CCNG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CCNG2_HUMAN
• UniProt AC: Q16589
• Protein Name: Cyclin-G2
• Gene Name: CCNG2
• Organism: Homo sapiens (Human).
• Sequence Length: 344
• Subcellular Localization: Cytoplasm.
• Protein Description: May play a role in growth regulation and in negative regulation of cell cycle progression..
• Protein Sequence: MKDLGAEHLAGHEGVQLLGLLNVYLEQEERFQPREKGLSLIEATPENDNTLCPGLRNAKVEDLRSLANFFGSCTETFVLAVNILDRFLALMKVKPKHLSCIGVCSFLLAARIVEEDCNIPSTHDVIRISQCKCTASDIKRMEKIISEKLHYELEATTALNFLHLYHTIILCHTSERKEILSLDKLEAQLKACNCRLIFSKAKPSVLALCLLNLEVETLKSVELLEILLLVKKHSKINDTEFFYWRELVSKCLAEYSSPECCKPDLKKLVWIVSRRTAQNLHNSYYSVPELPTIPEGGCFDESESEDSCEDMSCGEESLSSSPPSDQECTFFFNFKVAQTLCFPS

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
36	Ubiquitination	ERFQPREKGLSLIEA HHHCCCHHCCCCEEC	67.44	-
36	Ubiquitination	ERFQPREKGLSLIEA HHHCCCHHCCCCEEC	67.44	-
134	Phosphorylation	RISQCKCTASDIKRM EEHHCCCCHHHHHHH	18.07	-
136	Phosphorylation	SQCKCTASDIKRMEK HHCCCCHHHHHHHHH	23.01	-
146	Phosphorylation	KRMEKIISEKLHYEL HHHHHHHHHHHHHHH	31.95	24719451
184	Ubiquitination	KEILSLDKLEAQLKA HHHCCHHHHHHHHHH	54.22	-
199	Phosphorylation	CNCRLIFSKAKPSVL CCCEEEECCCCHHHH	25.39	24719451
220	Phosphorylation	LEVETLKSVELLEIL CCCCCHHHHHHHHHH	24.76	22817900
234	Phosphorylation	LLLVKKHSKINDTEF HHHHHHHCCCCCCHH	44.07	22817900

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CCNG2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CCNG2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CCNG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
2A5B_HUMAN	PPP2R5B	physical	11956189
2A5G_HUMAN	PPP2R5C	physical	11956189
PP2AA_HUMAN	PPP2CA	physical	11956189
SKP1_HUMAN	SKP1	physical	18784254
SKP2_HUMAN	SKP2	physical	18784254
NRIP2_HUMAN	NRIP2	physical	21988832
F208B_HUMAN	FAM208B	physical	25416956
EFHC2_HUMAN	EFHC2	physical	25416956
2A5D_HUMAN	PPP2R5D	physical	28514442
NDKB_HUMAN	NME2	physical	28514442
2A5G_HUMAN	PPP2R5C	physical	28514442
2A5E_HUMAN	PPP2R5E	physical	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-220 AND SER-234, ANDMASS SPECTROMETRY.
PubMed: 18187866