SELH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SELH_HUMAN
• UniProt AC: Q8IZQ5
• Protein Name: Selenoprotein H {ECO:0000305}
• Gene Name: SELENOH {ECO:0000303|PubMed:27645994, ECO:0000312|HGNC:HGNC:18251}
• Organism: Homo sapiens (Human).
• Sequence Length: 122
• Protein Description: May be involved in a redox-related process..
• Protein Sequence: MAPRGRKRKAEAAVVAVAEKREKLANGGEGMEEATVVIEHCTSURVYGRNAAALSQALRLEAPELPVKVNPTKPRRGSFEVTLLRPDGSSAELWTGIKKGPPRKLKFPEPQEVVEELKKYLS

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
20	Acetylation	AVVAVAEKREKLANG HHHHHHHHHHHHHCC	57.00	19608861
20	Ubiquitination	AVVAVAEKREKLANG HHHHHHHHHHHHHCC	57.00	24816145
35	Phosphorylation	GEGMEEATVVIEHCT CCCCCCEEEEEECCC	20.70	-
78	Phosphorylation	PTKPRRGSFEVTLLR CCCCCCCEEEEEEEC	19.20	24247654
89	Phosphorylation	TLLRPDGSSAELWTG EEECCCCCCCCHHCC	33.48	-
106	Ubiquitination	KGPPRKLKFPEPQEV CCCCCCCCCCCHHHH	63.01	-
118	Ubiquitination	QEVVEELKKYLS--- HHHHHHHHHHHC---	42.52	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SELH_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 SELH_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SELH_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

"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-20, AND MASS SPECTROMETRY.
PubMed: 19608861