BAKOR_HUMAN - dbPTM
BAKOR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAKOR_HUMAN
UniProt AC Q6ZNE5
Protein Name Beclin 1-associated autophagy-related key regulator {ECO:0000303|PubMed:19050071}
Gene Name ATG14 {ECO:0000303|PubMed:18843052}
Organism Homo sapiens (Human).
Sequence Length 492
Subcellular Localization Cytoplasm . Endoplasmic reticulum membrane
Peripheral membrane protein . Preautophagosomal structure membrane
Peripheral membrane protein . Cytoplasmic vesicle, autophagosome membrane
Peripheral membrane protein . Cytosolic under nutrient-rich
Protein Description Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1. [PubMed: 18843052]
Protein Sequence MASPSGKGARALEAPGCGPRPLARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSRLKSKQEEFQKEVLKAMEGKWITDQLRWKIMSCKMRIEQLKQTICKGNEEMEKNSEGLLKTKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTIDLRSHYERLANLRRSHILELTSVIFPIEEVKTGVRDPADVSSESDSAMTSSTVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYSWVEEKKTTQGPDMEQSNPAYTISAALCYATQLVNILSHILDVNLPKKLCNSEFCGENLSKQKFTRAVKKLNANILYLCFSQHVNLDQLQPLHTLRNLMYLVSPSSEHLGRSGPFEVRADLEESMEFVDPGVAGESDESGDERVSDEETDLGTDWENLPSPRFCDIPSQSVEVSQSQSTQASPPIASSSAGGMISSAAASVTSWFKAYTGHR
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
3Phosphorylation-----MASPSGKGAR
-----CCCCCCCCCC		20.5024719451
5Phosphorylation---MASPSGKGARAL
---CCCCCCCCCCCC		51.1226074081
29PhosphorylationLARDLVDSVDDAEGL
CHHHHHHCCCCCCCE		21.7030266825
37PhosphorylationVDDAEGLYVAVERCP
CCCCCCEEEEEECCC		9.3822817900
94UbiquitinationSKQEEFQKEVLKAME
HCHHHHHHHHHHHHC		55.9329967540
115PhosphorylationQLRWKIMSCKMRIEQ
HHHHHHHHHHHHHHH		17.6630622161
123 (in isoform 2)Ubiquitination-2.6221906983
123UbiquitinationCKMRIEQLKQTICKG
HHHHHHHHHHHHHCC		2.6222817900
124UbiquitinationKMRIEQLKQTICKGN
HHHHHHHHHHHHCCC		45.1229967540
136UbiquitinationKGNEEMEKNSEGLLK
CCCHHHHHCCCCCCC		65.5429967540
143UbiquitinationKNSEGLLKTKEKNQK
HCCCCCCCHHHHHHH		63.6929967540
150UbiquitinationKTKEKNQKLYSRAQR
CHHHHHHHHHHHHHH		59.8029967540
152PhosphorylationKEKNQKLYSRAQRHQ
HHHHHHHHHHHHHHH		11.8023612710
153PhosphorylationEKNQKLYSRAQRHQE
HHHHHHHHHHHHHHH		31.4124719451
171MalonylationKIQRHNRKLGDLVEK
HHHHHHHHHHHHHHH		63.2426320211
171UbiquitinationKIQRHNRKLGDLVEK
HHHHHHHHHHHHHHH		63.2429967540
180PhosphorylationGDLVEKKTIDLRSHY
HHHHHHHHHCHHHHH		30.69-
227PhosphorylationDVSSESDSAMTSSTV
CCCCCCCCCCCHHHH		29.2619060867
230PhosphorylationSESDSAMTSSTVSKL
CCCCCCCCHHHHHHH		21.1728348404
231PhosphorylationESDSAMTSSTVSKLA
CCCCCCCHHHHHHHH		15.7828348404
232PhosphorylationSDSAMTSSTVSKLAE
CCCCCCHHHHHHHHH		24.5425849741
236 (in isoform 1)Ubiquitination-47.5921906983
236UbiquitinationMTSSTVSKLAEARRT
CCHHHHHHHHHHHCC		47.5922817900
245PhosphorylationAEARRTTYLSGRWVC
HHHHCCCEECCEEEE		9.7727642862
328MalonylationLDVNLPKKLCNSEFC
HCCCCCHHHCCCCCC		57.2326320211
328UbiquitinationLDVNLPKKLCNSEFC
HCCCCCHHHCCCCCC		57.2329967540
341UbiquitinationFCGENLSKQKFTRAV
CCCCCCCHHHHHHHH		61.7529967540
380PhosphorylationHTLRNLMYLVSPSSE
HHHHHHHHHCCCCCH		13.7128555341
404PhosphorylationVRADLEESMEFVDPG
EECCHHHHHHCCCCC		17.7817192257
416PhosphorylationDPGVAGESDESGDER
CCCCCCCCCCCCCCC		45.8418691976
419PhosphorylationVAGESDESGDERVSD
CCCCCCCCCCCCCCH		57.4418691976
425PhosphorylationESGDERVSDEETDLG
CCCCCCCCHHCCCCC		45.5922817900
429PhosphorylationERVSDEETDLGTDWE
CCCCHHCCCCCCCHH		34.1825686604
440PhosphorylationTDWENLPSPRFCDIP
CCHHHCCCCCCCCCC		31.6924719451
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 BAKOR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAKOR_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 BAKOR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PK3C3_HUMANPIK3C3physical
20562859
PI3R4_HUMANPIK3R4physical
20562859
NRBF2_HUMANNRBF2physical
20562859
BECN1_HUMANBECN1physical
20562859
EXOC1_HUMANEXOC1physical
21241894
BECN1_HUMANBECN1physical
19270696
PK3C3_HUMANPIK3C3physical
19270696
PI3R4_HUMANPIK3R4physical
19270696
PK3C3_HUMANPIK3C3physical
23262492
PI3R4_HUMANPIK3R4physical
23262492
DACT1_HUMANDACT1physical
24980960
PK3C3_HUMANPIK3C3physical
24980960
BECN1_HUMANBECN1physical
18843052
PK3C3_HUMANPIK3C3physical
18843052
BECN1_HUMANBECN1physical
19050071
PK3C3_HUMANPIK3C3physical
19050071
UBP18_HUMANUSP18physical
25906440
BECN1_HUMANBECN1physical
28514442
PK3C3_HUMANPIK3C3physical
28514442
LRC58_HUMANLRRC58physical
28514442
PI3R4_HUMANPIK3R4physical
28514442
RAD50_HUMANRAD50physical
28514442
CETN2_HUMANCETN2physical
28514442
M4K4_HUMANMAP4K4physical
28514442
MTFR1_HUMANMTFR1physical
28514442
PDLI5_HUMANPDLIM5physical
28514442
PCM1_HUMANPCM1physical
28514442
BECN1_HUMANBECN1physical
28757208
PK3C3_HUMANPIK3C3physical
28757208
PI3R4_HUMANPIK3R4physical
28757208
PK3C3_HUMANPIK3C3physical
28404643
BECN1_HUMANBECN1physical
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 BAKOR_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 SER-29; SER-227; SER-416;SER-419; SER-425 AND THR-429, AND MASS SPECTROMETRY.
"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-29, AND MASSSPECTROMETRY.

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