ACNT1_MOUSE - dbPTM
ACNT1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACNT1_MOUSE
UniProt AC A2AKK5
Protein Name Acyl-coenzyme A amino acid N-acyltransferase 1 {ECO:0000303|PubMed:17116739}
Gene Name Acnat1 {ECO:0000312|EMBL:ABE98441.1}
Organism Mus musculus (Mouse).
Sequence Length 416
Subcellular Localization Peroxisome .
Protein Description Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine..
Protein Sequence MMIKLIATPSNALVDEPVSIRATGLPPSQIVTIKATVKDENDNVFQSQAFYKTNEAGEVDLEKTPALGGDYVGVHPMGLFFSLKPKKAFHRLMKKDVMNSPFCICLDLYDSVNWLETVRIPSKASQRVQRWFVGPGVKREQIQEGRVRGALFLPPGKGPFPGIIDLFGVIGGLVEFRASLLASHGFAVLALAYFAYKDLPEKLQEVDLEYFEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMACYLKQVIATVCINGATTTTAVPLRYQDLVVTPIQQALERMEVHVSGAVCFRHTTQYLQNKNILPVEKAQGKILFIVGENDELLDSKLHAQRAMDRLRRHGRSSGRMLAYPGAGHLIEPPYSPLCFASWQPVLGRPMCFGGDLMAHAAAQEHSWREIQKFFRKHLLQSGSKL
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
10PhosphorylationIKLIATPSNALVDEP
EEEEECCCCCCCCCC
30.3123140645
38AcetylationVTIKATVKDENDNVF
EEEEEEECCCCCCEE
55.78-
38UbiquitinationVTIKATVKDENDNVF
EEEEEEECCCCCCEE
55.78-
125PhosphorylationVRIPSKASQRVQRWF
CCCCCHHHHHHHHHH
23.43-
138AcetylationWFVGPGVKREQIQEG
HHCCCCCCHHHHHCC
57.01-
138UbiquitinationWFVGPGVKREQIQEG
HHCCCCCCHHHHHCC
57.01-
233PhosphorylationQPGIGVISTSKGAEI
CCCEEEEECCCCHHH
24.9929472430
234PhosphorylationPGIGVISTSKGAEIG
CCEEEEECCCCHHHH
24.2729472430
235PhosphorylationGIGVISTSKGAEIGL
CEEEEECCCCHHHHH
23.4629472430
305SuccinylationTTQYLQNKNILPVEK
HHHHHHCCCCCCCCC
32.1924315375
312UbiquitinationKNILPVEKAQGKILF
CCCCCCCCCCCCEEE
46.3622790023
331AcetylationNDELLDSKLHAQRAM
CHHHHHHHHHHHHHH
43.9123954790
331UbiquitinationNDELLDSKLHAQRAM
CHHHHHHHHHHHHHH
43.9122790023
403AcetylationHSWREIQKFFRKHLL
CCHHHHHHHHHHHHH
52.73-
407AcetylationEIQKFFRKHLLQSGS
HHHHHHHHHHHHHCC
33.19-
414PhosphorylationKHLLQSGSKL-----
HHHHHHCCCC-----
35.71-

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 ACNT1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACNT1_MOUSE !!

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 ACNT1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACNT1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACNT1_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND MASS SPECTROMETRY.

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