BEGIN_RAT
ID BEGIN_RAT Reviewed; 611 AA.
AC O88881; O88882;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Brain-enriched guanylate kinase-associated protein;
GN Name=Begain;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP INTERACTION WITH DLG4 AND DLGAP1.
RX PubMed=9756850; DOI=10.1074/jbc.273.41.26269;
RA Deguchi M., Hata Y., Takeuchi M., Ide N., Hirao K., Yao I., Irie M.,
RA Toyoda A., Takai Y.;
RT "BEGAIN (brain-enriched guanylate kinase-associated protein), a novel
RT neuronal PSD-95/SAP90-binding protein.";
RL J. Biol. Chem. 273:26269-26272(1998).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-474; SER-484;
RP SER-494 AND SER-496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May sustain the structure of the postsynaptic density (PSD).
CC -!- SUBUNIT: Interacts with DLG4 and DLGAP1 and forms a ternary complex.
CC {ECO:0000269|PubMed:9756850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=BEGAIN-2;
CC IsoId=O88881-1; Sequence=Displayed;
CC Name=2; Synonyms=BEGAIN-1;
CC IsoId=O88881-2; Sequence=VSP_012584;
CC -!- TISSUE SPECIFICITY: Brain-specific. Expressed in neurons and rather
CC enriched at synaptic junctions. {ECO:0000269|PubMed:9756850}.
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DR EMBL; AF064868; AAC63267.1; -; mRNA.
DR EMBL; AF064869; AAC63268.1; -; mRNA.
DR RefSeq; NP_001104585.1; NM_001111115.1. [O88881-2]
DR RefSeq; NP_077077.1; NM_024163.2. [O88881-1]
DR AlphaFoldDB; O88881; -.
DR SMR; O88881; -.
DR BioGRID; 249416; 1.
DR CORUM; O88881; -.
DR STRING; 10116.ENSRNOP00000049699; -.
DR iPTMnet; O88881; -.
DR PhosphoSitePlus; O88881; -.
DR PaxDb; O88881; -.
DR PRIDE; O88881; -.
DR Ensembl; ENSRNOT00000041903; ENSRNOP00000049699; ENSRNOG00000004650. [O88881-2]
DR Ensembl; ENSRNOT00000082216; ENSRNOP00000071412; ENSRNOG00000004650. [O88881-1]
DR GeneID; 79146; -.
DR KEGG; rno:79146; -.
DR UCSC; RGD:708347; rat. [O88881-1]
DR CTD; 57596; -.
DR RGD; 708347; Begain.
DR eggNOG; ENOG502QUGW; Eukaryota.
DR GeneTree; ENSGT00940000161760; -.
DR HOGENOM; CLU_020017_1_1_1; -.
DR InParanoid; O88881; -.
DR OrthoDB; 443898at2759; -.
DR PhylomeDB; O88881; -.
DR TreeFam; TF331612; -.
DR PRO; PR:O88881; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004650; Expressed in frontal cortex and 18 other tissues.
DR ExpressionAtlas; O88881; baseline and differential.
DR Genevisible; O88881; RN.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0098817; P:evoked excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; ISO:RGD.
DR InterPro; IPR033584; BEGAIN.
DR InterPro; IPR043441; Tjap1/BEGAIN.
DR PANTHER; PTHR28664; PTHR28664; 1.
DR PANTHER; PTHR28664:SF2; PTHR28664:SF2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Membrane; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..611
FT /note="Brain-enriched guanylate kinase-associated protein"
FT /id="PRO_0000064906"
FT REGION 520..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF6"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF6"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT MOD_RES 268
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF6"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT MOD_RES 399
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF6"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT VAR_SEQ 1..14
FT /note="MWTGGRRPGRLRRA -> MGSDQSSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9756850"
FT /id="VSP_012584"
SQ SEQUENCE 611 AA; 66993 MW; 1AA06C6389DDFFCF CRC64;
MWTGGRRPGR LRRAASAADM EKLSALQEQK GELRKRLSYT THKLEKLETE FDSTRHYLEI
ELRRAQEELD KVTEKLRRIQ SNYMALQRIN QELEDKLYRM GQHYEEEKRA MSHEIVALNS
HLLEAKVTID KLSEDNELYR KDCNLAAQLL QCSQTYGRVH KVSELPSDFQ QRVSLHMEKH
GCSLPSPLCH PSYADSVPTC VIAKVLEKPD PGSLSSRMSD ASARDLAYRD GVENPGPRPP
YKGDIYCSDT ALYCPDERDH DRRPSVDTPV TDVGFLRAQN STDSLAEEEE AEAAAFPEAY
RREAFQGYAA SLPTSSSYSS FSATSEEKEH AQASTLTASQ QAIYLNSREE LFSRKPPSAT
YGSSPRYAKA AATLGSPLEA QVAPGFARTV SPYPAEPYRY PASQQALMPP NLWSLRAKPS
GNRLAAREDI RGQWRPLSVE DVGAYSYQAG AAGRAASPCN FSERFYGGGG GGGSPGKNAE
GRASPLYASY KADSFSEGDD LSQGHLAEPC FLRAGGDLSL SPSRSADPLP GYATSDGDGD
RLGVQLCGPG SSPEPEHGSR DSLEPSSMEA SPEMHPPTRL SPQQAFPRTG GSGLSRKDSL
TKAQLYGTLL N
