CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017165
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 AFG3-like protein 2 
Protein Synonyms/Alias
  
Gene Name
 Afg3l2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
96PKEAVGEKKEPQPSGacetylation[1]
97KEAVGEKKEPQPSGPacetylation[2]
116GAGGGGGKRRGKKEDacetylation[2, 3]
116GAGGGGGKRRGKKEDsuccinylation[3]
299ETTAKVLKDEIDVKFacetylation[1]
305LKDEIDVKFKDVAGCacetylation[1]
307DEIDVKFKDVAGCEEacetylation[4, 5]
330VNFLKNPKQYQDLGAacetylation[3]
330VNFLKNPKQYQDLGAsuccinylation[3]
487KGRASIFKVHLRPLKacetylation[5]
501KLDSALEKDKLARKLacetylation[1, 5]
542LSDAINEKHFEQAIEacetylation[1, 4, 5, 6]
557RVIGGLEKKTQVLQPacetylation[5]
567QVLQPEEKKTVAYHEacetylation[1]
600VSIIPRGKGLGYAQYacetylation[3]
600VSIIPRGKGLGYAQYsuccinylation[3]
610GYAQYLPKEQYLYTKubiquitination[7]
686QGDMVLEKPYSEATAacetylation[1, 5]
737LEKEVLDKNDMVQLLacetylation[1]
790EKEEKKEKEKEEPLNacetylation[1]
792EEKKEKEKEEPLNEKacetylation[1]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [7] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 ATP-dependent protease which is essential for axonal development. 
Sequence Annotation
 NP_BIND 347 354 ATP (Potential).
 ACT_SITE 574 574 By similarity.
 METAL 573 573 Zinc; catalytic (By similarity).
 METAL 577 577 Zinc; catalytic (By similarity).
 METAL 648 648 Zinc; catalytic (By similarity).
 MOD_RES 307 307 N6-acetyllysine.
 MOD_RES 542 542 N6-acetyllysine.  
Keyword
 Acetylation; ATP-binding; Complete proteome; Direct protein sequencing; Disease mutation; Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion; Nucleotide-binding; Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 802 AA 
Protein Sequence
MAHRCLLLWS RGGCRRGLPP LLVPRGCLGP DRRPCLRTLY QYATVQTASS RRSLLRDVIA 60
AYQRFCSRPP KGFEKYFPNG KNGKKASEPK EAVGEKKEPQ PSGPQPSGGA GGGGGKRRGK 120
KEDSHWWSRF QKGDFPWDDK DFRMYFLWTA LFWGGVMIYF VFKSSGREIT WKDFVNNYLS 180
KGVVDRLEVV NKRFVRVTFT PGKTPVDGQY VWFNIGSVDT FERNLETLQQ ELGIEGENRV 240
PVVYIAESDG SFLLSMLPTV LIIAFLLYTI RRGPAGIGRT GRGMGGLFSV GETTAKVLKD 300
EIDVKFKDVA GCEEAKLEIM EFVNFLKNPK QYQDLGAKIP KGAILTGPPG TGKTLLAKAT 360
AGEANVPFIT VSGSEFLEMF VGVGPARVRD LFALARKNAP CILFIDEIDA VGRKRGRGNF 420
GGQSEQENTL NQLLVEMDGF NTTTNVVILA GTNRPDILDP ALLRPGRFDR QIFIGPPDIK 480
GRASIFKVHL RPLKLDSALE KDKLARKLAS LTPGFSGADV ANVCNEAALI AARHLSDAIN 540
EKHFEQAIER VIGGLEKKTQ VLQPEEKKTV AYHEAGHAVA GWYLEHADPL LKVSIIPRGK 600
GLGYAQYLPK EQYLYTKEQL LDRMCMTLGG RVSEEIFFGR ITTGAQDDLR KVTQSAYAQI 660
VQFGMNEKVG QISFDLPRQG DMVLEKPYSE ATARMIDDEV RILISDAYRR TVALLTEKKA 720
DVEKVALLLL EKEVLDKNDM VQLLGPRPFT EKSTYEEFVE GTGSLDEDTS LPEGLQDWNK 780
EREKEEKKEK EKEEPLNEKV VS 802 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007409; P:axonogenesis; IMP:MGI.
 GO:0042407; P:cristae formation; IGI:MGI.
 GO:0016265; P:death; IMP:MGI.
 GO:0008053; P:mitochondrial fusion; IGI:MGI.
 GO:0034982; P:mitochondrial protein processing; IGI:MGI.
 GO:0042552; P:myelination; IMP:MGI.
 GO:0021675; P:nerve development; IMP:MGI.
 GO:0007528; P:neuromuscular junction development; IMP:MGI.
 GO:0030163; P:protein catabolic process; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
 GO:0060013; P:righting reflex; IMP:MGI. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 IPR003960; ATPase_AAA_CS.
 IPR005936; FtsH.
 IPR027417; P-loop_NTPase.
 IPR011546; Pept_M41_FtsH_extracell.
 IPR000642; Peptidase_M41. 
Pfam
 PF00004; AAA
 PF06480; FtsH_ext
 PF01434; Peptidase_M41 
SMART
 SM00382; AAA 
PROSITE
 PS00674; AAA 
PRINTS