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Q9NT62

- ATG3_HUMAN

UniProt

Q9NT62 - ATG3_HUMAN

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Protein

Ubiquitin-like-conjugating enzyme ATG3

Gene

ATG3

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

Functioni

E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei169 – 1702Cleavage; by CASP8
Active sitei264 – 2641Glycyl thioester intermediate1 Publication

GO - Molecular functioni

  1. Atg12 ligase activity Source: UniProtKB
  2. Atg8 ligase activity Source: UniProtKB
  3. enzyme binding Source: UniProtKB
  4. small conjugating protein ligase activity Source: MGI

GO - Biological processi

  1. autophagic vacuole assembly Source: UniProtKB
  2. cellular protein modification process Source: MGI
  3. mitochondrial fragmentation involved in apoptotic process Source: UniProtKB
  4. mitochondrion degradation Source: RefGenome
  5. nucleophagy Source: RefGenome
  6. protein targeting to membrane Source: UniProtKB
  7. protein ubiquitination Source: UniProtKB
  8. regulation of cilium assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Autophagy, Protein transport, Transport, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like-conjugating enzyme ATG3 (EC:6.3.2.-)
Alternative name(s):
Autophagy-related protein 3
Short name:
APG3-like
Short name:
hApg3
Protein PC3-96
Gene namesi
Name:ATG3
Synonyms:APG3, APG3L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:20962. ATG3.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasmic ubiquitin ligase complex Source: MGI
  2. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi264 – 2641C → S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG3 (E2-like enzyme) and GABARAPL1/APG8L (substrate), a stable complex with an O-ester bond is formed. 1 Publication

Organism-specific databases

PharmGKBiPA134883444.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Ubiquitin-like-conjugating enzyme ATG3PRO_0000213569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Cross-linki243 – 243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12)By similarity

Post-translational modificationi

Conjugated to ATG12 at Lys-243. ATG12-conjugation plays a role in regulation of mitochondrial homeostasis and cell death, while it is not involved in PE-conjugation to ATG8-like proteins and autophagy.
Cleaved by CASP8 upon death ligand binding such as tumor necrosis factor-alpha. CASP8 cleavage blocks survival-related autophagy and favors apoptosis.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9NT62.
PaxDbiQ9NT62.
PRIDEiQ9NT62.

PTM databases

PhosphoSiteiQ9NT62.

Expressioni

Tissue specificityi

Widely expressed, with a highest expression in heart, skeletal muscle, kidney, liver and placenta.1 Publication

Gene expression databases

BgeeiQ9NT62.
CleanExiHS_ATG3.
ExpressionAtlasiQ9NT62. baseline and differential.
GenevestigatoriQ9NT62.

Organism-specific databases

HPAiCAB037260.

Interactioni

Subunit structurei

Interacts with ATG7 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5. Interacts with FNBP1L.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPO951665EBI-988094,EBI-712001
GABARAPL1Q9H0R83EBI-988094,EBI-746969
GABARAPL2P605205EBI-988094,EBI-720116
MAP1LC3BQ9GZQ87EBI-988094,EBI-373144
TECPR1Q7Z6L13EBI-988094,EBI-2946676

Protein-protein interaction databases

BioGridi122171. 32 interactions.
DIPiDIP-35052N.
IntActiQ9NT62. 20 interactions.
STRINGi9606.ENSP00000283290.

Structurei

Secondary structure

1
314
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi157 – 1637Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NAWX-ray2.20D/H/L/P140-170[»]
ProteinModelPortaliQ9NT62.
SMRiQ9NT62. Positions 28-84, 193-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi166 – 1694Caspase cleavage motif LETD

Sequence similaritiesi

Belongs to the ATG3 family.Curated

Phylogenomic databases

eggNOGiNOG237080.
GeneTreeiENSGT00390000010308.
HOGENOMiHOG000234613.
HOVERGENiHBG080876.
InParanoidiQ9NT62.
KOiK08343.
OMAiADEWVET.
OrthoDBiEOG7VMP5R.
PhylomeDBiQ9NT62.
TreeFamiTF105903.

Family and domain databases

InterProiIPR007135. Autophagy-rel_prot_3.
IPR019461. Autophagy-rel_prot_3_C.
IPR007134. Autophagy-rel_prot_3_N.
[Graphical view]
PfamiPF03987. Autophagy_act_C. 1 hit.
PF10381. Autophagy_Cterm. 1 hit.
PF03986. Autophagy_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NT62-1) [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
MQNVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC
60 70 80 90 100
PTWQWATGEE LKVKAYLPTG KQFLVTKNVP CYKRCKQMEY SDELEAIIEE
110 120 130 140 150
DDGDGGWVDT YHNTGITGIT EAVKEITLEN KDNIRLQDCS ALCEEEEDED
160 170 180 190 200
EGEAADMEEY EESGLLETDE ATLDTRKIVE ACKAKTDAGG EDAILQTRTY
210 220 230 240 250
DLYITYDKYY QTPRLWLFGY DEQRQPLTVE HMYEDISQDH VKKTVTIENH
260 270 280 290 300
PHLPPPPMCS VHPCRHAEVM KKIIETVAEG GGELGVHMYL LIFLKFVQAV
310
IPTIEYDYTR HFTM
Length:314
Mass (Da):35,864
Last modified:October 1, 2000 - v1
Checksum:i40EFE88DB5FE3EAB
GO
Isoform 2 (identifier: Q9NT62-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     290-314: LLIFLKFVQAVIPTIEYDYTRHFTM → PSLYVRLVAKWLLTIFFLRNLV

Note: No experimental confirmation available.Curated

Show »
Length:311
Mass (Da):35,467
Checksum:iF15A9F8BCBD021A1
GO

Sequence cautioni

The sequence AAH02830.1 differs from that shown. Reason: Frameshift at position 290. Curated
Isoform 2 : The sequence AAH02830.1 differs from that shown. Reason: Frameshift at position 311. Curated
The sequence BAB15237.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei290 – 31425LLIFL…RHFTM → PSLYVRLVAKWLLTIFFLRN LV in isoform 2. 2 PublicationsVSP_013037Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB079384 mRNA. Translation: BAB90843.1.
AF202092 mRNA. Translation: AAG35611.1.
AL137515 mRNA. Translation: CAB70781.1.
BC002830 mRNA. Translation: AAH02830.1. Frameshift.
BC024221 mRNA. Translation: AAH24221.1.
AK025778 mRNA. Translation: BAB15237.1. Different initiation.
CCDSiCCDS2966.1. [Q9NT62-1]
CCDS63721.1. [Q9NT62-2]
PIRiT46276.
RefSeqiNP_001265641.1. NM_001278712.1. [Q9NT62-2]
NP_071933.2. NM_022488.4. [Q9NT62-1]
UniGeneiHs.477126.

Genome annotation databases

EnsembliENST00000283290; ENSP00000283290; ENSG00000144848. [Q9NT62-1]
ENST00000402314; ENSP00000385943; ENSG00000144848. [Q9NT62-2]
GeneIDi64422.
KEGGihsa:64422.
UCSCiuc003dzc.3. human. [Q9NT62-2]
uc003dzd.3. human. [Q9NT62-1]

Polymorphism databases

DMDMi61212142.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB079384 mRNA. Translation: BAB90843.1 .
AF202092 mRNA. Translation: AAG35611.1 .
AL137515 mRNA. Translation: CAB70781.1 .
BC002830 mRNA. Translation: AAH02830.1 . Frameshift.
BC024221 mRNA. Translation: AAH24221.1 .
AK025778 mRNA. Translation: BAB15237.1 . Different initiation.
CCDSi CCDS2966.1. [Q9NT62-1 ]
CCDS63721.1. [Q9NT62-2 ]
PIRi T46276.
RefSeqi NP_001265641.1. NM_001278712.1. [Q9NT62-2 ]
NP_071933.2. NM_022488.4. [Q9NT62-1 ]
UniGenei Hs.477126.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4NAW X-ray 2.20 D/H/L/P 140-170 [» ]
ProteinModelPortali Q9NT62.
SMRi Q9NT62. Positions 28-84, 193-309.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122171. 32 interactions.
DIPi DIP-35052N.
IntActi Q9NT62. 20 interactions.
STRINGi 9606.ENSP00000283290.

PTM databases

PhosphoSitei Q9NT62.

Polymorphism databases

DMDMi 61212142.

Proteomic databases

MaxQBi Q9NT62.
PaxDbi Q9NT62.
PRIDEi Q9NT62.

Protocols and materials databases

DNASUi 64422.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000283290 ; ENSP00000283290 ; ENSG00000144848 . [Q9NT62-1 ]
ENST00000402314 ; ENSP00000385943 ; ENSG00000144848 . [Q9NT62-2 ]
GeneIDi 64422.
KEGGi hsa:64422.
UCSCi uc003dzc.3. human. [Q9NT62-2 ]
uc003dzd.3. human. [Q9NT62-1 ]

Organism-specific databases

CTDi 64422.
GeneCardsi GC03M112251.
HGNCi HGNC:20962. ATG3.
HPAi CAB037260.
MIMi 609606. gene.
neXtProti NX_Q9NT62.
PharmGKBi PA134883444.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG237080.
GeneTreei ENSGT00390000010308.
HOGENOMi HOG000234613.
HOVERGENi HBG080876.
InParanoidi Q9NT62.
KOi K08343.
OMAi ADEWVET.
OrthoDBi EOG7VMP5R.
PhylomeDBi Q9NT62.
TreeFami TF105903.

Miscellaneous databases

ChiTaRSi ATG3. human.
GenomeRNAii 64422.
NextBioi 66413.
PROi Q9NT62.
SOURCEi Search...

Gene expression databases

Bgeei Q9NT62.
CleanExi HS_ATG3.
ExpressionAtlasi Q9NT62. baseline and differential.
Genevestigatori Q9NT62.

Family and domain databases

InterProi IPR007135. Autophagy-rel_prot_3.
IPR019461. Autophagy-rel_prot_3_C.
IPR007134. Autophagy-rel_prot_3_N.
[Graphical view ]
Pfami PF03987. Autophagy_act_C. 1 hit.
PF10381. Autophagy_Cterm. 1 hit.
PF03986. Autophagy_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF CYS-264, SUBCELLULAR LOCATION, FUNCTION, ACTIVE SITE, INTERACTION WITH ATG7 AND ATG12.
    Tissue: Brain.
  2. "Cloning and characterization of human PC3-96 gene."
    Wu B.X., Li Y., Laser M., Crosson C.E., Hazard E.S. III, Ma J.X.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "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 2).
    Tissue: Lung and Lymph.
  5. "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] OF 118-314 (ISOFORM 2).
  6. "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: FUNCTION, INTERACTION WITH THE ATG12-ATG5 CONJUGATE.
  7. "The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification."
    Nemoto T., Tanida I., Tanida-Miyake E., Minematsu-Ikeguchi N., Yokota M., Ohsumi M., Ueno T., Kominami E.
    J. Biol. Chem. 278:39517-39526(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation mediated by human Atg4B, Atg7 and Atg3."
    Tanida I., Sou Y.S., Minematsu-Ikeguchi N., Ueno T., Kominami E.
    FEBS J. 273:2553-2562(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "A novel hybrid yeast-human network analysis reveals an essential role for FNBP1L in antibacterial autophagy."
    Huett A., Ng A., Cao Z., Kuballa P., Komatsu M., Daly M.J., Podolsky D.K., Xavier R.J.
    J. Immunol. 182:4917-4930(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FNBP1L.
  13. "ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death."
    Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C., Debnath J.
    Cell 142:590-600(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATG12.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Cleavage of Atg3 protein by caspase-8 regulates autophagy during receptor-activated cell death."
    Oral O., Oz-Arslan D., Itah Z., Naghavi A., Deveci R., Karacali S., Gozuacik D.
    Apoptosis 17:810-820(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, CLEAVAGE BY CASP8.
  16. "The FAP motif within human ATG7, an autophagy-related E1-like enzyme, is essential for the E2-substrate reaction of LC3 lipidation."
    Tanida I., Yamasaki M., Komatsu M., Ueno T.
    Autophagy 8:88-97(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG3 AND ATG12.
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATG3_HUMAN
AccessioniPrimary (citable) accession number: Q9NT62
Secondary accession number(s): Q6PKC5, Q9H6L9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 111 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 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3