ABRAL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ABRAL_HUMAN
• UniProt AC: Q9P1F3
• Protein Name: Costars family protein ABRACL
• Gene Name: ABRACL
• Organism: Homo sapiens (Human).
• Sequence Length: 81
• Protein Sequence: MNVDHEVNLLVEEIHRLGSKNADGKLSVKFGVLFRDDKCANLFEALVGTLKAAKRRKIVTYPGELLLQGVHDDVDIILLQD

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
1	Acetylation	-------MNVDHEVN -------CCCHHHHH	11.28	25944712
20	Acetylation	EIHRLGSKNADGKLS HHHHHCCCCCCCCEE	55.12	23749302
20	Ubiquitination	EIHRLGSKNADGKLS HHHHHCCCCCCCCEE	55.12	27667366
25	Ubiquitination	GSKNADGKLSVKFGV CCCCCCCCEEEEEEE	37.83	29967540
25	Acetylation	GSKNADGKLSVKFGV CCCCCCCCEEEEEEE	37.83	25953088
38	Ubiquitination	GVLFRDDKCANLFEA EEEECCHHHHHHHHH	39.26	29967540
39	S-nitrosocysteine	VLFRDDKCANLFEAL EEECCHHHHHHHHHH	3.79	-
51	Ubiquitination	EALVGTLKAAKRRKI HHHHHHHHHHHHCCE	46.25	-
51	Acetylation	EALVGTLKAAKRRKI HHHHHHHHHHHHCCE	46.25	25953088

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ABRAL_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 ABRAL_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ABRAL_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.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330