P23819 (GRIA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate receptor 2
Short name=GluR-2

Alternative name(s):
AMPA-selective glutamate receptor 2
GluR-B
GluR-K2
Glutamate receptor ionotropic, AMPA 2
Short name=GluA2

Gene names

Name:	Gria2
Synonyms:	Glur2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	883 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate By similarity.
Subunit structure	Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and CSPG4. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 and leads to AMPAR complex disassembly. Interacts with GRIP2. Isoform 1, but not isoform 3, interacts with PICK1/PRKCABP. Interacts with GRIA1 and SYNDIG1. Interacts with LRFN1 By similarity. Found in a complex with GRIA1, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 By similarity. Ref.5 Ref.7 Ref.8 Ref.11 Ref.13 Ref.14
Subcellular location	Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression By similarity. Ref.10 Ref.11
Tissue specificity	Detected in brain cortex, hippocampus and cerebellum (at protein level). Detected in hippocampus. Ref.10 Ref.11
Developmental stage	Detected at low levels in newborns. Levels increase strongly and are highest in hippocampus from 7 day olds. Detected at low levels in hippocampus and olfactory bulb of 3 month olds (at protein level). Ref.10
Post-translational modification	Palmitoylated. Depalmitoylated upon glutamate stimulation. ZDHHC3/GODZ specifically palmitoylates Cys-610, which leads to Golgi retention and decreased cell surface expression. In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis. Ref.9 N-glycosylated. Ref.10
Miscellaneous	The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.
Sequence similarities	Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIA2 subfamily. [View classification]
RNA editing	Edited at position 607. Fully edited in the brain. Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent ions. Ref.4

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Endoplasmic reticulum Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing RNA editing
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	synaptic transmission Inferred from direct assay Ref.10. Source: MGI
Cellular_component	alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Inferred from direct assay PubMed 15883194PubMed 22632720. Source: MGI cell junction Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell neuron projection Inferred from direct assay PubMed 21558424. Source: BHF-UCL postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synaptic vesicle Inferred from direct assay PubMed 20418887. Source: MGI
Molecular_function	alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Inferred from sequence or structural similarity. Source: UniProtKB extracellular-glutamate-gated ion channel activity Inferred from direct assay Ref.10. Source: MGI kainate selective glutamate receptor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P23819-1)

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: P23819-2)

The sequence of this isoform differs from the canonical sequence as follows:
     761-761: S → T
     765-767: NAV → WVE
     768-883: Missing.

Isoform 3 (identifier: P23819-3)

The sequence of this isoform differs from the canonical sequence as follows:
     802-802: K → KTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGSK
     848-883: VAKNAQNINP...NVYGIESVKI → MTLSAATRNK...GMNVSVTDLS

Isoform 4 (identifier: P23819-4)

The sequence of this isoform differs from the canonical sequence as follows:
     802-802: K → KTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGSK

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 883	859	Glutamate receptor 2		PRO_0000011533
Regions
	Topological domain	25 – 543	519	Extracellular By similarity
	Transmembrane	544 – 564	21	Helical; By similarity
	Topological domain	565 – 591	27	Cytoplasmic By similarity
	Intramembrane	592 – 607	16	Helical; Pore-forming; By similarity
	Intramembrane	608 – 610	3	By similarity
	Topological domain	611 – 616	6	Cytoplasmic By similarity
	Transmembrane	617 – 637	21	Helical; By similarity
	Topological domain	638 – 812	175	Extracellular By similarity
	Transmembrane	813 – 833	21	Helical; By similarity
	Topological domain	834 – 883	50	Cytoplasmic By similarity
Sites
	Binding site	471	1	Glutamate By similarity
	Binding site	506	1	Glutamate By similarity
	Binding site	726	1	Glutamate By similarity
Amino acid modifications
	Modified residue	683	1	Phosphoserine; by PKC By similarity
	Modified residue	717	1	Phosphoserine; by PKG By similarity
	Modified residue	869	1	Phosphotyrosine Ref.12
	Modified residue	876	1	Phosphotyrosine Ref.11 Ref.12
	Modified residue	880	1	Phosphoserine Ref.6
	Lipidation	610	1	S-palmitoyl cysteine Ref.9
	Lipidation	836	1	S-palmitoyl cysteine Ref.9
	Glycosylation	256	1	N-linked (GlcNAc...) Potential
	Glycosylation	370	1	N-linked (GlcNAc...) Potential
	Glycosylation	406	1	N-linked (GlcNAc...) Potential
	Glycosylation	413	1	N-linked (GlcNAc...) Potential
	Disulfide bond	78 ↔ 330		By similarity
	Disulfide bond	739 ↔ 794		By similarity
Natural variations
	Alternative sequence	761	1	S → T in isoform 2.		VSP_000106
	Alternative sequence	765 – 767	3	NAV → WVE in isoform 2.		VSP_000107
	Alternative sequence	768 – 883	116	Missing in isoform 2.		VSP_000108
	Alternative sequence	802	1	K → KTPVNLAVLKLSEQGVLDKL KNKWWYDKGECGAKDSGSK in isoform 3 and isoform 4.		VSP_000109
	Alternative sequence	848 – 883	36	VAKNA…ESVKI → MTLSAATRNKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3.		VSP_000110
	Natural variant	607	1	Q → R in RNA edited version.
Experimental info
	Mutagenesis	869	1	Y → F: No effect on tyrosine phosphorylation. Reduced tyrosine phosphorylation; when associated with F-873 and F-876. Ref.11
	Mutagenesis	873	1	Y → F: No effect on tyrosine phosphorylation. Reduced tyrosine phosphorylation; when associated with F-869 and F-876. Ref.11
	Mutagenesis	876	1	Y → F: Loss of tyrosine phosphorylation at the C-terminus. Reduced tyrosine phosphorylation; when associated with F-869 and F-873. Interferes with accumulation at synapses. Interferes with AMPA-mediated receptor internalization. Ref.11
	Sequence conflict	264	1	D → V in CAA40735. Ref.1
	Sequence conflict	270	1	V → A in CAA40735. Ref.1
	Sequence conflict	282	1	E → G in CAA40735. Ref.1
	Sequence conflict	374	1	N → H in BAB29316. Ref.3
	Sequence conflict	482	1	N → K in BAC31557. Ref.3
	Sequence conflict	552	1	F → L in BAB29316. Ref.3
	Sequence conflict	764	1	G → R in AAC37653. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 2, 2002. Version 3. Checksum: C44B317027C1CCC1	FASTA	883	98,662
	10 20 30 40 50 60 MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP 70 80 90 100 110 120 HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG 130 140 150 160 170 180 THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV 190 200 210 220 230 240 GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL 250 260 270 280 290 300 GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT 310 320 330 340 350 360 YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI 370 380 390 400 410 420 KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT 430 440 450 460 470 480 ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI 490 500 510 520 530 540 WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD 550 560 570 580 590 600 PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF 610 620 630 640 650 660 SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL 670 680 690 700 710 720 SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK 730 740 750 760 770 780 YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL 790 800 810 820 830 840 DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR 850 860 870 880 AEAKRMKVAK NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI
	Isoform 2 [UniParc]. Checksum: 822F17FD67E4820E	FASTA	767	86,181
	10 20 30 40 50 60 MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP 70 80 90 100 110 120 HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG 130 140 150 160 170 180 THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV 190 200 210 220 230 240 GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL 250 260 270 280 290 300 GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT 310 320 330 340 350 360 YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI 370 380 390 400 410 420 KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT 430 440 450 460 470 480 ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI 490 500 510 520 530 540 WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD 550 560 570 580 590 600 PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF 610 620 630 640 650 660 SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL 670 680 690 700 710 720 SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK 730 740 750 760 YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG TSLGWVE
	Isoform 3 [UniParc]. Checksum: 2600BEDAF2C0583D	FASTA	939	104,523
	10 20 30 40 50 60 MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP 70 80 90 100 110 120 HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG 130 140 150 160 170 180 THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV 190 200 210 220 230 240 GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL 250 260 270 280 290 300 GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT 310 320 330 340 350 360 YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI 370 380 390 400 410 420 KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT 430 440 450 460 470 480 ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI 490 500 510 520 530 540 WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD 550 560 570 580 590 600 PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF 610 620 630 640 650 660 SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL 670 680 690 700 710 720 SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK 730 740 750 760 770 780 YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL 790 800 810 820 830 840 DKLKNKWWYD KGECGSGGGD SKTPVNLAVL KLSEQGVLDK LKNKWWYDKG ECGAKDSGSK 850 860 870 880 890 900 EKTSALSLSN VAGVFYILVG GLGLAMLVAL IEFCYKSRAE AKRMKMTLSA ATRNKARLSI 910 920 930 TGSTGENGRV MTPEFPKAVH AVPYVSPGMG MNVSVTDLS
	Isoform 4 [UniParc]. Checksum: E38D8C26ED029219	FASTA	921	102,851
	10 20 30 40 50 60 MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP 70 80 90 100 110 120 HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG 130 140 150 160 170 180 THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV 190 200 210 220 230 240 GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL 250 260 270 280 290 300 GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT 310 320 330 340 350 360 YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI 370 380 390 400 410 420 KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT 430 440 450 460 470 480 ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI 490 500 510 520 530 540 WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD 550 560 570 580 590 600 PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF 610 620 630 640 650 660 SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL 670 680 690 700 710 720 SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK 730 740 750 760 770 780 YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL 790 800 810 820 830 840 DKLKNKWWYD KGECGSGGGD SKTPVNLAVL KLSEQGVLDK LKNKWWYDKG ECGAKDSGSK 850 860 870 880 890 900 EKTSALSLSN VAGVFYILVG GLGLAMLVAL IEFCYKSRAE AKRMKVAKNA QNINPSSSQN 910 920 SQNFATYKEG YNVYGIESVK I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional expression from cloned cDNAs of glutamate receptor species responsive to kainate and quisqualate." Sakimura K., Bujo H., Kushiya E., Araki K., Yamazaki M., Yamazaki M., Meguro H., Warashina A., Numa S., Mishina M. FEBS Lett. 272:73-80(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"The organization of the gene for the functionally dominant alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluR-B." Koehler M., Kornau H.-C., Seeburg P.H. J. Biol. Chem. 269:17367-17370(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3 AND 4). Strain: BALB/c. Tissue: Liver.
[3]	"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. , 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] (ISOFORM 2). Strain: C57BL/6J. Tissue: Brain, Cerebellum, Medulla oblongata and Retina.
[4]	"RNA editing in brain controls a determinant of ion flow in glutamate-gated channels." Sommer B., Koehler M., Sprengel R., Seeburg P.H. Cell 67:11-19(1991) [PubMed] [Europe PMC] [Abstract] Cited for: RNA EDITING OF POSITION 607.
[5]	"rDLG6: a novel homolog of Drosophila DLG expressed in rat brain." Inagaki H., Maeda S., Lin K.H., Shimizu N., Saito T. Biochem. Biophys. Res. Commun. 265:462-468(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MPP4.
[6]	"Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein." Matsuda S., Mikawa S., Hirai H. J. Neurochem. 73:1765-1768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-880.
[7]	"The protein kinase C alpha binding protein PICK1 interacts with short but not long form alternative splice variants of AMPA receptor subunits." Dev K.K., Nishimune A., Henley J.M., Nakanishi S. Neuropharmacology 38:635-644(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRKCABP (ISOFORM 1).
[8]	"The proteoglycan NG2 is complexed with alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors by the PDZ glutamate receptor interaction protein (GRIP) in glial progenitor cells. Implications for glial-neuronal signaling." Stegmueller J., Werner H., Nave K.-A., Trotter J. J. Biol. Chem. 278:3590-3598(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRIP1 AND CSPG4.
[9]	"Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites." Hayashi T., Rumbaugh G., Huganir R.L. Neuron 47:709-723(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-610 AND CYS-836.
[10]	"Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors." Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T., Koehr G., Malinow R., Seeburg P.H., Osten P. Neuron 40:1199-1212(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF ISOFORM 3, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[11]	"Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family tyrosine kinases." Hayashi T., Huganir R.L. J. Neurosci. 24:6152-6160(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-876, MUTAGENESIS OF TYR-869; TYR-873 AND TYR-876, SUBCELLULAR LOCATION, INTERACTION WITH GRIP1; GRIP2 AND PICK1, TISSUE SPECIFICITY.
[12]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-869 AND TYR-876, MASS SPECTROMETRY. Tissue: Brain.
[13]	"SynDIG1: an activity-regulated, AMPA- receptor-interacting transmembrane protein that regulates excitatory synapse development." Kalashnikova E., Lorca R.A., Kaur I., Barisone G.A., Li B., Ishimaru T., Trimmer J.S., Mohapatra D.P., Diaz E. Neuron 65:80-93(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRIA1 AND SYNDIG1.
[14]	"The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic plasticity and behavior." Zhang J., Wang Y., Chi Z., Keuss M.J., Pai Y.M., Kang H.C., Shin J.H., Bugayenko A., Wang H., Xiong Y., Pletnikov M.V., Mattson M.P., Dawson T.M., Dawson V.L. Cell 145:284-299(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATAD1 AND GRIP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57498 mRNA. Translation: CAA40735.1. L32204 , L32189, L32190, L32192, L32194, L32196, L32198, L32200, L32202, L32203, L32201, L32199, L32197, L32195, L32193, L32191 Genomic DNA. Translation: AAC37653.1. L32372 , L32189, L32190, L32191, L32192, L32193, L32194, L32195, L32196, L32197, L32198, L32199, L32200, L32201, L32202, L32203, L32204 Genomic DNA. Translation: AAC37654.1. AK014389 mRNA. Translation: BAB29316.1. AK043490 mRNA. Translation: BAC31557.1. AK044574 mRNA. Translation: BAC31986.1. AK046861 mRNA. Translation: BAC32899.1.
IPI	IPI00136967. IPI00466699. IPI00608015. IPI00845711.
PIR	I49695. I49696.
RefSeq	NP_001034284.1. NM_001039195.1. NP_001077275.1. NM_001083806.1. NP_038568.2. NM_013540.2.
UniGene	Mm.220224.
3D structure databases
ProteinModelPortal	P23819.
SMR	P23819. Positions 25-838.
ModBase	Search...
Protein-protein interaction databases
IntAct	P23819. 22 interactions.
MINT	MINT-1776844.
STRING	10090.ENSMUSP00000103375.
PTM databases
PhosphoSite	P23819.
Proteomic databases
PaxDb	P23819.
PRIDE	P23819.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	14800.
KEGG	mmu:14800.
UCSC	uc008pof.1. mouse.
Organism-specific databases
CTD	2891.
MGI	MGI:95809. Gria2.
Phylogenomic databases
eggNOG	NOG316680.
HOGENOM	HOG000234372.
HOVERGEN	HBG051839.
KO	K05198.
OrthoDB	EOG4TB49K.
Gene expression databases
CleanEx	MM_GRIA2.
Genevestigator	P23819.
GermOnline	ENSMUSG00000033981. Mus musculus.
Family and domain databases
InterPro	IPR001828. ANF_lig-bd_rcpt. IPR019594. Glu_rcpt_Glu/Gly-bd. IPR001320. Iontro_glu_rcpt. IPR001508. NMDA_rcpt. [Graphical view]
Pfam	PF01094. ANF_receptor. 1 hit. PF00060. Lig_chan. 1 hit. PF10613. Lig_chan-Glu_bd. 1 hit. [Graphical view]
PRINTS	PR00177. NMDARECEPTOR.
SMART	SM00918. Lig_chan-Glu_bd. 1 hit. SM00079. PBPe. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P23819.
ChEMBL	CHEMBL3205.
NextBio	286957.
SOURCE	Search...

Entry information

Entry name

GRIA2_MOUSE

Accession

Primary (citable) accession number: P23819
Secondary accession number(s): Q61604 , Q61605, Q8BG69, Q8BXU3, Q9D6D3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	August 2, 2002
Last modified:	May 29, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program