Reviewed, UniProtKB/Swiss-Prot Q99767 (APBA2_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	749 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Ref.5
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 process	Protein transport Transport
Coding sequence diversity	Polymorphism
Domain	Repeat
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nervous system development Ref.2 Traceable author statement. Source: ProtInc protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Ref.2 Ref.5 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 749	749	Amyloid beta A4 precursor protein-binding family A member 2		PRO_0000064616
Regions
	Domain	368 – 555	188	PID
	Domain	568 – 654	87	PDZ 1
	Domain	659 – 734	76	PDZ 2
	Region	185 – 270	86	STXBP1-binding
	Compositional bias	92 – 95	4	Poly-Glu
Amino acid modifications
	Modified residue	208	1	Phosphoserine By similarity
Natural variations
	Natural variant	311	1	L → P: dbSNP rs8040932.		VAR_050665
Experimental info
	Sequence conflict	135	1	Q → H in BAA34734. Ref.2
	Sequence conflict	163	1	G → R in AAC39767. Ref.1
	Sequence conflict	170 – 214	45	DEPSV…YRLRR → MSPPSLRPMTRKKMVTMCQQ RGLPGLLPRGGQREHRRLPL PPEA in AAC39767. Ref.1
	Sequence conflict	344	1	E → K in BAA34734. Ref.2
	Sequence conflict	354	1	F → L in BAA34734. Ref.2
	Sequence conflict	364 – 365	2	ED → KN in BAA34734. Ref.2
	Sequence conflict	604	1	G → C in AAC39767. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99767-1 [UniParc]. Last modified May 30, 2000. Version 3. Checksum: C15AE9CFAEF51D85	FASTA	749	82,512
	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

References

	« Hide 'large scale' referencesShow '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
EMBLGenBankDDBJ	AF047348 mRNA. Translation: AAC39767.1. AB014719 mRNA. Translation: BAA34734.1. AF029108 mRNA. Translation: AAC05306.1. U79255 mRNA. Translation: AAB50203.1.
IPI	IPI00017817.
RefSeq	NP_001123886.1. NP_005494.2.
UniGene	Hs.618112
3D structure databases
HSSP	HSSP built from PDB template 1AQC based on UniProtKB Q02410.
SMR	Q99767. Positions 567-749.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99767. 1 interaction.
STRING	Q99767.
PTM databases
PhosphoSite	Q99767.
Proteomic databases
PRIDE	Q99767.
Genome annotation databases
Ensembl	ENST00000219865; ENSP00000219865; ENSG00000034053; Homo sapiens. [Genome view] ENST00000382938; ENSP00000372396; ENSG00000034053; Homo sapiens. [Genome view] ENST00000411764; ENSP00000409312; ENSG00000034053; Homo sapiens. [Genome view]
GeneID	321.
KEGG	hsa:321.
UCSC	uc001zck.1. human.
Organism-specific databases
CTD	321.
GeneCards	GC15P027001.
H-InvDB	HIX0021324.
HGNC	HGNC:579. APBA2.
MIM	602712. gene.
PharmGKB	PA24870.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q99767.
OMA	MLDHRVR.
Gene expression databases
ArrayExpress	Q99767.
Bgee	Q99767.
CleanEx	HS_APBA2.
Genevestigator	Q99767.
GermOnline	ENSG00000034053. Homo sapiens.
Family and domain databases
InterPro	IPR001478. PDZ/DHR/GLGF. IPR011993. PH_type. IPR006020. PTB_PID. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
Pfam	PF00595. PDZ. 2 hits. PF00640. PID. 1 hit. [Graphical view]
SMART	SM00228. PDZ. 2 hits. SM00462. PTB. 1 hit. [Graphical view]
PROSITE	PS50106. PDZ. 2 hits. PS01179. PID. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	1315.
SOURCE	Search...

Entry information

Entry name

APBA2_HUMAN

Accession

Primary (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:	November 3, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.