BECN1_RAT - dbPTM
BECN1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BECN1_RAT
UniProt AC Q91XJ1
Protein Name Beclin-1
Gene Name Becn1
Organism Rattus norvegicus (Rat).
Sequence Length 448
Subcellular Localization Cytoplasm . Golgi apparatus, trans-Golgi network membrane
Peripheral membrane protein . Endosome membrane
Peripheral membrane protein . Endoplasmic reticulum membrane
Peripheral membrane protein . Mitochondrion membrane
Peripheral membrane protein
Protein Description Plays a central role in autophagy. Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. May play a role in antiviral host defense (By similarity).; Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors..
Protein Sequence MEGSKASSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGESQEEEANSGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEMLEQMNEGDSEQLQRELKELALEEERLIQELEDVEKNRKVVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQMQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSAPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK
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
1Acetylation-------MEGSKASS
-------CCCCCCCC
13.69-
7Phosphorylation-MEGSKASSSTMQVS
-CCCCCCCCCCCEEE
28.6727097102
8PhosphorylationMEGSKASSSTMQVSF
CCCCCCCCCCCEEEE
34.3927097102
9PhosphorylationEGSKASSSTMQVSFV
CCCCCCCCCCEEEEE
25.9627097102
10PhosphorylationGSKASSSTMQVSFVC
CCCCCCCCCEEEEEE
17.3627097102
28PhosphorylationSQPLKLDTSFKILDR
CCCCCCCCCEEEECE
46.6425575281
29PhosphorylationQPLKLDTSFKILDRV
CCCCCCCCEEEECEE
24.9825575281
88PhosphorylationIPPARMMSTESANSF
CCCHHHCCCCCCCCE
21.49-
91PhosphorylationARMMSTESANSFTLI
HHHCCCCCCCCEEEE
32.6022276854
94PhosphorylationMSTESANSFTLIGEA
CCCCCCCCEEEEEEC
21.2322276854
117PhosphorylationLSRRLKVTGDLFDIM
HHHHHHHCCCHHHHH
24.32-
183AcetylationEQLQRELKELALEEE
HHHHHHHHHHHHHHH
46.0222902405
232PhosphorylationAQYQREYSEFKRQQL
HHHHHHHHHHHHHHC
31.63-
293PhosphorylationFRLGRLPSAPVEWNE
EECCCCCCCCCCHHH
50.20-

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
88SPhosphorylationKinaseAMPKQ09137
Uniprot
91SPhosphorylationKinaseAMPKQ09137
Uniprot
94SPhosphorylationKinaseAMPKQ09137
Uniprot
117TPhosphorylationKinaseDAPK1-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
11Kubiquitylation

-
117TPhosphorylation

-
400Kubiquitylation

-
400Kubiquitylation

-

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 BECN1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BECN1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BECN1_RAT

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Related Literatures of Post-Translational Modification

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