RCC1_MOUSE - dbPTM
RCC1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RCC1_MOUSE
UniProt AC Q8VE37
Protein Name Regulator of chromosome condensation
Gene Name Rcc1
Organism Mus musculus (Mouse).
Sequence Length 421
Subcellular Localization Nucleus . Chromosome . Cytoplasm . Predominantly nuclear in interphase cells. Binds to mitotic chromosomes.
Protein Description 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. 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. 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. Involved in the regulation of onset of chromosome condensation in the S phase. Binds both to the nucleosomes and double-stranded DNA..
Protein Sequence MPPKRIAKRRSPPEDAIPKSKKVKVSHRSHNTEPGLVLTLGQGDVGQLGLGESVLERKKPALVPLLQDVVQAEAGGMHTVCLSQSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTEDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDAPVVKVASGNDHLVMLTNDGDLYTLGCGEQGQLGRVPELFANRGGRQGLGRLLVPRCVLLKSRGTRGRVRFQDAFCGAYFTFAISREGHVYGFGLSNYHQLGTPGTGSCFIPQNLTSFKNSTKSWVGFSGGQHHTVCMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPVVSSVACGASVGYAVSKDGRVFAWGMGTNYQLGTGQDEDAWSPVEMTGKQLENRVVLTVSSGGQHTVLLVKDQAQS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Methylation------MPPKRIAKR
------CCHHHHCCC
43.0220668449
11PhosphorylationKRIAKRRSPPEDAIP
HHHCCCCCCCHHCCC
49.1726824392
29PhosphorylationKVKVSHRSHNTEPGL
CEEEECCCCCCCCCE
18.7022705319
32PhosphorylationVSHRSHNTEPGLVLT
EECCCCCCCCCEEEE
37.8322705319
103PhosphorylationEGALGRDTSVEGSEM
CCCCCCCCCCCCCCC
33.0528066266
104PhosphorylationGALGRDTSVEGSEMV
CCCCCCCCCCCCCCC
23.5928066266
214MethylationVPELFANRGGRQGLG
CCHHHCCCCCCCCCH
45.5830989211
403PhosphorylationLENRVVLTVSSGGQH
ECCEEEEEEECCCEE
13.5119854140
411PhosphorylationVSSGGQHTVLLVKDQ
EECCCEEEEEEEECC
12.6419854140

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of RCC1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RCC1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RCC1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RED2_HUMANADARB2physical
26496610
DECR_HUMANDECR1physical
26496610
FLII_HUMANFLIIphysical
26496610
H33_HUMANH3F3Aphysical
26496610
IMB1_HUMANKPNB1physical
26496610
IMA1_HUMANKPNA2physical
26496610
IMA4_HUMANKPNA3physical
26496610
IMA3_HUMANKPNA4physical
26496610
AFF1_HUMANAFF1physical
26496610
NEUR1_HUMANNEU1physical
26496610
NUP88_HUMANNUP88physical
26496610
NUP98_HUMANNUP98physical
26496610
RAD51_HUMANRAD51physical
26496610
RAN_HUMANRANphysical
26496610
RANG_HUMANRANBP1physical
26496610
RBP2_HUMANRANBP2physical
26496610
RAGP1_HUMANRANGAP1physical
26496610
KDM5A_HUMANKDM5Aphysical
26496610
RS2_HUMANRPS2physical
26496610
SUMO2_HUMANSUMO2physical
26496610
TBB2A_HUMANTUBB2Aphysical
26496610
UBC9_HUMANUBE2Iphysical
26496610
SUMO1_HUMANSUMO1physical
26496610
XPO1_HUMANXPO1physical
26496610
R113A_HUMANRNF113Aphysical
26496610
NU214_HUMANNUP214physical
26496610
AAAS_HUMANAAASphysical
26496610
H31_HUMANHIST1H3Aphysical
26496610
RAE1L_HUMANRAE1physical
26496610
GEMI2_HUMANGEMIN2physical
26496610
RB11A_HUMANRAB11Aphysical
26496610
WDR46_HUMANWDR46physical
26496610
NU155_HUMANNUP155physical
26496610
NUP93_HUMANNUP93physical
26496610
P121A_HUMANPOM121physical
26496610
NU153_HUMANNUP153physical
26496610
NXF1_HUMANNXF1physical
26496610
NUP50_HUMANNUP50physical
26496610
HPS5_HUMANHPS5physical
26496610
NU205_HUMANNUP205physical
26496610
PO210_HUMANNUP210physical
26496610
NU160_HUMANNUP160physical
26496610
NU188_HUMANNUP188physical
26496610
CHM2B_HUMANCHMP2Bphysical
26496610
NTM1A_HUMANNTMT1physical
26496610
FXL19_HUMANFBXL19physical
26496610
SAMD9_HUMANSAMD9physical
26496610
TM214_HUMANTMEM214physical
26496610
NDC1_HUMANNDC1physical
26496610
NU107_HUMANNUP107physical
26496610
GPAT1_HUMANGPAMphysical
26496610
GATD1_HUMANGATAD1physical
26496610
NUP85_HUMANNUP85physical
26496610
SEH1_HUMANSEH1Lphysical
26496610
TM209_HUMANTMEM209physical
26496610
IMP4_HUMANIMP4physical
26496610
NUP53_HUMANNUP35physical
26496610
CDCA2_HUMANCDCA2physical
26496610
R3HC1_HUMANR3HCC1physical
26496610
F177A_HUMANFAM177A1physical
26496610
NUP43_HUMANNUP43physical
26496610
RGPD8_HUMANRGPD8physical
26496610
RAN_MOUSERanphysical
26304119

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RCC1_MOUSE

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"NRMT is an alpha-N-methyltransferase that methylates RCC1 andretinoblastoma 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).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT PRO-2.
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.

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