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Q9BUH8

- BEGIN_HUMAN

UniProt

Q9BUH8 - BEGIN_HUMAN

Protein

Brain-enriched guanylate kinase-associated protein

Gene

BEGAIN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    May sustain the structure of the postsynaptic density (PSD).

    GO - Molecular functioni

    1. protein binding Source: IntAct

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Brain-enriched guanylate kinase-associated protein
    Gene namesi
    Name:BEGAIN
    Synonyms:KIAA1446
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:24163. BEGAIN.

    Subcellular locationi

    Cytoplasm By similarity. Membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. dendrite Source: Ensembl
    3. membrane Source: UniProtKB-SubCell
    4. neuronal cell body Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162377453.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 593593Brain-enriched guanylate kinase-associated proteinPRO_0000064904Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei137 – 1371PhosphotyrosineBy similarity
    Modified residuei246 – 2461Phosphoserine5 Publications
    Modified residuei465 – 4651Phosphoserine1 Publication
    Modified residuei500 – 5001Phosphoserine1 Publication
    Modified residuei502 – 5021Phosphoserine3 Publications
    Modified residuei563 – 5631Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BUH8.
    PaxDbiQ9BUH8.
    PRIDEiQ9BUH8.

    PTM databases

    PhosphoSiteiQ9BUH8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BUH8.
    BgeeiQ9BUH8.
    CleanExiHS_BEGAIN.
    GenevestigatoriQ9BUH8.

    Organism-specific databases

    HPAiHPA002899.

    Interactioni

    Subunit structurei

    Interacts with DLG4 and DLGAP1 and forms a ternary complex.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RBL1P287492EBI-742722,EBI-971402

    Protein-protein interaction databases

    BioGridi121647. 26 interactions.
    IntActiQ9BUH8. 24 interactions.
    MINTiMINT-1453141.
    STRINGi9606.ENSP00000347301.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BUH8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiNOG38797.
    HOGENOMiHOG000095194.
    HOVERGENiHBG050683.
    InParanoidiQ9BUH8.
    OMAiALSHEII.
    OrthoDBiEOG7JT6VT.
    PhylomeDBiQ9BUH8.
    TreeFamiTF331612.

    Sequencei

    Sequence statusi: Complete.

    Q9BUH8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKLSALQEQ KGELRKRLSY TTHKLEKLET EFDSTRHYLE IELRRAQEEL    50
    EKVTEKLRRI QSNYMALQRI NQELEDKLYR MGQHYEEEKR ALSHEIVALN 100
    SHLLEAKVTI DKLSEDNELY RKDCNLAAQL LQCSQTYGRV HKVSELPSDF 150
    QERVSLHMEK HGCSLPSPLC HPAYADSVPT CVIAKVLEKP DPASLSSRLS 200
    DASARDLAFC DGVEKPGPRP PYKGDIYCSD TALYCPEERR RDRRPSVDAP 250
    VTDVGFLRAQ NSTDSAAEEE EEAEAAAFPA GFQHEAFPSY AGSLPTSSSY 300
    SSFSATSEEK EHAQASTLTA SQQAIYLNSR DELFDRKPPA TTYEGSPRFA 350
    KATAAVAAPL EAEVAPGFGR TMSPYPAETF RFPASPGPQQ ALMPPNLWSL 400
    RAKPGTARLP GEDMRGQWRP LSVEDIGAYS YPVSAAGRAS PCSFSERYYG 450
    GAGGSPGKKA DGRASPLYAS YKADSFSEGD DLSQGHLAEP CFLRAGGDLS 500
    LSPGRSADPL PGYAPSEGGD GDRLGVQLCG TASSPEPEQG SRDSLEPSSM 550
    EASPEMHPAA RLSPQQAFPR TGGSGLSRKD SLTKAQLYGT LLN 593
    Length:593
    Mass (Da):64,803
    Last modified:June 1, 2001 - v1
    Checksum:iD4A25A463B8055F4
    GO

    Sequence cautioni

    The sequence BAA95970.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC002607 mRNA. Translation: AAH02607.1.
    AB040879 mRNA. Translation: BAA95970.1. Different initiation.
    AL390162 mRNA. Translation: CAB99094.1.
    CCDSiCCDS9962.1.
    PIRiT51877.
    RefSeqiNP_001153003.1. NM_001159531.1.
    NP_065887.1. NM_020836.3.
    XP_005267978.1. XM_005267921.1.
    UniGeneiHs.211751.

    Genome annotation databases

    EnsembliENST00000355173; ENSP00000347301; ENSG00000183092.
    ENST00000443071; ENSP00000411124; ENSG00000183092.
    GeneIDi57596.
    KEGGihsa:57596.
    UCSCiuc001yhp.3. human.

    Polymorphism databases

    DMDMi62511244.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC002607 mRNA. Translation: AAH02607.1 .
    AB040879 mRNA. Translation: BAA95970.1 . Different initiation.
    AL390162 mRNA. Translation: CAB99094.1 .
    CCDSi CCDS9962.1.
    PIRi T51877.
    RefSeqi NP_001153003.1. NM_001159531.1.
    NP_065887.1. NM_020836.3.
    XP_005267978.1. XM_005267921.1.
    UniGenei Hs.211751.

    3D structure databases

    ProteinModelPortali Q9BUH8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121647. 26 interactions.
    IntActi Q9BUH8. 24 interactions.
    MINTi MINT-1453141.
    STRINGi 9606.ENSP00000347301.

    PTM databases

    PhosphoSitei Q9BUH8.

    Polymorphism databases

    DMDMi 62511244.

    Proteomic databases

    MaxQBi Q9BUH8.
    PaxDbi Q9BUH8.
    PRIDEi Q9BUH8.

    Protocols and materials databases

    DNASUi 57596.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355173 ; ENSP00000347301 ; ENSG00000183092 .
    ENST00000443071 ; ENSP00000411124 ; ENSG00000183092 .
    GeneIDi 57596.
    KEGGi hsa:57596.
    UCSCi uc001yhp.3. human.

    Organism-specific databases

    CTDi 57596.
    GeneCardsi GC14M101003.
    HGNCi HGNC:24163. BEGAIN.
    HPAi HPA002899.
    neXtProti NX_Q9BUH8.
    PharmGKBi PA162377453.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG38797.
    HOGENOMi HOG000095194.
    HOVERGENi HBG050683.
    InParanoidi Q9BUH8.
    OMAi ALSHEII.
    OrthoDBi EOG7JT6VT.
    PhylomeDBi Q9BUH8.
    TreeFami TF331612.

    Miscellaneous databases

    GeneWikii BEGAIN.
    GenomeRNAii 57596.
    NextBioi 64202.
    PROi Q9BUH8.

    Gene expression databases

    ArrayExpressi Q9BUH8.
    Bgeei Q9BUH8.
    CleanExi HS_BEGAIN.
    Genevestigatori Q9BUH8.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "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: Brain.
    2. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-593.
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 549-593.
      Tissue: Amygdala.
    4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-465 AND SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-500; SER-502 AND SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiBEGIN_HUMAN
    AccessioniPrimary (citable) accession number: Q9BUH8
    Secondary accession number(s): Q9NPU3, Q9P282
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM

    External Data

    Dasty 3