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Q02410 (APBA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amyloid beta A4 precursor protein-binding family A member 1
Alternative name(s):
Adapter protein X11alpha
Neuron-specific X11 protein
Neuronal Munc18-1-interacting protein 1
Short name=Mint-1
Gene names
Name:APBA1
Synonyms:MINT1, X11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length837 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Putative function in synaptic vesicle exocytosis by binding to Munc18-1, 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 Munc18-1 and syntaxin-1. Also part of the brain-specific heterotrimeric complex LIN-10/X11-alpha, LIN-2/CASK, and LIN7. Both isoform 1 and isoform 2 bind to the cytoplasmic domain of amyloid protein (APP). Interacts (via PDZ 1 and 2 domains) with FSPB. Isoform 2, but not isoform 1, interacts (via its truncated PID domain) with active, GTP-bound RAB6A and RAB6B. Ref.7 Ref.8

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Nucleus. Note: Only about 5% of the protein is located in the nucleus. Ref.7 Ref.8

Isoform 2: Golgi apparatus Ref.7 Ref.8.

Tissue specificity

Brain and spinal cord. Isoform 2 is expressed in testis and brain, but not detected in lung, liver or spleen. Ref.8

Domain

Composed of an N-terminal domain that binds Munc18-1 and LIN-2/CASK, 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.

The autoinhibitory helix linker occludes the APP binding site By similarity.

The PID domain, truncated by 11 amino acids, as observed in isoform 2, but not full-length, mediates the interaction with RAB6A and RAB6B (Ref.8).

Sequence similarities

Contains 2 PDZ (DHR) domains.

Contains 1 PID domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Golgi apparatus
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon cargo transport

Traceable author statement PubMed 9822620. Source: ProtInc

cell adhesion

Traceable author statement PubMed 9753324. Source: ProtInc

gamma-aminobutyric acid secretion

Inferred from electronic annotation. Source: Ensembl

glutamate secretion

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

intracellular protein transport

Traceable author statement Ref.2. Source: ProtInc

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

nervous system development

Traceable author statement PubMed 9753324. Source: ProtInc

protein complex assembly

Traceable author statement Ref.2PubMed 9753324. Source: ProtInc

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Traceable author statement PubMed 9753324. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle

Traceable author statement PubMed 9753324. Source: ProtInc

   Molecular_functionbeta-amyloid binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-4,5-bisphosphate binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.8. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q02410-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q02410-2)

Also known as: Mint1_826;

The sequence of this isoform differs from the canonical sequence as follows:
     495-505: Missing.
Note: This isoform interacts with RAB6 GTPases.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 837837Amyloid beta A4 precursor protein-binding family A member 1
PRO_0000064614

Regions

Domain457 – 643187PID
Domain656 – 74287PDZ 1
Domain747 – 82276PDZ 2
Region226 – 31489Munc-18-1 binding
Region373 – 43664LIN-2/CASK binding
Region626 – 64116Autoinhibitory helix linker By similarity
Compositional bias67 – 704Poly-Glu
Compositional bias294 – 32835Pro-rich
Compositional bias368 – 45285Pro-rich

Amino acid modifications

Modified residue2631Phosphoserine Ref.6

Natural variations

Alternative sequence495 – 50511Missing in isoform 2.
VSP_053518
Natural variant1841S → A.
Corresponds to variant rs34788368 [ dbSNP | Ensembl ].
VAR_050664

Experimental info

Mutagenesis6081F → V: Diminishes interaction with APP. Ref.5
Sequence conflict1641A → V in AAA61307. Ref.4
Sequence conflict2081D → H in AAC05304. Ref.1
Sequence conflict427 – 4293AST → VPI in AAC05304. Ref.1
Sequence conflict427 – 4293AST → VPI in AAA61307. Ref.4
Sequence conflict5221S → L in AAC05304. Ref.1
Sequence conflict5221S → L in AAA61307. Ref.4
Sequence conflict5631M → I in AAC05304. Ref.1
Sequence conflict5631M → I in AAA61307. Ref.4
Sequence conflict7301K → E in AAC05304. Ref.1
Sequence conflict7301K → E in AAA61307. Ref.4

Secondary structure

....................................................... 837
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 29C3620BBC89534B

FASTA83792,865
        10         20         30         40         50         60 
MNHLEGSAEV EVTDEAAGGE VNESVEADLE HPEVEEEQQQ PPQQQHYVGR HQRGRALEDL 

        70         80         90        100        110        120 
RAQLGQEEEE RGECLARSAS TESGFHNHTD TAEGDVIAAA RDGYDAERAQ DPEDESAYAV 

       130        140        150        160        170        180 
QYRPEAEEYT EQAEAEHAEA THRRALPNHL HFHSLEHEEA MNAAYSGYVY THRLFHRGED 

       190        200        210        220        230        240 
EPYSEPYADY GGLQEHVYEE IGDAPELDAR DGLRLYEQER DEAAAYRQEA LGARLHHYDE 

       250        260        270        280        290        300 
RSDGESDSPE KEAEFAPYPR MDSYEQEEDI DQIVAEVKQS MSSQSLDKAA EDMPEAEQDL 

       310        320        330        340        350        360 
ERPPTPAGGR PDSPGLQAPA GQQRAVGPAG GGEAGQRYSK EKRDAISLAI KDIKEAIEEV 

       370        380        390        400        410        420 
KTRTIRSPYT PDEPKEPIWV MRQDISPTRD CDDQRPMDGD SPSPGSSSPL GAESSSTSLH 

       430        440        450        460        470        480 
PSDPVEASTN KESRKSLASF PTYVEVPGPC DPEDLIDGII FAANYLGSTQ LLSDKTPSKN 

       490        500        510        520        530        540 
VRMMQAQEAV SRIKMAQKLA KSRKKAPEGE SQPMTEVDLF ISTQRIKVLN ADTQETMMDH 

       550        560        570        580        590        600 
PLRTISYIAD IGNIVVLMAR RRMPRSNSQE NVEASHPSQD GKRQYKMICH VFESEDAQLI 

       610        620        630        640        650        660 
AQSIGQAFSV AYQEFLRANG INPEDLSQKE YSDLLNTQDM YNDDLIHFSK SENCKDVFIE 

       670        680        690        700        710        720 
KQKGEILGVV IVESGWGSIL PTVIIANMMH GGPAEKSGKL NIGDQIMSIN GTSLVGLPLS 

       730        740        750        760        770        780 
TCQSIIKGLK NQSRVKLNIV RCPPVTTVLI RRPDLRYQLG FSVQNGIICS LMRGGIAERG 

       790        800        810        820        830 
GVRVGHRIIE INGQSVVATP HEKIVHILSN AVGEIHMKTM PAAMYRLLTA QEQPVYI 

« Hide

Isoform 2 (Mint1_826) [UniParc].

Checksum: DD7B6C1C6D3D9FE7
Show »

FASTA82691,594

References

« Hide 'large scale' references
[1]"Mints, Munc18-interacting proteins in synaptic vesicle exocytosis."
Okamoto M., Suedhof T.C.
J. Biol. Chem. 272:31459-31464(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system."
Duclos F., Koenig M., Boschert U., Sirugo G., Hen R., Mandel J.-L.
Proc. Natl. Acad. Sci. U.S.A. 90:109-113(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 130-837 (ISOFORM 1).
Tissue: Fetal brain.
[5]"The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein."
Borg J.-P., Ooi J., Levy E., Margolis B.
Mol. Cell. Biol. 16:6229-6241(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PHE-608.
[6]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[7]"An X11alpha/FSBP complex represses transcription of the GSK3beta gene promoter."
Lau K.F., Perkinton M.S., Rodriguez L., McLoughlin D.M., Miller C.C.
NeuroReport 21:761-766(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FSBP.
[8]"A new Mint1 isoform, but not the conventional Mint1, interacts with the small GTPase Rab6."
Thyrock A., Ossendorf E., Stehling M., Kail M., Kurtz T., Pohlentz G., Waschbusch D., Eggert S., Formstecher E., Muthing J., Dreisewerd K., Kins S., Goud B., Barnekow A.
PLoS ONE 8:E64149-E64149(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2), INTERACTION WITH APP; RAB6A AND RAB6B, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
[9]"Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain."
Zhang Z., Lee C.-H., Mandiyan V., Borg J.-P., Margolis B., Schlessinger J., Kuriyan J.
EMBO J. 16:6141-6150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 452-617.
[10]"Solution structure of the first PDZ domain of amyloid beta A4 precursor protein-binding family A, member 1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 656-740.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF029106 mRNA. Translation: AAC05304.1.
AF047347 mRNA. Translation: AAC39766.1.
AL353693, AL355140 Genomic DNA. Translation: CAH74104.1.
AL355140, AL353693 Genomic DNA. Translation: CAI15443.1.
L04953 mRNA. Translation: AAA61307.1.
CCDSCCDS6630.1.
PIRA47176.
RefSeqNP_001154.2. NM_001163.3. [Q02410-1]
XP_005252024.1. XM_005251967.1. [Q02410-1]
XP_005252025.1. XM_005251968.1. [Q02410-2]
XP_006717156.1. XM_006717093.1. [Q02410-1]
UniGeneHs.171939.
Hs.592974.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQCX-ray2.30A/B453-623[»]
1U37NMR-A655-741[»]
1U38NMR-A655-741[»]
1U39NMR-A743-822[»]
1U3BNMR-A655-837[»]
1X11X-ray2.50A/B453-623[»]
1X45NMR-A656-740[»]
1Y7NNMR-A745-823[»]
ProteinModelPortalQ02410.
SMRQ02410. Positions 453-837.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106817. 12 interactions.
IntActQ02410. 11 interactions.
MINTMINT-153502.
STRING9606.ENSP00000265381.

Chemistry

ChEMBLCHEMBL2097170.

PTM databases

PhosphoSiteQ02410.

Polymorphism databases

DMDM116241250.

Proteomic databases

PaxDbQ02410.
PRIDEQ02410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265381; ENSP00000265381; ENSG00000107282. [Q02410-1]
GeneID320.
KEGGhsa:320.
UCSCuc004ahh.2. human. [Q02410-1]

Organism-specific databases

CTD320.
GeneCardsGC09M072042.
HGNCHGNC:578. APBA1.
HPACAB009338.
HPA019850.
MIM602414. gene.
neXtProtNX_Q02410.
PharmGKBPA24869.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283022.
HOGENOMHOG000033981.
HOVERGENHBG050523.
InParanoidQ02410.
KOK04531.
OMALQEHVYE.
OrthoDBEOG78PV8H.
PhylomeDBQ02410.
TreeFamTF315245.

Gene expression databases

BgeeQ02410.
CleanExHS_APBA1.
GenevestigatorQ02410.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
2.30.42.10. 2 hits.
InterProIPR001478. PDZ.
IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamPF00595. PDZ. 2 hits.
PF00640. PID. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 2 hits.
SM00462. PTB. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 2 hits.
PROSITEPS50106. PDZ. 2 hits.
PS01179. PID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02410.
GeneWikiAPBA1.
GenomeRNAi320.
NextBio1311.
PROQ02410.
SOURCESearch...

Entry information

Entry nameAPBA1_HUMAN
AccessionPrimary (citable) accession number: Q02410
Secondary accession number(s): O14914, O60570, Q5VYR8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM