LCLT1_HUMAN - dbPTM
LCLT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LCLT1_HUMAN
UniProt AC Q6UWP7
Protein Name Lysocardiolipin acyltransferase 1
Gene Name LCLAT1
Organism Homo sapiens (Human).
Sequence Length 414
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages..
Protein Sequence MHSRGREIVVLLNPWSINEAVSSYCTYFIKQDSKSFGIMVSWKGIYFILTLFWGSFFGSIFMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLETMFGVKVIITGDAFVPGERSVIIMNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPGFGWAMQAAAYIFIHRKWKDDKSHFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAFAEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFPREIHFHVHRYPIDTLPTSKEDLQLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKSELRVLVVKLLSILYWTLFSPAMCLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELACYRLLHKQPHLNSKKNE
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
16PhosphorylationVVLLNPWSINEAVSS
EEEECCCCHHHHHHH		19.4526074081
22PhosphorylationWSINEAVSSYCTYFI
CCHHHHHHHHHCEEE		23.7226074081
23PhosphorylationSINEAVSSYCTYFIK
CHHHHHHHHHCEEEE		20.0326074081
24PhosphorylationINEAVSSYCTYFIKQ
HHHHHHHHHCEEEEC		4.9426074081
26PhosphorylationEAVSSYCTYFIKQDS
HHHHHHHCEEEECCC		17.1526074081
27PhosphorylationAVSSYCTYFIKQDSK
HHHHHHCEEEECCCC		10.3526074081
33PhosphorylationTYFIKQDSKSFGIMV
CEEEECCCCCCCEEE		27.9221406692
35PhosphorylationFIKQDSKSFGIMVSW
EEECCCCCCCEEEEH		32.4321406692
41PhosphorylationKSFGIMVSWKGIYFI
CCCCEEEEHHHHHHH		12.9921406692
46PhosphorylationMVSWKGIYFILTLFW
EEEHHHHHHHHHHHH		8.0121406692
50PhosphorylationKGIYFILTLFWGSFF
HHHHHHHHHHHHHHH		18.3221406692
55PhosphorylationILTLFWGSFFGSIFM
HHHHHHHHHHHHHHH		14.1621406692
59PhosphorylationFWGSFFGSIFMLSPF
HHHHHHHHHHHHCCC		13.9021406692
64PhosphorylationFGSIFMLSPFLPLMF
HHHHHHHCCCCCEEE		11.2121406692
75PhosphorylationPLMFVNPSWYRWINN
CEEECCHHHHHHHHH		31.3821406692
77PhosphorylationMFVNPSWYRWINNRL
EECCHHHHHHHHHHH		10.6221406692
150UbiquitinationRLEKICLKASLKGVP
HHHHHHHHHHHCCCC		31.36-
183UbiquitinationKDDKSHFEDMIDYFC
CCCHHHHHHHHHHHH		41.0421890473
183 (in isoform 3)Acetylation-41.04-
183AcetylationKDDKSHFEDMIDYFC
CCCHHHHHHHHHHHH		41.0419608861
183UbiquitinationKDDKSHFEDMIDYFC
CCCHHHHHHHHHHHH		41.0419608861
188UbiquitinationHFEDMIDYFCDIHEP
HHHHHHHHHHCCCCC		8.6521890473
221UbiquitinationRSNAFAEKNGLQKYE
HHHHHHHHHCCCEEE		53.5421890473
221AcetylationRSNAFAEKNGLQKYE
HHHHHHHHHCCCEEE		53.5419608861
221MalonylationRSNAFAEKNGLQKYE
HHHHHHHHHCCCEEE		53.5426320211
221 (in isoform 2)Ubiquitination-53.5421890473
221 (in isoform 1)Ubiquitination-53.5421890473
226 (in isoform 1)Ubiquitination-45.1221890473
226 (in isoform 2)Ubiquitination-45.1221890473
226UbiquitinationAEKNGLQKYEYVLHP
HHHHCCCEEEEEECC		45.1221890473
229PhosphorylationNGLQKYEYVLHPRTT
HCCCEEEEEECCCCC		12.77110753395
235PhosphorylationEYVLHPRTTGFTFVV
EEEECCCCCCEEEEC		35.4027732954
236PhosphorylationYVLHPRTTGFTFVVD
EEECCCCCCEEEECC		31.4227732954
239PhosphorylationHPRTTGFTFVVDRLR
CCCCCCEEEECCCCC		19.5027732954
244DimethylationGFTFVVDRLREGKNL
CEEEECCCCCCCCCC		24.84-
244MethylationGFTFVVDRLREGKNL
CEEEECCCCCCCCCC		24.84-
246MethylationTFVVDRLREGKNLDA
EEECCCCCCCCCCCC		52.06-
249UbiquitinationVDRLREGKNLDAVHD
CCCCCCCCCCCCEEE		49.97-
258PhosphorylationLDAVHDITVAYPHNI
CCCEEEEEEECCCCC		12.7327732954
261PhosphorylationVHDITVAYPHNIPQS
EEEEEEECCCCCCHH		10.7327732954
268PhosphorylationYPHNIPQSEKHLLQG
CCCCCCHHHHHHHCC		43.1727732954
270 (in isoform 1)Ubiquitination-44.8121890473
270UbiquitinationHNIPQSEKHLLQGDF
CCCCHHHHHHHCCCC		44.812190698
270AcetylationHNIPQSEKHLLQGDF
CCCCHHHHHHHCCCC		44.8121466224
297UbiquitinationIDTLPTSKEDLQLWC
CCCCCCCHHHHHHHH		58.69-
297MalonylationIDTLPTSKEDLQLWC
CCCCCCCHHHHHHHH		58.6926320211
297AcetylationIDTLPTSKEDLQLWC
CCCCCCCHHHHHHHH		58.6923954790
306UbiquitinationDLQLWCHKRWEEKEE
HHHHHHHHHHHHHHH		56.95-
306SumoylationDLQLWCHKRWEEKEE
HHHHHHHHHHHHHHH		56.95-
306AcetylationDLQLWCHKRWEEKEE
HHHHHHHHHHHHHHH		56.9525825284
311UbiquitinationCHKRWEEKEERLRSF
HHHHHHHHHHHHHHH		54.05-
349PhosphorylationVLVVKLLSILYWTLF
HHHHHHHHHHHHHHH		22.4525867546
352PhosphorylationVKLLSILYWTLFSPA
HHHHHHHHHHHHCHH		8.4825867546
354PhosphorylationLLSILYWTLFSPAMC
HHHHHHHHHHCHHHH		12.3625867546
357PhosphorylationILYWTLFSPAMCLLI
HHHHHHHCHHHHHHH		18.1825867546
365PhosphorylationPAMCLLIYLYSLVKW
HHHHHHHHHHHHHHH		10.2725867546
367PhosphorylationMCLLIYLYSLVKWYF
HHHHHHHHHHHHHHH		5.2925867546
368PhosphorylationCLLIYLYSLVKWYFI
HHHHHHHHHHHHHHH		24.8825867546
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 LCLT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LCLT1_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 LCLT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LCLT1_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 LCLT1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221, AND MASS SPECTROMETRY.

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