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UniProtKB/Swiss-Prot entry Q9H1Y0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ATG5_HUMAN
Primary accession number Q9H1Y0
Secondary accession numbers O60875 Q5JVR2 Q68DI4 Q9H2B8 Q9HCZ7
Integrated into Swiss-Prot on November 16, 2001
Sequence was last modified on November 16, 2001 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 59)
Name and origin of the protein
Protein name Autophagy protein 5
Synonyms APG5-like
Apoptosis-specific protein
Gene name
Name: ATG5
Synonyms: APG5L, ASP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Fetal liver;
DOI=10.1016/S0014-5793(98)00266-X; PubMed=9563500 [NCBI, ExPASy, EBI, Israel, Japan]
Hammond E.M., Brunet C.L., Johnson G.D., Parkhill J., Milner A.E., Brady G., Gregory C.D., Grand R.J.A.;
"Homology between a human apoptosis specific protein and the product of APG5, a gene involved in autophagy in yeast.";
FEBS Lett. 425:391-395(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Chen Y., Piao Y.J., Jiang Y.;
"A novel splicing isoform of human APG5.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
TISSUE=Fetal brain;
The German cDNA consortium;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Endometrium, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION IN APOPTOSIS.
DOI=10.1006/excr.1995.1177; PubMed=7796880 [NCBI, ExPASy, EBI, Israel, Japan]
Grand R.J.A., Milner A.E., Mustoe T., Johnson G.D., Owen D., Grant M.L., Gregory C.D.;
"A novel protein expressed in mammalian cells undergoing apoptosis.";
Exp. Cell Res. 218:439-451(1995).
[7]
CONJUGATION TO ATG12, AND MUTAGENESIS OF LYS-130.
DOI=10.1074/jbc.273.51.33889; PubMed=9852036 [NCBI, ExPASy, EBI, Israel, Japan]
Mizushima N., Sugita H., Yoshimori T., Ohsumi Y.;
"A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy.";
J. Biol. Chem. 273:33889-33892(1998).
[8]
CONJUGATION TO ATG12, AND SUBCELLULAR LOCATION.
TISSUE=Embryonic stem cell;
DOI=10.1083/jcb.152.4.657; PubMed=11266458 [NCBI, ExPASy, EBI, Israel, Japan]
Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y., Suzuki K., Tokuhisa T., Ohsumi Y., Yoshimori T.;
"Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells.";
J. Cell Biol. 152:657-668(2001).
[9]
VARIANT [LARGE SCALE ANALYSIS] MET-58.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
  • FUNCTION: Required for autophagy. Conjugates to ATG12 and associates with isolation membrane to form cup-shaped isolation membrane and autophagosome. The conjugate detaches from the membrane immediately before or after autophagosome formation is completed (By similarity).
  • FUNCTION: May play an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity.
  • INTERACTION:
    O94817:ATG12; NbExp=1; IntAct=EBI-1047414, EBI-746742;
  • SUBCELLULAR LOCATION: Cytoplasm. Note=Colocalizes with nonmuscle actin.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    NameLong
    Isoform IDQ9H1Y0-1
    This is the isoform sequence displayed in this entry.
    NameShort
    SynonymsAPG5beta
    Isoform IDQ9H1Y0-2
    Features which should be applied to build the isoform sequence: VSP_003791.
  • TISSUE SPECIFICITY: Ubiquitous. The mRNA is present at similar levels in viable and apoptotic cells, whereas the protein is dramatically highly expressed in apoptotic cells.
  • INDUCTION: By apoptotic stimuli.
  • PTM: Conjugated to ATG12; which is essential for autophagy, but is not required for association with isolation membrane.
  • SIMILARITY: Belongs to the ATG5 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y11588; CAA72327.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF293841; AAG44955.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR749386; CAH18236.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022067; CAI42297.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133509; CAI42297.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138917; CAI42297.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022067; CAI42298.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133509; CAI42298.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138917; CAI42298.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133509; CAC19459.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022067; CAC19459.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138917; CAC19459.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133509; CAI42831.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022067; CAI42831.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138917; CAI42831.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138917; CAI20313.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133509; CAI20313.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022067; CAI20313.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138917; CAI20314.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022067; CAI20314.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133509; CAI20314.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002699; AAH02699.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093011; AAH93011.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_004840.1; -.
UniGene Hs.486063
3D structure databases
ModBase Q9H1Y0.
Protein-protein interaction databases
IntAct Q9H1Y0; -.
PTM databases
PhosphoSite Q9H1Y0; -.
Organism-specific databases
H-InvDB HIX0006100; -.
HGNC HGNC:589; ATG5.
GenAtlas ATG5.
MIM 604261; gene. [NCBI / EBI]
PharmGKB PA24880; -.
GeneCards Q9H1Y0.
Gene expression databases
ArrayExpress Q9H1Y0; -.
CleanEx HS_ATG5; -.
GermOnline ENSG00000057663; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0043231; Cellular component: intracellular membrane-bounded organelle (inferred from sequence or structural similarity from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0000045; Biological process: autophagosome formation (inferred from sequence or structural similarity from UniProtKB).
GO:0043687; Biological process: post-translational protein modification (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR007239; Autophagy_prot_5.
Graphical view of domain structure.
PANTHER PTHR13040; APG5; 1.
Pfam PF04106; APG5; 1.
Pfam graphical view of domain structure.
BLOCKS Q9H1Y0.
Genome annotation databases
Ensembl ENSG00000057663; Homo sapiens. [Contig view]
GeneID 9474; -.
KEGG hsa:9474; -.
Phylogenomic databases
HOGENOM Q9H1Y0; -.
HOVERGEN Q9H1Y0; -.
Other
LinkHub Q9H1Y0; -.
SOURCE ATG5; Homo sapiens.
ProtoNet Q9H1Y0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Apoptosis; Autophagy; Cytoplasm; Polymorphism; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   275  275     Autophagy protein 5. PRO_0000218994
CROSSLNK   130   130        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12) (By similarity). 
VAR_SEQ   1    79        MTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLP RVSYLTLVTDKVKKHFQKVMRQEDISEIWFEYEGTPLKW -> M (in isoform Short). VSP_003791
VARIANT   58    58  1     K -> M (in a colorectal cancer sample; somatic mutation). VAR_036243 
MUTAGEN   130   130        K->R: Loss of conjugation. 
CONFLICT   79    79        W -> M (in Ref. 4; CAC19459). 
Sequence information
Length: 275 AA [This is the length of the unprocessed precursor] Molecular weight: 32447 Da [This is the MW of the unprocessed precursor] CRC64: C33A1E0B3C1DBE5C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLP RVSYLTLVTD KVKKHFQKVM 

        70         80         90        100        110        120 
RQEDISEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNI TVHFKSFPEK DLLHCPSKDA 

       130        140        150        160        170        180 
IEAHFMSCMK EADALKHKSQ VINEMQKKDH KQLWMGLQND RFDQFWAINR KLMEYPAEEN 

       190        200        210        220        230        240 
GFRYIPFRIY QTTTERPFIQ KLFRPVAADG QLHTLGDLLK EVCPSAIDPE DGEKKNQVMI 

       250        260        270 
HGIEPMLETP LQWLSEHLSY PDNFLHISII PQPTD 

Q9H1Y0 in FASTA format

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