CCNG1_HUMAN - dbPTM
CCNG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCNG1_HUMAN
UniProt AC P51959
Protein Name Cyclin-G1
Gene Name CCNG1
Organism Homo sapiens (Human).
Sequence Length 295
Subcellular Localization Nucleus . DNA replication foci after DNA damage.
Protein Description May play a role in growth regulation. Is associated with G2/M phase arrest in response to DNA damage. May be an intermediate by which p53 mediates its role as an inhibitor of cellular proliferation (By similarity)..
Protein Sequence MIEVLTTTDSQKLLHQLNALLEQESRCQPKVCGLRLIESAHDNGLRMTARLRDFEVKDLLSLTQFFGFDTETFSLAVNLLDRFLSKMKVQPKHLGCVGLSCFYLAVKSIEEERNVPLATDLIRISQYRFTVSDLMRMEKIVLEKVCWKVKATTAFQFLQLYYSLLQENLPLERRNSINFERLEAQLKACHCRIIFSKAKPSVLALSIIALEIQAQKCVELTEGIECLQKHSKINGRDLTFWQELVSKCLTEYSSNKCSKPNVQKLKWIVSGRTARQLKHSYYRITHLPTIPEMVP
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
12AcetylationLTTTDSQKLLHQLNA
EECCCHHHHHHHHHH
57.907676423
25PhosphorylationNALLEQESRCQPKVC
HHHHHHHHCCCCCCC
37.74-
30UbiquitinationQESRCQPKVCGLRLI
HHHCCCCCCCCEEHH
25.03-
39PhosphorylationCGLRLIESAHDNGLR
CCEEHHHHHCCCCCE
24.74-
48PhosphorylationHDNGLRMTARLRDFE
CCCCCEEEEECCCCC
11.37-
53UbiquitinationRMTARLRDFEVKDLL
EEEEECCCCCHHHHH
48.96-
132PhosphorylationSQYRFTVSDLMRMEK
HHCEEEHHHHHHHHH
23.2024719451
187UbiquitinationERLEAQLKACHCRII
HHHHHHHHHHCHHHE
36.57-
196PhosphorylationCHCRIIFSKAKPSVL
HCHHHECCCCCHHHH
22.6924719451
247UbiquitinationFWQELVSKCLTEYSS
HHHHHHHHHHHHHHC
26.28-

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 CCNG1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCNG1_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 CCNG1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
12556559
MDM2_HUMANMDM2physical
12556559
CDN2A_HUMANCDKN2Aphysical
12556559
ARF_HUMANCDKN2Aphysical
12556559
P53_HUMANTP53physical
12642871
P73_HUMANTP73physical
12642871
CDK2_HUMANCDK2physical
18632610
A4_HUMANAPPphysical
21832049
TNIP1_HUMANTNIP1physical
21988832
SHKB1_HUMANSHKBP1physical
21988832
GRN_HUMANGRNphysical
21988832
LTBP3_HUMANLTBP3physical
21988832
NFAC4_HUMANNFATC4physical
21988832
AP2C_HUMANTFAP2Cphysical
21988832
PKHA4_HUMANPLEKHA4physical
21988832
PNMA1_HUMANPNMA1physical
25416956
TNIP1_HUMANTNIP1physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
TFP11_HUMANTFIP11physical
25416956
PAK5_HUMANPAK7physical
25416956
HMBX1_HUMANHMBOX1physical
25416956
LZTS2_HUMANLZTS2physical
25416956
K1C40_HUMANKRT40physical
25416956
SPERT_HUMANSPERTphysical
25416956
KR107_HUMANKRTAP10-7physical
25416956
ZZEF1_HUMANZZEF1physical
26186194
CUL4B_HUMANCUL4Bphysical
26186194
CUL4A_HUMANCUL4Aphysical
26186194
HECD3_HUMANHECTD3physical
26186194
2A5D_HUMANPPP2R5Dphysical
26186194
2A5E_HUMANPPP2R5Ephysical
26186194
2A5G_HUMANPPP2R5Cphysical
26186194
LAR1B_HUMANLARP1Bphysical
26186194
2A5D_HUMANPPP2R5Dphysical
28514442
2A5E_HUMANPPP2R5Ephysical
28514442
ZZEF1_HUMANZZEF1physical
28514442
CUL4A_HUMANCUL4Aphysical
28514442
CUL4B_HUMANCUL4Bphysical
28514442
2A5G_HUMANPPP2R5Cphysical
28514442
DDB1_HUMANDDB1physical
28514442
UBR4_HUMANUBR4physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CCNG1_HUMAN

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Related Literatures of Post-Translational Modification

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