S27A4_HUMAN - dbPTM
S27A4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S27A4_HUMAN
UniProt AC Q6P1M0
Protein Name Long-chain fatty acid transport protein 4
Gene Name SLC27A4
Organism Homo sapiens (Human).
Sequence Length 643
Subcellular Localization Membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane.
Protein Description Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids (VLCFAs). Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones (By similarity)..
Protein Sequence MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLLKVKAKVRQCLQERRTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAIVKDPLFYLDAQKGRYVPLDQEAYSRIQAGEEKL
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
6Phosphorylation--MLLGASLVGVLLF
--CCCCHHHHHHHHH		23.07-
14PhosphorylationLVGVLLFSKLVLKLP
HHHHHHHHHHHHHCC		25.6724719451
75PhosphorylationQCLQERRTVPILFAS
HHHHHCCCCCEEEEE		36.53-
82PhosphorylationTVPILFASTVRRHPD
CCCEEEEEEHHCCCC		21.7923312004
83PhosphorylationVPILFASTVRRHPDK
CCEEEEEEHHCCCCC		18.0123312004
90UbiquitinationTVRRHPDKTALIFEG
EHHCCCCCEEEEEEC		39.90-
170PhosphorylationDALLHCLTTSRARAL
HHHHHHHHHHHHHHH		28.28-
216UbiquitinationGAVPPSTEHLDPLLK
CCCCCCCCCCCHHHC		46.95-
227UbiquitinationPLLKDAPKHLPSCPD
HHHCCCCCCCCCCCC		60.54-
235UbiquitinationHLPSCPDKGFTDKLF
CCCCCCCCCCCCCEE		40.86-
243PhosphorylationGFTDKLFYIYTSGTT
CCCCCEEEEEECCCC		11.94-
245PhosphorylationTDKLFYIYTSGTTGL
CCCEEEEEECCCCCC		5.40-
263PhosphorylationAIVVHSRYYRMAALV
EEEEECHHHHHHHHH		9.84-
264PhosphorylationIVVHSRYYRMAALVY
EEEECHHHHHHHHHH		7.87-
373PhosphorylationSIWTNFSSRFHIPQV
HHHCCCCCCCCCCHH		34.52-
411PhosphorylationGFNSRILSFVYPIRL
CCCHHHHHCEEEEEE		15.4228152594
414PhosphorylationSRILSFVYPIRLVRV
HHHHHCEEEEEEEEE		7.3128152594
425PhosphorylationLVRVNEDTMELIRGP
EEEECCCHHHHHCCC		13.33-
426SulfoxidationVRVNEDTMELIRGPD
EEECCCHHHHHCCCC		6.4521406390
454UbiquitinationLVGRIIQKDPLRRFD
EEEEEECCCCCCCCC		51.40-
454MalonylationLVGRIIQKDPLRRFD
EEEEEECCCCCCCCC		51.4026320211
463PhosphorylationPLRRFDGYLNQGANN
CCCCCCCCCCCCCCC		12.3427642862
471UbiquitinationLNQGANNKKIAKDVF
CCCCCCCCHHHHHHH		45.42-
4712-HydroxyisobutyrylationLNQGANNKKIAKDVF
CCCCCCCCHHHHHHH		45.42-
471AcetylationLNQGANNKKIAKDVF
CCCCCCCCHHHHHHH		45.4226051181
471MalonylationLNQGANNKKIAKDVF
CCCCCCCCHHHHHHH		45.4226320211
475UbiquitinationANNKKIAKDVFKKGD
CCCCHHHHHHHHCCC		58.88-
512UbiquitinationTGDTFRWKGENVSTT
CCCCEEECCCCCCCC		52.68-
555PhosphorylationAGMAAVASPTGNCDL
CCCCEEECCCCCCCH		19.1821815630
571UbiquitinationRFAQVLEKELPLYAR
HHHHHHHHHCCHHHH		61.46-
576PhosphorylationLEKELPLYARPIFLR
HHHHCCHHHHHHHHH		9.91-
595UbiquitinationLHKTGTYKFQKTELR
HHHCCCCEECCHHHH		40.95-
598UbiquitinationTGTYKFQKTELRKEG
CCCCEECCHHHHHCC		47.28-
603UbiquitinationFQKTELRKEGFDPAI
ECCHHHHHCCCCHHH		74.86-
603AcetylationFQKTELRKEGFDPAI
ECCHHHHHCCCCHHH		74.8626051181
612UbiquitinationGFDPAIVKDPLFYLD
CCCHHHHCCCEEEEE		47.73-
622UbiquitinationLFYLDAQKGRYVPLD
EEEEECCCCCEEECC		47.2621906983
642UbiquitinationRIQAGEEKL------
HHHHCHHCC------		56.01-
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 S27A4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S27A4_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 S27A4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of S27A4_HUMAN !!
Drug and Disease Associations
Kegg Disease
H00741 Ichthyosis prematurity syndrome
OMIM Disease
608649Ichthyosis prematurity syndrome (IPS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of S27A4_HUMAN

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Related Literatures of Post-Translational Modification

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