Details for: AFG3L2

Gene ID: 10939

Symbol: AFG3L2

Ensembl ID: ENSG00000141385

Description: AFG3 like matrix AAA peptidase subunit 2

Associated with

Other Information

Genular Protein ID: 1523884383

Symbol: AFG32_HUMAN

Name: Paraplegin-like protein

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 10395799

Title: Identification and characterization of AFG3L2, a novel paraplegin-related gene.

PubMed ID: 10395799

DOI: 10.1006/geno.1999.5818

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 14623864

Title: Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia.

PubMed ID: 14623864

DOI: 10.1083/jcb.200304112

PubMed ID: 17101804

Title: Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia.

PubMed ID: 17101804

DOI: 10.1128/mcb.01470-06

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22354088

Title: Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment.

PubMed ID: 22354088

DOI: 10.1038/embor.2012.14

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26387735

Title: SPG7 is an essential and conserved component of the mitochondrial permeability transition pore.

PubMed ID: 26387735

DOI: 10.1016/j.molcel.2015.08.009

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27499296

Title: Mitochondrial protein interaction mapping identifies regulators of respiratory chain function.

PubMed ID: 27499296

DOI: 10.1016/j.molcel.2016.06.033

PubMed ID: 27642048

Title: The m-AAA protease associated with neurodegeneration limits MCU activity in mitochondria.

PubMed ID: 27642048

DOI: 10.1016/j.molcel.2016.08.020

PubMed ID: 35912435

Title: Regulation of mitochondrial proteostasis by the proton gradient.

PubMed ID: 35912435

DOI: 10.15252/embj.2021110476

PubMed ID: 20354562

Title: Early onset and slow progression of SCA28, a rare dominant ataxia in a large four-generation family with a novel AFG3L2 mutation.

PubMed ID: 20354562

DOI: 10.1038/ejhg.2010.40

PubMed ID: 20725928

Title: Missense mutations in the AFG3L2 proteolytic domain account for approximately 1.5% of European autosomal dominant cerebellar ataxias.

PubMed ID: 20725928

DOI: 10.1002/humu.21342

PubMed ID: 20208537

Title: Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28.

PubMed ID: 20208537

DOI: 10.1038/ng.544

PubMed ID: 22022284

Title: Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases.

PubMed ID: 22022284

DOI: 10.1371/journal.pgen.1002325

PubMed ID: 24293060

Title: A novel missense mutation in AFG3L2 associated with late onset and slow progression of spinocerebellar ataxia type 28.

PubMed ID: 24293060

DOI: 10.1007/s12031-013-0187-1

PubMed ID: 26677414

Title: Spinocerebellar ataxia 28: a novel AFG3L2 mutation in a German family with young onset, slow progression and saccadic slowing.

PubMed ID: 26677414

DOI: 10.1186/s40673-015-0038-7

PubMed ID: 26539208

Title: A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability.

PubMed ID: 26539208

DOI: 10.3389/fgene.2015.00311

PubMed ID: 29181157

Title: Non-syndromic isolated dominant optic atrophy caused by the p.R468C mutation in the AFG3 like matrix AAA peptidase subunit 2 gene.

PubMed ID: 29181157

DOI: 10.3892/br.2017.987

PubMed ID: 29053796

Title: Exome sequencing and network analysis identifies shared mechanisms underlying spinocerebellar ataxia.

PubMed ID: 29053796

DOI: 10.1093/brain/awx251

PubMed ID: 30252181

Title: Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation.

PubMed ID: 30252181

DOI: 10.1002/humu.23658

PubMed ID: 32600459

Title: A novel AFG3L2 mutation close to AAA domain leads to aberrant OMA1 and OPA1 processing in a family with optic atrophy.

PubMed ID: 32600459

DOI: 10.1186/s40478-020-00975-w

PubMed ID: 32219868

Title: ATPase domain AFG3L2 mutations alter OPA1 processing and cause optic neuropathy.

PubMed ID: 32219868

DOI: 10.1002/ana.25723

PubMed ID: 32548275

Title: Mutations in the m-AAA proteases AFG3L2 and SPG7 are causing isolated dominant optic atrophy.

PubMed ID: 32548275

DOI: 10.1212/nxg.0000000000000428

Sequence Information:

  • Length: 797
  • Mass: 88584
  • Checksum: EACBB7C5F2EE5E08
  • Sequence:
  • MAHRCLRLWG RGGCWPRGLQ QLLVPGGVGP GEQPCLRTLY RFVTTQARAS RNSLLTDIIA 
    AYQRFCSRPP KGFEKYFPNG KNGKKASEPK EVMGEKKESK PAATTRSSGG GGGGGGKRGG 
    KKDDSHWWSR FQKGDIPWDD KDFRMFFLWT ALFWGGVMFY LLLKRSGREI TWKDFVNNYL 
    SKGVVDRLEV VNKRFVRVTF TPGKTPVDGQ YVWFNIGSVD TFERNLETLQ QELGIEGENR 
    VPVVYIAESD GSFLLSMLPT VLIIAFLLYT IRRGPAGIGR TGRGMGGLFS VGETTAKVLK 
    DEIDVKFKDV AGCEEAKLEI MEFVNFLKNP KQYQDLGAKI PKGAILTGPP GTGKTLLAKA 
    TAGEANVPFI TVSGSEFLEM FVGVGPARVR DLFALARKNA PCILFIDEID AVGRKRGRGN 
    FGGQSEQENT LNQLLVEMDG FNTTTNVVIL AGTNRPDILD PALLRPGRFD RQIFIGPPDI 
    KGRASIFKVH LRPLKLDSTL EKDKLARKLA SLTPGFSGAD VANVCNEAAL IAARHLSDSI 
    NQKHFEQAIE RVIGGLEKKT QVLQPEEKKT VAYHEAGHAV AGWYLEHADP LLKVSIIPRG 
    KGLGYAQYLP KEQYLYTKEQ LLDRMCMTLG GRVSEEIFFG RITTGAQDDL RKVTQSAYAQ 
    IVQFGMNEKV GQISFDLPRQ GDMVLEKPYS EATARLIDDE VRILINDAYK RTVALLTEKK 
    ADVEKVALLL LEKEVLDKND MVELLGPRPF AEKSTYEEFV EGTGSLDEDT SLPEGLKDWN 
    KEREKEKEEP PGEKVAN

Genular Protein ID: 1782704397

Symbol: Q8TA92_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 812
  • Mass: 90194
  • Checksum: 781016A9C82F362A
  • Sequence:
  • GAGGRRRRVE SLGSSVSRRR ASLPGGLSPS RARFPRPPVV ACPRLREQPC LRTLYRFVTT 
    QARASRNSLL TDIIAAYQRF CSRPPKGFEK YFPNGKNGKK ASEPKEVMGE KKESKPAATT 
    RSSGGGGGGG GKRGGKKDDS HWWSRFQKGD IPWDDKDFRM FFLWTALFWG GVMFYLLLKR 
    SGREITWKDF VNNYLSKGVV DRLEVVNKRF VRVTFTPGKT PVDGQYVWFN IGSVDTFERN 
    LETLQQELGI EGENRVPVVY IAESDGSFLL SMLPTVLIIA FLLYTIRRGP AGIGRTGRGM 
    GGLFSVGETT AKVLKDEIDV KFKDVAGCEE AKLEIMEFVN FLKNPKQYQD LGAKIPKGAI 
    LTGPPGTGKT LLAKATAGEA NVPFITVSGS EFLEMFVGVG PARVRDLFAL ARKNAPCILF 
    IDEIDAVGRK RGRGNFGGQS EQENTLNQLL VEMDGFNTTT NVVILAGTNR PDILDPALLR 
    PGRFDRQIFI GPPDIKGRAS IFKVHLRPLK LDSTLEKDKL ARKLASLTPG FSGADVANVC 
    NEAALIAARH LSDSINQKHF EQAIERVIGG LEKKTQVLQP EEKKTVAYHE AGHAVAGWYL 
    EHADPLLKVS IIPRGKGLGY AQYLPKEQYL YTKEQLLDRM CMTLGGRVSE EIFFGRITTG 
    AQDDLRKVTQ SAYAQIVQFG MNEKVGQISF DLPRQGDMVL EKPYSEATAR LIDDEVRILI 
    NDAYKRTVAL LTEKKADVEK VALLLLEKEV LDKNDMVELL GPRPFAEKST YEEFVEGTGS 
    LDEDTSLPEG LKDWNKEREK EKEEPPGEKV AN

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.