KCAB3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCAB3_HUMAN
• UniProt AC: O43448
• Protein Name: Voltage-gated potassium channel subunit beta-3
• Gene Name: KCNAB3
• Organism: Homo sapiens (Human).
• Sequence Length: 404
• Subcellular Localization: Cytoplasm .
• Protein Description: Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.5..
• Protein Sequence: MQVSIACTEQNLRSRSSEDRLCGPRPGPGGGNGGPAGGGHGNPPGGGGSGPKARAALVPRPPAPAGALRESTGRGTGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVITTKIFWGGQAETERGLSRKHIIEGLRGSLERLQLGYVDIVFANRSDPNCPMEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYQWLKDKVQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQTVMEIDGLLGNKPHSKK

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
71	Phosphorylation	PAGALRESTGRGTGM CCCCCCCCCCCCCCC	29.72	22210691
72	Phosphorylation	AGALRESTGRGTGMK CCCCCCCCCCCCCCC	26.58	22210691
76	Phosphorylation	RESTGRGTGMKYRNL CCCCCCCCCCCCCCC	32.51	24719451
85	Ubiquitination	MKYRNLGKSGLRVSC CCCCCCCCCCCEEEE	44.51	-
154	Phosphorylation	KGWRRSSYVITTKIF CCCCCCCEEEEEEEE	9.34	22210691
157	Phosphorylation	RRSSYVITTKIFWGG CCCCEEEEEEEEECC	16.40	22210691
158	Phosphorylation	RSSYVITTKIFWGGQ CCCEEEEEEEEECCH	15.83	22210691
175	Ubiquitination	TERGLSRKHIIEGLR CCCCCCHHHHHHHHH	35.46	-
184	Phosphorylation	IIEGLRGSLERLQLG HHHHHHHHHHHHHCC	22.18	17081983
265	Acetylation	HHLFQREKVEMQLPE HHHHHHHHHHHHHHH	45.76	19821981
285	Phosphorylation	GVGSVTWYPLACGLI CCCCCCEEECCCCCC	4.49	-
293	Phosphorylation	PLACGLITSKYDGRV ECCCCCCCCCCCCCC	24.98	-
294	Phosphorylation	LACGLITSKYDGRVP CCCCCCCCCCCCCCC	23.40	-
295	Acetylation	ACGLITSKYDGRVPD CCCCCCCCCCCCCCC	38.42	19821991
309	Ubiquitination	DTCRASIKGYQWLKD CCCCHHHCCHHHHHH	49.42	32142685
315	Ubiquitination	IKGYQWLKDKVQSED HCCHHHHHHHHCCCC	53.17	-
315	Acetylation	IKGYQWLKDKVQSED HCCHHHHHHHHCCCC	53.17	25953088
325	Acetylation	VQSEDGKKQQAKVMD HCCCCCHHHHHHHHH	53.85	7266237

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

Oops, there are no upstream regulatory protein records of KCAB3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KCAB3_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 KCAB3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
KCAB2_HUMAN	KCNAB2	physical	26186194
HDAC6_HUMAN	HDAC6	physical	26186194
DHYS_HUMAN	DHPS	physical	26186194
MD1L1_HUMAN	MAD1L1	physical	26186194
KCAB2_HUMAN	KCNAB2	physical	28514442
HDAC6_HUMAN	HDAC6	physical	28514442
MD1L1_HUMAN	MAD1L1	physical	28514442
DHYS_HUMAN	DHPS	physical	28514442

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-315, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-184, AND MASSSPECTROMETRY.
PubMed: 17081983