTVLLVKDK
  mouse

 
P2 ______MPPKRIAKR
S11-p KRIAKRRsPPEDAIP
S20 PEDAIPKSKKVKVSH
- gap
S26 KSKKVKVSHRSHNTE
S29 KVKVSHRSHNTEPGL
T32 VSHRSHNTEPGLVLT
S85 HTVCLSQSGQVYSFG
Y89 LSQSGQVYSFGCNDE
S90 SQSGQVYSFGCNDEG
S104 GALGRDTSVEGSEMV
K114 GSEMVPGKVELQEKV
K160 IGLLEPMKKSMVPVQ
K161 GLLEPMKKSMVPVQV
S162 LLEPMKKSMVPVQVQ
R214-m1 VPELFANrGGRQGLG
T274 SNYHQLGTPGTGSCF
T306 FSGGQHHTVCMDSEG
S311 HHTVCMDSEGKAYSL
K335 LGEGAEEKSIPTLIS
S336 GEGAEEKSIPTLISR
T339 AEEKSIPTLISRLPV
S387 GQDEDAWSPVEMTGK
T403 LENRVVLTVSSGGQH
S405 NRVVLTVSSGGQHTV
S406 RVVLTVSSGGQHTVL
T411 VSSGGQHTVLLVKDQ
  rat

 
P2 ______MPPKRIAKR
S11-p KRIAKRRsPPEDAIP
S20 PEDAIPKSKKVKVSH
- gap
S26 KSKKVKVSHRSHNTE
S29 KVKVSHRSHNTEPGL
T32 VSHRSHNTEPGLVLT
S85 HTVCLSQSGQVYSFG
Y89 LSQSGQVYSFGCNDE
S90 SQSGQVYSFGCNDEG
S104 GALGRDTSVEGSEMV
K114 GSEMVPGKVELQEKV
K160 IGLLEPMKKSMVPVQ
K161 GLLEPMKKSMVPVQV
S162 LLEPMKKSMVPVQVQ
R214 VPELFANRGGRQGLE
T274 SNYHQLGTPGTGSCF
T306 FSGGQHHTVCMDSEG
S311 HHTVCMDSEGKAYSL
K335 LGEGAEEKSIPTLIS
S336 GEGAEEKSIPTLISR
T339 AEEKSIPTLISRLPV
S387 GQEDDAWSPVEMTGK
T403 LENREVLTVSSGGQH
S405 NREVLTVSSGGQHTV
S406 REVLTVSSGGQHTVL
T411 VSSGGQHTVLLVKDK
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