CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023863
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 AFG3-like protein 2 
Protein Synonyms/Alias
 Paraplegin-like protein 
Gene Name
 AFG3L2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
100MGEKKESKPAATTRSacetylation[1]
173SGREITWKDFVNNYLubiquitination[2, 3, 4, 5]
182FVNNYLSKGVVDRLEubiquitination[3, 5]
300ETTAKVLKDEIDVKFubiquitination[6]
306LKDEIDVKFKDVAGCacetylation[7]
342DLGAKIPKGAILTGPubiquitination[3, 5]
481FIGPPDIKGRASIFKubiquitination[3, 5]
508EKDKLARKLASLTPGubiquitination[6]
543LSDSINQKHFEQAIEacetylation[7, 8]
543LSDSINQKHFEQAIEubiquitination[3, 5]
558RVIGGLEKKTQVLQPubiquitination[6]
611GYAQYLPKEQYLYTKubiquitination[3, 5]
Reference
 [1] 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]
 [2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [3] 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]
 [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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] 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]
 [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] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 ATP-dependent protease which is essential for axonal development (By similarity). 
Sequence Annotation
 NP_BIND 348 355 ATP (Potential).
 ACT_SITE 575 575 By similarity.
 METAL 574 574 Zinc; catalytic (By similarity).
 METAL 578 578 Zinc; catalytic (By similarity).
 METAL 649 649 Zinc; catalytic (By similarity).
 MOD_RES 308 308 N6-acetyllysine (By similarity).
 MOD_RES 543 543 N6-acetyllysine (By similarity).  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Disease mutation; Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion; Neurodegeneration; Nucleotide-binding; Protease; Reference proteome; Spinocerebellar ataxia; Transmembrane; Transmembrane helix; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 797 AA 
Protein Sequence
MAHRCLRLWG RGGCWPRGLQ QLLVPGGVGP GEQPCLRTLY RFVTTQARAS RNSLLTDIIA 60
AYQRFCSRPP KGFEKYFPNG KNGKKASEPK EVMGEKKESK PAATTRSSGG GGGGGGKRGG 120
KKDDSHWWSR FQKGDIPWDD KDFRMFFLWT ALFWGGVMFY LLLKRSGREI TWKDFVNNYL 180
SKGVVDRLEV VNKRFVRVTF TPGKTPVDGQ YVWFNIGSVD TFERNLETLQ QELGIEGENR 240
VPVVYIAESD GSFLLSMLPT VLIIAFLLYT IRRGPAGIGR TGRGMGGLFS VGETTAKVLK 300
DEIDVKFKDV AGCEEAKLEI MEFVNFLKNP KQYQDLGAKI PKGAILTGPP GTGKTLLAKA 360
TAGEANVPFI TVSGSEFLEM FVGVGPARVR DLFALARKNA PCILFIDEID AVGRKRGRGN 420
FGGQSEQENT LNQLLVEMDG FNTTTNVVIL AGTNRPDILD PALLRPGRFD RQIFIGPPDI 480
KGRASIFKVH LRPLKLDSTL EKDKLARKLA SLTPGFSGAD VANVCNEAAL IAARHLSDSI 540
NQKHFEQAIE RVIGGLEKKT QVLQPEEKKT VAYHEAGHAV AGWYLEHADP LLKVSIIPRG 600
KGLGYAQYLP KEQYLYTKEQ LLDRMCMTLG GRVSEEIFFG RITTGAQDDL RKVTQSAYAQ 660
IVQFGMNEKV GQISFDLPRQ GDMVLEKPYS EATARLIDDE VRILINDAYK RTVALLTEKK 720
ADVEKVALLL LEKEVLDKND MVELLGPRPF AEKSTYEEFV EGTGSLDEDT SLPEGLKDWN 780
KEREKEKEEP PGEKVAN 797 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
 GO:0051082; F:unfolded protein binding; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007409; P:axonogenesis; IEA:Compara.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0042407; P:cristae formation; IEA:Compara.
 GO:0008053; P:mitochondrial fusion; IEA:Compara.
 GO:0034982; P:mitochondrial protein processing; IEA:Compara.
 GO:0042552; P:myelination; IEA:Compara.
 GO:0021675; P:nerve development; IEA:Compara.
 GO:0007528; P:neuromuscular junction development; IEA:Compara.
 GO:0030163; P:protein catabolic process; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0040014; P:regulation of multicellular organism growth; IEA:Compara.
 GO:0060013; P:righting reflex; IEA:Compara. 
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