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Protein

Autophagy protein 5

Gene

ATG5

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in autophagic vesicle formation.UniRule annotation

GO - Biological processi

  1. autophagic vacuole assembly Source: Ensembl
  2. blood vessel remodeling Source: Ensembl
  3. heart contraction Source: Ensembl
  4. negative regulation of apoptotic process Source: Ensembl
  5. negative regulation of histone H4-K16 acetylation Source: Ensembl
  6. negative regulation of protein ubiquitination Source: Ensembl
  7. negative stranded viral RNA replication Source: Ensembl
  8. otolith development Source: Ensembl
  9. positive regulation of mucus secretion Source: Ensembl
  10. post-translational protein modification Source: Ensembl
  11. regulation of cilium assembly Source: Ensembl
  12. regulation of cytokine secretion involved in immune response Source: Ensembl
  13. regulation of reactive oxygen species metabolic process Source: Ensembl
  14. regulation of release of sequestered calcium ion into cytosol Source: Ensembl
  15. response to drug Source: Ensembl
  16. response to fungus Source: Ensembl
  17. vasodilation Source: Ensembl
  18. ventricular cardiac muscle cell development Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

AutophagyUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Autophagy protein 5UniRule annotation
Gene namesi
Name:ATG5Imported
ORF Names:hCG_32959Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

  1. Preautophagosomal structure membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

  1. autophagic vacuole Source: Ensembl
  2. axoneme Source: Ensembl
  3. ER-mitochondrion membrane contact site Source: Ensembl
  4. pre-autophagosomal structure membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

MembraneUniRule annotation

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24880.

PTM / Processingi

Keywords - PTMi

Isopeptide bondUniRule annotation, Ubl conjugationUniRule annotation

Interactioni

Subunit structurei

Conjugated with ATG12.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
CCHCR1Q8TD31-33EBI-10175276,EBI-10175300
HEL-S-70V9HW803EBI-10175276,EBI-10175326
KEAP1Q141453EBI-10175276,EBI-751001
MEOX2A4D1273EBI-10175276,EBI-10172134
TEKT4Q8WW243EBI-10175276,EBI-750487

Family & Domainsi

Sequence similaritiesi

Belongs to the ATG5 family.UniRule annotation

Phylogenomic databases

HOVERGENiHBG018731.
KOiK08339.
OMAiETPIQWL.

Family and domain databases

InterProiIPR007239. Atg5.
[Graphical view]
PANTHERiPTHR13040. PTHR13040. 1 hit.
PfamiPF04106. APG5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9UGY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLP RVSYLTLVTD
60 70 80 90 100
KVKKHFQKVM RQEDISEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNI
110 120 130 140 150
TVHFKSFPEK DLLHCPSKDA IEAHFMSCMK EADALKHKSQ VINEMQKKDH
160 170 180 190 200
KQLWMGLQND RFDQFWAINR KLMEYPAEEN GFRYIPFRIY QTTTERPFIQ
210 220 230 240 250
KLFRPVAADG QLHTLGDLLK EVCPSAIDPE DGEKKNQVMI HGIEPMLETP
260 270
LQWLSEHLSY PDNFLHISII PQPTD
Length:275
Mass (Da):32,447
Last modified:February 5, 2008 - v1
Checksum:iC33A1E0B3C1DBE5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU283339 mRNA. Translation: ABX79918.1.
JQ924061 mRNA. Translation: AGC52703.1.
CH471051 Genomic DNA. Translation: EAW48415.1.
CH471051 Genomic DNA. Translation: EAW48416.1.
CH471051 Genomic DNA. Translation: EAW48418.1.
RefSeqiNP_001273035.1. NM_001286106.1.
NP_004840.1. NM_004849.3.
UniGeneiHs.486063.

Genome annotation databases

GeneIDi9474.
KEGGihsa:9474.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU283339 mRNA. Translation: ABX79918.1.
JQ924061 mRNA. Translation: AGC52703.1.
CH471051 Genomic DNA. Translation: EAW48415.1.
CH471051 Genomic DNA. Translation: EAW48416.1.
CH471051 Genomic DNA. Translation: EAW48418.1.
RefSeqiNP_001273035.1. NM_001286106.1.
NP_004840.1. NM_004849.3.
UniGeneiHs.486063.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

DNASUi9474.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9474.
KEGGihsa:9474.

Organism-specific databases

CTDi9474.
PharmGKBiPA24880.

Phylogenomic databases

HOVERGENiHBG018731.
KOiK08339.
OMAiETPIQWL.

Miscellaneous databases

ChiTaRSiATG5. human.
GenomeRNAii9474.
NextBioi35504.

Family and domain databases

InterProiIPR007239. Atg5.
[Graphical view]
PANTHERiPTHR13040. PTHR13040. 1 hit.
PfamiPF04106. APG5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE.
  3. "Expression of autophagy related genes in human CD14 cells infected with Streptococcus pyogenes."
    Mayo K., Miller K., Hakami R., Ulrich R., Elliott L.H.
    Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Cloning of cDNA of autophagy-related genes from human prostate cancer cell lines."
    Xu L.-H., Ouyang D.-Y., He X.-H.
    Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiA9UGY9_HUMAN
AccessioniPrimary (citable) accession number: A9UGY9
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: April 29, 2015
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

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.