CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023310
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Paraplegin 
Protein Synonyms/Alias
 Spastic paraplegia 7 protein 
Gene Name
 SPG7 
Gene Synonyms/Alias
 CAR; CMAR; PGN 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
340RFLQLGAKVPKGALLubiquitination[1]
395ARVRSLFKEARARAPubiquitination[1]
619RDQHLFTKEQLFERMubiquitination[1]
Reference
 [1] 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] 
Functional Description
 Putative ATP-dependent zinc metalloprotease. 
Sequence Annotation
 NP_BIND 349 357 ATP.
 ACT_SITE 575 575 By similarity.
 METAL 574 574 Zinc; catalytic (By similarity).
 METAL 578 578 Zinc; catalytic (By similarity).
 METAL 650 650 Zinc; catalytic (By similarity).
 BINDING 173 173 ATP; via amide nitrogen and carbonyl
 BINDING 492 492 ATP.
 MOD_RES 505 505 Nitrated tyrosine (By similarity).  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Disease mutation; Hereditary spastic paraplegia; Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion; Neurodegeneration; Nitration; Nucleotide-binding; Osteogenesis imperfecta; Polymorphism; Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 795 AA 
Protein Sequence
MAVLLLLLRA LRRGPGPGPR PLWGPGPAWS PGFPARPGRG RPYMASRPPG DLAEAGGRAL 60
QSLQLRLLTP TFEGINGLLL KQHLVQNPVR LWQLLGGTFY FNTSRLKQKN KEKDKSKGKA 120
PEEDEEERRR RERDDQMYRE RLRTLLVIAV VMSLLNALST SGGSISWNDF VHEMLAKGEV 180
QRVQVVPESD VVEVYLHPGA VVFGRPRLAL MYRMQVANID KFEEKLRAAE DELNIEAKDR 240
IPVSYKRTGF FGNALYSVGM TAVGLAILWY VFRLAGMTGR EGGFSAFNQL KMARFTIVDG 300
KMGKGVSFKD VAGMHEAKLE VREFVDYLKS PERFLQLGAK VPKGALLLGP PGCGKTLLAK 360
AVATEAQVPF LAMAGPEFVE VIGGLGAARV RSLFKEARAR APCIVYIDEI DAVGKKRSTT 420
MSGFSNTEEE QTLNQLLVEM DGMGTTDHVI VLASTNRADI LDGALMRPGR LDRHVFIDLP 480
TLQERREIFE QHLKSLKLTQ SSTFYSQRLA ELTPGFSGAD IANICNEAAL HAAREGHTSV 540
HTLNFEYAVE RVLAGTAKKS KILSKEEQKV VAFHESGHAL VGWMLEHTEA VMKVSITPRT 600
NAALGFAQML PRDQHLFTKE QLFERMCMAL GGRASEALSF NEVTSGAQDD LRKVTRIAYS 660
MVKQFGMAPG IGPISFPEAQ EGLMGIGRRP FSQGLQQMMD HEARLLVAKA YRHTEKVLQD 720
NLDKLQALAN ALLEKEVINY EDIEALIGPP PHGPKKMIAP QRWIDAQREK QDLGEEETEE 780
TQQPPLGGEE PTWPK 795 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
 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:0008089; P:anterograde axon cargo transport; IEA:Compara.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0007005; P:mitochondrion organization; IEA:Compara.
 GO:0007399; P:nervous system development; TAS:ProtInc.
 GO:0030163; P:protein catabolic process; IEA:InterPro.
 GO:0006508; P:proteolysis; TAS:ProtInc. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 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
  
PRINTS