APBA1_HUMAN
ID APBA1_HUMAN Reviewed; 837 AA.
AC Q02410; O14914; O60570; Q5VYR8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Amyloid-beta A4 precursor protein-binding family A member 1;
DE AltName: Full=Adapter protein X11alpha;
DE AltName: Full=Neuron-specific X11 protein;
DE AltName: Full=Neuronal Munc18-1-interacting protein 1;
DE Short=Mint-1;
GN Name=APBA1; Synonyms=MINT1, X11;
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-837 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=7678331; DOI=10.1073/pnas.90.1.109;
RA Duclos F., Koenig M., Boschert U., Sirugo G., Hen R., Mandel J.-L.;
RT "Gene in the region of the Friedreich ataxia locus encodes a putative
RT transmembrane protein expressed in the nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:109-113(1993).
RN [5]
RP MUTAGENESIS OF PHE-608.
RX PubMed=8887653; DOI=10.1128/mcb.16.11.6229;
RA Borg J.-P., Ooi J., Levy E., Margolis B.;
RT "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct
RT sites on the YENPTY motif of amyloid precursor protein.";
RL Mol. Cell. Biol. 16:6229-6241(1996).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FSBP.
RX PubMed=20531236; DOI=10.1097/wnr.0b013e32833bfca0;
RA Lau K.F., Perkinton M.S., Rodriguez L., McLoughlin D.M., Miller C.C.;
RT "An X11alpha/FSBP complex represses transcription of the GSK3beta gene
RT promoter.";
RL NeuroReport 21:761-766(2010).
RN [8]
RP ALTERNATIVE SPLICING (ISOFORM 2), INTERACTION WITH APP; RAB6A AND RAB6B,
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=23737971; DOI=10.1371/journal.pone.0064149;
RA Thyrock A., Ossendorf E., Stehling M., Kail M., Kurtz T., Pohlentz G.,
RA Waschbusch D., Eggert S., Formstecher E., Muthing J., Dreisewerd K.,
RA Kins S., Goud B., Barnekow A.;
RT "A new Mint1 isoform, but not the conventional Mint1, interacts with the
RT small GTPase Rab6.";
RL PLoS ONE 8:E64149-E64149(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-263; THR-305 AND
RP THR-370, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 452-617.
RX PubMed=9321393; DOI=10.1093/emboj/16.20.6141;
RA Zhang Z., Lee C.-H., Mandiyan V., Borg J.-P., Margolis B., Schlessinger J.,
RA Kuriyan J.;
RT "Sequence-specific recognition of the internalization motif of the
RT Alzheimer's amyloid precursor protein by the X11 PTB domain.";
RL EMBO J. 16:6141-6150(1997).
RN [11]
RP STRUCTURE BY NMR OF 656-740.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first PDZ domain of amyloid beta A4 precursor
RT protein-binding family A, member 1.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Putative function in synaptic vesicle exocytosis by binding
CC to Munc18-1, 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. Component of the LIN-10-
CC LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to
CC transport vesicles containing N-methyl-D-aspartate (NMDA) receptor
CC subunit NR2B along microtubules (By similarity).
CC {ECO:0000250|UniProtKB:B2RUJ5}.
CC -!- SUBUNIT: Part of a multimeric complex containing Munc18-1 and syntaxin-
CC 1. Also part of the brain-specific heterotrimeric complex LIN-10/X11-
CC alpha, LIN-2/CASK, and LIN7. Component of the brain-specific
CC heterotrimeric complex (LIN-10-LIN-2-LIN-7 complex) composed of at
CC least APBA1, CASK, and LIN7, which associates with the motor protein
CC KIF17 to transport vesicles along microtubules (By similarity). Within
CC the complex, interacts (via PDZ domain) with the motor protein KIF17;
CC the interaction is direct and is required for association of KIF17 with
CC the cargo that is to be transported (By similarity). Both isoform 1 and
CC isoform 2 bind to the cytoplasmic domain of amyloid protein (APP).
CC Interacts (via PDZ 1 and 2 domains) with FSPB. Isoform 2, but not
CC isoform 1, interacts (via its truncated PID domain) with active, GTP-
CC bound RAB6A and RAB6B. {ECO:0000250|UniProtKB:B2RUJ5,
CC ECO:0000269|PubMed:20531236, ECO:0000269|PubMed:23737971}.
CC -!- INTERACTION:
CC Q02410; P05067: APP; NbExp=4; IntAct=EBI-368690, EBI-77613;
CC Q02410; P49768: PSEN1; NbExp=4; IntAct=EBI-368690, EBI-297277;
CC Q02410-2; P20340-1: RAB6A; NbExp=4; IntAct=EBI-9247455, EBI-8851226;
CC Q02410-2; Q9NRW1: RAB6B; NbExp=4; IntAct=EBI-9247455, EBI-1760079;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20531236}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:20531236}. Nucleus
CC {ECO:0000269|PubMed:20531236}. Note=Only about 5% of the protein is
CC located in the nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus
CC {ECO:0000269|PubMed:23737971}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02410-1; Sequence=Displayed;
CC Name=2; Synonyms=Mint1_826;
CC IsoId=Q02410-2; Sequence=VSP_053518;
CC -!- TISSUE SPECIFICITY: Brain and spinal cord. Isoform 2 is expressed in
CC testis and brain, but not detected in lung, liver or spleen.
CC {ECO:0000269|PubMed:23737971}.
CC -!- DOMAIN: Composed of an N-terminal domain that binds Munc18-1 and LIN-
CC 2/CASK, a middle phosphotyrosine-binding domain (PID/PTB) that mediates
CC binding with the cytoplasmic domain of the amyloid-beta precursor
CC protein, and two C-terminal PDZ domains thought to attach proteins to
CC the plasma membrane.
CC -!- DOMAIN: The autoinhibitory helix linker occludes the APP binding site.
CC {ECO:0000250}.
CC -!- DOMAIN: The PID domain, truncated by 11 amino acids, as observed in
CC isoform 2, but not full-length, mediates the interaction with RAB6A and
CC RAB6B. {ECO:0000269|PubMed:23737971}.
CC -!- MISCELLANEOUS: [Isoform 2]: This isoform interacts with RAB6 GTPases.
CC {ECO:0000305}.
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DR EMBL; AF029106; AAC05304.1; -; mRNA.
DR EMBL; AF047347; AAC39766.1; -; mRNA.
DR EMBL; AL353693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L04953; AAA61307.1; -; mRNA.
DR CCDS; CCDS6630.1; -. [Q02410-1]
DR PIR; A47176; A47176.
DR RefSeq; NP_001154.2; NM_001163.3. [Q02410-1]
DR RefSeq; XP_005252025.1; XM_005251968.3. [Q02410-2]
DR RefSeq; XP_011516919.1; XM_011518617.2. [Q02410-1]
DR RefSeq; XP_016870159.1; XM_017014670.1. [Q02410-1]
DR PDB; 1AQC; X-ray; 2.30 A; A/B=453-623.
DR PDB; 1U37; NMR; -; A=655-741.
DR PDB; 1U38; NMR; -; A=655-741.
DR PDB; 1U39; NMR; -; A=743-822.
DR PDB; 1U3B; NMR; -; A=655-837.
DR PDB; 1X11; X-ray; 2.50 A; A/B=453-623.
DR PDB; 1X45; NMR; -; A=656-740.
DR PDB; 1Y7N; NMR; -; A=745-823.
DR PDBsum; 1AQC; -.
DR PDBsum; 1U37; -.
DR PDBsum; 1U38; -.
DR PDBsum; 1U39; -.
DR PDBsum; 1U3B; -.
DR PDBsum; 1X11; -.
DR PDBsum; 1X45; -.
DR PDBsum; 1Y7N; -.
DR AlphaFoldDB; Q02410; -.
DR BMRB; Q02410; -.
DR SMR; Q02410; -.
DR BioGRID; 106817; 94.
DR CORUM; Q02410; -.
DR ELM; Q02410; -.
DR IntAct; Q02410; 14.
DR MINT; Q02410; -.
DR STRING; 9606.ENSP00000265381; -.
DR TCDB; 8.A.24.2.2; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family.
DR iPTMnet; Q02410; -.
DR PhosphoSitePlus; Q02410; -.
DR BioMuta; APBA1; -.
DR DMDM; 116241250; -.
DR jPOST; Q02410; -.
DR MassIVE; Q02410; -.
DR PaxDb; Q02410; -.
DR PeptideAtlas; Q02410; -.
DR PRIDE; Q02410; -.
DR ProteomicsDB; 58088; -. [Q02410-1]
DR Antibodypedia; 12360; 218 antibodies from 38 providers.
DR DNASU; 320; -.
DR Ensembl; ENST00000265381.7; ENSP00000265381.3; ENSG00000107282.8. [Q02410-1]
DR GeneID; 320; -.
DR KEGG; hsa:320; -.
DR MANE-Select; ENST00000265381.7; ENSP00000265381.3; NM_001163.4; NP_001154.2.
DR UCSC; uc004ahh.3; human. [Q02410-1]
DR CTD; 320; -.
DR DisGeNET; 320; -.
DR GeneCards; APBA1; -.
DR HGNC; HGNC:578; APBA1.
DR HPA; ENSG00000107282; Tissue enhanced (brain).
DR MIM; 602414; gene.
DR neXtProt; NX_Q02410; -.
DR OpenTargets; ENSG00000107282; -.
DR PharmGKB; PA24869; -.
DR VEuPathDB; HostDB:ENSG00000107282; -.
DR eggNOG; KOG3605; Eukaryota.
DR GeneTree; ENSGT00940000156820; -.
DR HOGENOM; CLU_013563_1_0_1; -.
DR InParanoid; Q02410; -.
DR OMA; DCEDQRP; -.
DR OrthoDB; 436779at2759; -.
DR PhylomeDB; Q02410; -.
DR TreeFam; TF315245; -.
DR PathwayCommons; Q02410; -.
DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR SignaLink; Q02410; -.
DR SIGNOR; Q02410; -.
DR BioGRID-ORCS; 320; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; APBA1; human.
DR EvolutionaryTrace; Q02410; -.
DR GeneWiki; APBA1; -.
DR GenomeRNAi; 320; -.
DR Pharos; Q02410; Tbio.
DR PRO; PR:Q02410; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q02410; protein.
DR Bgee; ENSG00000107282; Expressed in superior frontal gyrus and 101 other tissues.
DR ExpressionAtlas; Q02410; baseline and differential.
DR Genevisible; Q02410; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; TAS:ProtInc.
DR GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR GO; GO:0008088; P:axo-dendritic transport; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; IEA:Ensembl.
DR GO; GO:0014047; P:glutamate secretion; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
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:0065003; P:protein-containing complex assembly; TAS:ProtInc.
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 IDEAL; IID00561; -.
DR InterPro; IPR030530; Apba1.
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:SF14; PTHR12345:SF14; 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 3D-structure; Alternative splicing; Cytoplasm; Golgi apparatus; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..837
FT /note="Amyloid-beta A4 precursor protein-binding family A
FT member 1"
FT /id="PRO_0000064614"
FT DOMAIN 457..643
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 656..742
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 747..822
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..314
FT /note="Munc-18-1 binding"
FT REGION 238..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..436
FT /note="LIN-2/CASK binding"
FT REGION 626..641
FT /note="Autoinhibitory helix linker"
FT /evidence="ECO:0000250"
FT COMPBIAS 51..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUJ5"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUJ5"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUJ5"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUJ5"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35430"
FT MOD_RES 305
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUJ5"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUJ5"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUJ5"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUJ5"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUJ5"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35430"
FT VAR_SEQ 495..505
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053518"
FT VARIANT 184
FT /note="S -> A (in dbSNP:rs34788368)"
FT /id="VAR_050664"
FT MUTAGEN 608
FT /note="F->V: Diminishes interaction with APP."
FT /evidence="ECO:0000269|PubMed:8887653"
FT CONFLICT 164
FT /note="A -> V (in Ref. 4; AAA61307)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="D -> H (in Ref. 1; AAC05304)"
FT /evidence="ECO:0000305"
FT CONFLICT 427..429
FT /note="AST -> VPI (in Ref. 1; AAC05304 and 4; AAA61307)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="S -> L (in Ref. 1; AAC05304 and 4; AAA61307)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="M -> I (in Ref. 1; AAC05304 and 4; AAA61307)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="K -> E (in Ref. 1; AAC05304 and 4; AAA61307)"
FT /evidence="ECO:0000305"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:1AQC"
FT STRAND 459..472
FT /evidence="ECO:0007829|PDB:1AQC"
FT HELIX 479..498
FT /evidence="ECO:0007829|PDB:1AQC"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:1AQC"
FT STRAND 523..530
FT /evidence="ECO:0007829|PDB:1AQC"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:1AQC"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:1AQC"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:1AQC"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:1AQC"
FT STRAND 554..559
FT /evidence="ECO:0007829|PDB:1AQC"
FT STRAND 586..593
FT /evidence="ECO:0007829|PDB:1AQC"
FT HELIX 597..616
FT /evidence="ECO:0007829|PDB:1AQC"
FT STRAND 655..660
FT /evidence="ECO:0007829|PDB:1U37"
FT STRAND 669..672
FT /evidence="ECO:0007829|PDB:1U37"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:1U37"
FT STRAND 684..688
FT /evidence="ECO:0007829|PDB:1U37"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:1U3B"
FT HELIX 693..697
FT /evidence="ECO:0007829|PDB:1U37"
FT STRAND 705..709
FT /evidence="ECO:0007829|PDB:1U37"
FT HELIX 719..727
FT /evidence="ECO:0007829|PDB:1U37"
FT STRAND 730..740
FT /evidence="ECO:0007829|PDB:1U37"
FT STRAND 746..756
FT /evidence="ECO:0007829|PDB:1U39"
FT STRAND 760..764
FT /evidence="ECO:0007829|PDB:1U39"
FT STRAND 767..771
FT /evidence="ECO:0007829|PDB:1U39"
FT HELIX 777..780
FT /evidence="ECO:0007829|PDB:1U39"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:1U39"
FT HELIX 796..798
FT /evidence="ECO:0007829|PDB:1U39"
FT HELIX 801..809
FT /evidence="ECO:0007829|PDB:1U39"
FT STRAND 813..821
FT /evidence="ECO:0007829|PDB:1U39"
SQ SEQUENCE 837 AA; 92865 MW; 29C3620BBC89534B CRC64;
MNHLEGSAEV EVTDEAAGGE VNESVEADLE HPEVEEEQQQ PPQQQHYVGR HQRGRALEDL
RAQLGQEEEE RGECLARSAS TESGFHNHTD TAEGDVIAAA RDGYDAERAQ DPEDESAYAV
QYRPEAEEYT EQAEAEHAEA THRRALPNHL HFHSLEHEEA MNAAYSGYVY THRLFHRGED
EPYSEPYADY GGLQEHVYEE IGDAPELDAR DGLRLYEQER DEAAAYRQEA LGARLHHYDE
RSDGESDSPE KEAEFAPYPR MDSYEQEEDI DQIVAEVKQS MSSQSLDKAA EDMPEAEQDL
ERPPTPAGGR PDSPGLQAPA GQQRAVGPAG GGEAGQRYSK EKRDAISLAI KDIKEAIEEV
KTRTIRSPYT PDEPKEPIWV MRQDISPTRD CDDQRPMDGD SPSPGSSSPL GAESSSTSLH
PSDPVEASTN KESRKSLASF PTYVEVPGPC DPEDLIDGII FAANYLGSTQ LLSDKTPSKN
VRMMQAQEAV SRIKMAQKLA KSRKKAPEGE SQPMTEVDLF ISTQRIKVLN ADTQETMMDH
PLRTISYIAD IGNIVVLMAR RRMPRSNSQE NVEASHPSQD GKRQYKMICH VFESEDAQLI
AQSIGQAFSV AYQEFLRANG INPEDLSQKE YSDLLNTQDM YNDDLIHFSK SENCKDVFIE
KQKGEILGVV IVESGWGSIL PTVIIANMMH GGPAEKSGKL NIGDQIMSIN GTSLVGLPLS
TCQSIIKGLK NQSRVKLNIV RCPPVTTVLI RRPDLRYQLG FSVQNGIICS LMRGGIAERG
GVRVGHRIIE INGQSVVATP HEKIVHILSN AVGEIHMKTM PAAMYRLLTA QEQPVYI
