MTCH2_HUMAN - dbPTM
MTCH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTCH2_HUMAN
UniProt AC Q9Y6C9
Protein Name Mitochondrial carrier homolog 2
Gene Name MTCH2
Organism Homo sapiens (Human).
Sequence Length 303
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description The substrate transported is not yet known. Induces mitochondrial depolarization..
Protein Sequence MADAASQVLLGSGLTILSQPLMYVKVLIQVGYEPLPPTIGRNIFGRQVCQLPGLFSYAQHIASIDGRRGLFTGLTPRLCSGVLGTVVHGKVLQHYQESDKGEELGPGNVQKEVSSSFDHVIKETTREMIARSAATLITHPFHVITLRSMVQFIGRESKYCGLCDSIITIYREEGILGFFAGLVPRLLGDILSLWLCNSLAYLVNTYALDSGVSTMNEMKSYSQAVTGFFASMLTYPFVLVSNLMAVNNCGLAGGCPPYSPIYTSWIDCWCMLQKEGNMSRGNSLFFRKVPFGKTYCCDLKMLI
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
2Acetylation------MADAASQVL
------CCHHHHHHH		18.3625944712
6Phosphorylation--MADAASQVLLGSG
--CCHHHHHHHHCCC		23.6524043423
12PhosphorylationASQVLLGSGLTILSQ
HHHHHHCCCCCHHCC		30.5129116813
15PhosphorylationVLLGSGLTILSQPLM
HHHCCCCCHHCCCCH		24.3329116813
18PhosphorylationGSGLTILSQPLMYVK
CCCCCHHCCCCHHHE		26.3829116813
22SulfoxidationTILSQPLMYVKVLIQ
CHHCCCCHHHEHHHH		4.6228183972
23PhosphorylationILSQPLMYVKVLIQV
HHCCCCHHHEHHHHC		12.5629116813
32PhosphorylationKVLIQVGYEPLPPTI
EHHHHCCCCCCCCCC		18.6024043423
38PhosphorylationGYEPLPPTIGRNIFG
CCCCCCCCCCCCCCC		33.8424043423
49S-palmitoylationNIFGRQVCQLPGLFS
CCCCCCHHCCCCHHH		2.3229575903
56PhosphorylationCQLPGLFSYAQHIAS
HCCCCHHHHHHHHHH		25.30-
57PhosphorylationQLPGLFSYAQHIASI
CCCCHHHHHHHHHHH		11.71-
63PhosphorylationSYAQHIASIDGRRGL
HHHHHHHHHCCCCCC		22.17-
72PhosphorylationDGRRGLFTGLTPRLC
CCCCCCCCCCCHHHC		36.0021406692
75PhosphorylationRGLFTGLTPRLCSGV
CCCCCCCCHHHCCCH		14.0124719451
79GlutathionylationTGLTPRLCSGVLGTV
CCCCHHHCCCHHCHH		3.3422555962
79S-palmitoylationTGLTPRLCSGVLGTV
CCCCHHHCCCHHCHH		3.3429575903
79S-nitrosylationTGLTPRLCSGVLGTV
CCCCHHHCCCHHCHH		3.3424105792
80PhosphorylationGLTPRLCSGVLGTVV
CCCHHHCCCHHCHHH		36.2123312004
90UbiquitinationLGTVVHGKVLQHYQE
HCHHHCHHHHHHHHH		25.54-
95PhosphorylationHGKVLQHYQESDKGE
CHHHHHHHHHCCCCC		10.8720873877
98PhosphorylationVLQHYQESDKGEELG
HHHHHHHCCCCCCCC		29.1520873877
100AcetylationQHYQESDKGEELGPG
HHHHHCCCCCCCCCC		76.9926051181
100UbiquitinationQHYQESDKGEELGPG
HHHHHCCCCCCCCCC		76.9921906983
111AcetylationLGPGNVQKEVSSSFD
CCCCCHHHHHHHCHH		56.6626051181
111UbiquitinationLGPGNVQKEVSSSFD
CCCCCHHHHHHHCHH		56.6621906983
114PhosphorylationGNVQKEVSSSFDHVI
CCHHHHHHHCHHHHH		22.7430622161
115PhosphorylationNVQKEVSSSFDHVIK
CHHHHHHHCHHHHHH		39.9530622161
116PhosphorylationVQKEVSSSFDHVIKE
HHHHHHHCHHHHHHH		27.4730622161
122MalonylationSSFDHVIKETTREMI
HCHHHHHHHHHHHHH		48.1732601280
122UbiquitinationSSFDHVIKETTREMI
HCHHHHHHHHHHHHH		48.1721906983
148PhosphorylationFHVITLRSMVQFIGR
CHHHHHHHHHHHHCC		26.81-
149SulfoxidationHVITLRSMVQFIGRE
HHHHHHHHHHHHCCC		1.9128183972
157PhosphorylationVQFIGRESKYCGLCD
HHHHCCCCCCCCCCC		27.80-
159PhosphorylationFIGRESKYCGLCDSI
HHCCCCCCCCCCCHH		10.8823403867
165PhosphorylationKYCGLCDSIITIYRE
CCCCCCCHHEEEHHH		18.20-
283PhosphorylationGNMSRGNSLFFRKVP
CCCCCCCEEEEEECC		29.4030266825
293AcetylationFRKVPFGKTYCCDLK
EEECCCCCEEECCHH		36.3825825284
293UbiquitinationFRKVPFGKTYCCDLK
EEECCCCCEEECCHH		36.38-
300UbiquitinationKTYCCDLKMLI----
CEEECCHHHCC----		20.57-
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 MTCH2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTCH2_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 MTCH2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AL3A2_HUMANALDH3A2physical
26344197
AT1A1_HUMANATP1A1physical
26344197
AT2A2_HUMANATP2A2physical
26344197
ATPG_HUMANATP5C1physical
26344197
VA0D1_HUMANATP6V0D1physical
26344197
CLH1_HUMANCLTCphysical
26344197
GNAI2_HUMANGNAI2physical
26344197
RM37_HUMANMRPL37physical
26344197
NDUAC_HUMANNDUFA12physical
26344197
NDUA2_HUMANNDUFA2physical
26344197
NDUA6_HUMANNDUFA6physical
26344197
NDUB8_HUMANNDUFB8physical
26344197
NDUB9_HUMANNDUFB9physical
26344197
NDUS1_HUMANNDUFS1physical
26344197
NDUS2_HUMANNDUFS2physical
26344197
NDUS3_HUMANNDUFS3physical
26344197
PHB_HUMANPHBphysical
26344197
PHB2_HUMANPHB2physical
26344197
RAB1A_HUMANRAB1Aphysical
26344197
RPN1_HUMANRPN1physical
26344197
SDHB_HUMANSDHBphysical
26344197
C560_HUMANSDHCphysical
26344197
SGPL1_HUMANSGPL1physical
26344197
TOM22_HUMANTOMM22physical
26344197
QCR2_HUMANUQCRC2physical
26344197
VDAC1_HUMANVDAC1physical
26344197
VDAC2_HUMANVDAC2physical
26344197
VDAC3_HUMANVDAC3physical
26344197
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 MTCH2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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