LCF2_YEAST - dbPTM
LCF2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LCF2_YEAST
UniProt AC P39518
Protein Name Long-chain-fatty-acid--CoA ligase 2
Gene Name FAA2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 744
Subcellular Localization Cytoplasm. Mitochondrion. The FAM1-1 mutant is imported in the mitochondria.
Protein Description Esterification, concomitant with transport, of endogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Preferentially acts on C9:0-C13:0 fatty acids although C7:0-C17:0 fatty acids are tolerated..
Protein Sequence MAAPDYALTDLIESDPRFESLKTRLAGYTKGSDEYIEELYSQLPLTSYPRYKTFLKKQAVAISNPDNEAGFSSIYRSSLSSENLVSCVDKNLRTAYDHFMFSARRWPQRDCLGSRPIDKATGTWEETFRFESYSTVSKRCHNIGSGILSLVNTKRKRPLEANDFVVAILSHNNPEWILTDLACQAYSLTNTALYETLGPNTSEYILNLTEAPILIFAKSNMYHVLKMVPDMKFVNTLVCMDELTHDELRMLNESLLPVKCNSLNEKITFFSLEQVEQVGCFNKIPAIPPTPDSLYTISFTSGTTGLPKGVEMSHRNIASGIAFAFSTFRIPPDKRNQQLYDMCFLPLAHIFERMVIAYDLAIGFGIGFLHKPDPTVLVEDLKILKPYAVALVPRILTRFEAGIKNALDKSTVQRNVANTILDSKSARFTARGGPDKSIMNFLVYHRVLIDKIRDSLGLSNNSFIITGSAPISKDTLLFLRSALDIGIRQGYGLTETFAGVCLSEPFEKDVGSCGAIGISAECRLKSVPEMGYHADKDLKGELQIRGPQVFERYFKNPNETSKAVDQDGWFSTGDVAFIDGKGRISVIDRVKNFFKLAHGEYIAPEKIENIYLSSCPYITQIFVFGDPLKTFLVGIVGVDVDAAQPILAAKHPEVKTWTKEVLVENLNRNKKLRKEFLNKINKCTDGLQGFEKLHNIKVGLEPLTLEDDVVTPTFKIKRAKASKFFKDTLDQLYAEGSLVKTEKL
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
32PhosphorylationLAGYTKGSDEYIEEL
HCCCCCCCHHHHHHH		28.9128889911
35PhosphorylationYTKGSDEYIEELYSQ
CCCCCHHHHHHHHHC		20.7228889911
41PhosphorylationEYIEELYSQLPLTSY
HHHHHHHHCCCCCCC		37.5528889911
46PhosphorylationLYSQLPLTSYPRYKT
HHHCCCCCCCHHHHH		25.0328889911
47PhosphorylationYSQLPLTSYPRYKTF
HHCCCCCCCHHHHHH		40.6028889911
80PhosphorylationSIYRSSLSSENLVSC
HHHHHCCCCCCHHHH		37.2427214570
226UbiquitinationSNMYHVLKMVPDMKF
CCHHHHHHHCCCCCH		36.4423749301
259UbiquitinationNESLLPVKCNSLNEK
CHHHCCEECCCCCCE		26.2623749301
423PhosphorylationVANTILDSKSARFTA
HHHHHHHCCCCCEEC		25.6827214570
711PhosphorylationTLEDDVVTPTFKIKR
CCCCCCCCCCEECCH		19.2329136822
713PhosphorylationEDDVVTPTFKIKRAK
CCCCCCCCEECCHHH		28.3529136822
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 LCF2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LCF2_YEAST !!
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 LCF2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PXA1_YEASTPXA1genetic
8670886
RIR1_YEASTRNR1physical
18719252
CHA4_YEASTCHA4physical
18719252
CYC2_YEASTCYC2genetic
20093466
SMD1_YEASTSMD1genetic
27708008
MPPA_YEASTMAS2genetic
27708008
BET1_YEASTBET1genetic
27708008
MED11_YEASTMED11genetic
27708008
OST2_YEASTOST2genetic
27708008
CYC2_YEASTCYC2genetic
27708008
CDC42_YEASTCDC42genetic
27453043
SNF5_YEASTSNF5genetic
27453043
CBS_HUMANCBSphysical
27107014
NDC80_HUMANNDC80physical
27107014
IKZF1_HUMANIKZF1physical
27107014
SIAH1_HUMANSIAH1physical
27107014
AR6P1_HUMANARL6IP1physical
27107014
HNRPC_HUMANHNRNPCphysical
27107014
MED4_HUMANMED4physical
27107014
PUR6_HUMANPAICSphysical
27107014
TRI38_HUMANTRIM38physical
27107014
RTN3_HUMANRTN3physical
27107014
BEND7_HUMANBEND7physical
27107014
PRAF1_HUMANRABAC1physical
27107014
ZBT8A_HUMANZBTB8Aphysical
27107014
RPGR1_HUMANRPGRIP1physical
27107014
CACO2_HUMANCALCOCO2physical
27107014
5NTC_HUMANNT5C2physical
27107014
ZBED1_HUMANZBED1physical
27107014
PDE9A_HUMANPDE9Aphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LCF2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-711, AND MASSSPECTROMETRY.

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