CKS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CKS2_HUMAN
• UniProt AC: P33552
• Protein Name: Cyclin-dependent kinases regulatory subunit 2
• Gene Name: CKS2
• Organism: Homo sapiens (Human).
• Sequence Length: 79
• Protein Description: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function..
• Protein Sequence: MAHKQIYYSDKYFDEHYEYRHVMLPRELSKQVPKTHLMSEEEWRRLGVQQSLGWVHYMIHEPEPHILLFRRPLPKDQQK

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
4	Acetylation	----MAHKQIYYSDK ----CCCCCEECCCC	28.93	19608861
4	Ubiquitination	----MAHKQIYYSDK ----CCCCCEECCCC	28.93	23000965
7	Phosphorylation	-MAHKQIYYSDKYFD -CCCCCEECCCCCCH	8.40	22817900
8	Phosphorylation	MAHKQIYYSDKYFDE CCCCCEECCCCCCHH	16.42	29978859
9	Phosphorylation	AHKQIYYSDKYFDEH CCCCEECCCCCCHHH	15.62	28152594
11	Ubiquitination	KQIYYSDKYFDEHYE CCEECCCCCCHHHCC	41.71	22817900
12	Phosphorylation	QIYYSDKYFDEHYEY CEECCCCCCHHHCCC	22.66	28152594
17	Phosphorylation	DKYFDEHYEYRHVML CCCCHHHCCCCCEEC	16.77	28796482
19	Phosphorylation	YFDEHYEYRHVMLPR CCHHHCCCCCEECCH	10.00	28796482
30	Ubiquitination	MLPRELSKQVPKTHL ECCHHHHHCCCCCCC	68.86	27667366
34	Ubiquitination	ELSKQVPKTHLMSEE HHHHCCCCCCCCCHH	50.12	29967540
39	Phosphorylation	VPKTHLMSEEEWRRL CCCCCCCCHHHHHHH	48.49	-
51	Phosphorylation	RRLGVQQSLGWVHYM HHHHHHHHHCCEEEE	16.26	27422710
57	Phosphorylation	QSLGWVHYMIHEPEP HHHCCEEEEECCCCC	6.53	28634298
75	Ubiquitination	LFRRPLPKDQQK--- EEECCCCHHHCC---	75.70	27667366
79	Ubiquitination	PLPKDQQK------- CCCHHHCC-------	57.59	24816145

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

Oops, there are no upstream regulatory protein records of CKS2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CKS2_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 CKS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
T22D4_HUMAN	TSC22D4	physical	16189514
EF1A1_HUMAN	EEF1A1	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
CKS2_HUMAN	CKS2	physical	8211159
SSBP_HUMAN	SSBP1	physical	19786724
GRB2_HUMAN	GRB2	physical	21988832
VTNC_HUMAN	VTN	physical	21988832
LDHB_HUMAN	LDHB	physical	19786724
CDC37_HUMAN	CDC37	physical	19786724
HS90A_HUMAN	HSP90AA1	physical	19786724
CCNB2_HUMAN	CCNB2	physical	19786724
CCNB1_HUMAN	CCNB1	physical	19786724
CCNA1_HUMAN	CCNA1	physical	19786724
CDK2_HUMAN	CDK2	physical	19786724
CDK1_HUMAN	CDK1	physical	19786724
CDK1_HUMAN	CDK1	physical	26344197
COF1_HUMAN	CFL1	physical	26344197
DUT_HUMAN	DUT	physical	26344197
GO45_HUMAN	BLZF1	physical	21516116
CDK1_HUMAN	CDK1	physical	28514442
CCNA2_HUMAN	CCNA2	physical	28514442
CDK2_HUMAN	CDK2	physical	28514442
CCNB2_HUMAN	CCNB2	physical	28514442
CCNB1_HUMAN	CCNB1	physical	28514442
GEMI_HUMAN	GMNN	physical	28514442
CDN1B_HUMAN	CDKN1B	physical	28514442
CDT1_HUMAN	CDT1	physical	28514442
PMYT1_HUMAN	PKMYT1	physical	28514442
CCNE1_HUMAN	CCNE1	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

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND MASS SPECTROMETRY.
PubMed: 19608861