ACSL5_HUMAN - dbPTM
ACSL5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACSL5_HUMAN
UniProt AC Q9ULC5
Protein Name Long-chain-fatty-acid--CoA ligase 5
Gene Name ACSL5
Organism Homo sapiens (Human).
Sequence Length 683
Subcellular Localization Mitochondrion. Endoplasmic reticulum. Mitochondrion outer membrane
Single-pass type III membrane protein. Endoplasmic reticulum membrane
Single-pass type III membrane protein.
Protein Description Acyl-CoA synthetases (ACSL) activate long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity). Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity). It was suggested that it may also stimulate fatty acid oxidation (By similarity). At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL. May have a role in the survival of glioma cells..
Protein Sequence MLFIFNFLFSPLPTPALICILTFGAAIFLWLITRPQPVLPLLDLNNQSVGIEGGARKGVSQKNNDLTSCCFSDAKTMYEVFQRGLAVSDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGSCLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVHIVNKADIAMVICDTPQKALVLIGNVEKGFTPSLKVIILMDPFDDDLKQRGEKSGIEILSLYDAENLGKEHFRKPVPPSPEDLSVICFTSGTTGDPKGAMITHQNIVSNAAAFLKCVEHAYEPTPDDVAISYLPLAHMFERIVQAVVYSCGARVGFFQGDIRLLADDMKTLKPTLFPAVPRLLNRIYDKVQNEAKTPLKKFLLKLAVSSKFKELQKGIIRHDSFWDKLIFAKIQDSLGGRVRVIVTGAAPMSTSVMTFFRAAMGCQVYEAYGQTECTGGCTFTLPGDWTSGHVGVPLACNYVKLEDVADMNYFTVNNEGEVCIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSQPVLQIFVHGESLRSSLVGVVVPDTDVLPSFAAKLGVKGSFEELCQNQVVREAILEDLQKIGKESGLKTFEQVKAIFLHPEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLYEHIQD
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
28 (in isoform 3)Phosphorylation-3.2526657352
32 (in isoform 3)Phosphorylation-1.7617192257
62UbiquitinationARKGVSQKNNDLTSC
CCCCCCCCCCCCCHH
50.6527667366
96PhosphorylationDNGPCLGYRKPNQPY
CCCCCCCCCCCCCCC
11.52119477
98UbiquitinationGPCLGYRKPNQPYRW
CCCCCCCCCCCCCEE
39.5827667366
107O-linked_GlycosylationNQPYRWLSYKQVSDR
CCCCEEEEEEEHHCH
24.2730397120
117PhosphorylationQVSDRAEYLGSCLLH
EHHCHHHHHHHHHHC
18.5129759185
118UbiquitinationVSDRAEYLGSCLLHK
HHCHHHHHHHHHHCC
2.8327667366
127PhosphorylationSCLLHKGYKSSPDQF
HHHHCCCCCCCHHHE
16.7029759185
154UbiquitinationISELACYTYSMVAVP
HHHHHHHHHCCCEEE
14.7027667366
163PhosphorylationSMVAVPLYDTLGPEA
CCCEEEHHHCCCHHH
10.7912306821
200 (in isoform 1)Ubiquitination-55.8521890473
200UbiquitinationVLIGNVEKGFTPSLK
EEECCCCCCCCCCEE
55.8521906983
220 (in isoform 1)Ubiquitination-44.9721890473
220UbiquitinationDPFDDDLKQRGEKSG
CCCCHHHHHHCHHCC
44.9721906983
225 (in isoform 1)Ubiquitination-57.7321890473
225UbiquitinationDLKQRGEKSGIEILS
HHHHHCHHCCEEEEE
57.7321906983
234PhosphorylationGIEILSLYDAENLGK
CEEEEEEECHHHHCC
15.1024425373
241UbiquitinationYDAENLGKEHFRKPV
ECHHHHCCHHCCCCC
51.7021906983
241"N6,N6-dimethyllysine"YDAENLGKEHFRKPV
ECHHHHCCHHCCCCC
51.70-
241 (in isoform 1)Ubiquitination-51.7021890473
241MethylationYDAENLGKEHFRKPV
ECHHHHCCHHCCCCC
51.70-
246UbiquitinationLGKEHFRKPVPPSPE
HCCHHCCCCCCCCHH
49.8023503661
256UbiquitinationPPSPEDLSVICFTSG
CCCHHHCEEEEEECC
23.0423503661
256 (in isoform 3)Ubiquitination-23.04-
276UbiquitinationKGAMITHQNIVSNAA
CCCEEECHHHHHHHH
32.4723503661
276 (in isoform 3)Ubiquitination-32.47-
281UbiquitinationTHQNIVSNAAAFLKC
ECHHHHHHHHHHHHH
23.7823503661
281 (in isoform 3)Ubiquitination-23.78-
293PhosphorylationLKCVEHAYEPTPDDV
HHHHHHHCCCCCCHH
25.0925332170
296PhosphorylationVEHAYEPTPDDVAIS
HHHHCCCCCCHHHHH
27.6625332170
297 (in isoform 3)Ubiquitination-46.66-
297UbiquitinationEHAYEPTPDDVAISY
HHHCCCCCCHHHHHH
46.6623503661
302UbiquitinationPTPDDVAISYLPLAH
CCCCHHHHHHHHHHH
2.5323503661
320PhosphorylationRIVQAVVYSCGARVG
HHHHHHHHHCCCCCE
7.5225332170
341UbiquitinationRLLADDMKTLKPTLF
HHHHHHHHHHCCCHH
58.6723503661
344UbiquitinationADDMKTLKPTLFPAV
HHHHHHHCCCHHHHH
40.9821906983
344 (in isoform 1)Ubiquitination-40.9821890473
359PhosphorylationPRLLNRIYDKVQNEA
HHHHHHHHHHHHHHC
13.3828152594
361UbiquitinationLLNRIYDKVQNEAKT
HHHHHHHHHHHHCCC
28.8427667366
361AcetylationLLNRIYDKVQNEAKT
HHHHHHHHHHHHCCC
28.84-
367UbiquitinationDKVQNEAKTPLKKFL
HHHHHHCCCHHHHHH
44.4927667366
380PhosphorylationFLLKLAVSSKFKELQ
HHHHHHHHHHHHHHH
23.3946158103
381PhosphorylationLLKLAVSSKFKELQK
HHHHHHHHHHHHHHH
35.20113334121
388UbiquitinationSKFKELQKGIIRHDS
HHHHHHHHCCCCCCC
65.7827667366
395PhosphorylationKGIIRHDSFWDKLIF
HCCCCCCCHHHHHHH
23.3227067055
397UbiquitinationIIRHDSFWDKLIFAK
CCCCCCHHHHHHHHH
13.0423503661
397 (in isoform 3)Ubiquitination-13.04-
399UbiquitinationRHDSFWDKLIFAKIQ
CCCCHHHHHHHHHHH
33.7922817900
400 (in isoform 3)Ubiquitination-3.45-
400UbiquitinationHDSFWDKLIFAKIQD
CCCHHHHHHHHHHHH
3.4527667366
404 (in isoform 4)Ubiquitination-30.1021890473
404UbiquitinationWDKLIFAKIQDSLGG
HHHHHHHHHHHHCCC
30.1022817900
404 (in isoform 1)Ubiquitination-30.1021890473
404UbiquitinationWDKLIFAKIQDSLGG
HHHHHHHHHHHHCCC
30.1021890473
408PhosphorylationIFAKIQDSLGGRVRV
HHHHHHHHCCCCEEE
16.7369338895
417UbiquitinationGGRVRVIVTGAAPMS
CCCEEEEEECCCCCC
3.5527667366
417 (in isoform 3)Ubiquitination-3.55-
418PhosphorylationGRVRVIVTGAAPMST
CCEEEEEECCCCCCH
15.2428509920
423UbiquitinationIVTGAAPMSTSVMTF
EEECCCCCCHHHHHH
6.1427667366
424PhosphorylationVTGAAPMSTSVMTFF
EECCCCCCHHHHHHH
19.2328509920
425PhosphorylationTGAAPMSTSVMTFFR
ECCCCCCHHHHHHHH
21.0628509920
444UbiquitinationCQVYEAYGQTECTGG
CCEEEECCCEECCCC
34.6727667366
455UbiquitinationCTGGCTFTLPGDWTS
CCCCCEEECCCCCCC
17.5622817900
460UbiquitinationTFTLPGDWTSGHVGV
EEECCCCCCCCCCCC
9.8121890473
460 (in isoform 3)Ubiquitination-9.8121890473
498PhosphorylationGEVCIKGTNVFKGYL
CCEEEECCEEECCCC
24.1726074081
502UbiquitinationIKGTNVFKGYLKDPE
EECCEEECCCCCCHH
42.2223503661
504PhosphorylationGTNVFKGYLKDPEKT
CCEEECCCCCCHHHH
15.9226074081
506 (in isoform 1)Ubiquitination-63.8521890473
506UbiquitinationNVFKGYLKDPEKTQE
EEECCCCCCHHHHHH
63.8521906983
510UbiquitinationGYLKDPEKTQEALDS
CCCCCHHHHHHHHHC
61.9823503661
511PhosphorylationYLKDPEKTQEALDSD
CCCCHHHHHHHHHCC
29.9469011261
546UbiquitinationDRKKNIFKLAQGEYI
ECCCCCHHHHCCCCC
38.8327667366
552PhosphorylationFKLAQGEYIAPEKIE
HHHHCCCCCCHHHHH
14.8125884760
557 (in isoform 1)Ubiquitination-55.0221890473
557UbiquitinationGEYIAPEKIENIYNR
CCCCCHHHHHHHHCC
55.0221906983
558UbiquitinationEYIAPEKIENIYNRS
CCCCHHHHHHHHCCC
4.7023503661
562 (in isoform 3)Ubiquitination-18.99-
562UbiquitinationPEKIENIYNRSQPVL
HHHHHHHHCCCCCEE
18.9923503661
566UbiquitinationENIYNRSQPVLQIFV
HHHHCCCCCEEEEEE
28.9623503661
580PhosphorylationVHGESLRSSLVGVVV
EECHHHHHHCCEEEE
33.0637817023
581PhosphorylationHGESLRSSLVGVVVP
ECHHHHHHCCEEEEC
22.2021406692
595PhosphorylationPDTDVLPSFAAKLGV
CCCCCHHHHHHHHCC
24.2920071362
599UbiquitinationVLPSFAAKLGVKGSF
CHHHHHHHHCCCCCH
42.202190698
599 (in isoform 1)Ubiquitination-42.2021890473
602UbiquitinationSFAAKLGVKGSFEEL
HHHHHHCCCCCHHHH
10.3327667366
603UbiquitinationFAAKLGVKGSFEELC
HHHHHCCCCCHHHHH
47.2227667366
605PhosphorylationAKLGVKGSFEELCQN
HHHCCCCCHHHHHHC
24.6230624053
628UbiquitinationEDLQKIGKESGLKTF
HHHHHHCHHHCCCHH
52.7827667366
634PhosphorylationGKESGLKTFEQVKAI
CHHHCCCHHHHHHHH
37.1337278147
656PhosphorylationSIENGLLTPTLKAKR
EECCCCCCHHEECCC
21.1927067055
659UbiquitinationNGLLTPTLKAKRGEL
CCCCCHHEECCCCHH
5.5227667366
678PhosphorylationRTQIDSLYEHIQD--
HHHHHHHHHHHCC--
14.9320732281
684UbiquitinationLYEHIQD--------
HHHHHCC--------
27667366

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 ACSL5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACSL5_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 ACSL5_HUMAN !!

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

Oops, there are no PPI records of ACSL5_HUMAN !!

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
There are no disease associations of PTM sites.
Regulatory Network of ACSL5_HUMAN

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Related Literatures of Post-Translational Modification

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