MBOA2_HUMAN - dbPTM
MBOA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBOA2_HUMAN
UniProt AC Q6ZWT7
Protein Name Lysophospholipid acyltransferase 2
Gene Name MBOAT2
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Acyltransferase which mediates the conversion of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Catalyzes also the acylation of lysophosphatidic acid (LPA) into phosphatidic acid (PA) (LPAAT activity). Has also a very weak lysophosphatidylcholine acyltransferase (LPCAT activity). Prefers oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle..
Protein Sequence MATTSTTGSTLLQPLSNAVQLPIDQVNFVVCQLFALLAAIWFRTYLHSSKTSSFIRHVVATLLGLYLALFCFGWYALHFLVQSGISYCIMIIIGVENMHNYCFVFALGYLTVCQVTRVYIFDYGQYSADFSGPMMIITQKITSLACEIHDGMFRKDEELTSSQRDLAVRRMPSLLEYLSYNCNFMGILAGPLCSYKDYITFIEGRSYHITQSGENGKEETQYERTEPSPNTAVVQKLLVCGLSLLFHLTICTTLPVEYNIDEHFQATASWPTKIIYLYISLLAARPKYYFAWTLADAINNAAGFGFRGYDENGAARWDLISNLRIQQIEMSTSFKMFLDNWNIQTALWLKRVCYERTSFSPTIQTFILSAIWHGVYPGYYLTFLTGVLMTLAARAMRNNFRHYFIEPSQLKLFYDVITWIVTQVAISYTVVPFVLLSIKPSLTFYSSWYYCLHILGILVLLLLPVKKTQRRKNTHENIQLSQSKKFDEGENSLGQNSFSTTNNVCNQNQEIASRHSSLKQ
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
53PhosphorylationLHSSKTSSFIRHVVA
HHCCCCHHHHHHHHH
29.8924719451
119PhosphorylationVCQVTRVYIFDYGQY
HCCEEEEEEEECCCC
7.8024043423
123PhosphorylationTRVYIFDYGQYSADF
EEEEEEECCCCCCCC
8.7224043423
126PhosphorylationYIFDYGQYSADFSGP
EEEECCCCCCCCCCC
11.0624043423
127PhosphorylationIFDYGQYSADFSGPM
EEECCCCCCCCCCCE
17.3024043423
131PhosphorylationGQYSADFSGPMMIIT
CCCCCCCCCCEEEEE
42.4024043423
138PhosphorylationSGPMMIITQKITSLA
CCCEEEEEHHHHHHH
16.9424043423
160PhosphorylationFRKDEELTSSQRDLA
CCCCHHCCHHHHHHH
29.6129083192
161PhosphorylationRKDEELTSSQRDLAV
CCCHHCCHHHHHHHH
36.7829083192
162PhosphorylationKDEELTSSQRDLAVR
CCHHCCHHHHHHHHH
24.8129083192
198PhosphorylationPLCSYKDYITFIEGR
CCCCCCCEEEEECCC
9.56-
217AcetylationTQSGENGKEETQYER
EECCCCCCEECCCCC
65.0523236377
217UbiquitinationTQSGENGKEETQYER
EECCCCCCEECCCCC
65.05-
220PhosphorylationGENGKEETQYERTEP
CCCCCEECCCCCCCC
37.2328796482
222PhosphorylationNGKEETQYERTEPSP
CCCEECCCCCCCCCC
18.1328796482
276PhosphorylationSWPTKIIYLYISLLA
CCCHHHHHHHHHHHH
9.2722817900
321PhosphorylationAARWDLISNLRIQQI
CCHHHHHHHHEEEEE
36.7924719451
331PhosphorylationRIQQIEMSTSFKMFL
EEEEEEECCCHHHHH
14.2224043423
332PhosphorylationIQQIEMSTSFKMFLD
EEEEEECCCHHHHHH
36.5524043423
333PhosphorylationQQIEMSTSFKMFLDN
EEEEECCCHHHHHHC
18.6324043423
437PhosphorylationVVPFVLLSIKPSLTF
HHCHHHEEECCCHHH
25.1424719451
472UbiquitinationVKKTQRRKNTHENIQ
CCCCHHHCCCCCCHH
69.27-
474PhosphorylationKTQRRKNTHENIQLS
CCHHHCCCCCCHHHH
33.3325159151
481PhosphorylationTHENIQLSQSKKFDE
CCCCHHHHHCCCCCC
18.9430266825
483PhosphorylationENIQLSQSKKFDEGE
CCHHHHHCCCCCCCC
34.1430266825
492PhosphorylationKFDEGENSLGQNSFS
CCCCCCCCCCCCCCH
29.5827251275
497PhosphorylationENSLGQNSFSTTNNV
CCCCCCCCCHHCCCC
16.8223898821
499PhosphorylationSLGQNSFSTTNNVCN
CCCCCCCHHCCCCHH
33.8628555341
500PhosphorylationLGQNSFSTTNNVCNQ
CCCCCCHHCCCCHHH
31.3728348404
501PhosphorylationGQNSFSTTNNVCNQN
CCCCCHHCCCCHHHH
24.4828348404
513PhosphorylationNQNQEIASRHSSLKQ
HHHHHHHHHHHHCCC
35.8728348404

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 MBOA2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBOA2_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 MBOA2_HUMAN !!

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

Oops, there are no PPI records of MBOA2_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 MBOA2_HUMAN

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Related Literatures of Post-Translational Modification

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