ATG13_HUMAN - dbPTM
ATG13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATG13_HUMAN
UniProt AC O75143
Protein Name Autophagy-related protein 13
Gene Name ATG13
Organism Homo sapiens (Human).
Sequence Length 517
Subcellular Localization Cytoplasm, cytosol . Preautophagosomal structure . Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane
the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome
Protein Description Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation..
Protein Sequence METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ
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-------METDLNSQ
-------CCCCCCCC		12.9622814378
3Phosphorylation-----METDLNSQDR
-----CCCCCCCCCH		44.4822199227
7Phosphorylation-METDLNSQDRKDLD
-CCCCCCCCCHHHHH		40.5322199227
41PhosphorylationGEKICTRSSSSPTGS
CCCCCCCCCCCCCCC		19.2023186163
42PhosphorylationEKICTRSSSSPTGSD
CCCCCCCCCCCCCCC		31.3823186163
43PhosphorylationKICTRSSSSPTGSDW
CCCCCCCCCCCCCCH		41.4023186163
44PhosphorylationICTRSSSSPTGSDWF
CCCCCCCCCCCCCHH		28.5623186163
56UbiquitinationDWFNLAIKDIPEVTH
CHHHHHHCCCHHCCH		43.95-
66AcetylationPEVTHEAKKALAGQL
HHCCHHHHHHHCCCC		35.2825953088
114O-linked_GlycosylationCDKEIKVSYTVYNRL
CCCCCEECHHHHHHH		15.3030620550
114PhosphorylationCDKEIKVSYTVYNRL
CCCCCEECHHHHHHH		15.3025693802
115PhosphorylationDKEIKVSYTVYNRLS
CCCCEECHHHHHHHH		11.8325693802
116PhosphorylationKEIKVSYTVYNRLSL
CCCEECHHHHHHHHH		14.7025693802
118PhosphorylationIKVSYTVYNRLSLLL
CEECHHHHHHHHHHH		6.1725693802
141PhosphorylationVTPAYRLSRKQGHEY
CCHHHHHHCCCCCEE		28.56-
143UbiquitinationPAYRLSRKQGHEYVI
HHHHHHCCCCCEEEE		58.20-
165 (in isoform 4)Phosphorylation-36.1828348404
169 (in isoform 4)Phosphorylation-50.3628348404
170PhosphorylationGLGEGFQTVRVGTVG
CCCCCCEEEEEECCC		14.1824719451
174 (in isoform 4)Phosphorylation-12.2428348404
175 (in isoform 4)Phosphorylation-16.9528348404
175PhosphorylationFQTVRVGTVGTPVGT
CEEEEEECCCCCCEE		16.9523401153
176 (in isoform 4)Phosphorylation-7.0828348404
178PhosphorylationVRVGTVGTPVGTITL
EEEECCCCCCEEEEE		15.5123401153
178 (in isoform 4)Phosphorylation-15.5128348404
179 (in isoform 4)Phosphorylation-19.3322210691
180 (in isoform 4)Phosphorylation-12.1128348404
182PhosphorylationTVGTPVGTITLSCAY
CCCCCCEEEEEEEHH		15.8323401153
184PhosphorylationGTPVGTITLSCAYRI
CCCCEEEEEEEHHHH		16.6823401153
189PhosphorylationTITLSCAYRINLAFM
EEEEEEHHHHHEEEE		19.1623401153
204PhosphorylationSTRQFERTPPIMGII
CCCCCCCCCCCEEEE		26.64-
220PhosphorylationDHFVDRPYPSSSPMH
HHCCCCCCCCCCCCC		19.3528348404
222PhosphorylationFVDRPYPSSSPMHPC
CCCCCCCCCCCCCCC		37.2928348404
223PhosphorylationVDRPYPSSSPMHPCN
CCCCCCCCCCCCCCC		33.6824719451
224PhosphorylationDRPYPSSSPMHPCNY
CCCCCCCCCCCCCCC		30.4928348404
244 (in isoform 2)Phosphorylation-22.5928348404
244 (in isoform 3)Phosphorylation-22.5928348404
248 (in isoform 2)Phosphorylation-18.0928348404
248 (in isoform 3)Phosphorylation-18.0928348404
253PhosphorylationEDSQEVCTTSFSTSP
CCCCCEEECCCCCCC		30.5627251275
253 (in isoform 2)Phosphorylation-30.5628348404
253 (in isoform 3)Phosphorylation-30.5628348404
254 (in isoform 3)Phosphorylation-23.7328348404
254 (in isoform 2)Phosphorylation-23.7328348404
255 (in isoform 3)Phosphorylation-10.0728348404
255 (in isoform 2)Phosphorylation-10.0728348404
257 (in isoform 2)Phosphorylation-27.9528348404
257 (in isoform 3)Phosphorylation-27.9528348404
258 (in isoform 3)Phosphorylation-43.1522210691
258 (in isoform 2)Phosphorylation-43.1522210691
259 (in isoform 2)Phosphorylation-33.3528348404
259 (in isoform 3)Phosphorylation-33.3528348404
318PhosphorylationPLAPNQPVHGTQADQ
ECCCCCCCCCCCCCH		4.72-
330PhosphorylationADQERLATCTPSDRT
CCHHHHCCCCCCCCC		22.8523312004
332PhosphorylationQERLATCTPSDRTHC
HHHHCCCCCCCCCCE		22.8221815630
334PhosphorylationRLATCTPSDRTHCAA
HHCCCCCCCCCCEEC		22.9021712546
337PhosphorylationTCTPSDRTHCAATPS
CCCCCCCCCEECCCC		26.7123927012
342PhosphorylationDRTHCAATPSSSEDT
CCCCEECCCCCCCCC		12.7423927012
344PhosphorylationTHCAATPSSSEDTET
CCEECCCCCCCCCCC		41.9928450419
345PhosphorylationHCAATPSSSEDTETV
CEECCCCCCCCCCCC		38.6628450419
346PhosphorylationCAATPSSSEDTETVS
EECCCCCCCCCCCCC		43.7728450419
349PhosphorylationTPSSSEDTETVSNSS
CCCCCCCCCCCCCCC		29.5123927012
351PhosphorylationSSSEDTETVSNSSEG
CCCCCCCCCCCCCCC		31.1823927012
353PhosphorylationSEDTETVSNSSEGRA
CCCCCCCCCCCCCCC		38.1123927012
355PhosphorylationDTETVSNSSEGRASP
CCCCCCCCCCCCCCH		23.4325159151
356PhosphorylationTETVSNSSEGRASPH
CCCCCCCCCCCCCHH		48.6023927012
361PhosphorylationNSSEGRASPHDVLET
CCCCCCCCHHHHHHH		22.7730266825
368PhosphorylationSPHDVLETIFVRKVG
CHHHHHHHHHHEEHH		18.6327050516
386PhosphorylationNKPINQVTLTSLDIP
CCCCCEEEEEECCCC		17.9829514088
388PhosphorylationPINQVTLTSLDIPFA
CCCEEEEEECCCCCE		20.2024719451
389PhosphorylationINQVTLTSLDIPFAM
CCEEEEEECCCCCEE		27.4529514088
394PhosphorylationLTSLDIPFAMFAPKN
EEECCCCCEEECCCC		8.6524719451
416PhosphorylationPMVNPPDSPETESPL
CCCCCCCCCCCCCCC		30.3426074081
419PhosphorylationNPPDSPETESPLQGS
CCCCCCCCCCCCCCC		45.1826074081
421PhosphorylationPDSPETESPLQGSLH
CCCCCCCCCCCCCCC		38.0324719451
422PhosphorylationDSPETESPLQGSLHS
CCCCCCCCCCCCCCC		23.5927251275
477PhosphorylationFQNPPQLSSLSIDIG
HCCCCCCCCEEEEEC		24.8028348404
478PhosphorylationQNPPQLSSLSIDIGA
CCCCCCCCEEEEECC		34.4328348404
480PhosphorylationPPQLSSLSIDIGAQS
CCCCCCEEEEECCHH		21.8428348404
487PhosphorylationSIDIGAQSMAEDLDS
EEEECCHHHHHHHHC		21.3028348404
504UbiquitinationEKLAVHEKNVREFDA
HHHHHHHHCHHHHHH		45.95-
504AcetylationEKLAVHEKNVREFDA
HHHHHHHHCHHHHHH		45.9525953088
511PhosphorylationKNVREFDAFVETLQ-
HCHHHHHHHHHHCC-		18.7227251275
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
44SPhosphorylationKinaseCDK1P06493
PSP
224SPhosphorylationKinaseCDK1P06493
PSP
332TPhosphorylationKinaseCDK1P06493
PSP
342TPhosphorylationKinaseCDK1P06493
PSP
355SPhosphorylationKinaseULK1O75385
Uniprot
389SPhosphorylationKinaseULK1O75385
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
355SPhosphorylation

21855797
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 ATG13_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATGA1_HUMANATG101physical
20562859
RBCC1_HUMANRB1CC1physical
20562859
TAB2_HUMANTAB2physical
21976705
A4_HUMANAPPphysical
21832049
ULK1_HUMANULK1physical
23524951
AMRA1_HUMANAMBRA1physical
23524951
SESN2_HUMANSESN2physical
25040165
ATGA1_HUMANATG101physical
19597335
RBCC1_HUMANRB1CC1physical
19597335
ULK1_HUMANULK1physical
19597335
ULK1_HUMANULK1physical
26018823
MUL1_HUMANMUL1physical
26018823
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 ATG13_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory