CABL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CABL2_HUMAN
• UniProt AC: Q9BTV7
• Protein Name: CDK5 and ABL1 enzyme substrate 2
• Gene Name: CABLES2
• Organism: Homo sapiens (Human).
• Sequence Length: 478
• Protein Description: Unknown. Probably involved in G1-S cell cycle transition..
• Protein Sequence: MAAAAAGGAPGPAPGPAGPPPPAAPTSAARAPPQALRRRGDSRRRQAALFFLNNISLDGRPPSLGPGGEKPPPPPAEAREPPAPPPPEPPTGLPARTPAPQGLLSPTQVPTGLGLDGQRQRKRVTSQRCSLEFLEDAVGCAPAQRTKHTSGSPRHKGLKKTHFIKNMRQYDTRNSRIVLICAKRSLCAAFSVLPYGEGLRISDLRVDSQKQRHPSGGVSVSSEMVFELEGVELGADGKVVSYAKFLYPTNALVTHKSDSHGLLPTPRPSVPRTLPGSRHKPAPTKSAPASTELGSDVGDTLEYNPNLLDDPQWPCGKHKRVLIFASYMTTVIEYVKPSDLKKDMNETFREKFPHVKLTLSKIRSLKREMRSLSEECSLEPVTVAMAYVYFEKLVLQGKLSKQNRKLCAGACVLLAAKISSDLRKSGVTQLIDKLEERFRFNRRDLIGFEFTVLVALELALYLPENQVLPHYRRLTQQF

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
56	Phosphorylation	LFFLNNISLDGRPPS HHHHHCCCCCCCCCC	23.64	28348404
97	Phosphorylation	PTGLPARTPAPQGLL CCCCCCCCCCCCCCC	26.38	30266825
105	Phosphorylation	PAPQGLLSPTQVPTG CCCCCCCCCCCCCCC	30.83	30266825
107	Phosphorylation	PQGLLSPTQVPTGLG CCCCCCCCCCCCCCC	38.53	30266825
111	Phosphorylation	LSPTQVPTGLGLDGQ CCCCCCCCCCCCCCH	46.30	30266825
125	Phosphorylation	QRQRKRVTSQRCSLE HHHHHCHHHCHHCHH	24.15	23312004
126	Phosphorylation	RQRKRVTSQRCSLEF HHHHCHHHCHHCHHH	16.87	30624053
130	Phosphorylation	RVTSQRCSLEFLEDA CHHHCHHCHHHHHHH	32.87	22617229
149	Phosphorylation	PAQRTKHTSGSPRHK CCCCCCCCCCCCCCC	36.02	29514088
150	Phosphorylation	AQRTKHTSGSPRHKG CCCCCCCCCCCCCCC	36.67	18691976
152	Phosphorylation	RTKHTSGSPRHKGLK CCCCCCCCCCCCCCC	20.66	29514088
170	Phosphorylation	FIKNMRQYDTRNSRI HHHHHHHHCCCCCEE	14.66	22210691
172	Phosphorylation	KNMRQYDTRNSRIVL HHHHHHCCCCCEEEE	27.15	22210691
202	Phosphorylation	YGEGLRISDLRVDSQ CCCCCCHHHEEECCC	24.94	24719451
208	Phosphorylation	ISDLRVDSQKQRHPS HHHEEECCCCCCCCC	36.10	28102081
257	Phosphorylation	NALVTHKSDSHGLLP CEEEEECCCCCCCCC	36.42	30266825
259	Phosphorylation	LVTHKSDSHGLLPTP EEEECCCCCCCCCCC	26.92	30266825
265	Phosphorylation	DSHGLLPTPRPSVPR CCCCCCCCCCCCCCC	31.72	23312004
269	Phosphorylation	LLPTPRPSVPRTLPG CCCCCCCCCCCCCCC	46.14	23312004
327	Phosphorylation	RVLIFASYMTTVIEY EEEEEEEEEHHHHHH	8.61	-
334	Phosphorylation	YMTTVIEYVKPSDLK EEHHHHHHCCHHHHH	11.58	-
361	Ubiquitination	HVKLTLSKIRSLKRE CHHHHHHHHHHHHHH	45.30	-
425	Phosphorylation	ISSDLRKSGVTQLID HCHHHHHCCHHHHHH	31.87	25627689
428	Phosphorylation	DLRKSGVTQLIDKLE HHHHCCHHHHHHHHH	22.60	25627689
475	O-linked_Glycosylation	LPHYRRLTQQF---- CHHHHHHHHCC----	20.65	29351928

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

Oops, there are no upstream regulatory protein records of CABL2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CABL2_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 CABL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK3_HUMAN	CDK3	physical	11955625
CDK5_HUMAN	CDK5	physical	11955625
ABL1_HUMAN	ABL1	physical	11955625

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

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-125; SER-126;SER-130 AND SER-208, AND MASS SPECTROMETRY.
PubMed: 19369195

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-130 ANDSER-208, AND MASS SPECTROMETRY.
PubMed: 18691976