ATG2A_HUMAN - dbPTM
ATG2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATG2A_HUMAN
UniProt AC Q2TAZ0
Protein Name Autophagy-related protein 2 homolog A
Gene Name ATG2A
Organism Homo sapiens (Human).
Sequence Length 1938
Subcellular Localization Preautophagosomal structure membrane
Peripheral membrane protein. Lipid droplet.
Protein Description Required for both autophagosome formation and regulation of lipid droplet morphology and dispersion..
Protein Sequence MSRWLWPWSNCVKERVCRYLLHHYLGHFFQEHLSLDQLSLDLYKGSVALRDIHLEIWSVNEVLESMESPLELVEGFVGSIEVAVPWAALLTDHCTVRVSGLQLTLQPRRGPAPGAADSQSWASCMTTSLQLAQECLRDGLPEPSEPPQPLEGLEMFAQTIETVLRRIKVTFLDTVVRVEHSPGDGERGVAVEVRVQRLEYCDEAVRDPSQAPPVDVHQPPAFLHKLLQLAGVRLHYEELPAQEEPPEPPLQIGSCSGYMELMVKLKQNEAFPGPKLEVAGQLGSLHLLLTPRQLQQLQELLSAVSLTDHEGLADKLNKSRPLGAEDLWLIEQDLNQQLQAGAVAEPLSPDPLTNPLLNLDNTDLFFSMAGLTSSVASALSELSLSDVDLASSVRSDMASRRLSAQAHPAGKMAPNPLLDTMRPDSLLKMTLGGVTLTLLQTSAPSSGPPDLATHFFTEFDATKDGPFGSRDFHHLRPRFQRACPCSHVRLTGTAVQLSWELRTGSRGRRTTSMEVHFGQLEVLECLWPRGTSEPEYTEILTFPGTLGSQASARPCAHLRHTQILRRVPKSRPRRSVACHCHSELALDLANFQADVELGALDRLAALLRLATVPAEPPAGLLTEPLPAMEQQTVFRLSAPRATLRLRFPIADLRPEPDPWAGQAVRAEQLRLELSEPQFRSELSSGPGPPVPTHLELTCSDLHGIYEDGGKPPVPCLRVSKALDPKSTGRKYFLPQVVVTVNPQSSSTQWEVAPEKGEELELSVESPCELREPEPSPFSSKRTMYETEEMVIPGDPEEMRTFQSRTLALSRCSLEVILPSVHIFLPSKEVYESIYNRINNDLLMWEPADLLPTPDPAAQPSGFPGPSGFWHDSFKMCKSAFKLANCFDLTPDSDSDDEDAHFFSVGASGGPQAAAPEAPSLHLQSTFSTLVTVLKGRITALCETKDEGGKRLEAVHGELVLDMEHGTLFSVSQYCGQPGLGYFCLEAEKATLYHRAAVDDYPLPSHLDLPSFAPPAQLAPTIYPSEEGVTERGASGRKGQGRGPHMLSTAVRIHLDPHKNVKEFLVTLRLHKATLRHYMALPEQSWHSQLLEFLDVLDDPVLGYLPPTVITILHTHLFSCSVDYRPLYLPVRVLITAETFTLSSNIIMDTSTFLLRFILDDSALYLSDKCEVETLDLRRDYVCVLDVDLLELVIKTWKGSTEGKLSQPLFELRCSNNVVHVHSCADSCALLVNLLQYVMSTGDLHPPPRPPSPTEIAGQKLSESPASLPSCPPVETALINQRDLADALLDTERSLRELAQPSGGHLPQASPISVYLFPGERSGAPPPSPPVGGPAGSLGSCSEEKEDEREEEGDGDTLDSDEFCILDAPGLGIPPRDGEPVVTQLHPGPIVVRDGYFSRPIGSTDLLRAPAHFPVPSTRVVLREVSLVWHLYGGRDFGPHPGHRARTGLSGPRSSPSRCSGPNRPQNSWRTQGGSGRQHHVLMEIQLSKVSFQHEVYPAEPATGPAAPSQELEERPLSRQVFIVQELEVRDRLASSQINKFLYLHTSERMPRRAHSNMLTIKALHVAPTTNLGGPECCLRVSLMPLRLNVDQDALFFLKDFFTSLVAGINPVVPGETSAEARPETRAQPSSPLEGQAEGVETTGSQEAPGGGHSPSPPDQQPIYFREFRFTSEVPIWLDYHGKHVTMDQVGTFAGLLIGLAQLNCSELKLKRLCCRHGLLGVDKVLGYALNEWLQDIRKNQLPGLLGGVGPMHSVVQLFQGFRDLLWLPIEQYRKDGRLMRGLQRGAASFGSSTASAALELSNRLVQAIQATAETVYDILSPAAPVSRSLQDKRSARRLRRGQQPADLREGVAKAYDTVREGILDTAQTICDVASRGHEQKGLTGAVGGVIRQLPPTVVKPLILATEATSSLLGGMRNQIVPDAHKDHALKWRSDSAQD
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
200PhosphorylationVRVQRLEYCDEAVRD
EEEEEEECCCHHCCC		15.14-
258PhosphorylationQIGSCSGYMELMVKL
CCEECCCHHHHHHHH		3.2317053785
403PhosphorylationDMASRRLSAQAHPAG
HHHHHHHHHHCCCCC		19.2728985074
411AcetylationAQAHPAGKMAPNPLL
HHCCCCCCCCCCCCH		33.7125953088
425PhosphorylationLDTMRPDSLLKMTLG
HHCCCCCHHHHHHHC		37.9824719451
491PhosphorylationPCSHVRLTGTAVQLS
CCCEEEEEEEEEEEE		23.1729262532
493PhosphorylationSHVRLTGTAVQLSWE
CEEEEEEEEEEEEEE		20.5829262532
498PhosphorylationTGTAVQLSWELRTGS
EEEEEEEEEEECCCC		11.0424719451
503PhosphorylationQLSWELRTGSRGRRT
EEEEEECCCCCCCCE		52.7329262532
505PhosphorylationSWELRTGSRGRRTTS
EEEECCCCCCCCEEE		30.8329262532
510PhosphorylationTGSRGRRTTSMEVHF
CCCCCCCEEEEEEEC		23.1224719451
511PhosphorylationGSRGRRTTSMEVHFG
CCCCCCEEEEEEECC		25.0224719451
512PhosphorylationSRGRRTTSMEVHFGQ
CCCCCEEEEEEECCE		16.6024719451
637PhosphorylationQQTVFRLSAPRATLR
CEEEEEEECCCCEEE		31.7824719451
642PhosphorylationRLSAPRATLRLRFPI
EEECCCCEEEEECCH		17.43-
762PhosphorylationKGEELELSVESPCEL
CCCCEEEEECCCCCC		17.9225159151
765PhosphorylationELELSVESPCELREP
CEEEEECCCCCCCCC		32.4725159151
775PhosphorylationELREPEPSPFSSKRT
CCCCCCCCCCCCCCC		36.5925627689
780UbiquitinationEPSPFSSKRTMYETE
CCCCCCCCCCEEEEE		51.17-
782PhosphorylationSPFSSKRTMYETEEM
CCCCCCCCEEEEEEC		28.0430576142
784PhosphorylationFSSKRTMYETEEMVI
CCCCCCEEEEEECCC		21.0630576142
800PhosphorylationGDPEEMRTFQSRTLA
CCHHHHHHHHHHHHH		25.39-
809PhosphorylationQSRTLALSRCSLEVI
HHHHHHHHHCCEEEE		26.1530576142
812PhosphorylationTLALSRCSLEVILPS
HHHHHHCCEEEEECC		26.84-
826PhosphorylationSVHIFLPSKEVYESI
CEEEECCCHHHHHHH		43.5324719451
852PhosphorylationEPADLLPTPDPAAQP
CCHHHCCCCCCCCCC		40.0526853621
866PhosphorylationPSGFPGPSGFWHDSF
CCCCCCCCCCCHHHH		53.1625627689
878PhosphorylationDSFKMCKSAFKLANC
HHHHHHHHHHHHHCC		33.73-
892PhosphorylationCFDLTPDSDSDDEDA
CEECCCCCCCCCCCC		39.97-
894PhosphorylationDLTPDSDSDDEDAHF
ECCCCCCCCCCCCCE		51.41-
1251PhosphorylationHPPPRPPSPTEIAGQ
CCCCCCCCCCCCCCE		47.3226657352
1261PhosphorylationEIAGQKLSESPASLP
CCCCEECCCCCCCCC		42.9630266825
1263 (in isoform 3)Phosphorylation-23.5330266825
1263PhosphorylationAGQKLSESPASLPSC
CCEECCCCCCCCCCC		23.5330266825
1265 (in isoform 3)Phosphorylation-32.7430266825
1266PhosphorylationKLSESPASLPSCPPV
ECCCCCCCCCCCCCC		44.1730266825
1268 (in isoform 3)Phosphorylation-31.2430266825
1269PhosphorylationESPASLPSCPPVETA
CCCCCCCCCCCCCHH		44.5430266825
1271 (in isoform 3)Phosphorylation-40.0730266825
1275PhosphorylationPSCPPVETALINQRD
CCCCCCCHHCCCHHH		27.3120068231
1277 (in isoform 3)Phosphorylation-5.0230266825
1290PhosphorylationLADALLDTERSLREL
HHHHHHHHHHHHHHH		33.0128348404
1293PhosphorylationALLDTERSLRELAQP
HHHHHHHHHHHHHCC		26.0828348404
1301PhosphorylationLRELAQPSGGHLPQA
HHHHHCCCCCCCCCC		45.3825159151
1309PhosphorylationGGHLPQASPISVYLF
CCCCCCCCCCEEEEE		19.9525159151
1312PhosphorylationLPQASPISVYLFPGE
CCCCCCCEEEEECCC		14.2126699800
1321PhosphorylationYLFPGERSGAPPPSP
EEECCCCCCCCCCCC		34.7021815630
1327PhosphorylationRSGAPPPSPPVGGPA
CCCCCCCCCCCCCCC		47.8426657352
1395PhosphorylationPIVVRDGYFSRPIGS
CEEEECCCCCCCCCC		11.5822817900
1397PhosphorylationVVRDGYFSRPIGSTD
EEECCCCCCCCCCCC		28.7623186163
1402PhosphorylationYFSRPIGSTDLLRAP
CCCCCCCCCCCCCCC		21.3325850435
1403PhosphorylationFSRPIGSTDLLRAPA
CCCCCCCCCCCCCCC		26.0025850435
1446PhosphorylationHPGHRARTGLSGPRS
CCCCCCCCCCCCCCC		41.3021712546
1449PhosphorylationHRARTGLSGPRSSPS
CCCCCCCCCCCCCCC		48.3629978859
1453PhosphorylationTGLSGPRSSPSRCSG
CCCCCCCCCCCCCCC		50.1328102081
1454PhosphorylationGLSGPRSSPSRCSGP
CCCCCCCCCCCCCCC		28.3328102081
1456PhosphorylationSGPRSSPSRCSGPNR
CCCCCCCCCCCCCCC		48.1128102081
1467PhosphorylationGPNRPQNSWRTQGGS
CCCCCCCCCCCCCCC		16.8228348404
1470PhosphorylationRPQNSWRTQGGSGRQ
CCCCCCCCCCCCCCC		25.8822210691
1488UbiquitinationLMEIQLSKVSFQHEV
EEEEEECEEEECCEE		50.95-
1545PhosphorylationNKFLYLHTSERMPRR
HHHHHHHCCCCCCCC		29.6828270605
1546PhosphorylationKFLYLHTSERMPRRA
HHHHHHCCCCCCCCC		16.6828270605
1555PhosphorylationRMPRRAHSNMLTIKA
CCCCCCHHCCEEEEE		23.9729514088
1629PhosphorylationPETRAQPSSPLEGQA
CCCCCCCCCCCCCCC		32.2926657352
1630PhosphorylationETRAQPSSPLEGQAE
CCCCCCCCCCCCCCC		39.9425159151
1641PhosphorylationGQAEGVETTGSQEAP
CCCCCEEECCCCCCC		33.7723663014
1642PhosphorylationQAEGVETTGSQEAPG
CCCCEEECCCCCCCC		22.7223663014
1644PhosphorylationEGVETTGSQEAPGGG
CCEEECCCCCCCCCC		23.8223663014
1653PhosphorylationEAPGGGHSPSPPDQQ
CCCCCCCCCCCCCCC		30.2825159151
1655PhosphorylationPGGGHSPSPPDQQPI
CCCCCCCCCCCCCCC		52.6723663014
1663PhosphorylationPPDQQPIYFREFRFT
CCCCCCCEEEEEEEC		11.8528450419
1857PhosphorylationGVAKAYDTVREGILD
HHHHHHHHHHHHHHH		14.58-
1933PhosphorylationDHALKWRSDSAQD--
HHCHHCCCCCCCC--		34.5024719451
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 ATG2A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATG2A_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 ATG2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WIPI4_HUMANWDR45physical
20562859
ATG2B_HUMANATG2Bphysical
20562859
DNJC7_HUMANDNAJC7physical
20562859
SMC1A_HUMANSMC1Aphysical
20562859
MAGD2_HUMANMAGED2physical
20562859
DNJB1_HUMANDNAJB1physical
20562859
PHB2_HUMANPHB2physical
20562859
HGH1_HUMANHGH1physical
20562859
ATG18_YEASTATG18physical
21887408
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 ATG2A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-1301, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-258, AND MASSSPECTROMETRY.

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