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Q6ZNE5 (BAKOR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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:
Beclin 1-associated autophagy-related key regulator

Short name=Barkor
Alternative name(s):
Autophagy-related protein 14-like protein
Short name=Atg14L
Gene names
Name:ATG14
Synonyms:KIAA0831
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex. Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine. Promotes BECN1 translocation from the trans-Golgi network to autophagosomes. Enhances PIK3C3 activity in a BECN1-dependent manner. Ref.6 Ref.8 Ref.10 Ref.11

Subunit structure

Component of the autophagy-specific PI3-kinase complex I composed of ATG14, BECN1, PIK3C3 and PIK3R4, but not UVRAG, nor KIAA0226/Rubicon. UVRAG and ATG14/Barkor form mutually exclusive complexes with BECN1 through direct competition. The complex containing ATG14 up-regulates autophagy, while the one containing Rubicon down-regulates autophagy By similarity. Interacts with PIK3CB By similarity. Interacts with BECN1P1/BECN2. Ref.6 Ref.8 Ref.10 Ref.12 Ref.13

Subcellular location

Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein. Preautophagosomal structure membrane; Peripheral membrane protein. Note: Cytosolic under nutrient-rich conditions. Following autophagy stimuli, such as starvation or rapamycin induction, predominantly detected in cytoplasmic foci, identified as isolation membranes and autophagosomes. Accumulates on highly curved PtdIns3P enriched autophagic membrane via its BATS domain to sense and maintain membrane curvature By similarity. Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme By similarity. Ref.6 Ref.8 Ref.10 Ref.11 Ref.12

Domain

The coiled-coil domain is required for BECN1- and PIK3C3-binding and for autophagy. Ref.11

The final 80 residues in the C-terminus define a minimum required region for autophagosome binding called BATS By similarity. Ref.11

The N-terminal cysteine repeats are required for proper localization to the endoplasmic reticulum (Ref.11). Ref.11

Sequence similarities

Belongs to the ATG14 family.

Sequence caution

The sequence BAA74854.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BECN1Q1445711EBI-2690371,EBI-949378

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6ZNE5-1)

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: Q6ZNE5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-113: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Beclin 1-associated autophagy-related key regulator
PRO_0000050774

Regions

Region43 – 5816Cysteine repeats
Region413 – 49280BATS By similarity
Coiled coil71 – 180110 Potential

Amino acid modifications

Modified residue291Phosphoserine Ref.7 Ref.9
Modified residue4161Phosphoserine Ref.9
Modified residue4291Phosphothreonine Ref.9

Natural variations

Alternative sequence1 – 113113Missing in isoform 2.
VSP_013931
Natural variant591V → I.
Corresponds to variant rs57295720 [ dbSNP | Ensembl ].
VAR_061240
Natural variant1311N → K.
Corresponds to variant rs17675076 [ dbSNP | Ensembl ].
VAR_049514

Experimental info

Mutagenesis431C → A in Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-46, A-55 and A-58. Ref.11
Mutagenesis461C → A in Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-43, A-55 and A-58. Ref.11
Mutagenesis551C → A in Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-43, A-46 and A-58. Ref.11
Mutagenesis581C → A in Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-43, A-46 and A-55. Ref.11
Sequence conflict2561N → S in AAI09090. Ref.5

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: A3EAB0580077D7A6

FASTA49255,309
        10         20         30         40         50         60 
MASPSGKGAR ALEAPGCGPR PLARDLVDSV DDAEGLYVAV ERCPLCNTTR RRLTCAKCVQ 

        70         80         90        100        110        120 
SGDFVYFDGR DRERFIDKKE RLSRLKSKQE EFQKEVLKAM EGKWITDQLR WKIMSCKMRI 

       130        140        150        160        170        180 
EQLKQTICKG NEEMEKNSEG LLKTKEKNQK LYSRAQRHQE KKEKIQRHNR KLGDLVEKKT 

       190        200        210        220        230        240 
IDLRSHYERL ANLRRSHILE LTSVIFPIEE VKTGVRDPAD VSSESDSAMT SSTVSKLAEA 

       250        260        270        280        290        300 
RRTTYLSGRW VCDDHNGDTS ISITGPWISL PNNGDYSAYY SWVEEKKTTQ GPDMEQSNPA 

       310        320        330        340        350        360 
YTISAALCYA TQLVNILSHI LDVNLPKKLC NSEFCGENLS KQKFTRAVKK LNANILYLCF 

       370        380        390        400        410        420 
SQHVNLDQLQ PLHTLRNLMY LVSPSSEHLG RSGPFEVRAD LEESMEFVDP GVAGESDESG 

       430        440        450        460        470        480 
DERVSDEETD LGTDWENLPS PRFCDIPSQS VEVSQSQSTQ ASPPIASSSA GGMISSAAAS 

       490 
VTSWFKAYTG HR 

« Hide

Isoform 2 [UniParc].

Checksum: D6051FFD708A9943
Show »

FASTA37942,434

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[2]"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] (ISOFORM 1).
Tissue: Hippocampus and Trachea.
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[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 1).
[6]"Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG."
Itakura E., Kishi C., Inoue K., Mizushima N.
Mol. Biol. Cell 19:5360-5372(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, FUNCTION, INTERACTION WITH BECN1; PIK3C3 AND PIK3R4, SUBCELLULAR LOCATION.
[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-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase."
Sun Q., Fan W., Chen K., Ding X., Chen S., Zhong Q.
Proc. Natl. Acad. Sci. U.S.A. 105:19211-19216(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BECN1, SUBCELLULAR LOCATION.
[9]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-416 AND THR-429, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages."
Matsunaga K., Saitoh T., Tabata K., Omori H., Satoh T., Kurotori N., Maejima I., Shirahama-Noda K., Ichimura T., Isobe T., Akira S., Noda T., Yoshimori T.
Nat. Cell Biol. 11:385-396(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BECN1; PIK3C3 AND PIK3R4, SUBCELLULAR LOCATION.
[11]"Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L."
Matsunaga K., Morita E., Saitoh T., Akira S., Ktistakis N.T., Izumi T., Noda T., Yoshimori T.
J. Cell Biol. 190:511-521(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-43; CYS-46; CYS-55 AND CYS-58.
[12]"Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG."
Li X., He L., Che K.H., Funderburk S.F., Pan L., Pan N., Zhang M., Yue Z., Zhao Y.
Nat. Commun. 3:662-662(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BECN1, SUBCELLULAR LOCATION.
[13]"Beclin 2 functions in autophagy, degradation of G protein-coupled receptors, and metabolism."
He C., Wei Y., Sun K., Li B., Dong X., Zou Z., Liu Y., Kinch L.N., Khan S., Sinha S., Xavier R.J., Grishin N.V., Xiao G., Eskelinen E.L., Scherer P.E., Whistler J.L., Levine B.
Cell 154:1085-1099(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BECN1P1/BECN2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB020638 mRNA. Translation: BAA74854.2. Different initiation.
AK131251 mRNA. Translation: BAD18430.1.
AK292810 mRNA. Translation: BAF85499.1.
AL158801 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80673.1.
BC109089 mRNA. Translation: AAI09090.1.
BC109090 mRNA. Translation: AAI09091.1.
BR000826 mRNA. Translation: FAA00433.1.
RefSeqNP_055739.2. NM_014924.4.
UniGeneHs.414809.

3D structure databases

ProteinModelPortalQ6ZNE5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116531. 7 interactions.
DIPDIP-48651N.
IntActQ6ZNE5. 7 interactions.
MINTMINT-8304673.

PTM databases

PhosphoSiteQ6ZNE5.

Polymorphism databases

DMDM67461020.

Proteomic databases

PaxDbQ6ZNE5.
PRIDEQ6ZNE5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247178; ENSP00000247178; ENSG00000126775. [Q6ZNE5-1]
GeneID22863.
KEGGhsa:22863.
UCSCuc001xbw.2. human. [Q6ZNE5-1]

Organism-specific databases

CTD22863.
GeneCardsGC14M055834.
HGNCHGNC:19962. ATG14.
HPACAB037242.
HPA053515.
MIM613515. gene.
neXtProtNX_Q6ZNE5.
PharmGKBPA165478560.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236057.
HOVERGENHBG081828.
InParanoidQ6ZNE5.
KOK17889.
OMACVQSGDF.
OrthoDBEOG7SV0WR.
PhylomeDBQ6ZNE5.
TreeFamTF323392.

Gene expression databases

BgeeQ6ZNE5.
CleanExHS_KIAA0831.
GenevestigatorQ6ZNE5.

Family and domain databases

InterProIPR018791. UV_resistance/autophagy_Atg14.
[Graphical view]
PfamPF10186. Atg14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi22863.
NextBio43375.
PROQ6ZNE5.
SOURCESearch...

Entry information

Entry nameBAKOR_HUMAN
AccessionPrimary (citable) accession number: Q6ZNE5
Secondary accession number(s): A6NJE4 expand/collapse secondary AC list , A8K9U5, B7ZWP5, O94920, Q32MK7, Q32MK8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 82 of the entry and version 1 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 14

Human chromosome 14: entries, gene names and cross-references to MIM