BECN1_HUMAN - dbPTM
BECN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BECN1_HUMAN
UniProt AC Q14457
Protein Name Beclin-1
Gene Name BECN1
Organism Homo sapiens (Human).
Sequence Length 450
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. [PubMed: 23184933]
Protein Sequence MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK
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-------MEGSKTSN
-------CCCCCCCC
13.6922814378
6Phosphorylation--MEGSKTSNNSTMQ
--CCCCCCCCCCCCE
38.0828985074
7Phosphorylation-MEGSKTSNNSTMQV
-CCCCCCCCCCCCEE
37.4427251275
10PhosphorylationGSKTSNNSTMQVSFV
CCCCCCCCCCEEEEE
29.5227251275
11PhosphorylationSKTSNNSTMQVSFVC
CCCCCCCCCEEEEEE
17.4727251275
15PhosphorylationNNSTMQVSFVCQRCS
CCCCCEEEEEECCCC
8.6227251275
26UbiquitinationQRCSQPLKLDTSFKI
CCCCCCCCCCCCEEE
51.50-
29PhosphorylationSQPLKLDTSFKILDR
CCCCCCCCCEEEECE
46.6423403867
30PhosphorylationQPLKLDTSFKILDRV
CCCCCCCCEEEECEE
24.9823403867
32UbiquitinationLKLDTSFKILDRVTI
CCCCCCEEEECEEEH
41.9721890473
32UbiquitinationLKLDTSFKILDRVTI
CCCCCCEEEECEEEH
41.9721890473
38PhosphorylationFKILDRVTIQELTAP
EEEECEEEHHHHCCC
20.1720068231
43PhosphorylationRVTIQELTAPLLTTA
EEEHHHHCCCHHHCC
26.0226657352
48PhosphorylationELTAPLLTTAQAKPG
HHCCCHHHCCCCCCC
27.9828122231
49PhosphorylationLTAPLLTTAQAKPGE
HCCCHHHCCCCCCCC
19.4228122231
53UbiquitinationLLTTAQAKPGETQEE
HHHCCCCCCCCCCCC
41.28-
57PhosphorylationAQAKPGETQEEETNS
CCCCCCCCCCCCCCC
47.3919369195
62PhosphorylationGETQEEETNSGEEPF
CCCCCCCCCCCCCCC
37.6526657352
64PhosphorylationTQEEETNSGEEPFIE
CCCCCCCCCCCCCCC
55.8129255136
72PhosphorylationGEEPFIETPRQDGVS
CCCCCCCCCCCCCCC
20.9628122231
90PhosphorylationIPPARMMSTESANSF
CCCHHHCCCCCCCCE
21.4923878393
91PhosphorylationPPARMMSTESANSFT
CCHHHCCCCCCCCEE
18.9630624053
93PhosphorylationARMMSTESANSFTLI
HHHCCCCCCCCEEEE
32.6023878393
96PhosphorylationMSTESANSFTLIGEA
CCCCCCCCEEEEEEC
21.2330624053
98PhosphorylationTESANSFTLIGEASD
CCCCCCEEEEEECCC
19.7930624053
104PhosphorylationFTLIGEASDGGTMEN
EEEEEECCCCCCHHH
32.2722210691
108PhosphorylationGEASDGGTMENLSRR
EECCCCCCHHHHHHH
27.17-
113PhosphorylationGGTMENLSRRLKVTG
CCCHHHHHHHHHHCC
27.2622210691
117UbiquitinationENLSRRLKVTGDLFD
HHHHHHHHHCCCHHH
35.6220501938
119PhosphorylationLSRRLKVTGDLFDIM
HHHHHHHCCCHHHHH
24.3217446862
203UbiquitinationQELEDVEKNRKIVAE
HHHHHHHHHHHHHHH
63.00-
206AcetylationEDVEKNRKIVAENLE
HHHHHHHHHHHHHHH
51.4220167786
206UbiquitinationEDVEKNRKIVAENLE
HHHHHHHHHHHHHHH
51.42-
214UbiquitinationIVAENLEKVQAEAER
HHHHHHHHHHHHHHH
42.70-
229PhosphorylationLDQEEAQYQREYSEF
CHHHHHHHHHHHHHH
19.3127642862
233PhosphorylationEAQYQREYSEFKRQQ
HHHHHHHHHHHHHHH
18.71-
234PhosphorylationAQYQREYSEFKRQQL
HHHHHHHHHHHHHHC
31.63-
237UbiquitinationQREYSEFKRQQLELD
HHHHHHHHHHHCCCH
45.29-
248UbiquitinationLELDDELKSVENQMR
CCCHHHHHHHHHHHH
50.86-
263UbiquitinationYAQTQLDKLKKTNVF
HHHHHHHHHHHCCCC
71.45-
266UbiquitinationTQLDKLKKTNVFNAT
HHHHHHHHCCCCEEE
56.63-
279PhosphorylationATFHIWHSGQFGTIN
EEEEEEECCCCCEEC
21.20-
295PhosphorylationFRLGRLPSVPVEWNE
EECCCCCCCCCCHHH
43.58-
324UbiquitinationLANKMGLKFQRYRLV
HHHHHCCCEEEEEEE
33.45-
337PhosphorylationLVPYGNHSYLESLTD
EECCCCCHHHHHHCC
35.10-
352PhosphorylationKSKELPLYCSGGLRF
CCCCCCEEECCCCEE
5.22-
388PhosphorylationEEVEKGETRFCLPYR
HHHHCCCCEEEEEEE
37.40-
402UbiquitinationRMDVEKGKIEDTGGS
EEEEECCEEEECCCC
54.7321890473
406PhosphorylationEKGKIEDTGGSGGSY
ECCEEEECCCCCCCE
30.5630619164
409PhosphorylationKIEDTGGSGGSYSIK
EEEECCCCCCCEEEE
41.1325159151
412PhosphorylationDTGGSGGSYSIKTQF
ECCCCCCCEEEEEEC
21.1626699800
413PhosphorylationTGGSGGSYSIKTQFN
CCCCCCCEEEEEECC
20.0726699800
414PhosphorylationGGSGGSYSIKTQFNS
CCCCCCEEEEEECCC
21.2126699800
417PhosphorylationGGSYSIKTQFNSEEQ
CCCEEEEEECCCHHH
36.4030619164
421PhosphorylationSIKTQFNSEEQWTKA
EEEEECCCHHHHHHH
43.7424850871
426PhosphorylationFNSEEQWTKALKFML
CCCHHHHHHHHHHHH
13.2130619164
427UbiquitinationNSEEQWTKALKFMLT
CCHHHHHHHHHHHHH
49.08-
430AcetylationEQWTKALKFMLTNLK
HHHHHHHHHHHHHHH
33.32126474619
430UbiquitinationEQWTKALKFMLTNLK
HHHHHHHHHHHHHHH
33.32-
437AcetylationKFMLTNLKWGLAWVS
HHHHHHHHHHHHHHH
41.09126474625
437UbiquitinationKFMLTNLKWGLAWVS
HHHHHHHHHHHHHHH
41.09-

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
15SPhosphorylationKinaseULK1O75385
PSP
30SPhosphorylationKinaseULK1O75385
PSP
57TPhosphorylationKinaseATMQ13315
PSP
90SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
90SPhosphorylationKinaseMAPKAPK2P49137
PSP
90SPhosphorylationKinaseAMPKQ9Y478
Uniprot
90SPhosphorylationKinaseMAPKAPK3Q16644
PSP
90SPhosphorylationKinaseDAPK3O43293
PSP
93SPhosphorylationKinaseAMPKQ9Y478
Uniprot
93SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
93SPhosphorylationKinaseAMPKA1Q13131
PSP
96SPhosphorylationKinaseULK1O75385
PSP
96SPhosphorylationKinaseAMPKA1Q13131
PSP
96SPhosphorylationKinaseAMPKQ9Y478
Uniprot
96SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
108TPhosphorylationKinaseSTK4Q13043
GPS
119TPhosphorylationKinaseDAPK1P53355
Uniprot
229YPhosphorylationKinaseEGFRP00533
PSP
233YPhosphorylationKinasePTK2Q05397
GPS
233YPhosphorylationKinaseEGFRP00533
PSP
234SPhosphorylationKinaseAKT1P31749
PSP
279SPhosphorylationKinaseULK1O75385
PSP
295SPhosphorylationKinaseAKT1P31749
PSP
337SPhosphorylationKinaseULK1O75385
PSP
352YPhosphorylationKinaseEGFRP00533
PSP
388TPhosphorylationKinasePRKAA1Q13131
GPS
406TPhosphorylationKinaseCSNK1G2P78368
GPS
409SPhosphorylationKinaseCSNK1G2P78368
GPS
-KUbiquitinationE3 ubiquitin ligaseTRAF6Q9Y4K3
PMID:20501938
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:21936852
-KUbiquitinationE3 ubiquitin ligaseAMBRA1Q9C0C7
PMID:23974797
-KUbiquitinationE3 ubiquitin ligaseKLHL20Q9Y2M5
PMID:26687681

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

24443581
119TPhosphorylation

19180116
402Kubiquitylation

28445460
402Kubiquitylation

28445460

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TSC1_HUMANTSC1physical
20562859
PK3C3_HUMANPIK3C3physical
20562859
PI3R4_HUMANPIK3R4physical
20562859
S27A4_HUMANSLC27A4physical
20562859
UVRAG_HUMANUVRAGphysical
20562859
DZIP3_HUMANDZIP3physical
20562859
PTOV1_HUMANPTOV1physical
20562859
TBCD7_HUMANTBC1D7physical
20562859
BAKOR_HUMANATG14physical
20562859
RUBIC_HUMANKIAA0226physical
20562859
TRABD_HUMANTRABDphysical
20562859
NRBF2_HUMANNRBF2physical
20562859
ASPP2_HUMANTP53BP2physical
20562859
AMRA1_HUMANAMBRA1physical
20562859
ERF3A_HUMANGSPT1physical
20562859
AFG32_HUMANAFG3L2physical
20562859
SEH1_HUMANSEH1Lphysical
20562859
PRKDC_HUMANPRKDCphysical
20562859
RUBCL_HUMANKIAA0226Lphysical
20562859
ZWINT_HUMANZWINTphysical
20562859
SMC1A_HUMANSMC1Aphysical
20562859
SMC3_HUMANSMC3physical
20562859
TRAF6_HUMANTRAF6physical
20501938
UBC_HUMANUBCphysical
20501938
TNAP3_HUMANTNFAIP3physical
20501938
BECN1_HUMANBECN1physical
20501938
NEDD4_HUMANNEDD4physical
21936852
PK3C3_HUMANPIK3C3physical
21936852
ITCH_HUMANITCHphysical
21936852
AMRA1_HUMANAMBRA1physical
21358617
TAB2_HUMANTAB2physical
21976705
B2CL1_HUMANBCL2L1physical
18628207
VMP1_RATVmp1physical
23316280
BCL2_HUMANBCL2physical
23316280
BCL2_HUMANBCL2physical
21971985
S10A8_HUMANS100A8physical
21971985
MCL1_HUMANMCL1physical
22219388
B2CL1_HUMANBCL2L1physical
22219388
BCL2_HUMANBCL2physical
23479509
PK3C3_HUMANPIK3C3physical
23974797
WASH1_HUMANWASH1physical
23974797
AMRA1_HUMANAMBRA1physical
23974797
UBP33_HUMANUSP33physical
24056301
EXOC2_HUMANEXOC2physical
24056301
BCL2_HUMANBCL2physical
23504944
EXOC8_HUMANEXOC8physical
21241894
BCL2_HUMANBCL2physical
20711182
PK3C3_HUMANPIK3C3physical
20711182
PI3R4_HUMANPIK3R4physical
20711182
AMRA1_HUMANAMBRA1physical
20711182
BAKOR_HUMANATG14physical
20711182
PI3R4_HUMANPIK3R4physical
19270696
RUBIC_HUMANKIAA0226physical
19270696
PK3C3_HUMANPIK3C3physical
19270696
UVRAG_HUMANUVRAGphysical
19270696
BAKOR_HUMANATG14physical
19270696
BECN1_HUMANBECN1physical
19270696
BCL2_HUMANBCL2physical
19347031
BRCA1_HUMANBRCA1physical
24378767
DACT1_HUMANDACT1physical
24980960
PK3C3_HUMANPIK3C3physical
24980960
BAKOR_HUMANATG14physical
24980960
RUBIC_HUMANKIAA0226physical
24980960
PK3C3_HUMANPIK3C3physical
24980959
WASH1_HUMANWASH1physical
24980959
BECN1_HUMANBECN1physical
18641390
BCL2_HUMANBCL2physical
18641390
B2CL1_HUMANBCL2L1physical
18641390
UVRAG_HUMANUVRAGphysical
18641390
UVRAG_HUMANUVRAGphysical
18843052
BAKOR_HUMANATG14physical
18843052
PK3C3_HUMANPIK3C3physical
18843052
B2CL1_HUMANBCL2L1physical
19049976
BAKOR_HUMANATG14physical
19050071
UVRAG_HUMANUVRAGphysical
19050071
PK3C3_HUMANPIK3C3physical
19050071
BCL2_HUMANBCL2physical
19050071
PI3R4_HUMANPIK3R4physical
19050071
PK3CG_HUMANPIK3CGphysical
19050071
PRKN_HUMANPARK2physical
24386307
DAPK1_HUMANDAPK1physical
19180116
B2CL1_HUMANBCL2L1physical
19180116
AMRA1_HUMANAMBRA1physical
20921139
DYL1_HUMANDYNLL1physical
20921139
BCL2_HUMANBCL2physical
23168911
AMRA1_HUMANAMBRA1physical
24587252
BCL2_HUMANBCL2physical
16179260
PK3C3_HUMANPIK3C3physical
16179260
B2CL1_HUMANBCL2L1physical
19713971
PK3C3_HUMANPIK3C3physical
19713971
BCL2_HUMANBCL2physical
19959994
BCL2_HUMANBCL2physical
20622903
PK3C3_HUMANPIK3C3physical
23315026
PK3C3_HUMANPIK3C3physical
23878393
PI3R4_HUMANPIK3R4physical
23878393
BAKOR_HUMANATG14physical
23878393
UVRAG_HUMANUVRAGphysical
23878393
DDB1_HUMANDDB1physical
25499913
AMRA1_HUMANAMBRA1physical
25499913
UBP18_HUMANUSP18physical
25906440
PK3C3_HUMANPIK3C3physical
25906440
PK3C3_HUMANPIK3C3physical
26496610
TCOF_HUMANTCOF1physical
26496610
UVRAG_HUMANUVRAGphysical
26496610
RUBIC_HUMANKIAA0226physical
26496610
TRIB1_HUMANTRIB1physical
26496610
BAKOR_HUMANATG14physical
26496610
MDN1_HUMANMDN1physical
26496610
NGDN_HUMANNGDNphysical
26496610
LSM3_HUMANLSM3physical
26496610
NRBF2_HUMANNRBF2physical
26496610
PI3R4_HUMANPIK3R4physical
26496610
RN216_HUMANRNF216physical
25484083
BIRC5_HUMANBIRC5physical
26148234
ULK1_HUMANULK1physical
25891078
IRGM_HUMANIRGMphysical
25891078
BAKOR_HUMANATG14physical
25891078
BCL2_HUMANBCL2physical
25891078
RUBIC_HUMANKIAA0226physical
25891078
BCL2_HUMANBCL2physical
25984893
PK3C3_HUMANPIK3C3physical
25825496
PK3C3_HUMANPIK3C3physical
16390869
EFTU_HUMANTUFMphysical
26876213
RUBIC_HUMANKIAA0226physical
26876213
P53_HUMANTP53physical
28128446
NEDD4_HUMANNEDD4physical
28128446
TF65_HUMANRELAphysical
28128446
BCL2_HUMANBCL2physical
28128446
PK3C3_HUMANPIK3C3physical
28128446
PK3C3_HUMANPIK3C3physical
25693418
BAKOR_HUMANATG14physical
25693418
TRAF2_HUMANTRAF2physical
28521610
SPHK1_HUMANSPHK1physical
28521610
PK3C3_HUMANPIK3C3physical
28404643
WDR81_HUMANWDR81physical
28404643
WDR91_HUMANWDR91physical
28404643
BAKOR_HUMANATG14physical
28404643

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 BECN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-29; SER-30; THR-57;THR-62; SER-64; SER-90; SER-93 AND SER-96, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57 AND SER-64, AND MASSSPECTROMETRY.
"DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1promotes dissociation of beclin 1 from Bcl-XL and induction ofautophagy.";
Zalckvar E., Berissi H., Mizrachy L., Idelchuk Y., Koren I.,Eisenstein M., Sabanay H., Pinkas-Kramarski R., Kimchi A.;
EMBO Rep. 10:285-292(2009).
Cited for: PHOSPHORYLATION AT THR-119, AND INTERACTION WITH DAPK1.

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