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APBA2_HUMAN
ID   APBA2_HUMAN             Reviewed;         749 AA.
AC   Q99767; E9PGI4; O60571; Q5XKC0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   03-AUG-2022, entry version 185.
DE   RecName: Full=Amyloid-beta A4 precursor protein-binding family A member 2;
DE   AltName: Full=Adapter protein X11beta;
DE   AltName: Full=Neuron-specific X11L protein;
DE   AltName: Full=Neuronal Munc18-1-interacting protein 2;
DE            Short=Mint-2;
GN   Name=APBA2; Synonyms=MINT2, X11L;
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 [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9614075; DOI=10.1074/jbc.273.24.14761;
RA   Borg J.-P., Yang Y., De Taddeo-Borg M., Margolis B., Turner R.S.;
RT   "The X11alpha protein slows cellular amyloid precursor protein processing
RT   and reduces Abeta40 and Abeta42 secretion.";
RL   J. Biol. Chem. 273:14761-14766(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9890987; DOI=10.1074/jbc.274.4.2243;
RA   Tomita S., Ozaki T., Taru H., Oguchi S., Takeda S., Yagi Y., Sakiyama S.,
RA   Kirino Y., Suzuki T.;
RT   "Interaction of a neuron-specific protein containing PDZ domains with
RT   Alzheimer's amyloid precursor protein.";
RL   J. Biol. Chem. 274:2243-2254(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-311.
RC   TISSUE=Ovary;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 532-749 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9395480; DOI=10.1074/jbc.272.50.31459;
RA   Okamoto M., Suedhof T.C.;
RT   "Mints, Munc18-interacting proteins in synaptic vesicle exocytosis.";
RL   J. Biol. Chem. 272:31459-31464(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 532-749 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA   Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA   Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT   "Large-scale concatenation cDNA sequencing.";
RL   Genome Res. 7:353-358(1997).
RN   [7]
RP   INTERACTION WITH NECAB3.
RC   TISSUE=Brain;
RX   PubMed=10833507; DOI=10.1074/jbc.c000302200;
RA   Lee D.-S., Tomita S., Kirino Y., Suzuki T.;
RT   "Regulation of X11L-dependent amyloid precursor protein metabolism by XB51,
RT   a novel X11L-binding protein.";
RL   J. Biol. Chem. 275:23134-23138(2000).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-208, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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: Putative function in synaptic vesicle exocytosis by binding
CC       to STXBP1, an essential component of the synaptic vesicle exocytotic
CC       machinery. May modulate processing of the amyloid-beta precursor
CC       protein (APP) and hence formation of APP-beta.
CC   -!- SUBUNIT: Part of a multimeric complex containing STXBP1 and syntaxin-1.
CC       Binds to the cytoplasmic domain of amyloid-beta protein, and to the
CC       nuclear factor NF-kappa-B/p65 via its PDZ domain. Interacts with the N-
CC       terminal domain of NECAB3. {ECO:0000269|PubMed:10833507}.
CC   -!- INTERACTION:
CC       Q99767; Q99767: APBA2; NbExp=2; IntAct=EBI-81711, EBI-81711;
CC       Q99767; P05067: APP; NbExp=2; IntAct=EBI-81711, EBI-77613;
CC       Q99767; O94985: CLSTN1; NbExp=2; IntAct=EBI-81711, EBI-522075;
CC       Q99767-2; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-12218351, EBI-6447163;
CC       Q99767-2; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-12218351, EBI-14096082;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99767-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99767-2; Sequence=VSP_045692;
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- DOMAIN: Composed of an N-terminal domain that binds STXBP1, a middle
CC       phosphotyrosine-binding domain (PID/PTB) that mediates binding with the
CC       cytoplasmic domain of the amyloid-beta precursor protein, and two C-
CC       terminal PDZ domains thought to attach proteins to the plasma membrane.
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DR   EMBL; AF047348; AAC39767.1; -; mRNA.
DR   EMBL; AB014719; BAA34734.1; -; mRNA.
DR   EMBL; AC024474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC174469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC082986; AAH82986.1; -; mRNA.
DR   EMBL; AF029108; AAC05306.1; -; mRNA.
DR   EMBL; U79255; AAB50203.1; -; mRNA.
DR   CCDS; CCDS10022.1; -. [Q99767-1]
DR   CCDS; CCDS45197.1; -. [Q99767-2]
DR   RefSeq; NP_001123886.1; NM_001130414.1. [Q99767-2]
DR   RefSeq; NP_005494.2; NM_005503.3. [Q99767-1]
DR   RefSeq; XP_011519790.1; XM_011521488.2. [Q99767-1]
DR   RefSeq; XP_011519791.1; XM_011521489.2. [Q99767-1]
DR   RefSeq; XP_011519792.1; XM_011521490.2. [Q99767-1]
DR   RefSeq; XP_011519793.1; XM_011521491.1. [Q99767-1]
DR   RefSeq; XP_011519794.1; XM_011521492.2. [Q99767-1]
DR   RefSeq; XP_016877590.1; XM_017022101.1.
DR   RefSeq; XP_016877591.1; XM_017022102.1.
DR   RefSeq; XP_016877592.1; XM_017022103.1.
DR   RefSeq; XP_016877593.1; XM_017022104.1.
DR   RefSeq; XP_016877594.1; XM_017022105.1.
DR   RefSeq; XP_016877595.1; XM_017022106.1.
DR   RefSeq; XP_016877596.1; XM_017022107.1.
DR   RefSeq; XP_016877597.1; XM_017022108.1.
DR   RefSeq; XP_016877598.1; XM_017022109.1.
DR   RefSeq; XP_016877599.1; XM_017022110.1. [Q99767-1]
DR   RefSeq; XP_016877600.1; XM_017022111.1.
DR   RefSeq; XP_016877601.1; XM_017022112.1. [Q99767-1]
DR   RefSeq; XP_016877602.1; XM_017022113.1.
DR   RefSeq; XP_016877603.1; XM_017022114.1.
DR   RefSeq; XP_016877604.1; XM_017022115.1.
DR   RefSeq; XP_016877605.1; XM_017022116.1.
DR   RefSeq; XP_016877606.1; XM_017022117.1.
DR   AlphaFoldDB; Q99767; -.
DR   SMR; Q99767; -.
DR   BioGRID; 106818; 41.
DR   ELM; Q99767; -.
DR   IntAct; Q99767; 33.
DR   MINT; Q99767; -.
DR   STRING; 9606.ENSP00000453293; -.
DR   TCDB; 8.A.24.2.3; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family.
DR   iPTMnet; Q99767; -.
DR   PhosphoSitePlus; Q99767; -.
DR   BioMuta; APBA2; -.
DR   DMDM; 6226950; -.
DR   EPD; Q99767; -.
DR   jPOST; Q99767; -.
DR   MassIVE; Q99767; -.
DR   MaxQB; Q99767; -.
DR   PaxDb; Q99767; -.
DR   PeptideAtlas; Q99767; -.
DR   PRIDE; Q99767; -.
DR   ProteomicsDB; 20327; -.
DR   ProteomicsDB; 78469; -. [Q99767-1]
DR   Antibodypedia; 22443; 209 antibodies from 35 providers.
DR   DNASU; 321; -.
DR   Ensembl; ENST00000411764.5; ENSP00000409312.1; ENSG00000034053.15. [Q99767-2]
DR   Ensembl; ENST00000558259.5; ENSP00000454171.1; ENSG00000034053.15. [Q99767-1]
DR   Ensembl; ENST00000558330.5; ENSP00000452722.1; ENSG00000034053.15. [Q99767-2]
DR   Ensembl; ENST00000558402.5; ENSP00000453293.1; ENSG00000034053.15. [Q99767-1]
DR   Ensembl; ENST00000561069.5; ENSP00000453144.1; ENSG00000034053.15. [Q99767-1]
DR   Ensembl; ENST00000612449.2; ENSP00000483174.1; ENSG00000276495.4. [Q99767-2]
DR   Ensembl; ENST00000620457.4; ENSP00000480384.1; ENSG00000276495.4. [Q99767-1]
DR   Ensembl; ENST00000631894.1; ENSP00000488107.1; ENSG00000276495.4. [Q99767-1]
DR   Ensembl; ENST00000683413.1; ENSP00000507394.1; ENSG00000034053.15. [Q99767-1]
DR   GeneID; 321; -.
DR   KEGG; hsa:321; -.
DR   MANE-Select; ENST00000683413.1; ENSP00000507394.1; NM_001353788.2; NP_001340717.1.
DR   UCSC; uc001zck.4; human. [Q99767-1]
DR   CTD; 321; -.
DR   DisGeNET; 321; -.
DR   GeneCards; APBA2; -.
DR   HGNC; HGNC:579; APBA2.
DR   HPA; ENSG00000034053; Tissue enhanced (brain, lymphoid tissue).
DR   MIM; 602712; gene.
DR   neXtProt; NX_Q99767; -.
DR   OpenTargets; ENSG00000034053; -.
DR   PharmGKB; PA24870; -.
DR   VEuPathDB; HostDB:ENSG00000034053; -.
DR   eggNOG; KOG3605; Eukaryota.
DR   GeneTree; ENSGT00940000158943; -.
DR   HOGENOM; CLU_013563_3_0_1; -.
DR   InParanoid; Q99767; -.
DR   OMA; KPLPHSC; -.
DR   OrthoDB; 436779at2759; -.
DR   PhylomeDB; Q99767; -.
DR   TreeFam; TF315245; -.
DR   PathwayCommons; Q99767; -.
DR   Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR   SignaLink; Q99767; -.
DR   SIGNOR; Q99767; -.
DR   BioGRID-ORCS; 321; 12 hits in 1074 CRISPR screens.
DR   ChiTaRS; APBA2; human.
DR   GeneWiki; APBA2; -.
DR   GenomeRNAi; 321; -.
DR   Pharos; Q99767; Tbio.
DR   PRO; PR:Q99767; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q99767; protein.
DR   Bgee; ENSG00000034053; Expressed in superior frontal gyrus and 97 other tissues.
DR   ExpressionAtlas; Q99767; baseline and differential.
DR   Genevisible; Q99767; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR   GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR030529; Apba2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   PANTHER; PTHR12345:SF12; PTHR12345:SF12; 1.
DR   Pfam; PF00595; PDZ; 2.
DR   Pfam; PF00640; PID; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SMART; SM00462; PTB; 1.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   PROSITE; PS50106; PDZ; 2.
DR   PROSITE; PS01179; PID; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Protein transport;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN           1..749
FT                   /note="Amyloid-beta A4 precursor protein-binding family A
FT                   member 2"
FT                   /id="PRO_0000064616"
FT   DOMAIN          368..555
FT                   /note="PID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   DOMAIN          568..654
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          659..734
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..270
FT                   /note="STXBP1-binding"
FT   REGION          238..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..94
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         406..417
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045692"
FT   VARIANT         311
FT                   /note="L -> P (in dbSNP:rs8040932)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_050665"
FT   CONFLICT        135
FT                   /note="Q -> H (in Ref. 2; BAA34734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="G -> R (in Ref. 1; AAC39767)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170..214
FT                   /note="DEPSVLEAHDQEEDGHYCASKEGYQDYYPEEANGNTGASPYRLRR -> MSP
FT                   PSLRPMTRKKMVTMCQQRGLPGLLPRGGQREHRRLPLPPEA (in Ref. 1;
FT                   AAC39767)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344
FT                   /note="E -> K (in Ref. 2; BAA34734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354
FT                   /note="F -> L (in Ref. 2; BAA34734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        364..365
FT                   /note="ED -> KN (in Ref. 2; BAA34734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        604
FT                   /note="G -> C (in Ref. 1; AAC39767)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   749 AA;  82512 MW;  C15AE9CFAEF51D85 CRC64;
     MAHRKLESVG SGMLDHRVRP GPVPHSQEPE SEDMELPLEG YVPEGLELAA LRPESPAPEE
     QECHNHSPDG DSSSDYVNNT SEEEDYDEGL PEEEEGITYY IRYCPEDDSY LEGMDCNGEE
     YLAHSAHPVD TDECQEAVEE WTDSAGPHPH GHEAEGSQDY PDGQLPIPED EPSVLEAHDQ
     EEDGHYCASK EGYQDYYPEE ANGNTGASPY RLRRGDGDLE DQEEDIDQIV AEIKMSLSMT
     SITSASEASP EHGPEPGPED SVEACPPIKA SCSPSRHEAR PKSLNLLPEA KHPGDPQRGF
     KPKTRTPEER LKWPHEQVCN GLEQPRKQQR SDLNGPVDNN NIPETKKVAS FPSFVAVPGP
     CEPEDLIDGI IFAANYLGST QLLSERNPSK NIRMMQAQEA VSRVKRMQKA AKIKKKANSE
     GDAQTLTEVD LFISTQRIKV LNADTQETMM DHALRTISYI ADIGNIVVLM ARRRMPRSAS
     QDCIETTPGA QEGKKQYKMI CHVFESEDAQ LIAQSIGQAF SVAYQEFLRA NGINPEDLSQ
     KEYSDIINTQ EMYNDDLIHF SNSENCKELQ LEKHKGEILG VVVVESGWGS ILPTVILANM
     MNGGPAARSG KLSIGDQIMS INGTSLVGLP LATCQGIIKG LKNQTQVKLN IVSCPPVTTV
     LIKRPDLKYQ LGFSVQNGII CSLMRGGIAE RGGVRVGHRI IEINGQSVVA TAHEKIVQAL
     SNSVGEIHMK TMPAAMFRLL TGQETPLYI
 
 
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