LIN52_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LIN52_HUMAN
• UniProt AC: Q52LA3
• Protein Name: Protein lin-52 homolog
• Gene Name: LIN52
• Organism: Homo sapiens (Human).
• Sequence Length: 116
• Protein Sequence: MGWKMASPTDGTDLEASLLSFEKLDRASPDLWPEQLPGVAEFAASFKSPITSSPPKWMAEIERDDIDMLKELGSLTTANLMEKVRGLQNLAYQLGLDESREMTRGKFLNILEKPKK

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
7	Phosphorylation	-MGWKMASPTDGTDL -CCCCCCCCCCCCCH	25.49	23663014
9	Phosphorylation	GWKMASPTDGTDLEA CCCCCCCCCCCCHHH	44.56	23663014
12	Phosphorylation	MASPTDGTDLEASLL CCCCCCCCCHHHHHH	39.97	23663014
17	Phosphorylation	DGTDLEASLLSFEKL CCCCHHHHHHHHHHH	22.07	23663014
20	Phosphorylation	DLEASLLSFEKLDRA CHHHHHHHHHHHHCC	36.33	21955146
28	Phosphorylation	FEKLDRASPDLWPEQ HHHHHCCCCCCCHHH	21.60	26846344
45	Phosphorylation	GVAEFAASFKSPITS CHHHHHHHCCCCCCC	29.76	22199227
48	Phosphorylation	EFAASFKSPITSSPP HHHHHCCCCCCCCCC	21.37	25159151
51	Phosphorylation	ASFKSPITSSPPKWM HHCCCCCCCCCCCHH	26.91	21955146
52	Phosphorylation	SFKSPITSSPPKWMA HCCCCCCCCCCCHHH	41.38	25159151
53	Phosphorylation	FKSPITSSPPKWMAE CCCCCCCCCCCHHHH	36.25	23401153
92	Phosphorylation	RGLQNLAYQLGLDES HHHHHHHHHHCCCHH	13.87	30257219
103	Phosphorylation	LDESREMTRGKFLNI CCHHHHHHCCCHHHH	31.36	30257219
106	Acetylation	SREMTRGKFLNILEK HHHHHCCCHHHHHHC	43.30	25953088
113	Acetylation	KFLNILEKPKK---- CHHHHHHCCCC----	59.71	25953088

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
28	S	Phosphorylation	Kinase	DYRK1A	Q13627	PSP
28	S	Phosphorylation	Kinase	DYRK1B	Q9Y463	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LIN52_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 LIN52_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LIN9_HUMAN	LIN9	physical	17531812
LIN54_HUMAN	LIN54	physical	17531812
MYBB_HUMAN	MYBL2	physical	17531812
LIN37_HUMAN	LIN37	physical	17531812
LIN9_HUMAN	LIN9	physical	17671431
LIN37_HUMAN	LIN37	physical	17671431
LIN54_HUMAN	LIN54	physical	17671431
MYBB_HUMAN	MYBL2	physical	17671431
RBBP4_HUMAN	RBBP4	physical	17671431

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

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND MASSSPECTROMETRY.
PubMed: 19413330

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASSSPECTROMETRY.
PubMed: 17081983