ACSL1_HUMAN - dbPTM
ACSL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACSL1_HUMAN
UniProt AC P33121
Protein Name Long-chain-fatty-acid--CoA ligase 1
Gene Name ACSL1
Organism Homo sapiens (Human).
Sequence Length 698
Subcellular Localization Mitochondrion outer membrane
Single-pass type III membrane protein. Peroxisome membrane
Single-pass type III membrane protein. Microsome membrane
Single-pass type III membrane protein. Endoplasmic reticulum membrane
Single-pass type III membrane prote
Protein Description Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate..
Protein Sequence MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQSVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV
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
1Acetylation-------MQAHELFR
-------CCHHHHHH		7.78-
9NitrationQAHELFRYFRMPELV
CHHHHHHHHCCHHHC		6.55-
9Nitrated tyrosineQAHELFRYFRMPELV
CHHHHHHHHCCHHHC		6.55-
21PhosphorylationELVDFRQYVRTLPTN
HHCCHHHHHHHCCCC		6.4022210691
24PhosphorylationDFRQYVRTLPTNTLM
CHHHHHHHCCCCCCC		27.3522210691
46PhosphorylationLTTFWYATRPKPLKP
HHHHHHHCCCCCCCC		31.6322210691
58PhosphorylationLKPPCDLSMQSVEVA
CCCCCCCEECEEEEC		11.0920068231
61PhosphorylationPCDLSMQSVEVAGSG
CCCCEECEEEECCCC		16.1720068231
67PhosphorylationQSVEVAGSGGARRSA
CEEEECCCCCCCHHH		25.0620068231
84PhosphorylationDSDEPLVYFYDDVTT
CCCCCEEEEECCHHH		12.2421082442
103PhosphorylationFQRGIQVSNNGPCLG
HHCCEECCCCCCCCC		14.2720068231
111PhosphorylationNNGPCLGSRKPDQPY
CCCCCCCCCCCCCCC		24.9620068231
122PhosphorylationDQPYEWLSYKQVAEL
CCCCCCCCHHHHHHH		31.2173680251
135O-linked_GlycosylationELSECIGSALIQKGF
HHHHHHHHHHHHCCC		10.45UniProtKB CARBOHYD
188PhosphorylationLGNEAITYIVNKAEL
CCCHHHHHHEECCEE		9.2146158043
207AcetylationVDKPEKAKLLLEGVE
ECCHHHHHHHHHHHH		51.22-
207 (in isoform 2)Ubiquitination-51.22-
216UbiquitinationLLEGVENKLIPGLKI
HHHHHHCCCCCCCEE		34.0021890473
216 (in isoform 2)Ubiquitination-34.0021890473
216 (in isoform 1)Ubiquitination-34.0021890473
216UbiquitinationLLEGVENKLIPGLKI
HHHHHHCCCCCCCEE		34.0021890473
222UbiquitinationNKLIPGLKIIVVMDA
CCCCCCCEEEEEEEC		35.98-
230PhosphorylationIIVVMDAYGSELVER
EEEEEECHHHHHHHH		19.5422673903
232PhosphorylationVVMDAYGSELVERGQ
EEEECHHHHHHHHHH		18.3255991913
279PhosphorylationVICFTSGTTGNPKGA
EEEEECCCCCCCCCC		31.1526437602
356 (in isoform 2)Ubiquitination-48.1421890473
356UbiquitinationRLLMDDLKVLQPTVF
HHHHHHHHHHCCCHH		48.1421906983
356AcetylationRLLMDDLKVLQPTVF
HHHHHHHHHHCCCHH		48.1425038526
356 (in isoform 1)Ubiquitination-48.1421890473
386UbiquitinationGQANTTLKRWLLDFA
CCCHHHHHHHHHHHH		39.16-
386AcetylationGQANTTLKRWLLDFA
CCCHHHHHHHHHHHH		39.162402811
394PhosphorylationRWLLDFASKRKEAEL
HHHHHHHHHHCHHHH		32.7420058876
395 (in isoform 1)Ubiquitination-65.1521890473
395UbiquitinationWLLDFASKRKEAELR
HHHHHHHHHCHHHHH		65.1521890473
395UbiquitinationWLLDFASKRKEAELR
HHHHHHHHHCHHHHH		65.1521890473
3952-HydroxyisobutyrylationWLLDFASKRKEAELR
HHHHHHHHHCHHHHH		65.15-
395AcetylationWLLDFASKRKEAELR
HHHHHHHHHCHHHHH		65.157623885
395 (in isoform 2)Ubiquitination-65.1521890473
410PhosphorylationSGIIRNNSLWDRLIF
CCCCCCCCHHHHHHH		34.0935088415
419UbiquitinationWDRLIFHKVQSSLGG
HHHHHHHHHHHHCCC		31.0821890473
419 (in isoform 2)Ubiquitination-31.0821890473
419UbiquitinationWDRLIFHKVQSSLGG
HHHHHHHHHHHHCCC		31.0821890473
419 (in isoform 1)Ubiquitination-31.0821890473
422PhosphorylationLIFHKVQSSLGGRVR
HHHHHHHHHCCCCEE		30.4425072903
423PhosphorylationIFHKVQSSLGGRVRL
HHHHHHHHCCCCEEE		17.5925072903
433PhosphorylationGRVRLMVTGAAPVSA
CCEEEEEECCCCCHH		13.7222673903
439PhosphorylationVTGAAPVSATVLTFL
EECCCCCHHHHHHHH		19.7081112075
441PhosphorylationGAAPVSATVLTFLRA
CCCCCHHHHHHHHHH		14.4522673903
444PhosphorylationPVSATVLTFLRAALG
CCHHHHHHHHHHHHC		19.1122673903
522 (in isoform 2)Ubiquitination-45.8821890473
532 (in isoform 1)Ubiquitination-60.0221890473
532UbiquitinationKTAEALDKDGWLHTG
HHHHHHCCCCCEECC		60.0221890473
532UbiquitinationKTAEALDKDGWLHTG
HHHHHHCCCCCEECC		60.0221890473
567PhosphorylationFKLAQGEYIAPEKIE
HHHHCCCEECHHHHE		14.8125884760
577PhosphorylationPEKIENIYMRSEPVA
HHHHEEEECCCCCEE		9.6920561283
620PhosphorylationQKRGFEGSFEELCRN
HHCCCCCCHHHHHCC		23.4528258704
622 (in isoform 2)Ubiquitination-52.32-
632AcetylationCRNKDVKKAILEDMV
HCCHHHHHHHHHHHH		40.27-
633 (in isoform 2)Ubiquitination-13.09-
638 (in isoform 2)Ubiquitination-1.06-
643UbiquitinationEDMVRLGKDSGLKPF
HHHHHHCCCCCCCCH		54.00-
664PhosphorylationTLHPELFSIDNGLLT
EECHHHHEECCCCCC		41.4869007009
671PhosphorylationSIDNGLLTPTMKAKR
EECCCCCCCCCCCCC		23.0428857561
673PhosphorylationDNGLLTPTMKAKRPE
CCCCCCCCCCCCCHH		26.5228857561
683 (in isoform 2)Phosphorylation-53.5827642862
684PhosphorylationKRPELRNYFRSQIDD
CCHHHHHHHHHHHHH		8.2430206219
687PhosphorylationELRNYFRSQIDDLYS
HHHHHHHHHHHHHHH		22.9130206219
687 (in isoform 2)Ubiquitination-22.91-
693PhosphorylationRSQIDDLYSTIKV--
HHHHHHHHHHCCC--		15.6828258704
694PhosphorylationSQIDDLYSTIKV---
HHHHHHHHHCCC---		30.8425693802
695PhosphorylationQIDDLYSTIKV----
HHHHHHHHCCC----		15.9728857561
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 ACSL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACSL1_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 ACSL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCR_HUMANNR3C2physical
21988832
BDH_HUMANBDH1physical
27173435
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
DB00131Adenosine monophosphate
DB00171Adenosine triphosphate
Regulatory Network of ACSL1_HUMAN

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Related Literatures of Post-Translational Modification

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