MIGA2_HUMAN - dbPTM
MIGA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MIGA2_HUMAN
UniProt AC Q7L4E1
Protein Name Mitoguardin 2 {ECO:0000303|PubMed:26711011}
Gene Name MIGA2 {ECO:0000303|PubMed:26711011, ECO:0000312|HGNC:HGNC:23621}
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Mitochondrion outer membrane
Multi-pass membrane protein .
Protein Description Regulator of mitochondrial fusion: acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of PLD6/MitoPLD dimers. May act by regulating phospholipid metabolism via PLD6/MitoPLD..
Protein Sequence MAFRRAEGTSMIQALAMTVAEIPVFLYTTFGQSAFSQLRLTPGLRKVLFATALGTVALALAAHQLKRRRRRKKQVGPEMGGEQLGTVPLPILLARKVPSVKKGYSSRRVQSPSSKSNDTLSGISSIEPSKHSGSSHSVASMMAVNSSSPTAACSGLWDARGMEESLTTSDGNAESLYMQGMELFEEALQKWEQALSVGQRGDSGSTPMPRDGLRNPETASEPLSEPESQRKEFAEKLESLLHRAYHLQEEFGSTFPADSMLLDLERTLMLPLTEGSLRLRADDEDSLTSEDSFFSATELFESLQTGDYPIPLSRPAAAYEEALQLVKEGRVPCRTLRTELLGCYSDQDFLAKLHCVRQAFEGLLEDKSNQLFFGKVGRQMVTGLMTKAEKSPKGFLESYEEMLSYALRPETWATTRLELEGRGVVCMSFFDIVLDFILMDAFEDLENPPASVLAVLRNRWLSDSFKETALATACWSVLKAKRRLLMVPDGFISHFYSVSEHVSPVLAFGFLGPKPQLAEVCAFFKHQIVQYLRDMFDLDNVRYTSLPALADDILQLSRRRSEILLGYLGVPAASSAGVNGALPRENGPLGELQ
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
36PhosphorylationTFGQSAFSQLRLTPG
CCCHHHHHHHCCCHH
24719451
86PhosphorylationMGGEQLGTVPLPILL
CCCCCCCCCCHHHHH
29514088
96MethylationLPILLARKVPSVKKG
HHHHHHCCCCCCCCC
-
99PhosphorylationLLARKVPSVKKGYSS
HHHCCCCCCCCCCCC
23403867
111PhosphorylationYSSRRVQSPSSKSND
CCCCCCCCCCCCCCC
28985074
116PhosphorylationVQSPSSKSNDTLSGI
CCCCCCCCCCCCCCC
22199227
119PhosphorylationPSSKSNDTLSGISSI
CCCCCCCCCCCCCCC
25159151
121PhosphorylationSKSNDTLSGISSIEP
CCCCCCCCCCCCCCC
29083192
124PhosphorylationNDTLSGISSIEPSKH
CCCCCCCCCCCCCCC
25159151
125PhosphorylationDTLSGISSIEPSKHS
CCCCCCCCCCCCCCC
25159151
132PhosphorylationSIEPSKHSGSSHSVA
CCCCCCCCCCCCCHH
28270605
134PhosphorylationEPSKHSGSSHSVASM
CCCCCCCCCCCHHHH
28270605
135PhosphorylationPSKHSGSSHSVASMM
CCCCCCCCCCHHHHH
28270605
137PhosphorylationKHSGSSHSVASMMAV
CCCCCCCCHHHHHCC
28270605
140PhosphorylationGSSHSVASMMAVNSS
CCCCCHHHHHCCCCC
28270605
146PhosphorylationASMMAVNSSSPTAAC
HHHHCCCCCCCCHHH
29449344
147PhosphorylationSMMAVNSSSPTAACS
HHHCCCCCCCCHHHC
28270605
148PhosphorylationMMAVNSSSPTAACSG
HHCCCCCCCCHHHCC
28270605
150PhosphorylationAVNSSSPTAACSGLW
CCCCCCCCHHHCCCC
28270605
154PhosphorylationSSPTAACSGLWDARG
CCCCHHHCCCCCCCC
28270605
196PhosphorylationQKWEQALSVGQRGDS
HHHHHHHHHCCCCCC
28348404
203PhosphorylationSVGQRGDSGSTPMPR
HHCCCCCCCCCCCCC
25849741
205PhosphorylationGQRGDSGSTPMPRDG
CCCCCCCCCCCCCCC
29255136
206PhosphorylationQRGDSGSTPMPRDGL
CCCCCCCCCCCCCCC
29255136
218PhosphorylationDGLRNPETASEPLSE
CCCCCCCCCCCCCCC
23927012
220PhosphorylationLRNPETASEPLSEPE
CCCCCCCCCCCCCCH
29255136
224PhosphorylationETASEPLSEPESQRK
CCCCCCCCCCHHHHH
29255136
228 (in isoform 2)Phosphorylation-24260401
228PhosphorylationEPLSEPESQRKEFAE
CCCCCCHHHHHHHHH
29255136
239PhosphorylationEFAEKLESLLHRAYH
HHHHHHHHHHHHHHH
23312004
254PhosphorylationLQEEFGSTFPADSML
HHHHHCCCCCCHHHH
30576142
267PhosphorylationMLLDLERTLMLPLTE
HHHHHHHHHEEECCC
23403867
273PhosphorylationRTLMLPLTEGSLRLR
HHHEEECCCCCEEEC
29255136
276PhosphorylationMLPLTEGSLRLRADD
EEECCCCCEEECCCC
19664994
286PhosphorylationLRADDEDSLTSEDSF
ECCCCCCCCCCCCCC
17081983
288PhosphorylationADDEDSLTSEDSFFS
CCCCCCCCCCCCCCC
17081983
289PhosphorylationDDEDSLTSEDSFFSA
CCCCCCCCCCCCCCH
17081983
292PhosphorylationDSLTSEDSFFSATEL
CCCCCCCCCCCHHHH
17081983
295PhosphorylationTSEDSFFSATELFES
CCCCCCCCHHHHHHH
17081983
297PhosphorylationEDSFFSATELFESLQ
CCCCCCHHHHHHHHC
17081983
342 (in isoform 3)Phosphorylation-25262027
346 (in isoform 3)Phosphorylation-25262027
352UbiquitinationSDQDFLAKLHCVRQA
CCHHHHHHHHHHHHH
-
382PhosphorylationKVGRQMVTGLMTKAE
CHHHHHHHHHHHHHH
22210691
386PhosphorylationQMVTGLMTKAEKSPK
HHHHHHHHHHHHCCC
22210691
391PhosphorylationLMTKAEKSPKGFLES
HHHHHHHCCCCHHHH
24706070
561PhosphorylationLQLSRRRSEILLGYL
HHHHHHHHHHHHHHH
24247654

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 MIGA2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MIGA2_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 MIGA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBB_HUMANUBBphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
NIF3L_HUMANNIF3L1physical
28514442
S27A2_HUMANSLC27A2physical
28514442
HSP72_HUMANHSPA2physical
28514442
UBR4_HUMANUBR4physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MIGA2_HUMAN

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Related Literatures of Post-Translational Modification

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