dbPTM

SNAB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SNAB_HUMAN
UniProt AC	Q9H115
Protein Name	Beta-soluble NSF attachment protein
Gene Name	NAPB
Organism	Homo sapiens (Human).
Sequence Length	298
Subcellular Localization	Membrane Peripheral membrane protein.
Protein Description	Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus..
Protein Sequence	MDNAGKEREAVQLMAEAEKRVKASHSFLRGLFGGNTRIEEACEMYTRAANMFKMAKNWSAAGNAFCQAAKLHMQLQSKHDSATSFVDAGNAYKKADPQEAINCLNAAIDIYTDMGRFTIAAKHHITIAEIYETELVDIEKAIAHYEQSADYYKGEESNSSANKCLLKVAAYAAQLEQYQKAIEIYEQVGANTMDNPLLKYSAKDYFFKAALCHFIVDELNAKLALEKYEEMFPAFTDSRECKLLKKLLEAHEEQNSEAYTEAVKEFDSISRLDQWLTTMLLRIKKSIQGDGEGDGDLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDNAGKER -------CCCCHHHH	8.94	-
2 (in isoform 3)	Phosphorylation	-	54.40	20068231
26	Phosphorylation	KRVKASHSFLRGLFG HHHHHHHHHHHHHHC	24.39	-
59	Ubiquitination	FKMAKNWSAAGNAFC HHHHHCHHHHHHHHH	20.03	21890473
83	Phosphorylation	QSKHDSATSFVDAGN HCCCCCCHHHHCCCH	27.01	-
84	Phosphorylation	SKHDSATSFVDAGNA CCCCCCHHHHCCCHH	24.00	-
93	Ubiquitination	VDAGNAYKKADPQEA HCCCHHHHCCCHHHH	38.79	-
109	Ubiquitination	NCLNAAIDIYTDMGR HHHHHHHHHHHHCCC	24.10	21890473
114	Ubiquitination	AIDIYTDMGRFTIAA HHHHHHHCCCCHHHH	2.98	21890473
118	Phosphorylation	YTDMGRFTIAAKHHI HHHCCCCHHHHCCCE	14.35	28060719
124	Ubiquitination	FTIAAKHHITIAEIY CHHHHCCCEEEEEEE	20.41	-
145	Phosphorylation	IEKAIAHYEQSADYY HHHHHHHHHHHCCCC	13.47	22210691
151	Phosphorylation	HYEQSADYYKGEESN HHHHHCCCCCCCCCC	13.54	22817900
152	Phosphorylation	YEQSADYYKGEESNS HHHHCCCCCCCCCCC	17.05	-
153	Ubiquitination	EQSADYYKGEESNSS HHHCCCCCCCCCCCH	54.33	21890473
153	2-Hydroxyisobutyrylation	EQSADYYKGEESNSS HHHCCCCCCCCCCCH	54.33	-
157	Ubiquitination	DYYKGEESNSSANKC CCCCCCCCCCHHHHH	37.40	21890473
157	Phosphorylation	DYYKGEESNSSANKC CCCCCCCCCCHHHHH	37.40	26714015
163	Ubiquitination	ESNSSANKCLLKVAA CCCCHHHHHHHHHHH	26.44	-
164	Acetylation	SNSSANKCLLKVAAY CCCHHHHHHHHHHHH	5.58	-
164	Ubiquitination	SNSSANKCLLKVAAY CCCHHHHHHHHHHHH	5.58	21890473
171	Phosphorylation	CLLKVAAYAAQLEQY HHHHHHHHHHHHHHH	7.85	22210691
178	Phosphorylation	YAAQLEQYQKAIEIY HHHHHHHHHHHHHHH	11.56	22210691
185	Phosphorylation	YQKAIEIYEQVGANT HHHHHHHHHHHCCCC	6.37	29888752
192	Phosphorylation	YEQVGANTMDNPLLK HHHHCCCCCCCCCHH	25.93	29888752
200	Phosphorylation	MDNPLLKYSAKDYFF CCCCCHHHHHHHHHH	17.52	29888752
201	Phosphorylation	DNPLLKYSAKDYFFK CCCCHHHHHHHHHHH	27.53	29888752
203	2-Hydroxyisobutyrylation	PLLKYSAKDYFFKAA CCHHHHHHHHHHHHH	47.20	-
203	Ubiquitination	PLLKYSAKDYFFKAA CCHHHHHHHHHHHHH	47.20	21890473
203	Acetylation	PLLKYSAKDYFFKAA CCHHHHHHHHHHHHH	47.20	22647375
268	Phosphorylation	EAVKEFDSISRLDQW HHHHHHHHHHHHHHH	27.99	24945436
277	Phosphorylation	SRLDQWLTTMLLRIK HHHHHHHHHHHHHHH	13.75	-

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SNAB_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SNAB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TAF1B_HUMAN	TAF1B	physical	21988832

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.

Regulatory Network of SNAB_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-203, AND MASS SPECTROMETRY.	19608861 [Abstract]