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
18PhosphoserinePRWKRHISEQLRRRD
CHHHHHHHHHHHHHH
17.1122135298
70PhosphoserineVPNRHEISPGHDGTW
CHHHHHHHCCCCCCC
23.1120068231
76PhosphothreonineISPGHDGTWNDNQLQ
HHCCCCCCCCHHHHH
27.4420873877
139PhosphoserineAECLQTISDLETECL
HHHHHHHHHHHHHHH
39.2626083323
247PhosphothreonineIEVIVDETSDHTEET
CEEEECCCCCCCCCC
34.6818669648
251PhosphothreonineVDETSDHTEETSPVR
ECCCCCCCCCCCEEE
40.2725627689
254PhosphothreonineTSDHTEETSPVRAIS
CCCCCCCCCEEEEEE
31.9018669648
255PhosphoserineSDHTEETSPVRAISR
CCCCCCCCEEEEEEE
25.3621659604
16381945
23193290
22135298
25627689
265PhosphothreonineRAISRAATKRLSQPA
EEEEECCCEEEEECC
18.7322135298
268PhosphoserineSRAATKRLSQPAGGL
EECCCEEEEECCCCC
6.2518669648
269PhosphoserineRAATKRLSQPAGGLL
ECCCEEEEECCCCCC
37.8420068231
270PhosphoserineAATKRLSQPAGGLLD
CCCEEEEECCCCCCC
36.1318669648
271PhosphoserineATKRLSQPAGGLLDS
CCEEEEECCCCCCCC
29.5118669648
278PhosphoserinePAGGLLDSITNIFGR
CCCCCCCCEEEECCC
31.1422135298
285PhosphoserineSITNIFGRRSVSSFP
CEEEECCCCCEEEEE
19.5617924679
287PhosphoserineTNIFGRRSVSSFPVP
EEECCCCCEEEEECC
25.6218669648
20068231
23186163
289PhosphoserineIFGRRSVSSFPVPQD
ECCCCCEEEEECCCC
27.7518669648
290PhosphoserineFGRRSVSSFPVPQDN
CCCCCEEEEECCCCC
31.2618669648
304PhosphoserineNVDTHPGSGKEVRVP
CEEEECCCCCEEEEC
51.6617924679
16381945
23193290
20068231
18988627
19060867
22135298
331PhosphoserineEVNAVQFSPGSRLLA
CEEEEEECCCCCEEE
15.9722135298
25627689
334UbiquitinlysineAVQFSPGSRLLATGG
EEEECCCCCEEEEEC
24.1221890473
350UbiquitinlysineDRRVKLWEVFGEKCE
CCEEEEEEEECCCEE
38.1021890473
433N6-acetyllysineGSHDRTLKLWDLRSK
EECCCEEEEEECCCC
47.0925953088
26051181
494UbiquitinlysineLLGKITALDLNPERT
CCCCEEEEEECCCCC
6.0321890473
513UbiquitinlysineCSRDDLLKVIDLRTN
EECCCEEEEEECCCC
44.432189047
513UbiquitinlysineCSRDDLLKVIDLRTN
EECCCEEEEEECCCC
44.4321890473

Disease-associated PTM Sites based on nsSNP

* Distance = the distance between SNP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SNP Related Disease Reference
290Phosphorylation300 (10)TArs2241880Crohn's disease: Crohn's disease17435756
290Phosphorylation300 (10)TArs2241880Crohn's disease: Crohn's disease20570966
290Phosphorylation300 (10)TArs2241880Crohn's disease: Crohn's disease22412388
304Phosphorylation307 (3)EKrs1866878--
304Phosphorylation300 (4)TArs2241880Crohn's disease: Crohn's disease17435756
304Phosphorylation300 (4)TArs2241880Crohn's disease: Crohn's disease20570966
304Phosphorylation300 (4)TArs2241880Crohn's disease: Crohn's disease22412388

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.
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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