LIMD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LIMD2_HUMAN
• UniProt AC: Q9BT23
• Protein Name: LIM domain-containing protein 2 {ECO:0000305}
• Gene Name: LIMD2 {ECO:0000312|HGNC:HGNC:28142}
• Organism: Homo sapiens (Human).
• Sequence Length: 127
• Subcellular Localization: Cytoplasm . Nucleus . Mainly found in cytoplasm, concentrated in membrane ruffles and in streaks reminiscent of focal adhesion plaques (PubMed:24590809). Also found in nucleus (PubMed:24590809).
• Protein Description: Acts as an activator of the protein-kinase ILK, thereby regulating cell motility. [PubMed: 24590809]
• Protein Sequence: MFQAAGAAQATPSHDAKGGGSSTVQRSKSFSLRAQVKETCAACQKTVYPMERLVADKLIFHNSCFCCKHCHTKLSLGSYAALHGEFYCKPHFQQLFKSKGNYDEGFGRKQHKELWAHKEVDPGTKTA

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	-------MFQAAGAA -------CCCCCCCC	5.18	19413330
11	Phosphorylation	AAGAAQATPSHDAKG CCCCCCCCCCCCCCC	17.16	26074081
13	Phosphorylation	GAAQATPSHDAKGGG CCCCCCCCCCCCCCC	29.64	26074081
17	Acetylation	ATPSHDAKGGGSSTV CCCCCCCCCCCCCCC	65.23	25953088
21	Phosphorylation	HDAKGGGSSTVQRSK CCCCCCCCCCCCCCC	26.55	26074081
22	Phosphorylation	DAKGGGSSTVQRSKS CCCCCCCCCCCCCCC	35.55	26074081
23	Phosphorylation	AKGGGSSTVQRSKSF CCCCCCCCCCCCCCC	23.50	26074081
27	Phosphorylation	GSSTVQRSKSFSLRA CCCCCCCCCCCCCHH	18.63	30266825
29	Phosphorylation	STVQRSKSFSLRAQV CCCCCCCCCCCHHHH	22.70	23401153
31	Phosphorylation	VQRSKSFSLRAQVKE CCCCCCCCCHHHHHH	24.84	30266825
45	Ubiquitination	ETCAACQKTVYPMER HHHHHHHCCCCCHHH	39.58	-
46	Phosphorylation	TCAACQKTVYPMERL HHHHHHCCCCCHHHH	10.21	28102081
48	Phosphorylation	AACQKTVYPMERLVA HHHHCCCCCHHHHHC	11.33	28102081
63	Phosphorylation	DKLIFHNSCFCCKHC CEEEECCCCEECCCC	10.45	27080861
78	Phosphorylation	HTKLSLGSYAALHGE CCEEEHHHHHHHHCE	19.52	27251275
87	Phosphorylation	AALHGEFYCKPHFQQ HHHHCEEEECHHHHH	8.68	-
98	Phosphorylation	HFQQLFKSKGNYDEG HHHHHHHCCCCCCCC	38.16	-
102	Phosphorylation	LFKSKGNYDEGFGRK HHHCCCCCCCCCCHH	24.84	28796482
118	Acetylation	HKELWAHKEVDPGTK HHHHHCCCCCCCCCC	52.25	23749302
126	Phosphorylation	EVDPGTKTA------ CCCCCCCCC------	37.12	27251275

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

Oops, there are no upstream regulatory protein records of LIMD2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LIMD2_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 LIMD2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of LIMD2_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