BEGIN_HUMAN
ID BEGIN_HUMAN Reviewed; 593 AA.
AC Q9BUH8; Q9NPU3; Q9P282;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Brain-enriched guanylate kinase-associated protein;
GN Name=BEGAIN; Synonyms=KIAA1446;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-593.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 549-593.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-465 AND SER-502, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-500; SER-502 AND
RP SER-563, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-246; SER-346;
RP SER-373; SER-455; SER-465; SER-502; SER-506; SER-553 AND SER-563, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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:0000250}.
CC -!- INTERACTION:
CC Q9BUH8; P29972: AQP1; NbExp=3; IntAct=EBI-742722, EBI-745213;
CC Q9BUH8; Q8N5M1: ATPAF2; NbExp=5; IntAct=EBI-742722, EBI-1166928;
CC Q9BUH8; P18075: BMP7; NbExp=3; IntAct=EBI-742722, EBI-1035195;
CC Q9BUH8; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-742722, EBI-396137;
CC Q9BUH8; P26196: DDX6; NbExp=3; IntAct=EBI-742722, EBI-351257;
CC Q9BUH8; O60941-5: DTNB; NbExp=3; IntAct=EBI-742722, EBI-11984733;
CC Q9BUH8; Q9H0I2: ENKD1; NbExp=4; IntAct=EBI-742722, EBI-744099;
CC Q9BUH8; Q3B820: FAM161A; NbExp=3; IntAct=EBI-742722, EBI-719941;
CC Q9BUH8; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-742722, EBI-6658203;
CC Q9BUH8; P55040: GEM; NbExp=5; IntAct=EBI-742722, EBI-744104;
CC Q9BUH8; Q96IK5: GMCL1; NbExp=5; IntAct=EBI-742722, EBI-2548508;
CC Q9BUH8; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-742722, EBI-11978177;
CC Q9BUH8; P56524-2: HDAC4; NbExp=3; IntAct=EBI-742722, EBI-11953488;
CC Q9BUH8; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-742722, EBI-14069005;
CC Q9BUH8; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-742722, EBI-726510;
CC Q9BUH8; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-742722, EBI-10268010;
CC Q9BUH8; Q96CV9: OPTN; NbExp=3; IntAct=EBI-742722, EBI-748974;
CC Q9BUH8; Q99633: PRPF18; NbExp=3; IntAct=EBI-742722, EBI-2798416;
CC Q9BUH8; P0CG20: PRR35; NbExp=3; IntAct=EBI-742722, EBI-11986293;
CC Q9BUH8; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-742722, EBI-3437896;
CC Q9BUH8; P28749: RBL1; NbExp=2; IntAct=EBI-742722, EBI-971402;
CC Q9BUH8; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-742722, EBI-3957636;
CC Q9BUH8; Q9BT92: TCHP; NbExp=3; IntAct=EBI-742722, EBI-740781;
CC Q9BUH8; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-742722, EBI-3650647;
CC Q9BUH8; Q9P2F9: ZNF319; NbExp=5; IntAct=EBI-742722, EBI-11993110;
CC Q9BUH8; Q8TAU3: ZNF417; NbExp=6; IntAct=EBI-742722, EBI-740727;
CC Q9BUH8; Q7Z3I7: ZNF572; NbExp=5; IntAct=EBI-742722, EBI-10172590;
CC Q9BUH8; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-742722, EBI-6427977;
CC Q9BUH8; Q5T619: ZNF648; NbExp=5; IntAct=EBI-742722, EBI-11985915;
CC Q9BUH8; Q6NX45: ZNF774; NbExp=6; IntAct=EBI-742722, EBI-10251462;
CC Q9BUH8; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-742722, EBI-5667516;
CC Q9BUH8; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-742722, EBI-11962574;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95970.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC002607; AAH02607.1; -; mRNA.
DR EMBL; AB040879; BAA95970.1; ALT_INIT; mRNA.
DR EMBL; AL390162; CAB99094.1; -; mRNA.
DR CCDS; CCDS9962.1; -.
DR PIR; T51877; T51877.
DR RefSeq; NP_001153003.1; NM_001159531.1.
DR RefSeq; NP_065887.1; NM_020836.3.
DR RefSeq; XP_005267978.1; XM_005267921.3.
DR RefSeq; XP_016877010.1; XM_017021521.1.
DR AlphaFoldDB; Q9BUH8; -.
DR SMR; Q9BUH8; -.
DR BioGRID; 121647; 63.
DR IntAct; Q9BUH8; 62.
DR MINT; Q9BUH8; -.
DR STRING; 9606.ENSP00000411124; -.
DR iPTMnet; Q9BUH8; -.
DR PhosphoSitePlus; Q9BUH8; -.
DR BioMuta; BEGAIN; -.
DR DMDM; 62511244; -.
DR jPOST; Q9BUH8; -.
DR MassIVE; Q9BUH8; -.
DR MaxQB; Q9BUH8; -.
DR PaxDb; Q9BUH8; -.
DR PeptideAtlas; Q9BUH8; -.
DR PRIDE; Q9BUH8; -.
DR ProteomicsDB; 79087; -.
DR Antibodypedia; 146; 171 antibodies from 27 providers.
DR DNASU; 57596; -.
DR Ensembl; ENST00000355173.7; ENSP00000347301.2; ENSG00000183092.18.
DR Ensembl; ENST00000553553.6; ENSP00000451397.2; ENSG00000183092.18.
DR Ensembl; ENST00000556188.6; ENSP00000452157.2; ENSG00000183092.18.
DR Ensembl; ENST00000557378.6; ENSP00000450722.2; ENSG00000183092.18.
DR GeneID; 57596; -.
DR KEGG; hsa:57596; -.
DR UCSC; uc001yhq.4; human.
DR CTD; 57596; -.
DR DisGeNET; 57596; -.
DR GeneCards; BEGAIN; -.
DR HGNC; HGNC:24163; BEGAIN.
DR HPA; ENSG00000183092; Tissue enhanced (brain, pancreas, pituitary gland).
DR MIM; 618597; gene.
DR neXtProt; NX_Q9BUH8; -.
DR OpenTargets; ENSG00000183092; -.
DR PharmGKB; PA162377453; -.
DR VEuPathDB; HostDB:ENSG00000183092; -.
DR eggNOG; ENOG502QUGW; Eukaryota.
DR GeneTree; ENSGT00940000161760; -.
DR HOGENOM; CLU_020017_1_1_1; -.
DR InParanoid; Q9BUH8; -.
DR PhylomeDB; Q9BUH8; -.
DR TreeFam; TF331612; -.
DR PathwayCommons; Q9BUH8; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q9BUH8; -.
DR BioGRID-ORCS; 57596; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; BEGAIN; human.
DR GeneWiki; BEGAIN; -.
DR GenomeRNAi; 57596; -.
DR Pharos; Q9BUH8; Tbio.
DR PRO; PR:Q9BUH8; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9BUH8; protein.
DR Bgee; ENSG00000183092; Expressed in right hemisphere of cerebellum and 110 other tissues.
DR ExpressionAtlas; Q9BUH8; baseline and differential.
DR Genevisible; Q9BUH8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IBA:GO_Central.
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 Acetylation; Cytoplasm; Membrane; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..593
FT /note="Brain-enriched guanylate kinase-associated protein"
FT /id="PRO_0000064904"
FT REGION 499..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 137
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF6"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF6"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF6"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 381
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF6"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF6"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF6"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
SQ SEQUENCE 593 AA; 64803 MW; D4A25A463B8055F4 CRC64;
MEKLSALQEQ KGELRKRLSY TTHKLEKLET EFDSTRHYLE IELRRAQEEL EKVTEKLRRI
QSNYMALQRI NQELEDKLYR MGQHYEEEKR ALSHEIVALN SHLLEAKVTI DKLSEDNELY
RKDCNLAAQL LQCSQTYGRV HKVSELPSDF QERVSLHMEK HGCSLPSPLC HPAYADSVPT
CVIAKVLEKP DPASLSSRLS DASARDLAFC DGVEKPGPRP PYKGDIYCSD TALYCPEERR
RDRRPSVDAP VTDVGFLRAQ NSTDSAAEEE EEAEAAAFPA GFQHEAFPSY AGSLPTSSSY
SSFSATSEEK EHAQASTLTA SQQAIYLNSR DELFDRKPPA TTYEGSPRFA KATAAVAAPL
EAEVAPGFGR TMSPYPAETF RFPASPGPQQ ALMPPNLWSL RAKPGTARLP GEDMRGQWRP
LSVEDIGAYS YPVSAAGRAS PCSFSERYYG GAGGSPGKKA DGRASPLYAS YKADSFSEGD
DLSQGHLAEP CFLRAGGDLS LSPGRSADPL PGYAPSEGGD GDRLGVQLCG TASSPEPEQG
SRDSLEPSSM EASPEMHPAA RLSPQQAFPR TGGSGLSRKD SLTKAQLYGT LLN
