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Q02410 (APBA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 108. 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·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)
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. Binds to the cytoplasmic domain of amyloid protein (APP).

Tissue specificity

Brain and spinal cord.

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.

Sequence similarities

Contains 2 PDZ (DHR) domains.

Contains 1 PID domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP050673EBI-368690,EBI-77613

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
Compositional bias67 – 704Poly-Glu
Compositional bias294 – 32835Pro-rich
Compositional bias368 – 45285Pro-rich

Amino acid modifications

Modified residue2631Phosphoserine Ref.6

Natural variations

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
Q02410 [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

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: 9395480] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 9614075] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 15164053] [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: 7678331] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 130-837.
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: 8887653] [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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[7]"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: 9321393] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 452-617.
[8]"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.
IPIIPI00294556.
PIRA47176.
RefSeqNP_001154.2. NM_001163.3.
UniGeneHs.171939.

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 453-621, 655-837.
ModBaseSearch...

Protein-protein interaction databases

IntActQ02410. 4 interactions.
MINTMINT-153502.
STRINGQ02410.

PTM databases

PhosphoSiteQ02410.

Polymorphism databases

DMDM116241250.

Proteomic databases

PRIDEQ02410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265381; ENSP00000265381; ENSG00000107282.
GeneID320.
KEGGhsa:320.
UCSCuc004ahh.1. human.

Organism-specific databases

CTD320.
GeneCardsGC09M072042.
H-InvDBHIX0034751.
HGNCHGNC:578. APBA1.
HPACAB009338.
HPA019850.
MIM602414. gene.
neXtProtNX_Q02410.
PharmGKBPA24869.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05150.
GeneTreeENSGT00390000013578.
HOGENOMHBG714692.
HOVERGENHBG050523.
InParanoidQ02410.
OMALHHYDER.
OrthoDBEOG43JC42.
PhylomeDBQ02410.

Gene expression databases

ArrayExpressQ02410.
BgeeQ02410.
CleanExHS_APBA1.
GenevestigatorQ02410.
GermOnlineENSG00000107282. Homo sapiens.

Family and domain databases

InterProIPR001478. PDZ/DHR/GLGF.
IPR011993. PH_type.
IPR006020. PTyr_interaction_dom.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
KOK04531.
PfamPF00595. PDZ. 2 hits.
PF00640. PID. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 2 hits.
SM00462. PTB. 1 hit.
[Graphical view]
SUPFAMSSF50156. PDZ. 2 hits.
PROSITEPS50106. PDZ. 2 hits.
PS01179. PID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio1311.
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: January 25, 2012
This is version 108 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

Human chromosome 9

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families