S27A2_HUMAN - dbPTM
S27A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S27A2_HUMAN
UniProt AC O14975
Protein Name Very long-chain acyl-CoA synthetase
Gene Name SLC27A2
Organism Homo sapiens (Human).
Sequence Length 620
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein. Peroxisome membrane
Multi-pass membrane protein. Peripheral membrane associated with the lumenal side of peroxisomes.
Protein Description Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precursors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes (By similarity)..
Protein Sequence MLSAIYTVLAGLLFLPLLVNLCCPYFFQDIGYFLKVAAVGRRVRSYGKRRPARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVCKITQLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPAVIKDALYFLDDTAKMYVPMTEDIYNAISAKTLKL
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
22S-palmitoylationLPLLVNLCCPYFFQD
HHHHHHHHCHHHHHH		1.5329575903
23S-palmitoylationPLLVNLCCPYFFQDI
HHHHHHHCHHHHHHH		3.2729575903
158PhosphorylationGAKVLLVSPELQAAV
CCEEEEECHHHHHHH		16.78-
171PhosphorylationAVEEILPSLKKDDVS
HHHHHHHHCCCCCEE		49.7524719451
173UbiquitinationEEILPSLKKDDVSIY
HHHHHHCCCCCEEEE		59.5032015554
1742-HydroxyisobutyrylationEILPSLKKDDVSIYY
HHHHHCCCCCEEEEE		65.54-
174UbiquitinationEILPSLKKDDVSIYY
HHHHHCCCCCEEEEE		65.5433845483
225O-linked_GlycosylationTPALYIYTSGTTGLP
CCEEEEEECCCCCCC		15.8928510447
226O-linked_GlycosylationPALYIYTSGTTGLPK
CEEEEEECCCCCCCC		19.7128510447
238PhosphorylationLPKAAMITHQRIWYG
CCCCHHCCCCCEECC		10.0020068231
244PhosphorylationITHQRIWYGTGLTFV
CCCCCEECCCCCCHH		11.4820068231
246PhosphorylationHQRIWYGTGLTFVSG
CCCEECCCCCCHHCC		17.2020068231
249PhosphorylationIWYGTGLTFVSGLKA
EECCCCCCHHCCCCC		24.2820068231
252PhosphorylationGTGLTFVSGLKADDV
CCCCCHHCCCCCCCE		33.9320068231
272UbiquitinationPFYHSAALLIGIHGC
CCCHHHHHHHHHHHH		3.4224816145
279UbiquitinationLLIGIHGCIVAGATL
HHHHHHHHHHHHHHH		1.0824816145
291AcetylationATLALRTKFSASQFW
HHHHHHCCCCHHHHH		30.7825825284
293PhosphorylationLALRTKFSASQFWDD
HHHHCCCCHHHHHHH		28.6828857561
295PhosphorylationLRTKFSASQFWDDCR
HHCCCCHHHHHHHHH		25.3928857561
303UbiquitinationQFWDDCRKYNVTVIQ
HHHHHHHHCCCCHHH		47.73-
304PhosphorylationFWDDCRKYNVTVIQY
HHHHHHHCCCCHHHH		8.77-
322PhosphorylationLLRYLCNSPQKPNDR
HHHHHHCCCCCCCCC		27.9320873877
325UbiquitinationYLCNSPQKPNDRDHK
HHHCCCCCCCCCCCH		49.5324816145
332UbiquitinationKPNDRDHKVRLALGN
CCCCCCCHHHHHHCC		33.0824816145
336UbiquitinationRDHKVRLALGNGLRG
CCCHHHHHHCCCCCH		11.6729967540
337UbiquitinationDHKVRLALGNGLRGD
CCHHHHHHCCCCCHH		6.9229967540
345NeddylationGNGLRGDVWRQFVKR
CCCCCHHHHHHHHHH		5.1732015554
345UbiquitinationGNGLRGDVWRQFVKR
CCCCCHHHHHHHHHH		5.1721890473
345UbiquitinationGNGLRGDVWRQFVKR
CCCCCHHHHHHHHHH		5.1722817900
350UbiquitinationGDVWRQFVKRFGDIC
HHHHHHHHHHHHCEE		3.0922817900
366UbiquitinationYEFYAATEGNIGFMN
EEEEECCCCCCCCHH		45.5833845483
389UbiquitinationGRVNYLQKKIITYDL
HHHHHHHHHEEEEEE		43.2632015554
3892-HydroxyisobutyrylationGRVNYLQKKIITYDL
HHHHHHHHHEEEEEE		43.26-
390UbiquitinationRVNYLQKKIITYDLI
HHHHHHHHEEEEEEE		26.7829967540
393PhosphorylationYLQKKIITYDLIKYD
HHHHHEEEEEEEECE		17.92-
394UbiquitinationLQKKIITYDLIKYDV
HHHHEEEEEEEECEE		9.8023503661
395UbiquitinationQKKIITYDLIKYDVE
HHHEEEEEEEECEEC		33.0123503661
398UbiquitinationIITYDLIKYDVEKDE
EEEEEEEECEECCCC		42.5722817900
398NeddylationIITYDLIKYDVEKDE
EEEEEEEECEECCCC		42.5732015554
4032-HydroxyisobutyrylationLIKYDVEKDEPVRDE
EEECEECCCCCCCCC		68.21-
403UbiquitinationLIKYDVEKDEPVRDE
EEECEECCCCCCCCC		68.2122817900
419UbiquitinationGYCVRVPKGEVGLLV
CEEEEECCCCEEEEE		65.9229901268
442UbiquitinationFNGYAGAKAQTEKKK
CCCCCCCCCHHCHHH		39.8632015554
447UbiquitinationGAKAQTEKKKLRDVF
CCCCHHCHHHHHHHH		59.6023503661
448UbiquitinationAKAQTEKKKLRDVFK
CCCHHCHHHHHHHHH		51.3023503661
487UbiquitinationRVGDTFRWKGENVAT
CCCCCEEECCCCCEE		14.6029967540
522UbiquitinationVHVPDHEGRIGMASI
EECCCCCCCEEEEEE		24.0829967540
528PhosphorylationEGRIGMASIKMKENH
CCCEEEEEEEEECCC		17.53-
5322-HydroxyisobutyrylationGMASIKMKENHEFDG
EEEEEEEECCCCCCH		50.81-
536UbiquitinationIKMKENHEFDGKKLF
EEEECCCCCCHHHHH		57.9529967540
540UbiquitinationENHEFDGKKLFQHIA
CCCCCCHHHHHHHHH		48.4229967540
547UbiquitinationKKLFQHIADYLPSYA
HHHHHHHHHHCHHHC		9.4029967540
552PhosphorylationHIADYLPSYARPRFL
HHHHHCHHHCCCCEE		28.9127050516
563UbiquitinationPRFLRIQDTIEITGT
CCEEEEEEEEEEEEC		47.4829967540
564PhosphorylationRFLRIQDTIEITGTF
CEEEEEEEEEEEECC		12.2530301811
568PhosphorylationIQDTIEITGTFKHRK
EEEEEEEEECCCCCC		19.8530301811
570PhosphorylationDTIEITGTFKHRKMT
EEEEEEECCCCCCEE		22.3630301811
575UbiquitinationTGTFKHRKMTLVEEG
EECCCCCCEEEHHCC		35.6429967540
576SulfoxidationGTFKHRKMTLVEEGF
ECCCCCCEEEHHCCC		3.3621406390
577PhosphorylationTFKHRKMTLVEEGFN
CCCCCCEEEHHCCCC		30.5925159151
589UbiquitinationGFNPAVIKDALYFLD
CCCHHHHHHHHHHHC		30.2829967540
600UbiquitinationYFLDDTAKMYVPMTE
HHHCCCCCCCCCCCH		32.6229967540
602PhosphorylationLDDTAKMYVPMTEDI
HCCCCCCCCCCCHHH		10.74-
610PhosphorylationVPMTEDIYNAISAKT
CCCCHHHHHHHHHHH		15.74-
616UbiquitinationIYNAISAKTLKL---
HHHHHHHHHCCC---		47.8229967540
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 S27A2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S27A2_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 S27A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABCD1_HUMANABCD1physical
16781659
PEX14_HUMANPEX14physical
10198260
SDHA_HUMANSDHAphysical
10198260
CALR_HUMANCALRphysical
10198260
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 S27A2_HUMAN

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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 THR-577, AND MASSSPECTROMETRY.

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