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Q9DCD6 (GBRAP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Gene names
Name:Gabarap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 play 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 By similarity.

Subunit structure

Interacts with ATG3, ATG7, CALR, DDX47, GABRG2, TUBA1, ULK1 and NSF By similarity. Interacts with beta-tubulin and GPHN. Interacts with TP53INP1 and TP53INP2 By similarity. Interacts with TBC1D25. Directly interacts with SQSTM1 By similarity. Interacts with MAPK15 By similarity. Interacts with TECPR2 By similarity. Ref.1 Ref.5 Ref.7 Ref.8

Subcellular location

Endomembrane system By similarity. Cytoplasmcytoskeleton By similarity. Golgi apparatus membrane By similarity. Cytoplasmic vesicleautophagosome By similarity. 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. Ref.1 Ref.6 Ref.9

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.6

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 termComplete 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 sequence or structural similarity. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from direct assay Ref.1. Source: MGI

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 11146101. Source: MGI

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

actin cytoskeleton

Inferred from direct assay Ref.1. Source: MGI

autophagic vacuole

Inferred from sequence or structural similarity. Source: UniProtKB

autophagic vacuole membrane

Inferred from electronic annotation. Source: Ensembl

axoneme

Inferred from direct assay Ref.9. Source: UniProtKB

cell body

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle

Inferred from electronic annotation. Source: UniProtKB-KW

lysosome

Inferred from direct assay PubMed 11146101. Source: MGI

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Inferred from direct assay Ref.1. Source: MGI

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.7. Source: MGI

smooth endoplasmic reticulum

Inferred from direct assay PubMed 11146101. Source: MGI

   Molecular_functionmicrotubule binding

Inferred from direct assay Ref.1. Source: MGI

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 116116Gamma-aminobutyric acid receptor-associated protein
PRO_0000212364
Propeptide1171Removed in mature form
PRO_0000423066

Regions

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

Sites

Site116 – 1172Cleavage; by ATG4B

Amino acid modifications

Lipidation1161Phosphatidylethanolamine amidated glycine Probable

Experimental info

Sequence conflict121E → D in BAB22426. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9DCD6 [UniParc].

Last modified March 1, 2004. Version 2.
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]"Binding of the GABA(A) receptor-associated protein (GABARAP) to microtubules and microfilaments suggests involvement of the cytoskeleton in GABARAPGABA(A) receptor interaction."
Wang H., Olsen R.W.
J. Neurochem. 75:644-655(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH BETA-TUBULIN.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Kidney.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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].
Tissue: Liver and Mammary tumor.
[5]"Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs."
Tanida I., Tanida-Miyake E., Nishitani T., Komatsu M., Yamazaki H., Ueno T., Kominami E.
Biochem. Biophys. Res. Commun. 292:256-262(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG7.
[6]"A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L."
Hemelaar J., Lelyveld V.S., Kessler B.M., Ploegh H.L.
J. Biol. Chem. 278:51841-51850(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY ATG4B, SUBCELLULAR LOCATION.
[7]"The gamma-aminobutyric acid type A receptor (GABAAR)-associated protein GABARAP interacts with gephyrin but is not involved in receptor anchoring at the synapse."
Kneussel M., Haverkamp S., Fuhrmann J.C., Wang H., Waessle H., Olsen R.W., Betz H.
Proc. Natl. Acad. Sci. U.S.A. 97:8594-8599(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GPHN.
[8]"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.
[9]"Functional interaction between autophagy and ciliogenesis."
Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I., Codogno P., Satir B.H., Satir P., Cuervo A.M.
Nature 502:194-200(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF161587 mRNA. Translation: AAD47642.1.
AK002879 mRNA. Translation: BAB22426.1.
AK011731 mRNA. Translation: BAB27806.1.
AL596185 Genomic DNA. Translation: CAI35162.1.
BC002126 mRNA. Translation: AAH02126.1.
BC024621 mRNA. Translation: AAH24621.1.
BC030350 mRNA. Translation: AAH30350.1.
CCDSCCDS24928.1.
RefSeqNP_062723.1. NM_019749.4.
UniGeneMm.272460.

3D structure databases

ProteinModelPortalQ9DCD6.
SMRQ9DCD6. Positions 1-116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208012. 2 interactions.
STRING10090.ENSMUSP00000018711.

PTM databases

PhosphoSiteQ9DCD6.

Proteomic databases

MaxQBQ9DCD6.
PaxDbQ9DCD6.
PRIDEQ9DCD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018711; ENSMUSP00000018711; ENSMUSG00000018567.
GeneID56486.
KEGGmmu:56486.
UCSCuc007jtg.2. mouse.

Organism-specific databases

CTD11337.
MGIMGI:1861742. Gabarap.

Phylogenomic databases

eggNOGNOG263746.
GeneTreeENSGT00390000012937.
HOGENOMHOG000232034.
HOVERGENHBG051706.
InParanoidB1AR49.
KOK08341.
OMATTMGQLY.
OrthoDBEOG70KGRK.
PhylomeDBQ9DCD6.
TreeFamTF314556.

Gene expression databases

BgeeQ9DCD6.
GenevestigatorQ9DCD6.

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. mouse.
NextBio312758.
PROQ9DCD6.
SOURCESearch...

Entry information

Entry nameGBRAP_MOUSE
AccessionPrimary (citable) accession number: Q9DCD6
Secondary accession number(s): B1AR49, Q9QUI7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: July 9, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot