CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001529
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mitofusin-2 
Protein Synonyms/Alias
 Transmembrane GTPase MFN2 
Gene Name
 MFN2 
Gene Synonyms/Alias
 CPRP1; KIAA0214 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30EVNASPLKHFVTAKKubiquitination[1]
79EEQVLDVKGYLSKVRubiquitination[1, 2, 3]
84DVKGYLSKVRGISEVubiquitination[1]
98VLARRHMKVAFFGRTubiquitination[4]
154LTEGSEEKRSAKTVNubiquitination[1, 2, 3, 5, 6]
158SEEKRSAKTVNQLAHubiquitination[1, 2, 3]
171AHALHQDKQLHAGSLubiquitination[2]
243TEKHFFHKVSERLSRacetylation[7]
243TEKHFFHKVSERLSRubiquitination[3]
307RIFFVSAKEVLNARIubiquitination[1, 2, 3, 5, 6, 8]
316VLNARIQKAQGMPEGubiquitination[1, 2, 3, 5, 6]
355CISQSAVKTKFEQHTacetylation[9]
355CISQSAVKTKFEQHTubiquitination[5, 6]
357SQSAVKTKFEQHTVRubiquitination[1, 2]
406DRLKFIDKQLELLAQubiquitination[1, 2, 3, 4, 6, 10]
416ELLAQDYKLRIKQITubiquitination[1, 2, 3, 4, 10]
420QDYKLRIKQITEEVEubiquitination[1, 2, 3, 6]
460HPSPVVLKVYKNELHubiquitination[1, 2, 5]
560VNRFLGPKNSRRALMubiquitination[3]
719QEIAAMNKKIEVLDSubiquitination[1, 2]
720EIAAMNKKIEVLDSLubiquitination[1, 2, 3]
730VLDSLQSKAKLLRNKubiquitination[1, 2, 3]
737KAKLLRNKAGWLDSEubiquitination[1, 2, 5]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [10] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional Description
 Essential transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. MFN2 acts independently of the cytoskeleton. It therefore plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes. Overexpression induces the formation of mitochondrial networks. Plays an important role in the regulation of vascular smooth muscle cell proliferation. 
Sequence Annotation
 NP_BIND 103 110 GTP (Probable).
 NP_BIND 199 203 GTP (Probable).
 NP_BIND 258 261 GTP (Probable).  
Keyword
 Alternative splicing; Charcot-Marie-Tooth disease; Coiled coil; Complete proteome; Disease mutation; GTP-binding; Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane; Neuropathy; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 757 AA 
Protein Sequence
MSLLFSRCNS IVTVKKNKRH MAEVNASPLK HFVTAKKKIN GIFEQLGAYI QESATFLEDT 60
YRNAELDPVT TEEQVLDVKG YLSKVRGISE VLARRHMKVA FFGRTSNGKS TVINAMLWDK 120
VLPSGIGHTT NCFLRVEGTD GHEAFLLTEG SEEKRSAKTV NQLAHALHQD KQLHAGSLVS 180
VMWPNSKCPL LKDDLVLMDS PGIDVTTELD SWIDKFCLDA DVFVLVANSE STLMQTEKHF 240
FHKVSERLSR PNIFILNNRW DASASEPEYM EEVRRQHMER CTSFLVDELG VVDRSQAGDR 300
IFFVSAKEVL NARIQKAQGM PEGGGALAEG FQVRMFEFQN FERRFEECIS QSAVKTKFEQ 360
HTVRAKQIAE AVRLIMDSLH MAAREQQVYC EEMREERQDR LKFIDKQLEL LAQDYKLRIK 420
QITEEVERQV STAMAEEIRR LSVLVDDYQM DFHPSPVVLK VYKNELHRHI EEGLGRNMSD 480
RCSTAITNSL QTMQQDMIDG LKPLLPVSVR SQIDMLVPRQ CFSLNYDLNC DKLCADFQED 540
IEFHFSLGWT MLVNRFLGPK NSRRALMGYN DQVQRPIPLT PANPSMPPLP QGSLTQEEFM 600
VSMVTGLASL TSRTSMGILV VGGVVWKAVG WRLIALSFGL YGLLYVYERL TWTTKAKERA 660
FKRQFVEHAS EKLQLVISYT GSNCSHQVQQ ELSGTFAHLC QQVDVTRENL EQEIAAMNKK 720
IEVLDSLQSK AKLLRNKAGW LDSELNMFTH QYLQPSR 757 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031306; C:intrinsic to mitochondrial outer membrane; ISS:UniProtKB.
 GO:0015630; C:microtubule cytoskeleton; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0001825; P:blastocyst formation; IEA:Compara.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0048593; P:camera-type eye morphogenesis; IEA:Compara.
 GO:0008053; P:mitochondrial fusion; NAS:UniProtKB.
 GO:0007006; P:mitochondrial membrane organization; IDA:UniProtKB.
 GO:0051646; P:mitochondrion localization; IDA:UniProtKB.
 GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:UniProtKB.
 GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISS:UniProtKB.
 GO:0006626; P:protein targeting to mitochondrion; IDA:UniProtKB. 
Interpro
 IPR001401; Dynamin_GTPase.
 IPR006884; Fzo/mitofusin_HR2.
 IPR027089; Mitofusin-2.
 IPR027094; Mitofusin_fam.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00350; Dynamin_N
 PF04799; Fzo_mitofusin 
SMART
  
PROSITE
  
PRINTS