CCPG1_HUMAN - dbPTM
CCPG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCPG1_HUMAN
UniProt AC Q9ULG6
Protein Name Cell cycle progression protein 1
Gene Name CCPG1
Organism Homo sapiens (Human).
Sequence Length 757
Subcellular Localization Cytoplasmic granule membrane
Single-pass type II membrane protein.
Protein Description Acts as an assembly platform for Rho protein signaling complexes. Limits guanine nucleotide exchange activity of MCF2L toward RHOA, which results in an inhibition of both its transcriptional activation ability and its transforming activity. Does not inhibit activity of MCF2L toward CDC42, or activity of MCF2 toward either RHOA or CDC42 (By similarity). May be involved in cell cycle regulation..
Protein Sequence MSENSSDSDSSCGWTVISHEGSDIEMLNSVTPTDSCEPAPECSSLEQEELQALQIEQGESSQNGTVLMEETAYPALEETSSTIEAEEQKIPEDSIYIGTASDDSDIVTLEPPKLEEIGNQEVVIVEEAQSSEDFNMGSSSSSQYTFCQPETVFSSQPSDDESSSDETSNQPSPAFRRRRARKKTVSASESEDRLVAEQETEPSKELSKRQFSSGLNKCVILALVIAISMGFGHFYGTIQIQKRQQLVRKIHEDELNDMKDYLSQCQQEQESFIDYKSLKENLARCWTLTEAEKMSFETQKTNLATENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDKGTSTELVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLVTTALRGELQQLSGSQLHGKSDSPNVYTEKKEIAILRERLTELERKLTFEQQRSDLWERLYVEAKDQNGKQGTDGKKKGGRGSHRAKNKSKETFLGSVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKGNKRFGATKEAAEKPRTVFSDYLHPQYKAPTENHHNRGPTMQNDGRKEKPVHFKEFRKNTNSKKCSPGHDCRENSHSFRKACSGVFDCAQQESMSLFNTVVNPIRMDEFRQIIQRYMLKELDTFCHWNELDQFINKFFLNGVFIHDQKLFTDFVNDVKDYLRNMKEYEVDNDGVFEKLDEYIYRHFFGHTFSPPYGPRSVYIKPCHYSSL
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
99PhosphorylationEDSIYIGTASDDSDI
CCCEEEEECCCCCCC
17.2722817900
101PhosphorylationSIYIGTASDDSDIVT
CEEEEECCCCCCCEE
41.6122817900
104PhosphorylationIGTASDDSDIVTLEP
EEECCCCCCCEEECC
33.9422817900
156 (in isoform 2)Ubiquitination-40.08-
158PhosphorylationTVFSSQPSDDESSSD
EEECCCCCCCCCCCC
50.4824275569
162PhosphorylationSQPSDDESSSDETSN
CCCCCCCCCCCCCCC
41.9824275569
167PhosphorylationDESSSDETSNQPSPA
CCCCCCCCCCCCCHH
37.6624275569
172PhosphorylationDETSNQPSPAFRRRR
CCCCCCCCHHHHHHH
21.0624719451
184PhosphorylationRRRARKKTVSASESE
HHHHHCCCCCCCHHH
23.8025159151
186 (in isoform 5)Phosphorylation-31.1724719451
186PhosphorylationRARKKTVSASESEDR
HHHCCCCCCCHHHHH
31.1729255136
188PhosphorylationRKKTVSASESEDRLV
HCCCCCCCHHHHHHH
33.8629255136
188 (in isoform 5)Phosphorylation-33.8627251275
190PhosphorylationKTVSASESEDRLVAE
CCCCCCHHHHHHHHC
42.1525159151
190 (in isoform 5)Phosphorylation-42.1524719451
200PhosphorylationRLVAEQETEPSKELS
HHHHCCCCCCCHHHH
53.5423403867
203PhosphorylationAEQETEPSKELSKRQ
HCCCCCCCHHHHHHH
32.3123403867
204UbiquitinationEQETEPSKELSKRQF
CCCCCCCHHHHHHHH
73.68-
208UbiquitinationEPSKELSKRQFSSGL
CCCHHHHHHHHCCHH
63.94-
249UbiquitinationKRQQLVRKIHEDELN
HHHHHHHHHCHHHHH
40.72-
259UbiquitinationEDELNDMKDYLSQCQ
HHHHHHHHHHHHHHH
46.19-
276UbiquitinationQESFIDYKSLKENLA
HHHCCCHHHHHHHHH
45.63-
279UbiquitinationFIDYKSLKENLARCW
CCCHHHHHHHHHHHH
52.20-
287PhosphorylationENLARCWTLTEAEKM
HHHHHHHHHHHHHHC
27.6826546556
295PhosphorylationLTEAEKMSFETQKTN
HHHHHHCCHHHCCCC
30.88-
300UbiquitinationKMSFETQKTNLATEN
HCCHHHCCCCCCCCC
46.96-
301PhosphorylationMSFETQKTNLATENQ
CCHHHCCCCCCCCCC
26.16-
305PhosphorylationTQKTNLATENQYLRV
HCCCCCCCCCCEEEE
38.3425159151
309PhosphorylationNLATENQYLRVSLEK
CCCCCCCEEEEEHHH
14.20-
316UbiquitinationYLRVSLEKEEKALSS
EEEEEHHHHHHHHHH
76.18-
319UbiquitinationVSLEKEEKALSSLQE
EEHHHHHHHHHHHHH
56.57-
322 (in isoform 3)Ubiquitination-33.5821906983
322PhosphorylationEKEEKALSSLQEELN
HHHHHHHHHHHHHHH
33.58-
323PhosphorylationKEEKALSSLQEELNK
HHHHHHHHHHHHHHH
34.62-
330UbiquitinationSLQEELNKLREQIRI
HHHHHHHHHHHHHHH
62.64-
338 (in isoform 2)Ubiquitination-5.1021906983
341UbiquitinationQIRILEDKGTSTELV
HHHHHHCCCCCHHHH
55.50-
359 (in isoform 3)Phosphorylation-63.0822468782
362 (in isoform 3)Phosphorylation-71.3622468782
365UbiquitinationLEEEKQKKHSFLSQR
HHHHHHHHHHHHHHH
41.82-
386 (in isoform 2)Ubiquitination-9.7421906983
393 (in isoform 2)Ubiquitination-15.7921906983
393PhosphorylationLERERLVTTALRGEL
HHHHHHHHHHHHHHH
15.79-
404PhosphorylationRGELQQLSGSQLHGK
HHHHHHHCCCCCCCC
31.8722210691
411UbiquitinationSGSQLHGKSDSPNVY
CCCCCCCCCCCCCCC
40.10-
414PhosphorylationQLHGKSDSPNVYTEK
CCCCCCCCCCCCCCH
26.0122210691
418PhosphorylationKSDSPNVYTEKKEIA
CCCCCCCCCCHHHHH
18.8022210691
421UbiquitinationSPNVYTEKKEIAILR
CCCCCCCHHHHHHHH
48.16-
424 (in isoform 3)Phosphorylation-3.87-
437UbiquitinationRLTELERKLTFEQQR
HHHHHHHHHCHHHHH
42.37-
456UbiquitinationERLYVEAKDQNGKQG
HHHHHHECCCCCCCC
46.47-
482 (in isoform 1)Ubiquitination-63.4821906983
482 (in isoform 4)Ubiquitination-63.4821906983
482UbiquitinationHRAKNKSKETFLGSV
HHCCCCCCCCHHHHH
63.4821906983
490UbiquitinationETFLGSVKETFDAMK
CCHHHHHHHHHHHHH
53.38-
499PhosphorylationTFDAMKNSTKEFVRH
HHHHHHHHHHHHHHH
35.02-
501UbiquitinationDAMKNSTKEFVRHHK
HHHHHHHHHHHHHHH
49.31-
508UbiquitinationKEFVRHHKEKIKQAK
HHHHHHHHHHHHHHH
55.36-
519UbiquitinationKQAKEAVKENLKKFS
HHHHHHHHHHHHHHH
48.18-
524UbiquitinationAVKENLKKFSDSVKS
HHHHHHHHHHHHHHH
53.95-
530 (in isoform 1)Ubiquitination-47.9721906983
530 (in isoform 4)Ubiquitination-47.9721906983
530UbiquitinationKKFSDSVKSTFRHFK
HHHHHHHHHHHHHCH
47.9721906983
537 (in isoform 1)Ubiquitination-48.3021906983
537UbiquitinationKSTFRHFKDTTKNIF
HHHHHHCHHHHCCCC
48.3021906983
537 (in isoform 4)Ubiquitination-48.3021906983
541UbiquitinationRHFKDTTKNIFDEKG
HHCHHHHCCCCCCCC
50.57-
547UbiquitinationTKNIFDEKGNKRFGA
HCCCCCCCCCCCCCC
70.41-
556UbiquitinationNKRFGATKEAAEKPR
CCCCCCCHHHHHCCC
44.84-
561 (in isoform 2)Ubiquitination-34.7621906983
569PhosphorylationPRTVFSDYLHPQYKA
CCEECHHCCCCCCCC
13.00-
596UbiquitinationQNDGRKEKPVHFKEF
CCCCCCCCCCCHHHH
56.21-
705 (in isoform 1)Ubiquitination-43.4421906983
705UbiquitinationTDFVNDVKDYLRNMK
HHHHHHHHHHHHHCH
43.442190698
712UbiquitinationKDYLRNMKEYEVDND
HHHHHHCHHCEECCC
61.77-
742 (in isoform 5)Phosphorylation-43.0522468782
745 (in isoform 5)Phosphorylation-34.1022468782
807 (in isoform 5)Phosphorylation--

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 CCPG1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCPG1_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 CCPG1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CCPG1_HUMAN !!

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 CCPG1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-99; SER-101 AND SER-104,AND MASS SPECTROMETRY.

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