ATG9A_HUMAN - dbPTM
ATG9A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATG9A_HUMAN
UniProt AC Q7Z3C6
Protein Name Autophagy-related protein 9A
Gene Name ATG9A
Organism Homo sapiens (Human).
Sequence Length 839
Subcellular Localization Cytoplasmic vesicle, autophagosome membrane
Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane
Multi-pass membrane protein. Late endosome membrane
Multi-pass membrane protein. Endoplasmic reticulum membrane
Multi-pass membrane
Protein Description Involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a key role in the organization of the preautophagosomal structure/phagophore assembly site (PAS), the nucleating site for formation of the sequestering vesicle. Cycles between a juxta-nuclear trans-Golgi network compartment and late endosomes. Nutrient starvation induces accumulation on autophagosomes. Starvation-dependent trafficking requires ULK1, ATG13 and SUPT20H..
Protein Sequence MAQFDTEYQRLEASYSDSPPGEEDLLVHVAEGSKSPWHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFANKMVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEAVFFTRGLKYNFELILFWGPGSLFLNEWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNRGYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVLAVEHVLTTVTLLGVTVTVCRSFIPDQHMVFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQHGHPQWLSAGQTEASVYQQAEDGKTELSLMHFAITNPGWQPPRESTAFLGFLKEQVQRDGAAASLAQGGLLPENALFTSIQSLQSESEPLSLIANVVAGSSCRGPPLPRDLQGSRHRAEVASALRSFSPLQPGQAPTGRAHSTMTGSGVDARTASSGSSVWEGQLQSLVLSEYASTEMSLHALYMHQLHKQQAQAEPERHVWHRRESDESGESAPDEGGEGARAPQSIPRSASYPCAAPRPGAPETTALHGGFQRRYGGITDPGTVPRVPSHFSRLPLGGWAEDGQSASRHPEPVPEEGSEDELPPQVHKV
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
2Acetylation------MAQFDTEYQ
------CCCCCHHHH		20.8122223895
8PhosphorylationMAQFDTEYQRLEASY
CCCCCHHHHHHHHHC		10.8827642862
14PhosphorylationEYQRLEASYSDSPPG
HHHHHHHHCCCCCCC		18.7822167270
15PhosphorylationYQRLEASYSDSPPGE
HHHHHHHCCCCCCCC		24.4422167270
16PhosphorylationQRLEASYSDSPPGEE
HHHHHHCCCCCCCCC		29.1730266825
18PhosphorylationLEASYSDSPPGEEDL
HHHHCCCCCCCCCCE		27.3625159151
33PhosphorylationLVHVAEGSKSPWHHI
EEEEECCCCCCCHHH		22.8223403867
99N-linked_GlycosylationLFANKMVNHSLHPTE
HHCCCCCCCCCCCCC		18.6116940348
164 (in isoform 2)Ubiquitination-10.6921890473
192UbiquitinationARIVQTQKEHQICIH
HHHHHHHHHHCEEEE		61.63-
2002-HydroxyisobutyrylationEHQICIHKRELTELD
HHCEEEECCCCCHHH		27.88-
209PhosphorylationELTELDIYHRILRFQ
CCCHHHHHHHHHHHC		5.68-
225 (in isoform 3)Ubiquitination-34.6921890473
225 (in isoform 1)Ubiquitination-34.6921890473
225UbiquitinationYMVALVNKSLLPLRF
HHHHHHCCCCCCCCC		34.6921890473
225UbiquitinationYMVALVNKSLLPLRF
HHHHHHCCCCCCCCC		34.6921890473
518O-linked_GlycosylationEVVGVGDTCSFAQMD
EEEEECCCCCCHHCC		12.2429237092
520 (in isoform 2)Ubiquitination-26.2121890473
536PhosphorylationHGHPQWLSAGQTEAS
HCCCHHHCCCCCEEH		27.6529449344
540PhosphorylationQWLSAGQTEASVYQQ
HHHCCCCCEEHHEHH		32.3829449344
543PhosphorylationSAGQTEASVYQQAED
CCCCCEEHHEHHHHC		18.3529449344
545PhosphorylationGQTEASVYQQAEDGK
CCCEEHHEHHHHCCC		7.75-
556PhosphorylationEDGKTELSLMHFAIT
HCCCCEEEEEEEEEC		19.88-
581 (in isoform 1)Ubiquitination-43.7921890473
581UbiquitinationTAFLGFLKEQVQRDG
HHHHHHHHHHHHHCC		43.7921890473
581UbiquitinationTAFLGFLKEQVQRDG
HHHHHHHHHHHHHCC		43.7921890473
642PhosphorylationLPRDLQGSRHRAEVA
CCCCCCCCHHHHHHH		16.3821406692
645MethylationDLQGSRHRAEVASAL
CCCCCHHHHHHHHHH		31.19-
650PhosphorylationRHRAEVASALRSFSP
HHHHHHHHHHHHCCC		32.7726657352
654PhosphorylationEVASALRSFSPLQPG
HHHHHHHHCCCCCCC		30.8123401153
656PhosphorylationASALRSFSPLQPGQA
HHHHHHCCCCCCCCC		26.4125159151
665PhosphorylationLQPGQAPTGRAHSTM
CCCCCCCCCCCCCCC		42.1729449344
670PhosphorylationAPTGRAHSTMTGSGV
CCCCCCCCCCCCCCC		20.9129255136
671PhosphorylationPTGRAHSTMTGSGVD
CCCCCCCCCCCCCCC		14.6429255136
673PhosphorylationGRAHSTMTGSGVDAR
CCCCCCCCCCCCCCC		28.4329255136
675PhosphorylationAHSTMTGSGVDARTA
CCCCCCCCCCCCCCC		26.8629255136
681PhosphorylationGSGVDARTASSGSSV
CCCCCCCCCCCCCCH		32.3924043423
683PhosphorylationGVDARTASSGSSVWE
CCCCCCCCCCCCHHH		34.3224043423
684PhosphorylationVDARTASSGSSVWEG
CCCCCCCCCCCHHHH		39.9824043423
686PhosphorylationARTASSGSSVWEGQL
CCCCCCCCCHHHHHH		24.5424043423
687PhosphorylationRTASSGSSVWEGQLQ
CCCCCCCCHHHHHHH		34.4724043423
695PhosphorylationVWEGQLQSLVLSEYA
HHHHHHHHHHHHHHC		29.1024043423
699PhosphorylationQLQSLVLSEYASTEM
HHHHHHHHHHCCCHH		22.5324043423
701PhosphorylationQSLVLSEYASTEMSL
HHHHHHHHCCCHHHH		11.5024043423
703PhosphorylationLVLSEYASTEMSLHA
HHHHHHCCCHHHHHH		24.8124043423
704PhosphorylationVLSEYASTEMSLHAL
HHHHHCCCHHHHHHH		27.7724043423
707PhosphorylationEYASTEMSLHALYMH
HHCCCHHHHHHHHHH		15.6924043423
712PhosphorylationEMSLHALYMHQLHKQ
HHHHHHHHHHHHHHH		8.0424043423
735PhosphorylationHVWHRRESDESGESA
CCCCCCCCCCCCCCC		44.8829255136
738PhosphorylationHRRESDESGESAPDE
CCCCCCCCCCCCCCC		53.5023401153
741PhosphorylationESDESGESAPDEGGE
CCCCCCCCCCCCCCC		48.9429255136
755PhosphorylationEGARAPQSIPRSASY
CCCCCCCCCCCCCCC		33.2423927012
759PhosphorylationAPQSIPRSASYPCAA
CCCCCCCCCCCCCCC		19.0624972180
761PhosphorylationQSIPRSASYPCAAPR
CCCCCCCCCCCCCCC		30.7424972180
762PhosphorylationSIPRSASYPCAAPRP
CCCCCCCCCCCCCCC		11.3121712546
774PhosphorylationPRPGAPETTALHGGF
CCCCCCCCCCCCCCC		19.1326074081
775PhosphorylationRPGAPETTALHGGFQ
CCCCCCCCCCCCCCH		26.0926074081
784MethylationLHGGFQRRYGGITDP
CCCCCHHHCCCCCCC		24.54-
785PhosphorylationHGGFQRRYGGITDPG
CCCCHHHCCCCCCCC		23.1521722762
793PhosphorylationGGITDPGTVPRVPSH
CCCCCCCCCCCCCCC		32.5024719451
799PhosphorylationGTVPRVPSHFSRLPL
CCCCCCCCCCCCCCC		34.0224719451
815PhosphorylationGWAEDGQSASRHPEP
CCCCCCCCCCCCCCC		33.4725850435
817PhosphorylationAEDGQSASRHPEPVP
CCCCCCCCCCCCCCC		36.0527251275
828PhosphorylationEPVPEEGSEDELPPQ
CCCCCCCCCCCCCCC		45.1929255136
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
8YPhosphorylationKinaseSRCP12931
PSP
14SPhosphorylationKinaseULK1O75385
PSP
15YPhosphorylationKinaseSRCP12931
PSP
761SPhosphorylationKinasePRKAA1Q13131
GPS
761SPhosphorylationKinaseULK1O75385
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATG9A_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 ATG9A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KRA42_HUMANKRTAP4-2physical
25416956
LONF1_HUMANLONRF1physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
SP20H_HUMANSUPT20Hphysical
19893488
MYH9_HUMANMYH9physical
21169990
1433Z_HUMANYWHAZphysical
25770209
ZFN2B_HUMANZFAND2Bphysical
28514442
HERP1_HUMANHERPUD1physical
28514442
UBXN7_HUMANUBXN7physical
28514442
NPL4_HUMANNPLOC4physical
28514442
AMFR_HUMANAMFRphysical
28514442
GHDC_HUMANGHDCphysical
28514442
PSD11_HUMANPSMD11physical
28514442
TERA_HUMANVCPphysical
28514442
BI1_HUMANTMBIM6physical
28514442
PSMD6_HUMANPSMD6physical
28514442
UFD1_HUMANUFD1Lphysical
28514442
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 ATG9A_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Starvation and ULK1-dependent cycling of mammalian Atg9 between theTGN and endosomes.";
Young A.R., Chan E.Y., Hu X.W., Kochl R., Crawshaw S.G., High S.,Hailey D.W., Lippincott-Schwartz J., Tooze S.A.;
J. Cell Sci. 119:3888-3900(2006).
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION AT ASN-99.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-18; SER-656;SER-735; SER-738; SER-741 AND SER-828, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656, AND MASSSPECTROMETRY.
"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-828, AND MASSSPECTROMETRY.

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