dbPTM

BET1L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BET1L_HUMAN
UniProt AC	Q9NYM9
Protein Name	BET1-like protein
Gene Name	BET1L {ECO:0000312\|HGNC:HGNC:19348}
Organism	Homo sapiens (Human).
Sequence Length	111
Subcellular Localization	Golgi apparatus membrane Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi network membrane. Present throughout the Golgi apparatus, with increasing concentration from cis-Golgi to the trans-Golgi face of the stacks..
Protein Description	Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity)..
Protein Sequence	MADWARAQSPGAVEEILDRENKRMADSLASKVTRLKSLALDIDRDAEDQNRYLDGMDSDFTSMTSLLTGSVKRFSTMARSGQDNRKLLCGMAVGLIVAFFILSYFLSRART

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	ADWARAQSPGAVEEI CHHHHCCCCCHHHHH	25.06	19664994
22	Ubiquitination	EILDRENKRMADSLA HHHHHHCHHHHHHHH	38.51	-
27	Phosphorylation	ENKRMADSLASKVTR HCHHHHHHHHHHHHH	19.12	-
30	Phosphorylation	RMADSLASKVTRLKS HHHHHHHHHHHHHHH	32.71	-
31	Ubiquitination	MADSLASKVTRLKSL HHHHHHHHHHHHHHH	41.86	21906983
36	Ubiquitination	ASKVTRLKSLALDID HHHHHHHHHHHHCCC	39.88	21906983
37	Phosphorylation	SKVTRLKSLALDIDR HHHHHHHHHHHCCCC	24.38	23401153
44	Methylation	SLALDIDRDAEDQNR HHHHCCCCCHHHHHH	45.43	-
52	Phosphorylation	DAEDQNRYLDGMDSD CHHHHHHHHCCCCCC	19.39	28796482
58	Phosphorylation	RYLDGMDSDFTSMTS HHHCCCCCCHHHHHH	26.23	28796482
61	Phosphorylation	DGMDSDFTSMTSLLT CCCCCCHHHHHHHHH	23.68	28348404
62	Phosphorylation	GMDSDFTSMTSLLTG CCCCCHHHHHHHHHH	21.76	28985074
64	Phosphorylation	DSDFTSMTSLLTGSV CCCHHHHHHHHHHHH	18.91	28348404
65	Phosphorylation	SDFTSMTSLLTGSVK CCHHHHHHHHHHHHH	16.85	28985074
70	Phosphorylation	MTSLLTGSVKRFSTM HHHHHHHHHHHHHHH	21.16	28985074
72	Ubiquitination	SLLTGSVKRFSTMAR HHHHHHHHHHHHHHH	49.80	21906983
75	Phosphorylation	TGSVKRFSTMARSGQ HHHHHHHHHHHHCCC	22.70	23312004
76	Phosphorylation	GSVKRFSTMARSGQD HHHHHHHHHHHCCCC	16.49	23312004

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 BET1L_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BET1L_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 BET1L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GOSR1_HUMAN	GOSR1	physical	11927603
STX5_HUMAN	STX5	physical	11927603
YKT6_HUMAN	YKT6	physical	11927603
STX5_HUMAN	STX5	physical	12388752
GOSR1_HUMAN	GOSR1	physical	12388752
YKT6_HUMAN	YKT6	physical	12388752
COPA_HUMAN	COPA	physical	12388752
A4_HUMAN	APP	physical	21832049
GORAB_HUMAN	GORAB	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 BET1L_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-9, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.	18669648 [Abstract]