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Protein Page:
ATG13 (human)

Overview
ATG13 an autophagy factor required for autophagosome formation. 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. 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 formation. Phosphorylated by ULK1 and ULK2. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. Part of a complex consisting of ATG13, ULK1 and RB1CC1. Interacts with ATG101. Interacts with ULK1 and -2 via C-terminus. Three isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Vesicle protein; Autophagy
Chromosomal Location of Human Ortholog: 11p11.2
Cellular Component: cytosol
Molecular Function: protein binding; protein kinase binding
Biological Process: autophagic vacuole formation
Reference #:  O75143 (UniProtKB)
Alt. Names/Synonyms: ATG13; Autophagy-related protein 13; FLJ20698; KIAA0652
Gene Symbols: ATG13
Molecular weight: 56,572 Da
Basal Isoelectric point: 4.98  Predict pI for various phosphorylation states
CST Pathways:  Autophagy Signaling  |  mTOR Signaling  |  PI3K/Akt Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ATG13

Protein Structure Not Found.


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Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S7-p _METDLNsQDRKDLD
0 1 T24 IKFFALKTVQVIVQA
0 1 S141-p VTPAYRLsRKQGHEY
0 1 T204-p STRQFERtPPIMGII
0 1 S334-p RLATCTPsDRTHCAA
2 2 S355-p DTETVSNssEGRAsP
0 1 S356-p TETVSNssEGRAsPH
0 12 S361-p NssEGRAsPHDVLET
  mouse

 
S7 _METELSSQDRKDLD
T24-p IKFFALKtVQVIVQA
S141 VTPAYRLSRKQGHEY
T204 STRQFERTPPIMGII
S333 RLVMHMPSDGTHCAA
S354 DTETVSNSSEGRAsP
S355 TETVSNSSEGRAsPH
S360-p NSSEGRAsPHDILET
  rat

 
S7 _METDLSSQDRKDLD
T24 IKFFALKTVQVIVQA
S141 VTPAYRLSRKQGHEY
T204 STRQFERTPPIMGII
S296 RLVVHMPSDGTHCAA
S317 DTETVSNSSEGRAsP
S318 TETVSNSSEGRAsPH
S323-p NSSEGRAsPHDILET
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