BET1_HUMAN - dbPTM
BET1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BET1_HUMAN
UniProt AC O15155
Protein Name BET1 homolog
Gene Name BET1
Organism Homo sapiens (Human).
Sequence Length 118
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type IV membrane protein. Golgi apparatus, cis-Golgi network membrane. Golgi apparatus membrane. Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Grea
Protein Description Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity)..
Protein Sequence MRRAGLGEGVPPGNYGNYGYANSGYSACEEENERLTESLRSKVTAIKSLSIEIGHEVKTQNKLLAEMDSQFDSTTGFLGKTMGKLKILSRGSQTKLLCYMMLFSLFVFFIIYWIIKLR
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 Orthologous
Protein Cluster
18PhosphorylationPPGNYGNYGYANSGY
CCCCCCCCCCCCCCC
13.7219060867
20PhosphorylationGNYGNYGYANSGYSA
CCCCCCCCCCCCCCC
7.7019060867
25PhosphorylationYGYANSGYSACEEEN
CCCCCCCCCCCHHHH
7.91-
38PhosphorylationENERLTESLRSKVTA
HHHHHHHHHHHHHHH
24.6921815630
41PhosphorylationRLTESLRSKVTAIKS
HHHHHHHHHHHHHHH
36.4524702127
422-HydroxyisobutyrylationLTESLRSKVTAIKSL
HHHHHHHHHHHHHHH
36.85-
42UbiquitinationLTESLRSKVTAIKSL
HHHHHHHHHHHHHHH
36.85-
47UbiquitinationRSKVTAIKSLSIEIG
HHHHHHHHHHHHHHC
42.77-
48PhosphorylationSKVTAIKSLSIEIGH
HHHHHHHHHHHHHCC
22.6423927012
50PhosphorylationVTAIKSLSIEIGHEV
HHHHHHHHHHHCCCH
25.8526846344
58UbiquitinationIEIGHEVKTQNKLLA
HHHCCCHHHHCHHHH
41.21-
62UbiquitinationHEVKTQNKLLAEMDS
CCHHHHCHHHHHHHH
34.7521890473
67SulfoxidationQNKLLAEMDSQFDST
HCHHHHHHHHHCCCC
5.1021406390
69PhosphorylationKLLAEMDSQFDSTTG
HHHHHHHHHCCCCCC
31.2830108239
73PhosphorylationEMDSQFDSTTGFLGK
HHHHHCCCCCCHHHH
29.2030108239
74PhosphorylationMDSQFDSTTGFLGKT
HHHHCCCCCCHHHHH
32.5530108239
75PhosphorylationDSQFDSTTGFLGKTM
HHHCCCCCCHHHHHH
29.8630108239
80UbiquitinationSTTGFLGKTMGKLKI
CCCCHHHHHHHHHHH
37.17-
84UbiquitinationFLGKTMGKLKILSRG
HHHHHHHHHHHHCCC
35.47-

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 BET1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BET1_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 BET1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
USBP1_HUMANUSHBP1physical
16189514
B2L13_HUMANBCL2L13physical
25416956
KASH5_HUMANCCDC155physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956

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 BET1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-50, AND MASSSPECTROMETRY.
"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-50, AND MASSSPECTROMETRY.

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