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Protein

Cysteine protease ATG4A

Gene

ATG4A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP. Has also an activity of delipidating enzyme for the PE-conjugated forms.6 Publications

Enzyme regulationi

Inhibited by N-ethylmaleimide. Redox-regulated during autophagy since reducing conditions activate ATG4A whereas an oxidizing environment such as the presence of H2O2 inhibits its activity.2 Publications

Kineticsi

  1. KM=33.9 µM for MAP1LC3B2 Publications
  2. KM=20.8 µM for GABARAP2 Publications
  3. KM=36.7 µM for GABARAPL12 Publications
  4. KM=15.7 µM for GABARAPL22 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei77 – 771NucleophileBy similarity
    Active sitei279 – 2791Sequence Analysis
    Active sitei281 – 2811By similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Autophagy, Protein transport, Transport, Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC54.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cysteine protease ATG4A (EC:3.4.22.-)
    Alternative name(s):
    AUT-like 2 cysteine endopeptidase
    Autophagin-2
    Autophagy-related cysteine endopeptidase 2
    Autophagy-related protein 4 homolog A
    Short name:
    hAPG4A
    Gene namesi
    Name:ATG4A
    Synonyms:APG4A, AUTL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:16489. ATG4A.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: GO_Central
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi81 – 811C → A: Reduces the redox sensitivity and retains activity in presence of H(2)O(2). 1 Publication

    Organism-specific databases

    PharmGKBiPA25184.

    Polymorphism and mutation databases

    BioMutaiATG4A.
    DMDMi61211859.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 398398Cysteine protease ATG4APRO_0000215838Add
    BLAST

    Proteomic databases

    MaxQBiQ8WYN0.
    PaxDbiQ8WYN0.
    PRIDEiQ8WYN0.

    Expressioni

    Tissue specificityi

    Widely expressed, at a low level, and the highest expression is observed in skeletal muscle and brain. Also detected in fetal liver.2 Publications

    Gene expression databases

    BgeeiQ8WYN0.
    ExpressionAtlasiQ8WYN0. baseline and differential.
    GenevisibleiQ8WYN0. HS.

    Organism-specific databases

    HPAiHPA036374.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDKL3Q8IVW43EBI-3044060,EBI-3919850
    GABARAPL1Q9H0R83EBI-3044060,EBI-3464833

    Protein-protein interaction databases

    BioGridi125418. 10 interactions.
    IntActiQ8WYN0. 4 interactions.
    MINTiMINT-3048289.
    STRINGi9606.ENSP00000361306.

    Structurei

    Secondary structure

    1
    398
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 314Combined sources
    Beta strandi34 – 374Combined sources
    Turni38 – 414Combined sources
    Helixi42 – 509Combined sources
    Beta strandi57 – 615Combined sources
    Turni64 – 674Combined sources
    Turni73 – 753Combined sources
    Helixi77 – 9418Combined sources
    Helixi110 – 1167Combined sources
    Beta strandi119 – 1213Combined sources
    Helixi128 – 1369Combined sources
    Turni137 – 1393Combined sources
    Helixi148 – 15912Combined sources
    Turni163 – 1653Combined sources
    Beta strandi168 – 1714Combined sources
    Beta strandi176 – 1783Combined sources
    Helixi179 – 1868Combined sources
    Beta strandi223 – 2308Combined sources
    Beta strandi233 – 2353Combined sources
    Helixi238 – 2403Combined sources
    Helixi241 – 2499Combined sources
    Beta strandi253 – 2608Combined sources
    Beta strandi263 – 2719Combined sources
    Beta strandi274 – 2785Combined sources
    Beta strandi282 – 2854Combined sources
    Helixi298 – 3003Combined sources
    Beta strandi307 – 3104Combined sources
    Helixi311 – 3133Combined sources
    Beta strandi316 – 32611Combined sources
    Helixi327 – 34014Combined sources
    Turni341 – 3433Combined sources
    Beta strandi344 – 3463Combined sources
    Beta strandi348 – 3547Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FUYmodel-A1-398[»]
    2P82X-ray2.10A/B/C/D23-359[»]
    ProteinModelPortaliQ8WYN0.
    SMRiQ8WYN0. Positions 26-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WYN0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C54 family.Curated

    Phylogenomic databases

    eggNOGiNOG239662.
    GeneTreeiENSGT00530000063000.
    HOVERGENiHBG050536.
    InParanoidiQ8WYN0.
    KOiK08342.
    OMAiRILHCFL.
    OrthoDBiEOG73V6KD.
    PhylomeDBiQ8WYN0.
    TreeFamiTF314847.

    Family and domain databases

    InterProiIPR005078. Peptidase_C54.
    [Graphical view]
    PANTHERiPTHR22624. PTHR22624. 1 hit.
    PfamiPF03416. Peptidase_C54. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q8WYN0-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MESVLSKYED QITIFTDYLE EYPDTDELVW ILGKQHLLKT EKSKLLSDIS
    60 70 80 90 100
    ARLWFTYRRK FSPIGGTGPS SDAGWGCMLR CGQMMLAQAL ICRHLGRDWS
    110 120 130 140 150
    WEKQKEQPKE YQRILQCFLD RKDCCYSIHQ MAQMGVGEGK SIGEWFGPNT
    160 170 180 190 200
    VAQVLKKLAL FDEWNSLAVY VSMDNTVVIE DIKKMCRVLP LSADTAGDRP
    210 220 230 240 250
    PDSLTASNQS KGTSAYCSAW KPLLLIVPLR LGINQINPVY VDAFKECFKM
    260 270 280 290 300
    PQSLGALGGK PNNAYYFIGF LGDELIFLDP HTTQTFVDTE ENGTVNDQTF
    310 320 330 340 350
    HCLQSPQRMN ILNLDPSVAL GFFCKEEKDF DNWCSLVQKE ILKENLRMFE
    360 370 380 390
    LVQKHPSHWP PFVPPAKPEV TTTGAEFIDS TEQLEEFDLE EDFEILSV
    Length:398
    Mass (Da):45,378
    Last modified:March 1, 2002 - v1
    Checksum:i3BE892E22E432151
    GO
    Isoform 2 (identifier: Q8WYN0-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         211-272: Missing.

    Show »
    Length:336
    Mass (Da):38,601
    Checksum:i61D7819B73A0D8A9
    GO
    Isoform 3 (identifier: Q8WYN0-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-77: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:321
    Mass (Da):36,533
    Checksum:i5F6CAD07A44EC130
    GO
    Isoform 4 (identifier: Q8WYN0-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         41-64: Missing.

    Note: Gene prediction based on EST data.
    Show »
    Length:374
    Mass (Da):42,453
    Checksum:i4BB385D3C84939CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491I → Y in AAH41862 (PubMed:15489334).Curated
    Sequence conflicti218 – 2181S → T in CAC69076 (Ref. 3) Curated
    Sequence conflicti218 – 2181S → T in CAC69077 (Ref. 3) Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7777Missing in isoform 3. 1 PublicationVSP_025902Add
    BLAST
    Alternative sequencei41 – 6424Missing in isoform 4. CuratedVSP_030499Add
    BLAST
    Alternative sequencei211 – 27262Missing in isoform 2. 1 PublicationVSP_013025Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ504651 mRNA. Translation: CAD43218.1.
    AB066214 mRNA. Translation: BAB83889.1.
    AJ320508 mRNA. Translation: CAC69076.1.
    AJ320509 mRNA. Translation: CAC69077.1.
    AK314429 mRNA. Translation: BAG37044.1.
    AL031177 Genomic DNA. Translation: CAI43137.1.
    AL031177 Genomic DNA. Translation: CAI43138.1.
    AL031177 Genomic DNA. Translation: CAI43141.1.
    AL031177 Genomic DNA. Translation: CAI43142.1.
    CH471120 Genomic DNA. Translation: EAX02689.1.
    CH471120 Genomic DNA. Translation: EAX02691.1.
    CH471120 Genomic DNA. Translation: EAX02693.1.
    BC041862 mRNA. Translation: AAH41862.1.
    BC061696 mRNA. Translation: AAH61696.1.
    CCDSiCCDS14538.1. [Q8WYN0-1]
    CCDS14539.1. [Q8WYN0-2]
    RefSeqiNP_443168.2. NM_052936.3. [Q8WYN0-1]
    NP_840054.1. NM_178270.2. [Q8WYN0-2]
    XP_005262121.1. XM_005262064.2. [Q8WYN0-3]
    XP_011529144.1. XM_011530842.1. [Q8WYN0-3]
    XP_011529145.1. XM_011530843.1. [Q8WYN0-3]
    XP_011529146.1. XM_011530844.1. [Q8WYN0-3]
    UniGeneiHs.8763.

    Genome annotation databases

    EnsembliENST00000345734; ENSP00000298131; ENSG00000101844. [Q8WYN0-2]
    ENST00000372232; ENSP00000361306; ENSG00000101844.
    GeneIDi115201.
    KEGGihsa:115201.
    UCSCiuc004enr.3. human. [Q8WYN0-1]
    uc004ent.3. human. [Q8WYN0-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ504651 mRNA. Translation: CAD43218.1.
    AB066214 mRNA. Translation: BAB83889.1.
    AJ320508 mRNA. Translation: CAC69076.1.
    AJ320509 mRNA. Translation: CAC69077.1.
    AK314429 mRNA. Translation: BAG37044.1.
    AL031177 Genomic DNA. Translation: CAI43137.1.
    AL031177 Genomic DNA. Translation: CAI43138.1.
    AL031177 Genomic DNA. Translation: CAI43141.1.
    AL031177 Genomic DNA. Translation: CAI43142.1.
    CH471120 Genomic DNA. Translation: EAX02689.1.
    CH471120 Genomic DNA. Translation: EAX02691.1.
    CH471120 Genomic DNA. Translation: EAX02693.1.
    BC041862 mRNA. Translation: AAH41862.1.
    BC061696 mRNA. Translation: AAH61696.1.
    CCDSiCCDS14538.1. [Q8WYN0-1]
    CCDS14539.1. [Q8WYN0-2]
    RefSeqiNP_443168.2. NM_052936.3. [Q8WYN0-1]
    NP_840054.1. NM_178270.2. [Q8WYN0-2]
    XP_005262121.1. XM_005262064.2. [Q8WYN0-3]
    XP_011529144.1. XM_011530842.1. [Q8WYN0-3]
    XP_011529145.1. XM_011530843.1. [Q8WYN0-3]
    XP_011529146.1. XM_011530844.1. [Q8WYN0-3]
    UniGeneiHs.8763.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FUYmodel-A1-398[»]
    2P82X-ray2.10A/B/C/D23-359[»]
    ProteinModelPortaliQ8WYN0.
    SMRiQ8WYN0. Positions 26-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi125418. 10 interactions.
    IntActiQ8WYN0. 4 interactions.
    MINTiMINT-3048289.
    STRINGi9606.ENSP00000361306.

    Protein family/group databases

    MEROPSiC54.002.

    Polymorphism and mutation databases

    BioMutaiATG4A.
    DMDMi61211859.

    Proteomic databases

    MaxQBiQ8WYN0.
    PaxDbiQ8WYN0.
    PRIDEiQ8WYN0.

    Protocols and materials databases

    DNASUi115201.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000345734; ENSP00000298131; ENSG00000101844. [Q8WYN0-2]
    ENST00000372232; ENSP00000361306; ENSG00000101844.
    GeneIDi115201.
    KEGGihsa:115201.
    UCSCiuc004enr.3. human. [Q8WYN0-1]
    uc004ent.3. human. [Q8WYN0-2]

    Organism-specific databases

    CTDi115201.
    GeneCardsiGC0XP107334.
    HGNCiHGNC:16489. ATG4A.
    HPAiHPA036374.
    MIMi300663. gene.
    neXtProtiNX_Q8WYN0.
    PharmGKBiPA25184.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG239662.
    GeneTreeiENSGT00530000063000.
    HOVERGENiHBG050536.
    InParanoidiQ8WYN0.
    KOiK08342.
    OMAiRILHCFL.
    OrthoDBiEOG73V6KD.
    PhylomeDBiQ8WYN0.
    TreeFamiTF314847.

    Miscellaneous databases

    EvolutionaryTraceiQ8WYN0.
    GeneWikiiATG4A.
    GenomeRNAii115201.
    NextBioi79530.
    PROiQ8WYN0.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8WYN0.
    ExpressionAtlasiQ8WYN0. baseline and differential.
    GenevisibleiQ8WYN0. HS.

    Family and domain databases

    InterProiIPR005078. Peptidase_C54.
    [Graphical view]
    PANTHERiPTHR22624. PTHR22624. 1 hit.
    PfamiPF03416. Peptidase_C54. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy."
      Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J., Lopez-Otin C.
      J. Biol. Chem. 278:3671-3678(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Ovary.
    2. "LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation."
      Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y., Yoshimori T.
      J. Cell Sci. 117:2805-2812(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN GABARAPL2; GABARAP AND MAP1LC3 CLEAVAGE, TISSUE SPECIFICITY.
    3. "Cloning and sequencing of a second human homologue of the yeast Apg4 cysteine endopeptidase involved in autophagy."
      Chen J.M., Barrett A.J.
      Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Prostate and Testis.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Kidney and Testis.
    8. "The COOH terminus of GATE-16, an intra-Golgi transport modulator, is cleaved by the human cysteine protease HsApg4A."
      Scherz-Shouval R., Sagiv Y., Shorer H., Elazar Z.
      J. Biol. Chem. 278:14053-14058(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN GABARAPL2 CLEAVAGE, ENZYME REGULATION.
    9. "Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4."
      Scherz-Shouval R., Shvets E., Fass E., Shorer H., Gil L., Elazar Z.
      EMBO J. 26:1749-1760(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF CYS-81.
    10. "Kinetics comparisons of mammalian Atg4 homologues indicate selective preferences toward diverse Atg8 substrates."
      Li M., Hou Y., Wang J., Chen X., Shao Z.M., Yin X.M.
      J. Biol. Chem. 286:7327-7338(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "High-throughput fluorescence assay for small-molecule inhibitors of autophagins/Atg4."
      Shu C.W., Madiraju C., Zhai D., Welsh K., Diaz P., Sergienko E., Sano R., Reed J.C.
      J. Biomol. Screen. 16:174-182(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "A high-throughput FRET-based assay for determination of Atg4 activity."
      Li M., Chen X., Ye Q.Z., Vogt A., Yin X.M.
      Autophagy 8:401-412(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    13. "Human cysteine protease ATG4A."
      Walker J.R., Davis T., Mujib S., Butler-Cole C., Finerty P.J., Weigelt J., Sundstrom M., Arrowsmith C.H., Edwards A.M., Bochkarev A., Dhe-Paganon S.
      Submitted (MAR-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 23-359.

    Entry informationi

    Entry nameiATG4A_HUMAN
    AccessioniPrimary (citable) accession number: Q8WYN0
    Secondary accession number(s): A6NCH2
    , B2RAZ7, D3DUY0, O95534, Q5JYY9, Q5JYZ0, Q86VE5, Q96KQ0, Q96KQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 1, 2002
    Last modified: July 22, 2015
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.