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O95166 (GBRAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-aminobutyric acid receptor-associated protein
Alternative name(s):
GABA(A) receptor-associated protein
MM46
Gene names
Name:GABARAP
Synonyms:FLC3B
ORF Names:HT004
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Ref.10

Subunit structure

Interacts with GPHN and NSF By similarity. Interacts with ATG3, ATG7, ATG13, RB1CC1, GABRG2, beta-tubulin and ULK1. Interacts with CALR. Interacts with DDX47. Interacts with TP53INP1 and TP53INP2. Interacts with TBC1D25. Directly interacts with SQSTM1. Interacts with MAPK15. Interacts with TECPR2 and PCM1. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.25

Subcellular location

Endomembrane system By similarity. Cytoplasmcytoskeleton By similarity. Golgi apparatus membrane By similarity. Cytoplasmic vesicleautophagosome. Note: Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae. Colocalizes with microtubules By similarity. Localizes also to discrete punctae along the ciliary axoneme By similarity. Ref.8 Ref.9 Ref.11 Ref.12

Tissue specificity

Heart, brain, placenta, liver, skeletal muscle, kidney and pancreas. Ref.1 Ref.2

Post-translational modification

The precursor molecule is cleaved by ATG4B to form the cytosolic form, GABARAP-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, GABARAP-II. Ref.9

Sequence similarities

Belongs to the ATG8 family.

Ontologies

Keywords
   Biological processApoptosis
Autophagy
Protein transport
Transport
   Cellular componentCytoplasm
Cytoplasmic vesicle
Cytoskeleton
Golgi apparatus
Membrane
Microtubule
   PTMLipoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processautophagy

Inferred from electronic annotation. Source: UniProtKB-KW

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from direct assay Ref.10. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

protein targeting

Traceable author statement Ref.1. Source: ProtInc

synaptic transmission

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

actin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

autophagic vacuole

Inferred from direct assay Ref.12. Source: UniProtKB

autophagic vacuole membrane

Inferred from direct assay Ref.9. Source: UniProtKB

axoneme

Inferred from sequence or structural similarity. Source: UniProtKB

cell body

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle

Inferred from electronic annotation. Source: UniProtKB-KW

lysosome

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement Ref.1. Source: ProtInc

smooth endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGABA receptor binding

Inferred from physical interaction Ref.1. Source: UniProtKB

beta-tubulin binding

Inferred from direct assay Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6Ref.2Ref.10Ref.11Ref.12PubMed 22267086Ref.17Ref.19Ref.20. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 116116Gamma-aminobutyric acid receptor-associated protein
PRO_0000212363
Propeptide1171Removed in mature form
PRO_0000423065

Regions

Region1 – 2222Interaction with beta-tubulin
Region36 – 11782Interaction with GPHN By similarity
Region36 – 6833Interaction with GABRG2 Potential

Sites

Site116 – 1172Cleavage; by ATG4B

Amino acid modifications

Lipidation1161Phosphatidylethanolamine amidated glycine Ref.8

Experimental info

Mutagenesis49 – 502YL → AA: Inhibits interaction with TECPR2.
Mutagenesis671R → A: No effect on interaction with TECPR2. Ref.13
Mutagenesis1161G → A: Impairs localization at the autophagosomal membrane. Ref.9

Secondary structure

.................... 117
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O95166 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: BC0B84B8A51C1E32

FASTA11713,918
        10         20         30         40         50         60 
MKFVYKEEHP FEKRRSEGEK IRKKYPDRVP VIVEKAPKAR IGDLDKKKYL VPSDLTVGQF 

        70         80         90        100        110 
YFLIRKRIHL RAEDALFFFV NNVIPPTSAT MGQLYQEHHE EDFFLYIAYS DESVYGL 

« Hide

References

« Hide 'large scale' references
[1]"GABA(A)-receptor-associated protein links GABA(A) receptors and the cytoskeleton."
Wang H., Bedford F.K., Brandon N.J., Moss S.J., Olsen R.W.
Nature 397:69-72(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH GABRG2 AND BETA-TUBULIN.
Tissue: Brain.
[2]"Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation."
Okazaki N., Yan J., Yuasa S., Ueno T., Kominami E., Masuho Y., Koga H., Muramatsu M.-A.
Brain Res. Mol. Brain Res. 85:1-12(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH ULK1.
Tissue: Frontal cortex.
[3]Iijima M., Mitsui Y.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]Ye M., Fu G., Wu J., Zhou J., Zhang Q., Shen Y., Kan L., He K., Gu B., Chen S., Mao M., Chen Z.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hypothalamus.
[6]"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: INTERACTION WITH ATG7.
[7]"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.
[8]"GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and Apg3."
Tanida I., Komatsu M., Ueno T., Kominami E.
Biochem. Biophys. Res. Commun. 300:637-644(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LIPIDATION AT GLY-116, INTERACTION WITH ATG3 AND ATG7, SUBCELLULAR LOCATION.
[9]"LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation."
Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y., Yoshimori T.
J. Cell Sci. 117:2805-2812(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-116.
[10]"GABAA receptor-associated protein (GABARAP) induces apoptosis by interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX 47)."
Lee J.H., Rho S.B., Chun T.
Biotechnol. Lett. 27:623-628(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DDX47.
[11]"p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy."
Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H., Overvatn A., Bjorkoy G., Johansen T.
J. Biol. Chem. 282:24131-24145(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
[12]"The TP53INP2 protein is required for autophagy in mammalian cells."
Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P., Pebusque M.J., Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.
Mol. Biol. Cell 20:870-881(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TP53INP2.
[13]"Network organization of the human autophagy system."
Behrends C., Sowa M.E., Gygi S.P., Harper J.W.
Nature 466:68-76(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TECPR2, MUTAGENESIS OF 49-TYR-LEU-50 AND ARG-67.
[14]"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].
[15]"OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation."
Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.
J. Cell Biol. 192:839-853(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TBC1D25.
[16]"MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP proteins."
Colecchia D., Strambi A., Sanzone S., Iavarone C., Rossi M., Dall'Armi C., Piccioni F., Verrotti di Pianella A., Chiariello M.
Autophagy 8:1724-1740(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPK15.
[17]"TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death."
Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M., Carrier A., Iovanna J.L., Dusetti N.J.
Cell Death Differ. 19:1525-1535(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53INP1.
[18]"ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs."
Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B., Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.
J. Biol. Chem. 287:39275-39290(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG13; RB1CC1 AND ULK1.
[19]"DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual regulators of autophagy and transcription."
Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T., Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M., Johansen T., Zorzano A.
PLoS ONE 7:E34034-E34034(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53INP1 AND TP53INP2.
[20]"Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION PCM1.
[21]"The X-ray crystal structure and putative ligand-derived peptide binding properties of gamma-aminobutyric acid receptor type A receptor-associated protein."
Knight D., Harris R., McAlister M.S.B., Phelan J.P., Geddes S., Moss S.J., Driscoll P.C., Keep N.H.
J. Biol. Chem. 277:5556-5561(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), INTERACTION WITH GABRG2; TUBULIN ALPHA AND TUBULIN BETA.
[22]"Solution structure of human GABA(A) receptor-associated protein GABARAP: implications for biological function and its regulation."
Stangler T., Mayr L.M., Willbold D.
J. Biol. Chem. 277:13363-13366(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[23]"1H, 13C and '5N resonance assignments of GABARAP, GABAA receptor associated protein."
Kouno T., Miura K., Kanematsu T., Shirakawa M., Hirata M., Kawano K.
J. Biomol. NMR 22:97-98(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[24]"Ligand binding mode of GABAA receptor-associated protein."
Weiergraber O.H., Stangler T., Thielmann Y., Mohrluder J., Wiesehan K., Willbold D.
J. Mol. Biol. 381:1320-1331(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
[25]"Structural framework of the GABARAP-calreticulin interface --implications for substrate binding to endoplasmic reticulum chaperones."
Thielmann Y., Weiergraber O.H., Mohrluder J., Willbold D.
FEBS J. 276:1140-1152(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALR, INTERACTION WITH CALR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF161586 mRNA. Translation: AAD47641.1.
AB030711 mRNA. Translation: BAB21549.1.
AF044671 mRNA. Translation: AAD02337.1.
AF067171 mRNA. Translation: AAD32455.1.
AF183425 mRNA. Translation: AAG09694.1.
CCDSCCDS11092.1.
RefSeqNP_009209.1. NM_007278.1.
UniGeneHs.647421.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GNUX-ray1.75A1-117[»]
1KLVNMR-A1-117[»]
1KM7NMR-A1-117[»]
1KOTNMR-A1-117[»]
3D32X-ray1.30A/B1-117[»]
3DOWX-ray2.30A1-117[»]
3WIMX-ray2.60A1-117[»]
ProteinModelPortalO95166.
SMRO95166. Positions 1-116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116465. 43 interactions.
DIPDIP-35050N.
IntActO95166. 474 interactions.
MINTMINT-206256.
STRING9606.ENSP00000306866.

Protein family/group databases

TCDB1.A.9.5.2. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

PTM databases

PhosphoSiteO95166.

Proteomic databases

MaxQBO95166.
PaxDbO95166.
PRIDEO95166.

Protocols and materials databases

DNASU11337.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302386; ENSP00000306866; ENSG00000170296.
GeneID11337.
KEGGhsa:11337.
UCSCuc002gfb.3. human.

Organism-specific databases

CTD11337.
GeneCardsGC17M007143.
HGNCHGNC:4067. GABARAP.
MIM605125. gene.
neXtProtNX_O95166.
PharmGKBPA28480.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263746.
HOGENOMHOG000232034.
HOVERGENHBG051706.
InParanoidO95166.
KOK08341.
OMATTMGQLY.
OrthoDBEOG70KGRK.
PhylomeDBO95166.
TreeFamTF314556.

Gene expression databases

BgeeO95166.
CleanExHS_GABARAP.
GenevestigatorO95166.

Family and domain databases

InterProIPR004241. Atg8_like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR10969. PTHR10969. 1 hit.
PfamPF02991. Atg8. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGABARAP. human.
EvolutionaryTraceO95166.
GeneWikiGABARAP.
GenomeRNAi11337.
NextBio43075.
PMAP-CutDBO95166.
PROO95166.
SOURCESearch...

Entry information

Entry nameGBRAP_HUMAN
AccessionPrimary (citable) accession number: O95166
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 118 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

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 chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM