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Q8WYN0

- ATG4A_HUMAN

UniProt

Q8WYN0 - ATG4A_HUMAN

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Protein
Cysteine protease ATG4A
Gene
ATG4A, APG4A, AUTL2
Organism
Homo sapiens (Human)
Status
Reviewed - 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 GABARAP
  3. KM=36.7 µM for GABARAPL1
  4. KM=15.7 µM for GABARAPL2

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei77 – 771Nucleophile By similarity
Active sitei279 – 2791 Reviewed prediction
Active sitei281 – 2811 By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: RefGenome
  2. cysteine-type peptidase activity Source: UniProtKB

GO - Biological processi

  1. C-terminal protein lipidation Source: RefGenome
  2. autophagic vacuole assembly Source: RefGenome
  3. cellular response to nitrogen starvation Source: RefGenome
  4. late nucleophagy Source: RefGenome
  5. mitochondrion degradation Source: RefGenome
  6. piecemeal microautophagy of nucleus Source: RefGenome
  7. protein delipidation Source: RefGenome
  8. protein processing Source: RefGenome
  9. protein targeting to membrane Source: RefGenome
  10. proteolysis Source: UniProtKB
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: Chromosome X

Organism-specific databases

HGNCiHGNC:16489. ATG4A.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: RefGenome
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Cysteine protease ATG4A
PRO_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

ArrayExpressiQ8WYN0.
BgeeiQ8WYN0.
GenevestigatoriQ8WYN0.

Organism-specific databases

HPAiHPA036374.

Interactioni

Protein-protein interaction databases

BioGridi125418. 3 interactions.
IntActiQ8WYN0. 2 interactions.
MINTiMINT-3048289.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8WYN0.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C54 family.

Phylogenomic databases

eggNOGiNOG239662.
HOVERGENiHBG050536.
InParanoidiQ8WYN0.
KOiK08342.
OMAiKGTSAYC.
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. Align

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

MESVLSKYED QITIFTDYLE EYPDTDELVW ILGKQHLLKT EKSKLLSDIS    50
ARLWFTYRRK FSPIGGTGPS SDAGWGCMLR CGQMMLAQAL ICRHLGRDWS 100
WEKQKEQPKE YQRILQCFLD RKDCCYSIHQ MAQMGVGEGK SIGEWFGPNT 150
VAQVLKKLAL FDEWNSLAVY VSMDNTVVIE DIKKMCRVLP LSADTAGDRP 200
PDSLTASNQS KGTSAYCSAW KPLLLIVPLR LGINQINPVY VDAFKECFKM 250
PQSLGALGGK PNNAYYFIGF LGDELIFLDP HTTQTFVDTE ENGTVNDQTF 300
HCLQSPQRMN ILNLDPSVAL GFFCKEEKDF DNWCSLVQKE ILKENLRMFE 350
LVQKHPSHWP PFVPPAKPEV TTTGAEFIDS TEQLEEFDLE EDFEILSV 398
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7777Missing in isoform 3.
VSP_025902Add
BLAST
Alternative sequencei41 – 6424Missing in isoform 4.
VSP_030499Add
BLAST
Alternative sequencei211 – 27262Missing in isoform 2.
VSP_013025Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491I → Y in AAH41862. 1 Publication
Sequence conflicti218 – 2181S → T in CAC69076. 1 Publication
Sequence conflicti218 – 2181S → T in CAC69077. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005262064.1. [Q8WYN0-3]
UniGeneiHs.8763.

Genome annotation databases

EnsembliENST00000345734; ENSP00000298131; ENSG00000101844. [Q8WYN0-2]
ENST00000372232; ENSP00000361306; ENSG00000101844. [Q8WYN0-1]
ENST00000372254; ENSP00000361328; ENSG00000101844. [Q8WYN0-5]
GeneIDi115201.
KEGGihsa:115201.
UCSCiuc004enr.3. human. [Q8WYN0-1]
uc004ent.3. human. [Q8WYN0-2]

Polymorphism databases

DMDMi61211859.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14538.1. [Q8WYN0-1 ]
CCDS14539.1. [Q8WYN0-2 ]
RefSeqi NP_443168.2. NM_052936.3. [Q8WYN0-1 ]
NP_840054.1. NM_178270.2. [Q8WYN0-2 ]
XP_005262121.1. XM_005262064.1. [Q8WYN0-3 ]
UniGenei Hs.8763.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FUY model - A 1-398 [» ]
2P82 X-ray 2.10 A/B/C/D 23-359 [» ]
ProteinModelPortali Q8WYN0.
SMRi Q8WYN0. Positions 26-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125418. 3 interactions.
IntActi Q8WYN0. 2 interactions.
MINTi MINT-3048289.

Protein family/group databases

MEROPSi C54.002.

Polymorphism databases

DMDMi 61211859.

Proteomic databases

MaxQBi Q8WYN0.
PaxDbi Q8WYN0.
PRIDEi Q8WYN0.

Protocols and materials databases

DNASUi 115201.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000345734 ; ENSP00000298131 ; ENSG00000101844 . [Q8WYN0-2 ]
ENST00000372232 ; ENSP00000361306 ; ENSG00000101844 . [Q8WYN0-1 ]
ENST00000372254 ; ENSP00000361328 ; ENSG00000101844 . [Q8WYN0-5 ]
GeneIDi 115201.
KEGGi hsa:115201.
UCSCi uc004enr.3. human. [Q8WYN0-1 ]
uc004ent.3. human. [Q8WYN0-2 ]

Organism-specific databases

CTDi 115201.
GeneCardsi GC0XP107334.
HGNCi HGNC:16489. ATG4A.
HPAi HPA036374.
MIMi 300663. gene.
neXtProti NX_Q8WYN0.
PharmGKBi PA25184.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239662.
HOVERGENi HBG050536.
InParanoidi Q8WYN0.
KOi K08342.
OMAi KGTSAYC.
OrthoDBi EOG73V6KD.
PhylomeDBi Q8WYN0.
TreeFami TF314847.

Miscellaneous databases

EvolutionaryTracei Q8WYN0.
GeneWikii ATG4A.
GenomeRNAii 115201.
NextBioi 79530.
PROi Q8WYN0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8WYN0.
Bgeei Q8WYN0.
Genevestigatori Q8WYN0.

Family and domain databases

InterProi IPR005078. Peptidase_C54.
[Graphical view ]
PANTHERi PTHR22624. PTHR22624. 1 hit.
Pfami PF03416. Peptidase_C54. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 102 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

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