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Q7Z3C6 (ATG9A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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-related protein 9A
Alternative name(s):
APG9-like 1
mATG9
Gene names
Name:ATG9A
Synonyms:APG9L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length839 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a key role in the organization of the preautophagosomal structure/phagophore assembly site (PAS), the nucleating site for formation of the sequestering vesicle. Cycles between a juxta-nuclear trans-Golgi network compartment and late endosomes. Nutrient starvation induces accumulation on autophagosomes. Starvation-dependent trafficking requires ULK1, ATG13 and SUPT20H. Ref.8

Subunit structure

Interacts with SUPT20H. Ref.11

Subcellular location

Cytoplasmic vesicleautophagosome membrane; Multi-pass membrane protein. Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note: Under amino acid starvation or rapamycin treatment, redistributes from a juxtanuclear clustered pool to a dispersed peripheral cytosolic pool. The starvation-induced redistribution depends on ULK1, ATG13, as well as SH3GLB1. Ref.8 Ref.10 Ref.12 Ref.13 Ref.15

Sequence similarities

Belongs to the ATG9 family.

Sequence caution

The sequence BAB13882.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB15246.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB55119.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z3C6-1)

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 2 (identifier: Q7Z3C6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
Isoform 3 (identifier: Q7Z3C6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     455-528: NAHRSQTRDE...CSFAQMDVRQ → VHFGRVAEPH...ADRGLSVPAS
     529-839: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 839838Autophagy-related protein 9A
PRO_0000119820

Regions

Topological domain2 – 6665Cytoplasmic By similarity
Transmembrane67 – 8721Helical; Potential
Topological domain88 – 13144Lumenal By similarity
Transmembrane132 – 15221Helical; Potential
Topological domain153 – 289137Cytoplasmic By similarity
Transmembrane290 – 31021Helical; Potential
Topological domain311 – 37161Lumenal By similarity
Transmembrane372 – 39221Helical; Potential
Topological domain393 – 4008Cytoplasmic By similarity
Transmembrane401 – 42121Helical; Potential
Topological domain422 – 47352Lumenal By similarity
Transmembrane474 – 49421Helical; Potential
Topological domain495 – 839345Cytoplasmic By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.17 Ref.18
Modified residue181Phosphoserine Ref.9
Modified residue6561Phosphoserine Ref.9
Modified residue7351Phosphoserine Ref.16
Modified residue7381Phosphoserine Ref.16
Modified residue7411Phosphoserine Ref.16
Modified residue8281Phosphoserine Ref.7 Ref.14
Glycosylation991N-linked (GlcNAc...) Ref.8

Natural variations

Alternative sequence1 – 6161Missing in isoform 2.
VSP_013396
Alternative sequence455 – 52874NAHRS…MDVRQ → VHFGRVAEPHCHTPHPHLLP APTGPGDYRLLPKLHRGGRW CGRYLLLCSDGCSPAWSSPV AICWADRGLSVPAS in isoform 3.
VSP_013397
Alternative sequence529 – 839311Missing in isoform 3.
VSP_013398
Natural variant5921S → G. Ref.1 Ref.5
Corresponds to variant rs2276635 [ dbSNP | Ensembl ].
VAR_021835
Natural variant6591Q → H.
Corresponds to variant rs2276634 [ dbSNP | Ensembl ].
VAR_055534

Experimental info

Sequence conflict391H → R in CAD97944. Ref.1
Sequence conflict3001L → P in CAD97944. Ref.1
Sequence conflict3811A → T in AAH65534. Ref.4
Sequence conflict5191C → R in CAD98061. Ref.1
Sequence conflict5671W → R in CAD98061. Ref.1
Sequence conflict6691H → N in BAB15246. Ref.5
Sequence conflict7651A → V in CAD97944. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 69BE087CA550DC42

FASTA83994,447
        10         20         30         40         50         60 
MAQFDTEYQR LEASYSDSPP GEEDLLVHVA EGSKSPWHHI ENLDLFFSRV YNLHQKNGFT 

        70         80         90        100        110        120 
CMLIGEIFEL MQFLFVVAFT TFLVSCVDYD ILFANKMVNH SLHPTEPVKV TLPDAFLPAQ 

       130        140        150        160        170        180 
VCSARIQENG SLITILVIAG VFWIHRLIKF IYNICCYWEI HSFYLHALRI PMSALPYCTW 

       190        200        210        220        230        240 
QEVQARIVQT QKEHQICIHK RELTELDIYH RILRFQNYMV ALVNKSLLPL RFRLPGLGEA 

       250        260        270        280        290        300 
VFFTRGLKYN FELILFWGPG SLFLNEWSLK AEYKRGGQRL ELAQRLSNRI LWIGIANFLL 

       310        320        330        340        350        360 
CPLILIWQIL YAFFSYAEVL KREPGALGAR CWSLYGRCYL RHFNELEHEL QSRLNRGYKP 

       370        380        390        400        410        420 
ASKYMNCFLS PLLTLLAKNG AFFAGSILAV LIALTIYDED VLAVEHVLTT VTLLGVTVTV 

       430        440        450        460        470        480 
CRSFIPDQHM VFCPEQLLRV ILAHIHYMPD HWQGNAHRSQ TRDEFAQLFQ YKAVFILEEL 

       490        500        510        520        530        540 
LSPIVTPLIL IFCLRPRALE IIDFFRNFTV EVVGVGDTCS FAQMDVRQHG HPQWLSAGQT 

       550        560        570        580        590        600 
EASVYQQAED GKTELSLMHF AITNPGWQPP RESTAFLGFL KEQVQRDGAA ASLAQGGLLP 

       610        620        630        640        650        660 
ENALFTSIQS LQSESEPLSL IANVVAGSSC RGPPLPRDLQ GSRHRAEVAS ALRSFSPLQP 

       670        680        690        700        710        720 
GQAPTGRAHS TMTGSGVDAR TASSGSSVWE GQLQSLVLSE YASTEMSLHA LYMHQLHKQQ 

       730        740        750        760        770        780 
AQAEPERHVW HRRESDESGE SAPDEGGEGA RAPQSIPRSA SYPCAAPRPG APETTALHGG 

       790        800        810        820        830 
FQRRYGGITD PGTVPRVPSH FSRLPLGGWA EDGQSASRHP EPVPEEGSED ELPPQVHKV 

« Hide

Isoform 2 [UniParc].

Checksum: DBF1B239460D7250
Show »

FASTA77887,379
Isoform 3 [UniParc].

Checksum: FB9BEBBFA794B352
Show »

FASTA52860,694

References

« Hide 'large scale' references
[1]"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] (ISOFORMS 1 AND 2), VARIANT GLY-592.
Tissue: Fetal brain, Lung endothelial cell, Rectum tumor and Testis.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 3).
Tissue: Brain 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. expand/collapse author list , 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 156-839, VARIANT GLY-592.
Tissue: Embryo.
[6]"Endothelial nitric-oxide synthase antisense (NOS3AS) gene encodes an autophagy-related protein (APG9-like2) highly expressed in trophoblast."
Yamada T., Carson A.R., Caniggia I., Umebayashi K., Yoshimori T., Nakabayashi K., Scherer S.W.
J. Biol. Chem. 280:18283-18290(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes."
Young A.R., Chan E.Y., Hu X.W., Kochl R., Crawshaw S.G., High S., Hailey D.W., Lippincott-Schwartz J., Tooze S.A.
J. Cell Sci. 119:3888-3900(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-99.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism."
Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.
Mol. Cell. Biol. 29:157-171(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Coordinated regulation of autophagy by p38alpha MAPK through mAtg9 and p38IP."
Webber J.L., Tooze S.A.
EMBO J. 29:27-40(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUPT20H.
[12]"Biochemical isolation and characterization of the tubulovesicular LC3-positive autophagosomal compartment."
Gao W., Kang J.H., Liao Y., Ding W.X., Gambotto A.A., Watkins S.C., Liu Y.J., Stolz D.B., Yin X.M.
J. Biol. Chem. 285:1371-1383(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"Atg9A protein, an autophagy-related membrane protein, is localized in the neurons of mouse brains."
Tamura H., Shibata M., Koike M., Sasaki M., Uchiyama Y.
J. Histochem. Cytochem. 58:443-453(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Bif-1 regulates Atg9 trafficking by mediating the fission of Golgi membranes during autophagy."
Takahashi Y., Meyerkord C.L., Hori T., Runkle K., Fox T.E., Kester M., Loughran T.P., Wang H.G.
Autophagy 7:61-73(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TRAFFICKING.
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735; SER-738 AND SER-741, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[18]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL833865 mRNA. Translation: CAD38723.1.
BX537984 mRNA. Translation: CAD97944.1.
BX538192 mRNA. Translation: CAD98061.1.
BX538198 mRNA. Translation: CAD98064.1.
AC068946 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70706.1.
BC001098 mRNA. Translation: AAH01098.2.
BC021202 mRNA. Translation: AAH21202.2.
BC065534 mRNA. Translation: AAH65534.1.
AK021732 mRNA. Translation: BAB13882.1. Different initiation.
AK027448 mRNA. Translation: BAB55119.1. Different initiation.
AK025822 mRNA. Translation: BAB15246.1. Different initiation.
BK004018 mRNA. Translation: DAA05199.1.
RefSeqNP_001070666.1. NM_001077198.2.
NP_076990.4. NM_024085.4.
UniGeneHs.323363.

3D structure databases

ProteinModelPortalQ7Z3C6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122518. 3 interactions.
IntActQ7Z3C6. 12 interactions.
MINTMINT-1422125.

PTM databases

PhosphoSiteQ7Z3C6.

Polymorphism databases

DMDM296439428.

Proteomic databases

PaxDbQ7Z3C6.
PRIDEQ7Z3C6.

Protocols and materials databases

DNASU79065.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361242; ENSP00000355173; ENSG00000198925. [Q7Z3C6-1]
ENST00000396761; ENSP00000379983; ENSG00000198925. [Q7Z3C6-1]
ENST00000409033; ENSP00000386482; ENSG00000198925. [Q7Z3C6-3]
ENST00000409422; ENSP00000386535; ENSG00000198925. [Q7Z3C6-2]
ENST00000409618; ENSP00000386710; ENSG00000198925. [Q7Z3C6-1]
GeneID79065.
KEGGhsa:79065.
UCSCuc002vke.1. human. [Q7Z3C6-1]

Organism-specific databases

CTD79065.
GeneCardsGC02M220074.
H-InvDBHIX0002853.
HIX0077803.
HGNCHGNC:22408. ATG9A.
HPAHPA059551.
MIM612204. gene.
neXtProtNX_Q7Z3C6.
PharmGKBPA134931318.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298729.
HOVERGENHBG050539.
InParanoidQ7Z3C6.
KOK17907.
OMAEVVFFTR.
OrthoDBEOG72C4ZM.
PhylomeDBQ7Z3C6.
TreeFamTF313665.

Gene expression databases

ArrayExpressQ7Z3C6.
BgeeQ7Z3C6.
CleanExHS_ATG9A.
GenevestigatorQ7Z3C6.

Family and domain databases

InterProIPR007241. Autophagy-rel_prot_9.
[Graphical view]
PANTHERPTHR13038. PTHR13038. 1 hit.
PfamPF04109. APG9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiATG9A.
GenomeRNAi79065.
NextBio67835.
PROQ7Z3C6.
SOURCESearch...

Entry information

Entry nameATG9A_HUMAN
AccessionPrimary (citable) accession number: Q7Z3C6
Secondary accession number(s): Q3ZAQ6 expand/collapse secondary AC list , Q6P0N7, Q7Z317, Q7Z320, Q8NDK6, Q8WU65, Q9BVL5, Q9H6L1, Q9HAG7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 99 of the entry and version 3 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

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 2

Human chromosome 2: entries, gene names and cross-references to MIM