RCC1_HUMAN - dbPTM
RCC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RCC1_HUMAN
UniProt AC P18754
Protein Name Regulator of chromosome condensation
Gene Name RCC1
Organism Homo sapiens (Human).
Sequence Length 421
Subcellular Localization Nucleus . Chromosome . Cytoplasm . Predominantly nuclear in interphase cells (PubMed:12194828). Binds to mitotic chromosomes (PubMed:12194828, PubMed:17435751, PubMed:20668449).
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. [PubMed: 1944575]
Protein Sequence MSPKRIAKRRSPPADAIPKSKKVKVSHRSHSTEPGLVLTLGQGDVGQLGLGENVMERKKPALVSIPEDVVQAEAGGMHTVCLSKSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTDDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASGNDHLVMLTADGDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHVRFQDAFCGAYFTFAISHEGHVYGFGLSNYHQLGTPGTESCFIPQNLTSFKNSTKSWVGFSGGQHHTVCMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPAVSSVACGASVGYAVTKDGRVFAWGMGTNYQLGTGQDEDAWSPVEMMGKQLENRVVLSVSSGGQHTVLLVKDKEQS
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
2"N,N,N-trimethylserine"------MSPKRIAKR
------CCHHHHHCC		38.85-
2Phosphorylation------MSPKRIAKR
------CCHHHHHCC		38.8518568422
2Methylation------MSPKRIAKR
------CCHHHHHCC		38.8518762580
11PhosphorylationKRIAKRRSPPADAIP
HHHHCCCCCCHHCCC		38.9929255136
11 (in isoform 2)Phosphorylation-38.9925849741
20PhosphorylationPADAIPKSKKVKVSH
CHHCCCCCCCEEEEC		32.1418568422
26PhosphorylationKSKKVKVSHRSHSTE
CCCCEEEECCCCCCC		13.8918568422
29PhosphorylationKVKVSHRSHSTEPGL
CEEEECCCCCCCCCE		19.1618568422
31PhosphorylationKVSHRSHSTEPGLVL
EEECCCCCCCCCEEE		35.3930624053
32PhosphorylationVSHRSHSTEPGLVLT
EECCCCCCCCCEEEE		40.5518568422
39PhosphorylationTEPGLVLTLGQGDVG
CCCCEEEEECCCCHH		22.7428450419
47 (in isoform 2)Phosphorylation-32.0025159151
60 (in isoform 2)Phosphorylation-33.5825159151
79PhosphorylationAEAGGMHTVCLSKSG
HHCCCCEEEEECCCC		12.2025022875
81GlutathionylationAGGMHTVCLSKSGQV
CCCCEEEEECCCCCE		3.5922555962
83PhosphorylationGMHTVCLSKSGQVYS
CCEEEEECCCCCEEE		21.4626126808
85PhosphorylationHTVCLSKSGQVYSFG
EEEEECCCCCEEEEE		30.9528152594
89PhosphorylationLSKSGQVYSFGCNDE
ECCCCCEEEEECCCC		7.1528152594
90PhosphorylationSKSGQVYSFGCNDEG
CCCCCEEEEECCCCC		19.1228152594
93GlutathionylationGQVYSFGCNDEGALG
CCEEEEECCCCCCCC		5.6722555962
103PhosphorylationEGALGRDTSVEGSEM
CCCCCCCCCCCCCCC		33.0520873877
104PhosphorylationGALGRDTSVEGSEMV
CCCCCCCCCCCCCCC		23.5920873877
108PhosphorylationRDTSVEGSEMVPGKV
CCCCCCCCCCCCCEE		14.7125627689
110SulfoxidationTSVEGSEMVPGKVEL
CCCCCCCCCCCEEEE		4.7621406390
114SumoylationGSEMVPGKVELQEKV
CCCCCCCEEEEEEEE		26.85-
114AcetylationGSEMVPGKVELQEKV
CCCCCCCEEEEEEEE		26.8526051181
114UbiquitinationGSEMVPGKVELQEKV
CCCCCCCEEEEEEEE		26.8521906983
114SumoylationGSEMVPGKVELQEKV
CCCCCCCEEEEEEEE		26.85-
120AcetylationGKVELQEKVVQVSAG
CEEEEEEEEEEECCC		34.4426051181
120UbiquitinationGKVELQEKVVQVSAG
CEEEEEEEEEEECCC		34.44-
131PhosphorylationVSAGDSHTAALTDDG
ECCCCCCEEEECCCC		19.9923911959
135PhosphorylationDSHTAALTDDGRVFL
CCCEEEECCCCEEEE		27.58-
145O-linked_GlycosylationGRVFLWGSFRDNNGV
CEEEEEEEECCCCCE		12.9128510447
145 (in isoform 2)Ubiquitination-12.91-
151UbiquitinationGSFRDNNGVIGLLEP
EEECCCCCEEEEEEC		20.7621890473
159SulfoxidationVIGLLEPMKKSMVPV
EEEEEECCCCCCCCE		6.6121406390
160UbiquitinationIGLLEPMKKSMVPVQ
EEEEECCCCCCCCEE		53.0321906983
160AcetylationIGLLEPMKKSMVPVQ
EEEEECCCCCCCCEE		53.0325953088
161UbiquitinationGLLEPMKKSMVPVQV
EEEECCCCCCCCEEE		37.2221890473
162PhosphorylationLLEPMKKSMVPVQVQ
EEECCCCCCCCEEEE		21.3530622161
163SulfoxidationLEPMKKSMVPVQVQL
EECCCCCCCCEEEEE		5.6221406390
179PhosphorylationVPVVKVASGNDHLVM
CCEEEECCCCCEEEE		40.9126126808
188PhosphorylationNDHLVMLTADGDLYT
CCEEEEEECCCCEEE		12.4726126808
191 (in isoform 2)Ubiquitination-25.10-
192UbiquitinationVMLTADGDLYTLGCG
EEEECCCCEEEECCC		36.7321890473
192 (in isoform 2)Ubiquitination-36.73-
192UbiquitinationVMLTADGDLYTLGCG
EEEECCCCEEEECCC		36.7321890473
194PhosphorylationLTADGDLYTLGCGEQ
EECCCCEEEECCCCC		12.5026126808
195PhosphorylationTADGDLYTLGCGEQG
ECCCCEEEECCCCCC		24.7926126808
198GlutathionylationGDLYTLGCGEQGQLG
CCEEEECCCCCCCCC		6.4522555962
214MethylationVPELFANRGGRQGLE
CCHHHCCCCCCHHHH		45.5830989213
227UbiquitinationLERLLVPKCVMLKSR
HHHHHCCEEEEECCC		31.79-
232AcetylationVPKCVMLKSRGSRGH
CCEEEEECCCCCCCC		21.7325953088
232UbiquitinationVPKCVMLKSRGSRGH
CCEEEEECCCCCCCC		21.73-
258 (in isoform 2)Ubiquitination-44.17-
263 (in isoform 2)Ubiquitination-14.73-
274PhosphorylationSNYHQLGTPGTESCF
CCCCCCCCCCCCCCC		27.4318568422
306PhosphorylationFSGGQHHTVCMDSEG
ECCCCEEEEEECCCC		17.18-
311PhosphorylationHHTVCMDSEGKAYSL
EEEEEECCCCCEEEE		22.74-
314AcetylationVCMDSEGKAYSLGRA
EEECCCCCEEEECCC		39.8526051181
317PhosphorylationDSEGKAYSLGRAEYG
CCCCCEEEECCCCCC		29.2521601212
335AcetylationLGEGAEEKSIPTLIS
CCCCCCCCCCCHHHH		45.2325953088
335SumoylationLGEGAEEKSIPTLIS
CCCCCCCCCCCHHHH		45.23-
335SumoylationLGEGAEEKSIPTLIS
CCCCCCCCCCCHHHH		45.23-
335UbiquitinationLGEGAEEKSIPTLIS
CCCCCCCCCCCHHHH		45.232190698
336O-linked_GlycosylationGEGAEEKSIPTLISR
CCCCCCCCCCHHHHC		36.7628510447
336PhosphorylationGEGAEEKSIPTLISR
CCCCCCCCCCHHHHC		36.7623312004
339PhosphorylationAEEKSIPTLISRLPA
CCCCCCCHHHHCCCC		34.7523312004
342PhosphorylationKSIPTLISRLPAVSS
CCCCHHHHCCCCCCC		30.7723312004
348PhosphorylationISRLPAVSSVACGAS
HHCCCCCCCCCCCCC		22.6221130716
349PhosphorylationSRLPAVSSVACGASV
HCCCCCCCCCCCCCC		13.7223312004
352GlutathionylationPAVSSVACGASVGYA
CCCCCCCCCCCCEEE		4.3622555962
355PhosphorylationSSVACGASVGYAVTK
CCCCCCCCCEEEEEC		11.0228152594
358PhosphorylationACGASVGYAVTKDGR
CCCCCCEEEEECCCC		8.8528152594
361PhosphorylationASVGYAVTKDGRVFA
CCCEEEEECCCCEEE		18.4228152594
362UbiquitinationSVGYAVTKDGRVFAW
CCEEEEECCCCEEEE		52.14-
362AcetylationSVGYAVTKDGRVFAW
CCEEEEECCCCEEEE		52.1426051181
366 (in isoform 2)Ubiquitination-4.73-
387PhosphorylationGQDEDAWSPVEMMGK
CCCCCCCCHHHHHHH		22.3118568422
393 (in isoform 2)Ubiquitination-17.16-
403PhosphorylationLENRVVLSVSSGGQH
ECCEEEEEEECCCEE		14.3520068231
405PhosphorylationNRVVLSVSSGGQHTV
CEEEEEEECCCEEEE		21.6420068231
406PhosphorylationRVVLSVSSGGQHTVL
EEEEEEECCCEEEEE		44.8016964243
411PhosphorylationVSSGGQHTVLLVKDK
EECCCEEEEEEEECC		12.6416964243
421PhosphorylationLVKDKEQS-------
EEECCCCC-------		43.1926714015
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
11SPhosphorylationKinaseCDK1P06493
PSP
274TPhosphorylationKinaseCDK1P06493
PSP
387SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RCC1_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAN_HUMANRANphysical
10811801
RAN_HUMANRANphysical
11336674
RANB3_HUMANRANBP3physical
11932251
XPO1_HUMANXPO1physical
11932251
RAN_HUMANRANphysical
7891706
IMA3_HUMANKPNA4physical
17855385
H31_HUMANHIST1H3Aphysical
20347844
H2A2C_HUMANHIST2H2ACphysical
20347844
H2B2E_HUMANHIST2H2BEphysical
20347844
RAN_HUMANRANphysical
20565941
SCG1_HUMANCHGBphysical
21900206
SPRE1_HUMANSPRED1physical
21900206
UBP4_HUMANUSP4physical
21900206
P53_HUMANTP53physical
21900206
CSAD_HUMANCSADphysical
21900206
KPYM_HUMANPKMphysical
21900206
TNR16_HUMANNGFRphysical
21900206
DC1I1_HUMANDYNC1I1physical
21900206
ODPB_HUMANPDHBphysical
21900206
GBB2_HUMANGNB2physical
21900206
CAB45_HUMANSDF4physical
21900206
RFA1_HUMANRPA1physical
21900206
FAD1_HUMANFLAD1physical
21900206
DDAH2_HUMANDDAH2physical
21900206
APLP1_HUMANAPLP1physical
21900206
U119A_HUMANUNC119physical
21900206
ECHB_HUMANHADHBphysical
21900206
ZN135_HUMANZNF135physical
21900206
WIZ_HUMANWIZphysical
21900206
TLE1_HUMANTLE1physical
21900206
KMT2B_HUMANKMT2Bphysical
21900206
TRM2A_HUMANTRMT2Aphysical
21900206
ACTB_HUMANACTBphysical
21900206
TCPH_HUMANCCT7physical
21900206
BAG6_HUMANBAG6physical
21900206
HXD8_HUMANHOXD8physical
21900206
LRIF1_HUMANLRIF1physical
21900206
FAF1_HUMANFAF1physical
21900206
TBB3_HUMANTUBB3physical
21900206
U2AF1_HUMANU2AF1physical
22939629
HMGA1_HUMANHMGA1physical
18850631
NUSAP_HUMANNUSAP1physical
26186194
RGPD3_HUMANRGPD3physical
26186194
RGPD8_HUMANRGPD8physical
26186194
RBP2_HUMANRANBP2physical
26186194
RGPD5_HUMANRGPD5physical
26186194
RAGP1_HUMANRANGAP1physical
26186194
RAN_HUMANRANphysical
26186194
IMA3_HUMANKPNA4physical
26186194
IMA4_HUMANKPNA3physical
26186194
RANG_HUMANRANBP1physical
26186194
NAV1_HUMANNAV1physical
26186194
RRP44_HUMANDIS3physical
26344197
GLYR1_HUMANGLYR1physical
26344197
RAN_HUMANRANphysical
26344197
XPO1_HUMANXPO1physical
26344197
RGPD8_HUMANRGPD8physical
28514442
RGPD5_HUMANRGPD5physical
28514442
RGPD3_HUMANRGPD3physical
28514442
DLGP5_HUMANDLGAP5physical
28514442
RANG_HUMANRANBP1physical
28514442
RAGP1_HUMANRANGAP1physical
28514442
RBP2_HUMANRANBP2physical
28514442
NAV1_HUMANNAV1physical
28514442
IMA3_HUMANKPNA4physical
28514442
IMA4_HUMANKPNA3physical
28514442
NUSAP_HUMANNUSAP1physical
28514442
IMB1_HUMANKPNB1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RCC1_HUMAN

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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, METHYLATION AT SER-2, ANDMUTAGENESIS OF LYS-4.
"Regulation of chromatin binding by a conformational switch in thetail of the Ran exchange factor RCC1.";
Hao Y., Macara I.G.;
J. Cell Biol. 182:827-836(2008).
Cited for: METHYLATION AT SER-2.
"N-terminal alpha-methylation of RCC1 is necessary for stablechromatin 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).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, SUBCELLULAR LOCATION,HISTONE-BINDING, INTERACTION WITH RAN, PHOSPHORYLATION AT SER-2,METHYLATION AT SER-2, AND MUTAGENESIS OF SER-2; PRO-3; LYS-4 ANDASP-182.
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.
"N-terminal alpha-methylation of RCC1 is necessary for stablechromatin 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).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, SUBCELLULAR LOCATION,HISTONE-BINDING, INTERACTION WITH RAN, PHOSPHORYLATION AT SER-2,METHYLATION AT SER-2, AND MUTAGENESIS OF SER-2; PRO-3; LYS-4 ANDASP-182.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-405; SER-406AND THR-411, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.

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