A16L1_HUMAN - dbPTM
A16L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID A16L1_HUMAN
UniProt AC Q676U5
Protein Name Autophagy-related protein 16-1
Gene Name ATG16L1
Organism Homo sapiens (Human).
Sequence Length 607
Subcellular Localization Cytoplasm . Preautophagosomal structure membrane
Peripheral membrane protein. Recruited to omegasomes membranes by WIPI2. Omegasomes are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Localized to preautoph
Protein Description Plays an essential role in autophagy: interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a membrane-bound activated form of LC3 named LC3-II. Thereby, controls the elongation of the nascent autophagosomal membrane. [PubMed: 24553140]
Protein Sequence MSSGLRAADFPRWKRHISEQLRRRDRLQRQAFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRVPATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSCNDIVCTEQCVMSGHFDKKIRFWDIRSESIVREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPGFKCGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSKQHSSSINAVAWSPSGSHVVSVDKGCKAVLWAQY
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
2Phosphorylation------MSSGLRAAD
------CCCCCCCCC		32.8729514088
3Phosphorylation-----MSSGLRAADF
-----CCCCCCCCCC		40.3129514088
18PhosphorylationPRWKRHISEQLRRRD
HHHHHHHHHHHHHHH		17.11-
39PhosphorylationFEEIILQYNKLLEKS
HHHHHHHHHHHHCCC		15.7228064214
45UbiquitinationQYNKLLEKSDLHSVL
HHHHHHCCCCHHHHH		49.60-
55UbiquitinationLHSVLAQKLQAEKHD
HHHHHHHHHHHHHCC		36.64-
60UbiquitinationAQKLQAEKHDVPNRH
HHHHHHHHCCCCCCC		48.39-
70PhosphorylationVPNRHEISPGHDGTW
CCCCCCCCCCCCCCC		23.1125159151
76PhosphorylationISPGHDGTWNDNQLQ
CCCCCCCCCCHHHHH		27.4425850435
91UbiquitinationEMAQLRIKHQEELTE
HHHHHHHHHHHHHHH		32.57-
107 (in isoform 5)Phosphorylation-9.0725849741
121 (in isoform 5)Phosphorylation-54.7029414761
124 (in isoform 5)Phosphorylation-4.8225849741
126 (in isoform 5)Phosphorylation-4.7729116813
127 (in isoform 5)Phosphorylation-29.2329116813
139PhosphorylationAECLQTISDLETECL
HHHHHHHHHHHHHHH		39.2626083323
151MethylationECLDLRTKLCDLERA
HHHHHHHHHHCHHHH		40.46-
183PhosphorylationLEGKLRKTTEENQEL
HHCCCCCCHHHHHHH		32.7624114839
184PhosphorylationEGKLRKTTEENQELV
HCCCCCCHHHHHHHH		44.3224114839
192PhosphorylationEENQELVTRWMAEKA
HHHHHHHHHHHHHHH		31.1024114839
198UbiquitinationVTRWMAEKAQEANRL
HHHHHHHHHHHHHHC		45.92-
222UbiquitinationRRQARLQKELAEAAK
HHHHHHHHHHHHHHC		60.32-
247PhosphorylationIEVIVDETSDHTEET
CEEEEECCCCCCCCC		34.6830266825
248PhosphorylationEVIVDETSDHTEETS
EEEEECCCCCCCCCC		25.9130266825
251PhosphorylationVDETSDHTEETSPVR
EECCCCCCCCCCHHH		40.2725849741
251 (in isoform 2)Phosphorylation-40.2725849741
254PhosphorylationTSDHTEETSPVRAIS
CCCCCCCCCHHHHHH		31.9030266825
255PhosphorylationSDHTEETSPVRAISR
CCCCCCCCHHHHHHH		25.3630266825
265PhosphorylationRAISRAATKRLSQPA
HHHHHHHHHHHCCCC		18.73-
265 (in isoform 2)Phosphorylation-18.7329414761
268 (in isoform 2)Phosphorylation-6.2525849741
269PhosphorylationRAATKRLSQPAGGLL
HHHHHHHCCCCCHHH		37.8426846344
270 (in isoform 2)Phosphorylation-36.1329116813
271 (in isoform 2)Phosphorylation-29.5129116813
278PhosphorylationPAGGLLDSITNIFGR
CCCHHHHHHHHHCCC		31.1429255136
280PhosphorylationGGLLDSITNIFGRRS
CHHHHHHHHHCCCCC		26.6429255136
287PhosphorylationTNIFGRRSVSSFPVP
HHHCCCCCCCCCCCC		25.6229255136
289PhosphorylationIFGRRSVSSFPVPQD
HCCCCCCCCCCCCCC		27.7530266825
290PhosphorylationFGRRSVSSFPVPQDN
CCCCCCCCCCCCCCC		31.2630266825
300PhosphorylationVPQDNVDTHPGSGKE
CCCCCCCCCCCCCCE		26.2030266825
304PhosphorylationNVDTHPGSGKEVRVP
CCCCCCCCCCEEEEC		51.6623927012
331PhosphorylationEVNAVQFSPGSRLLA
CEEEEEECCCCCEEE		15.9725159151
334 (in isoform 4)Ubiquitination-24.1221890473
350UbiquitinationDRRVKLWEVFGEKCE
CHHHHHHHHHCCCCE		38.1021890473
394PhosphorylationDFASRIWTVDDYRLR
CCHHHCEEECCHHHH		16.2223403867
433AcetylationGSHDRTLKLWDLRSK
CCCCCHHHHHHCCCC		47.0925953088
494 (in isoform 2)Ubiquitination-6.0321890473
513 (in isoform 1)Ubiquitination-44.4321890473
513UbiquitinationCSRDDLLKVIDLRTN
ECHHHHHHHHHHCCH		44.4321890473
523UbiquitinationDLRTNAIKQTFSAPG
HHCCHHHHHHCCCCC		40.66-
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
139SPhosphorylationKinaseCK2-Uniprot
278SPhosphorylationKinaseCHUKO15111
GPS
278SPhosphorylationKinaseULK1O75385
PSP
-KUbiquitinationE3 ubiquitin ligaseGANQ9H2C0
PMID:30770803
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
139SPhosphorylation

26083323
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 A16L1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GAN_HUMANGANphysical
20562859
ATG5_HUMANATG5physical
20562859
ADAS_HUMANAGPSphysical
20562859
TCPH_HUMANCCT7physical
20562859
TCPB_HUMANCCT2physical
20562859
TCPG_HUMANCCT3physical
20562859
SNPC4_HUMANSNAPC4physical
20562859
ATG5_HUMANATG5physical
22342342
CLH1_HUMANCLTCphysical
20639872
HSP74_HUMANHSPA4physical
20639872
FCGRN_HUMANFCGRTphysical
20639872
ATG5_HUMANATG5physical
20639872
AP2M1_HUMANAP2M1physical
20639872
RB33B_HUMANRAB33Bphysical
18448665
RAB3D_HUMANRAB3Dphysical
18448665
RB33A_HUMANRAB33Aphysical
18448665
RAB35_HUMANRAB35physical
18448665
ATG5_HUMANATG5physical
18448665
A4_HUMANAPPphysical
21832049
RBCC1_HUMANRB1CC1physical
24100292
ACK1_HUMANTNK2physical
24413169
RBCC1_HUMANRB1CC1physical
23262492
ATG5_HUMANATG5physical
23262492
ATG13_HUMANATG13physical
23262492
ULK1_HUMANULK1physical
23262492
TMM59_HUMANTMEM59physical
23376921
NOD2_HUMANNOD2physical
23376921
TLR2_HUMANTLR2physical
23376921
T3JAM_HUMANTRAF3IP3physical
23376921
DEDD2_HUMANDEDD2physical
23376921
RBCC1_HUMANRB1CC1physical
24954904
A16L1_HUMANATG16L1physical
24086718
NOD1_HUMANNOD1physical
19898471
NOD2_HUMANNOD2physical
19898471
ATG5_HUMANATG5physical
25484072
IRGM_HUMANIRGMphysical
25891078
TRI16_HUMANTRIM16physical
27693506
Drug and Disease Associations
Kegg Disease
H00286 Crohn's disease
OMIM Disease
611081Inflammatory bowel disease 10 (IBD10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of A16L1_HUMAN

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Related Literatures of Post-Translational Modification
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-287, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287; SER-290 ANDSER-304, AND MASS SPECTROMETRY.

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