MFN2_HUMAN - dbPTM
MFN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MFN2_HUMAN
UniProt AC O95140
Protein Name Mitofusin-2
Gene Name MFN2
Organism Homo sapiens (Human).
Sequence Length 757
Subcellular Localization Mitochondrion outer membrane
Multi-pass membrane protein . Colocalizes with BAX during apoptosis.
Protein Description Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion. [PubMed: 11181170]
Protein Sequence MSLLFSRCNSIVTVKKNKRHMAEVNASPLKHFVTAKKKINGIFEQLGAYIQESATFLEDTYRNAELDPVTTEEQVLDVKGYLSKVRGISEVLARRHMKVAFFGRTSNGKSTVINAMLWDKVLPSGIGHTTNCFLRVEGTDGHEAFLLTEGSEEKRSAKTVNQLAHALHQDKQLHAGSLVSVMWPNSKCPLLKDDLVLMDSPGIDVTTELDSWIDKFCLDADVFVLVANSESTLMQTEKHFFHKVSERLSRPNIFILNNRWDASASEPEYMEEVRRQHMERCTSFLVDELGVVDRSQAGDRIFFVSAKEVLNARIQKAQGMPEGGGALAEGFQVRMFEFQNFERRFEECISQSAVKTKFEQHTVRAKQIAEAVRLIMDSLHMAAREQQVYCEEMREERQDRLKFIDKQLELLAQDYKLRIKQITEEVERQVSTAMAEEIRRLSVLVDDYQMDFHPSPVVLKVYKNELHRHIEEGLGRNMSDRCSTAITNSLQTMQQDMIDGLKPLLPVSVRSQIDMLVPRQCFSLNYDLNCDKLCADFQEDIEFHFSLGWTMLVNRFLGPKNSRRALMGYNDQVQRPIPLTPANPSMPPLPQGSLTQEEFMVSMVTGLASLTSRTSMGILVVGGVVWKAVGWRLIALSFGLYGLLYVYERLTWTTKAKERAFKRQFVEHASEKLQLVISYTGSNCSHQVQQELSGTFAHLCQQVDVTRENLEQEIAAMNKKIEVLDSLQSKAKLLRNKAGWLDSELNMFTHQYLQPSR
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
6 (in isoform 2)Phosphorylation-35.5724043423
6Phosphorylation--MSLLFSRCNSIVT
--CCCHHHCCCEEEE		35.5729514088
7 (in isoform 2)Phosphorylation-19.1224043423
9 (in isoform 2)Phosphorylation-33.3924043423
10PhosphorylationLLFSRCNSIVTVKKN
CHHHCCCEEEEEECC		23.2825159151
13PhosphorylationSRCNSIVTVKKNKRH
HCCCEEEEEECCCCC		25.5729514088
27PhosphorylationHMAEVNASPLKHFVT
CCEECCCCHHHHHHH		26.0925159151
30UbiquitinationEVNASPLKHFVTAKK
ECCCCHHHHHHHHHH		38.0832015554
36AcetylationLKHFVTAKKKINGIF
HHHHHHHHHHHCHHH		45.2888527
36UbiquitinationLKHFVTAKKKINGIF
HHHHHHHHHHHCHHH		45.2823503661
70PhosphorylationNAELDPVTTEEQVLD
CCCCCCCCCHHHHHC		33.6020068231
71PhosphorylationAELDPVTTEEQVLDV
CCCCCCCCHHHHHCH		37.4520068231
79UbiquitinationEEQVLDVKGYLSKVR
HHHHHCHHHHHHHHC		41.3221906983
79 (in isoform 1)Ubiquitination-41.3221890473
84UbiquitinationDVKGYLSKVRGISEV
CHHHHHHHHCCHHHH		33.1027667366
89PhosphorylationLSKVRGISEVLARRH
HHHHCCHHHHHHHCC		25.2023909892
98UbiquitinationVLARRHMKVAFFGRT
HHHHCCCEEEEEEEC		25.04-
105 (in isoform 2)Ubiquitination-27.2421890473
105PhosphorylationKVAFFGRTSNGKSTV
EEEEEEECCCCCCCE		27.2422210691
111PhosphorylationRTSNGKSTVINAMLW
ECCCCCCCEEEHHHC		28.9723620051
115 (in isoform 2)Ubiquitination-5.3721890473
119 (in isoform 2)Ubiquitination-27.5021890473
154 (in isoform 1)Ubiquitination-47.8321890473
154UbiquitinationLTEGSEEKRSAKTVN
ECCCCHHHHHHHHHH		47.8321906983
158 (in isoform 1)Ubiquitination-55.0121890473
158UbiquitinationSEEKRSAKTVNQLAH
CHHHHHHHHHHHHHH		55.0121906983
159 (in isoform 2)Ubiquitination-25.1421890473
171 (in isoform 1)Ubiquitination-48.4621890473
171UbiquitinationAHALHQDKQLHAGSL
HHHHHHCCCCCCCCE		48.4622817900
192UbiquitinationNSKCPLLKDDLVLMD
CCCCCCCCCCEEEEC		57.80-
243AcetylationTEKHFFHKVSERLSR
HHHHHHHHHHHHHCC		42.1519608861
243UbiquitinationTEKHFFHKVSERLSR
HHHHHHHHHHHHHCC		42.1519608861
249PhosphorylationHKVSERLSRPNIFIL
HHHHHHHCCCCEEEE		52.4920873877
282PhosphorylationRQHMERCTSFLVDEL
HHHHHHHHHHHHHHC		28.8328348404
283PhosphorylationQHMERCTSFLVDELG
HHHHHHHHHHHHHCC		21.8728348404
307 (in isoform 1)Ubiquitination-40.6321890473
307UbiquitinationRIFFVSAKEVLNARI
EEEEEEHHHHHHHHH		40.6321906983
316 (in isoform 1)Ubiquitination-40.0621890473
316UbiquitinationVLNARIQKAQGMPEG
HHHHHHHHHCCCCCC		40.0621906983
355AcetylationCISQSAVKTKFEQHT
HHCHHHHHHHHHHHC		45.7920167786
355UbiquitinationCISQSAVKTKFEQHT
HHCHHHHHHHHHHHC		45.7921963094
357UbiquitinationSQSAVKTKFEQHTVR
CHHHHHHHHHHHCHH		40.9822817900
366UbiquitinationEQHTVRAKQIAEAVR
HHHCHHHHHHHHHHH		31.5027667366
402UbiquitinationEERQDRLKFIDKQLE
HHHHHHHHHHHHHHH		40.9623000965
406UbiquitinationDRLKFIDKQLELLAQ
HHHHHHHHHHHHHHH		52.5523000965
406 (in isoform 1)Ubiquitination-52.5521890473
416 (in isoform 1)Ubiquitination-39.3121890473
416UbiquitinationELLAQDYKLRIKQIT
HHHHHHHHHHHHHHH		39.3123000965
420UbiquitinationQDYKLRIKQITEEVE
HHHHHHHHHHHHHHH		29.2523000965
420 (in isoform 1)Ubiquitination-29.2521890473
423PhosphorylationKLRIKQITEEVERQV
HHHHHHHHHHHHHHH		24.49-
442PhosphorylationAEEIRRLSVLVDDYQ
HHHHHHHHHHHHCCC		16.1616762064
460UbiquitinationHPSPVVLKVYKNELH
CCCCEEEEEHHHHHH		31.7321906983
460 (in isoform 1)Ubiquitination-31.7321890473
463UbiquitinationPVVLKVYKNELHRHI
CEEEEEHHHHHHHHH		47.1127667366
560UbiquitinationVNRFLGPKNSRRALM
HHHHHCCCCHHCHHC		66.8032142685
611PhosphorylationVTGLASLTSRTSMGI
HHHHHHHCCCCCCEE		17.4224719451
651PhosphorylationLYVYERLTWTTKAKE
HHHHHHHHCCHHHHH		27.3025278378
653PhosphorylationVYERLTWTTKAKERA
HHHHHHCCHHHHHHH		17.1225278378
654PhosphorylationYERLTWTTKAKERAF
HHHHHCCHHHHHHHH		22.1425278378
655UbiquitinationERLTWTTKAKERAFK
HHHHCCHHHHHHHHH		50.5127667366
662UbiquitinationKAKERAFKRQFVEHA
HHHHHHHHHHHHHHH		44.2829967540
719 (in isoform 1)Ubiquitination-41.8821890473
719UbiquitinationQEIAAMNKKIEVLDS
HHHHHHHHHHHHHHH		41.8821906983
720UbiquitinationEIAAMNKKIEVLDSL
HHHHHHHHHHHHHHH		38.8121906983
720 (in isoform 1)Ubiquitination-38.8121890473
730 (in isoform 1)Ubiquitination-36.2621890473
730UbiquitinationVLDSLQSKAKLLRNK
HHHHHHHHHHHHHHC		36.2621906983
732UbiquitinationDSLQSKAKLLRNKAG
HHHHHHHHHHHHCCC		52.3622817900
737 (in isoform 1)Ubiquitination-41.6721890473
737UbiquitinationKAKLLRNKAGWLDSE
HHHHHHHCCCCHHHH		41.6721963094
756PhosphorylationTHQYLQPSR------
HHHHCCCCC------		37.3524719451
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
27SPhosphorylationKinaseMAPK9P45984-2
GPS
111TPhosphorylationKinasePINK1Q9BXM7
Uniprot
442SPhosphorylationKinasePINK1Q9BXM7
Uniprot
-KUbiquitinationE3 ubiquitin ligaseMARCHF5Q9NX47
PMID:23727017
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:20871098
-KUbiquitinationE3 ubiquitin ligaseAMFRQ9UKV5
PMID:23427266
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MFN2_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 MFN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HUWE1_HUMANHUWE1physical
22748923
MARH5_HUMANMARCH5physical
23727017
MFN2_HUMANMFN2physical
23727017
HDAC6_HUMANHDAC6physical
26210454
MARH5_HUMANMARCH5physical
26210454
S2538_HUMANSLC25A38physical
26813789
MFN1_HUMANMFN1physical
27713096
Drug and Disease Associations
Kegg Disease
H00264 Charcot-Marie-Tooth disease (CMT); Hereditary motor and sensory neuropathy; Peroneal muscular atroph
OMIM Disease
609260Charcot-Marie-Tooth disease 2A2 (CMT2A2)
601152Charcot-Marie-Tooth disease 6 (CMT6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MFN2_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-243, AND MASS SPECTROMETRY.

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