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Reviewed, UniProtKB/Swiss-Prot Q99767 (APBA2_HUMAN)

Last modified July 22, 2008. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Amyloid beta A4 precursor protein-binding family A member 2
Alternative name(s):
    Neuron-specific X11L protein
    Neuronal Munc18-1-interacting protein 2
      Short name=Mint-2
    Adapter protein X11beta
Gene names
Name: APBA2
Synonyms: MINT2, X11L
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length749 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP.

Subunit structure

Part of a multimeric complex containing STXBP1 and syntaxin-1. Binds to the cytoplasmic domain of amyloid protein beta, and to the nuclear factor NF-kappa-B/p65 via its PDZ domain. Interacts with the amino-terminal domain of APBA2BP.

Tissue specificity

Brain.

Domain

Composed of an N-terminal domain that binds STXBP1, a middle phosphotyrosine-binding domain (PID/PTB) that mediates binding with the cytoplasmic domain of the beta-amyloid precursor protein, and two C-terminal PDZ domains thought to attach proteins to the plasma membrane.

Sequence similarities

Contains 2 PDZ (DHR) domains.

Contains 1 PID domain.

Ontologies

Keywords

   Biological processProtein transport
Transport
   DomainRepeat
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processnervous system development Ref.2

Traceable author statement. Source: ProtInc

   Molecular functionprotein binding Ref.2 Ref.5

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 749749Amyloid beta A4 precursor protein-binding family A member 2

Regions

Domain368 – 555188PID
Domain568 – 65487PDZ 1
Domain659 – 73476PDZ 2
Region185 – 27086STXBP1-binding
Compositional bias92 – 954Poly-Glu

Amino acid modifications

Modified residue2081Phosphoserine By similarity

Experimental info

Sequence conflict1351Q → H in BAA34734. Ref.2
Sequence conflict1631G → R in AAC39767. Ref.1
Sequence conflict170 – 21445DEPSV…YRLRR → MSPPSLRPMTRKKMVTMCQQ RGLPGLLPRGGQREHRRLPL PPEA in AAC39767. Ref.1
Sequence conflict3441E → K in BAA34734. Ref.2
Sequence conflict3541F → L in BAA34734. Ref.2
Sequence conflict364 – 3652ED → KN in BAA34734. Ref.2
Sequence conflict6041G → C in AAC39767. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99767-1 [UniParc].

Last modified May 30, 2000. Version 3.
Checksum: C15AE9CFAEF51D85

FASTA74982,512
        10         20         30         40         50         60 
MAHRKLESVG SGMLDHRVRP GPVPHSQEPE SEDMELPLEG YVPEGLELAA LRPESPAPEE 

        70         80         90        100        110        120 
QECHNHSPDG DSSSDYVNNT SEEEDYDEGL PEEEEGITYY IRYCPEDDSY LEGMDCNGEE 

       130        140        150        160        170        180 
YLAHSAHPVD TDECQEAVEE WTDSAGPHPH GHEAEGSQDY PDGQLPIPED EPSVLEAHDQ 

       190        200        210        220        230        240 
EEDGHYCASK EGYQDYYPEE ANGNTGASPY RLRRGDGDLE DQEEDIDQIV AEIKMSLSMT 

       250        260        270        280        290        300 
SITSASEASP EHGPEPGPED SVEACPPIKA SCSPSRHEAR PKSLNLLPEA KHPGDPQRGF 

       310        320        330        340        350        360 
KPKTRTPEER LKWPHEQVCN GLEQPRKQQR SDLNGPVDNN NIPETKKVAS FPSFVAVPGP 

       370        380        390        400        410        420 
CEPEDLIDGI IFAANYLGST QLLSERNPSK NIRMMQAQEA VSRVKRMQKA AKIKKKANSE 

       430        440        450        460        470        480 
GDAQTLTEVD LFISTQRIKV LNADTQETMM DHALRTISYI ADIGNIVVLM ARRRMPRSAS 

       490        500        510        520        530        540 
QDCIETTPGA QEGKKQYKMI CHVFESEDAQ LIAQSIGQAF SVAYQEFLRA NGINPEDLSQ 

       550        560        570        580        590        600 
KEYSDIINTQ EMYNDDLIHF SNSENCKELQ LEKHKGEILG VVVVESGWGS ILPTVILANM 

       610        620        630        640        650        660 
MNGGPAARSG KLSIGDQIMS INGTSLVGLP LATCQGIIKG LKNQTQVKLN IVSCPPVTTV 

       670        680        690        700        710        720 
LIKRPDLKYQ LGFSVQNGII CSLMRGGIAE RGGVRVGHRI IEINGQSVVA TAHEKIVQAL 

       730        740 
SNSVGEIHMK TMPAAMFRLL TGQETPLYI 

« Hide

References

« Hide 'large scale' references
[1]"The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion."
Borg J.-P., Yang Y., De Taddeo-Borg M., Margolis B., Turner R.S.
J. Biol. Chem. 273:14761-14766(1998) [PubMed: 9614075] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein."
Tomita S., Ozaki T., Taru H., Oguchi S., Takeda S., Yagi Y., Sakiyama S., Kirino Y., Suzuki T.
J. Biol. Chem. 274:2243-2254(1999) [PubMed: 9890987] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Mints, Munc18-interacting proteins in synaptic vesicle exocytosis."
Okamoto M., Suedhof T.C.
J. Biol. Chem. 272:31459-31464(1997) [PubMed: 9395480] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 532-749.
Tissue: Brain.
[4]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed: 9110174] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 532-749.
Tissue: Brain.
[5]"Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein."
Lee D.-S., Tomita S., Kirino Y., Suzuki T.
J. Biol. Chem. 275:23134-23138(2000) [PubMed: 10833507] [Abstract]
Cited for: INTERACTION WITH APBA2BP.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF047348 mRNA. Translation: AAC39767.1.
AB014719 mRNA. Translation: BAA34734.1.
AF029108 mRNA. Translation: AAC05306.1.
U79255 mRNA. Translation: AAB50203.1.
RefSeqNP_005494.2.
UniGeneHs.618112

3D structure databases

HSSPHSSP built from PDB template 1AQC based on UniProtKB Q02410.
SMRQ99767. Positions 567-749.
ModBaseSearch...

PTM databases

PhosphoSiteQ99767.

Genome annotation databases

EnsemblENSG00000034053. Homo sapiens. [Contig view]
GeneID321.
KEGGhsa:321.

Organism-specific databases

H-InvDBHIX0021324.
HGNCHGNC:579. APBA2.
MIM602712. gene.
PharmGKBPA24870.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ99767.

Gene expression databases

ArrayExpressQ99767.
CleanExHS_APBA2.
GermOnlineENSG00000034053. Homo sapiens.

Family and domain databases

InterProIPR001478. PDZ.
IPR011993. PH_type.
IPR006020. PTB_PID.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
PfamPF00595. PDZ. 2 hits.
PF00640. PID. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 2 hits.
SM00462. PTB. 1 hit.
[Graphical view]
PROSITEPS50106. PDZ. 2 hits.
PS01179. PID. 1 hit.
[Graphical view]
ProDomQ99767.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubQ99767.
SOURCESearch...
ProtoNetSearch...

Entry information

Entry nameAPBA2_HUMAN
AccessionPrimary (citable) accession number: Q99767
Secondary accession number(s): O60571
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: July 22, 2008
This is version 67 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents