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Q9H1Y0 (ATG5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Autophagy protein 5
Alternative name(s):
APG5-like
Apoptosis-specific protein
Gene names
Name:ATG5
Synonyms:APG5L, ASP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. The ATG12-ATG5 conjugate also negatively regulates the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Also plays a role in translation or delivery of incoming viral RNA to the translation apparatus. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway. Ref.6 Ref.10 Ref.12 Ref.14 Ref.16 Ref.19

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. Plays a crucial role in IFN-gamma-induced autophagic cell death by interacting with FADD. Ref.6 Ref.10 Ref.12 Ref.14 Ref.16 Ref.19

Subunit structure

Forms a conjugate with ATG12. The ATG5-ATG12 conjugate forms a complex with several units of ATG16L. Interacts with TECPR1; the interaction is direct and does not take place when ATG16L is associated with the ATG5-ATG12 conjugate. ATG12-ATG5 interacts with MAVS, MGA and RARRES3. Interacts with ATG3, ATG7 and ATG10. Interacts with FADD. Interacts transiently interacts with hepatitis C virus (HCV) protein NS5B during HCV infection. Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.18 Ref.20

Subcellular location

Cytoplasm. Preautophagosomal structure membrane; Peripheral membrane protein. Note: Colocalizes with nonmuscle actin. The conjugate detaches from the membrane immediately before or after autophagosome formation is completed By similarity. Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme. Ref.9 Ref.12 Ref.16

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.

Post-translational modification

Conjugated to ATG12; which is essential for autophagy, but is not required for association with isolation membrane.

Acetylated by EP300. Ref.15

Sequence similarities

Belongs to the ATG5 family.

Ontologies

Keywords
   Biological processApoptosis
Autophagy
Immunity
Innate immunity
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

autophagic vacuole assembly

Inferred from sequence or structural similarity. Source: UniProtKB

autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

heart contraction

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

negative regulation of type I interferon production

Traceable author statement. Source: Reactome

otolith development

Inferred from electronic annotation. Source: Ensembl

post-translational protein modification

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cilium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cytokine secretion involved in immune response

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to fungus

Inferred from electronic annotation. Source: Ensembl

vasodilation

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentautophagic vacuole

Inferred from direct assay PubMed 15292400. Source: MGI

axoneme

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

pre-autophagosomal structure membrane

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q9H1Y0-1)

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.
Isoform Short (identifier: Q9H1Y0-2)

Also known as: APG5beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: MTDDKDVLRD...FEYEGTPLKW → M

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 275275Autophagy protein 5
PRO_0000218994

Amino acid modifications

Modified residue11N-acetylmethionine Ref.21
Cross-link130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12) Probable

Natural variations

Alternative sequence1 – 7979MTDDK…TPLKW → M in isoform Short.
VSP_003791
Natural variant581K → M in a colorectal cancer sample; somatic mutation. Ref.23
VAR_036243

Experimental info

Mutagenesis1301K → R: Loss of conjugation. Ref.7
Sequence conflict791W → M in CAC19459. Ref.4

Secondary structure

.................................................. 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified November 16, 2001. Version 2.
Checksum: C33A1E0B3C1DBE5C

FASTA27532,447
        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 

« Hide

Isoform Short (APG5beta) [UniParc].

Checksum: 05FC581F6EABB753
Show »

FASTA19722,931

References

« Hide 'large scale' references
[1]"Homology between a human apoptosis specific protein and the product of APG5, a gene involved in autophagy in yeast."
Hammond E.M., Brunet C.L., Johnson G.D., Parkhill J., Milner A.E., Brady G., Gregory C.D., Grand R.J.A.
FEBS Lett. 425:391-395(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Fetal liver.
[2]"A novel splicing isoform of human APG5."
Chen Y., Piao Y.J., Jiang Y.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
Tissue: Fetal brain.
[4]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM LONG).
Tissue: Endometrium and Placenta.
[6]"A novel protein expressed in mammalian cells undergoing apoptosis."
Grand R.J.A., Milner A.E., Mustoe T., Johnson G.D., Owen D., Grant M.L., Gregory C.D.
Exp. Cell Res. 218:439-451(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOSIS.
[7]"A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy."
Mizushima N., Sugita H., Yoshimori T., Ohsumi Y.
J. Biol. Chem. 273:33889-33892(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CONJUGATION TO ATG12 AT LYS-130, MUTAGENESIS OF LYS-130.
[8]"The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3."
Tanida I., Tanida-Miyake E., Ueno T., Kominami E.
J. Biol. Chem. 276:1701-1706(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CONJUGATION TO ATG12.
[9]"Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells."
Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y., Suzuki K., Tokuhisa T., Ohsumi Y., Yoshimori T.
J. Cell Biol. 152:657-668(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CONJUGATION TO ATG12, SUBCELLULAR LOCATION.
Tissue: Embryonic stem cell.
[10]"Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3 processing."
Tanida I., Nishitani T., Nemoto T., Ueno T., Kominami E.
Biochem. Biophys. Res. Commun. 296:1164-1170(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG3, CONJUGATION TO ATG12, FUNCTION.
[11]"Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p."
Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.
J. Biol. Chem. 277:13739-13744(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG3, CONJUGATION TO ATG12.
[12]"Essential roles of Atg5 and FADD in autophagic cell death: dissection of autophagic cell death into vacuole formation and cell death."
Pyo J.O., Jang M.H., Kwon Y.K., Lee H.J., Jun J.I., Woo H.N., Cho D.H., Choi B., Lee H., Kim J.H., Mizushima N., Oshumi Y., Jung Y.K.
J. Biol. Chem. 280:20722-20729(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FADD.
[13]"Stimulation of ATG12-ATG5 conjugation by ribonucleic acid."
Shao Y., Gao Z., Feldman T., Jiang X.
Autophagy 3:10-16(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CONJUGATION TO ATG12.
[14]"The Atg5-Atg12 conjugate associates with innate antiviral immune responses."
Jounai N., Takeshita F., Kobiyama K., Sawano A., Miyawaki A., Xin K.Q., Ishii K.J., Kawai T., Akira S., Suzuki K., Okuda K.
Proc. Natl. Acad. Sci. U.S.A. 104:14050-14055(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INNATE IMMUNE RESPONSE, INTERACTION WITH MAVS; MGA AND RARRES3.
[15]"Regulation of autophagy by the p300 acetyltransferase."
Lee I.H., Finkel T.
J. Biol. Chem. 284:6322-6328(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION BY EP300.
[16]"Autophagy protein ATG5 interacts transiently with the hepatitis C virus RNA polymerase (NS5B) early during infection."
Guevin C., Manna D., Belanger C., Konan K.V., Mak P., Labonte P.
Virology 405:1-7(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HEPATITIS C VIRUS PROTEIN NS5B.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"A Tecpr1-dependent selective autophagy pathway targets bacterial pathogens."
Ogawa M., Yoshikawa Y., Kobayashi T., Mimuro H., Fukumatsu M., Kiga K., Piao Z., Ashida H., Yoshida M., Kakuta S., Koyama T., Goto Y., Nagatake T., Nagai S., Kiyono H., Kawalec M., Reichhart J.M., Sasakawa C.
Cell Host Microbe 9:376-389(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TECPR1.
[19]"Autophagy proteins LC3B, ATG5 and ATG12 participate in quality control after mitochondrial damage and influence lifespan."
Mai S., Muster B., Bereiter-Hahn J., Jendrach M.
Autophagy 8:47-62(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"A mammalian autophagosome maturation mechanism mediated by TECPR1 and the Atg12-Atg5 conjugate."
Chen D., Fan W., Lu Y., Ding X., Chen S., Zhong Q.
Mol. Cell 45:629-641(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TECPR1.
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Structure of the human ATG12-ATG5 conjugate required for LC3 lipidation in autophagy."
Otomo C., Metlagel Z., Takaesu G., Otomo T.
Nat. Struct. Mol. Biol. 20:59-66(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN CONJUGATION WITH ATG12.
[23]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-58.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11588 mRNA. Translation: CAA72327.1.
AF293841 mRNA. Translation: AAG44955.1.
CR749386 mRNA. Translation: CAH18236.1.
AL022067, AL133509, AL138917 Genomic DNA. Translation: CAI42297.1.
AL022067, AL133509, AL138917 Genomic DNA. Translation: CAI42298.1.
AL133509, AL022067, AL138917 Genomic DNA. Translation: CAC19459.2.
AL133509, AL022067, AL138917 Genomic DNA. Translation: CAI42831.1.
AL138917, AL133509, AL022067 Genomic DNA. Translation: CAI20313.1.
AL138917, AL022067, AL133509 Genomic DNA. Translation: CAI20314.1.
BC002699 mRNA. Translation: AAH02699.1.
BC093011 mRNA. Translation: AAH93011.1.
RefSeqNP_001273035.1. NM_001286106.1.
NP_001273036.1. NM_001286107.1.
NP_001273037.1. NM_001286108.1.
NP_001273040.1. NM_001286111.1.
NP_004840.1. NM_004849.3.
UniGeneHs.486063.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GDKX-ray2.70B/E1-275[»]
4GDLX-ray2.88B1-275[»]
4NAWX-ray2.20B/F/J/N1-275[»]
ProteinModelPortalQ9H1Y0.
SMRQ9H1Y0. Positions 3-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114859. 16 interactions.
DIPDIP-29758N.
IntActQ9H1Y0. 33 interactions.
STRING9606.ENSP00000343313.

PTM databases

PhosphoSiteQ9H1Y0.

Polymorphism databases

DMDM17366828.

Proteomic databases

PaxDbQ9H1Y0.
PRIDEQ9H1Y0.

Protocols and materials databases

DNASU9474.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343245; ENSP00000343313; ENSG00000057663. [Q9H1Y0-1]
ENST00000369070; ENSP00000358066; ENSG00000057663. [Q9H1Y0-2]
ENST00000369076; ENSP00000358072; ENSG00000057663. [Q9H1Y0-1]
GeneID9474.
KEGGhsa:9474.
UCSCuc003prf.3. human. [Q9H1Y0-1]
uc003prg.3. human. [Q9H1Y0-2]

Organism-specific databases

CTD9474.
GeneCardsGC06M106632.
HGNCHGNC:589. ATG5.
HPACAB034432.
CAB037309.
HPA042973.
MIM604261. gene.
neXtProtNX_Q9H1Y0.
PharmGKBPA24880.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271554.
HOGENOMHOG000007893.
HOVERGENHBG018731.
InParanoidQ9H1Y0.
KOK08339.
OMASCIKEAD.
OrthoDBEOG72C50T.
PhylomeDBQ9H1Y0.
TreeFamTF314415.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9H1Y0.
BgeeQ9H1Y0.
CleanExHS_ATG5.
GenevestigatorQ9H1Y0.

Family and domain databases

InterProIPR007239. Atg5.
[Graphical view]
PANTHERPTHR13040. PTHR13040. 1 hit.
PfamPF04106. APG5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATG5. human.
GeneWikiATG5.
GenomeRNAi9474.
NextBio35504.
PROQ9H1Y0.
SOURCESearch...

Entry information

Entry nameATG5_HUMAN
AccessionPrimary (citable) accession number: Q9H1Y0
Secondary accession number(s): O60875 expand/collapse secondary AC list , Q5JVR2, Q68DI4, Q9H2B8, Q9HCZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM