MBOA7_HUMAN - dbPTM
MBOA7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBOA7_HUMAN
UniProt AC Q96N66
Protein Name Lysophospholipid acyltransferase 7 {ECO:0000305}
Gene Name MBOAT7 {ECO:0000312|HGNC:HGNC:15505}
Organism Homo sapiens (Human).
Sequence Length 472
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Acyltransferase which contributes to the regulation of free arachidonic acid (AA) in the cell through the remodeling of phospholipids. Mediates the conversion of lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) (LPIAT activity). Prefers arachidonoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. Required for cortical lamination during brain development (By similarity)..
Protein Sequence MSPEEWTYLVVLLISIPIGFLFKKAGPGLKRWGAAAVGLGLTLFTCGPHTLHSLVTILGTWALIQAQPCSCHALALAWTFSYLLFFRALSLLGLPTPTPFTNAVQLLLTLKLVSLASEVQDLHLAQRKEMASGFSKGPTLGLLPDVPSLMETLSYSYCYVGIMTGPFFRYRTYLDWLEQPFPGAVPSLRPLLRRAWPAPLFGLLFLLSSHLFPLEAVREDAFYARPLPARLFYMIPVFFAFRMRFYVAWIAAECGCIAAGFGAYPVAAKARAGGGPTLQCPPPSSPEKAASLEYDYETIRNIDCYSTDFCVRVRDGMRYWNMTVQWWLAQYIYKSAPARSYVLRSAWTMLLSAYWHGLHPGYYLSFLTIPLCLAAEGRLESALRGRLSPGGQKAWDWVHWFLKMRAYDYMCMGFVLLSLADTLRYWASIYFCIHFLALAALGLGLALGGGSPSRRKAASQPTSLAPEKLREE
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
2Phosphorylation------MSPEEWTYL
------CCHHHHHHH		40.8124043423
7Phosphorylation-MSPEEWTYLVVLLI
-CCHHHHHHHHHHHH		15.4024043423
8PhosphorylationMSPEEWTYLVVLLIS
CCHHHHHHHHHHHHH		9.8924043423
15PhosphorylationYLVVLLISIPIGFLF
HHHHHHHHCHHHHHH		23.4524043423
55 (in isoform 2)Ubiquitination-3.3321890473
55UbiquitinationPHTLHSLVTILGTWA
HHHHHHHHHHHHHHH		3.3323000965
114PhosphorylationLLTLKLVSLASEVQD
HHHHHHHHHHHHHHH		28.7520068231
117PhosphorylationLKLVSLASEVQDLHL
HHHHHHHHHHHHHHH		43.5220068231
128 (in isoform 3)Ubiquitination-39.5021890473
128 (in isoform 1)Ubiquitination-39.5021890473
128UbiquitinationDLHLAQRKEMASGFS
HHHHHHHHHHHHCCC		39.5023000965
172PhosphorylationGPFFRYRTYLDWLEQ
CCCCCCHHHHHHHHC		21.3624719451
173PhosphorylationPFFRYRTYLDWLEQP
CCCCCHHHHHHHHCC		8.1524719451
187PhosphorylationPFPGAVPSLRPLLRR
CCCCCCCCHHHHHHH		30.3424719451
212PhosphorylationFLLSSHLFPLEAVRE
HHHHHCCCCHHHHHC		5.6332142685
215UbiquitinationSSHLFPLEAVREDAF
HHCCCCHHHHHCCCC		45.4121963094
277PhosphorylationARAGGGPTLQCPPPS
HHCCCCCCCCCCCCC		32.5123403867
284PhosphorylationTLQCPPPSSPEKAAS
CCCCCCCCCHHHHHH		65.3823401153
285PhosphorylationLQCPPPSSPEKAASL
CCCCCCCCHHHHHHC		42.7429255136
288AcetylationPPPSSPEKAASLEYD
CCCCCHHHHHHCCCC		53.2726051181
288UbiquitinationPPPSSPEKAASLEYD
CCCCCHHHHHHCCCC		53.2721963094
291PhosphorylationSSPEKAASLEYDYET
CCHHHHHHCCCCHHH		26.9626552605
294PhosphorylationEKAASLEYDYETIRN
HHHHHCCCCHHHHCC		29.1730576142
296PhosphorylationAASLEYDYETIRNID
HHHCCCCHHHHCCCE		17.6726552605
298PhosphorylationSLEYDYETIRNIDCY
HCCCCHHHHCCCEEE		21.0026552605
321N-linked_GlycosylationRDGMRYWNMTVQWWL
CCCCCHHHHHHHHHH		13.81UniProtKB CARBOHYD
383UbiquitinationEGRLESALRGRLSPG
CCCHHHHHCCCCCCC		9.2133845483
395 (in isoform 2)Ubiquitination-13.6621890473
395UbiquitinationSPGGQKAWDWVHWFL
CCCCHHHHHHHHHHH		13.6627667366
456UbiquitinationGGSPSRRKAASQPTS
CCCHHHHHHHCCCCC		47.3927667366
459PhosphorylationPSRRKAASQPTSLAP
HHHHHHHCCCCCCCH		41.3725159151
462PhosphorylationRKAASQPTSLAPEKL
HHHHCCCCCCCHHHH		28.8323312004
463PhosphorylationKAASQPTSLAPEKLR
HHHCCCCCCCHHHHH		29.2627251275
468UbiquitinationPTSLAPEKLREE---
CCCCCHHHHHCC---		52.3527667366
4682-HydroxyisobutyrylationPTSLAPEKLREE---
CCCCCHHHHHCC---		52.35-
468 (in isoform 1)Ubiquitination-52.3521890473
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 MBOA7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBOA7_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 MBOA7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPTSA_HUMANSPTSSAphysical
23510452
STOM_HUMANSTOMphysical
27173435
ACAP2_HUMANACAP2physical
27173435
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 MBOA7_HUMAN

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Related Literatures of Post-Translational Modification

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