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O96018

- APBA3_HUMAN

UniProt

O96018 - APBA3_HUMAN

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Protein

Amyloid beta A4 precursor protein-binding family A member 3

Gene

APBA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN.1 Publication

GO - Molecular functioni

  1. beta-amyloid binding Source: Ensembl
  2. enzyme binding Source: UniProtKB
  3. enzyme inhibitor activity Source: UniProtKB

GO - Biological processi

  1. in utero embryonic development Source: Ensembl
  2. negative regulation of catalytic activity Source: UniProtKB
  3. protein transport Source: UniProtKB-KW
  4. regulation of gene expression Source: Ensembl
  5. synaptic transmission Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Amyloid beta A4 precursor protein-binding family A member 3
Alternative name(s):
Adapter protein X11gamma
Neuron-specific X11L2 protein
Neuronal Munc18-1-interacting protein 3
Short name:
Mint-3
Gene namesi
Name:APBA3
Synonyms:MINT3, X11L2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:580. APBA3.

Subcellular locationi

Cytoplasmperinuclear region 1 Publication

GO - Cellular componenti

  1. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24872.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Amyloid beta A4 precursor protein-binding family A member 3PRO_0000064620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei372 – 3721Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO96018.
PaxDbiO96018.
PRIDEiO96018.

PTM databases

PhosphoSiteiO96018.

Expressioni

Tissue specificityi

Expressed in all tissues examined with lower levels in brain and testis.

Gene expression databases

BgeeiO96018.
CleanExiHS_APBA3.
ExpressionAtlasiO96018. baseline and differential.
GenevestigatoriO96018.

Organism-specific databases

HPAiHPA045577.

Interactioni

Subunit structurei

Binds to the cytoplasmic domain of amyloid protein (APP) in vivo. Interacts with HIF1AN (via N-terminus).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Azi2Q9QYP62EBI-6115839,EBI-6115874From a different organism.
TANKQ928442EBI-6115839,EBI-356349
TBKBP1A7MCY62EBI-6115839,EBI-359969

Protein-protein interaction databases

BioGridi114920. 10 interactions.
IntActiO96018. 4 interactions.
MINTiMINT-1207318.
STRINGi9606.ENSP00000315136.

Structurei

Secondary structure

1
575
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi393 – 3986Combined sources
Beta strandi407 – 4115Combined sources
Beta strandi415 – 4184Combined sources
Beta strandi421 – 4266Combined sources
Helixi433 – 4353Combined sources
Beta strandi443 – 4497Combined sources
Helixi457 – 46610Combined sources
Turni467 – 4693Combined sources
Beta strandi470 – 4778Combined sources
Beta strandi483 – 4908Combined sources
Beta strandi493 – 4953Combined sources
Beta strandi498 – 5025Combined sources
Beta strandi505 – 5095Combined sources
Helixi515 – 5184Combined sources
Beta strandi525 – 5295Combined sources
Helixi539 – 54810Combined sources
Beta strandi551 – 5588Combined sources
Helixi560 – 5667Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YT7NMR-A390-483[»]
2YT8NMR-A483-569[»]
ProteinModelPortaliO96018.
SMRiO96018. Positions 213-575.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO96018.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini217 – 381165PIDPROSITE-ProRule annotationAdd
BLAST
Domaini394 – 48087PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini485 – 56076PDZ 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi165 – 1717Poly-Ser

Domaini

Composed of an N-terminal domain, 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 similaritiesi

Contains 2 PDZ (DHR) domains.PROSITE-ProRule annotation
Contains 1 PID domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG283022.
GeneTreeiENSGT00390000013578.
HOGENOMiHOG000033981.
HOVERGENiHBG050523.
InParanoidiO96018.
OMAiALHTISY.
OrthoDBiEOG78PV8H.
PhylomeDBiO96018.
TreeFamiTF315245.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
2.30.42.10. 2 hits.
InterProiIPR001478. PDZ.
IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00595. PDZ. 2 hits.
PF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 2 hits.
SM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 2 hits.
PROSITEiPS50106. PDZ. 2 hits.
PS01179. PID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O96018-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDFPTISRSP SGPPAMDLEG PRDILVPSED LTPDSQWDPM PGGPGSLSRM
60 70 80 90 100
ELDESSLQEL VQQFEALPGD LVGPSPGGAP CPLHIATGHG LASQEIADAH
110 120 130 140 150
GLLSAEAGRD DLLGLLHCEE CPPSQTGPEE PLEPAPRLLQ PPEDPDEDSD
160 170 180 190 200
SPEWVEGASA EQEGSRSSSS SPEPWLETVP LVTPEEPPAG AQSPETLASY
210 220 230 240 250
PAPQEVPGPC DHEDLLDGVI FGARYLGSTQ LVSERNPPTS TRMAQAREAM
260 270 280 290 300
DRVKAPDGET QPMTEVDLFV STKRIKVLTA DSQEAMMDHA LHTISYTADI
310 320 330 340 350
GCVLVLMARR RLARRPAPQD HGRRLYKMLC HVFYAEDAQL IAQAIGQAFA
360 370 380 390 400
AAYSQFLRES GIDPSQVGVH PSPGACHLHN GDLDHFSNSD NCREVHLEKR
410 420 430 440 450
RGEGLGVALV ESGWGSLLPT AVIANLLHGG PAERSGALSI GDRLTAINGT
460 470 480 490 500
SLVGLPLAAC QAAVRETKSQ TSVTLSIVHC PPVTTAIIHR PHAREQLGFC
510 520 530 540 550
VEDGIICSLL RGGIAERGGI RVGHRIIEIN GQSVVATPHA RIIELLTEAY
560 570
GEVHIKTMPA ATYRLLTGQE QPVYL
Length:575
Mass (Da):61,454
Last modified:May 1, 1999 - v1
Checksum:i3B910CC74C5F3840
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti505 – 5051I → IVRPRPLAPGWGGRAALSTA PEQPPPLSRAPLFLPQ in AAC17979. (PubMed:9860131)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541W → L.
Corresponds to variant rs35932323 [ dbSNP | Ensembl ].
VAR_050666
Natural varianti276 – 2761K → T.
Corresponds to variant rs3746119 [ dbSNP | Ensembl ].
VAR_020134
Natural varianti376 – 3761C → R.1 Publication
Corresponds to variant rs8102086 [ dbSNP | Ensembl ].
VAR_047952
Natural varianti527 – 5271I → F.
Corresponds to variant rs1045236 [ dbSNP | Ensembl ].
VAR_011822

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021638 mRNA. Translation: BAA74430.1.
AC005954 Genomic DNA. Translation: AAC72275.1.
BC086306 mRNA. Translation: AAH86306.1.
AB023431 Genomic DNA. Translation: BAA83094.1.
AF029110 mRNA. Translation: AAC17979.1.
CCDSiCCDS12110.1.
PIRiJG0181.
RefSeqiNP_004877.1. NM_004886.3.
UniGeneiHs.25527.
Hs.465607.

Genome annotation databases

EnsembliENST00000316757; ENSP00000315136; ENSG00000011132.
GeneIDi9546.
KEGGihsa:9546.
UCSCiuc002lyo.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021638 mRNA. Translation: BAA74430.1 .
AC005954 Genomic DNA. Translation: AAC72275.1 .
BC086306 mRNA. Translation: AAH86306.1 .
AB023431 Genomic DNA. Translation: BAA83094.1 .
AF029110 mRNA. Translation: AAC17979.1 .
CCDSi CCDS12110.1.
PIRi JG0181.
RefSeqi NP_004877.1. NM_004886.3.
UniGenei Hs.25527.
Hs.465607.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YT7 NMR - A 390-483 [» ]
2YT8 NMR - A 483-569 [» ]
ProteinModelPortali O96018.
SMRi O96018. Positions 213-575.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114920. 10 interactions.
IntActi O96018. 4 interactions.
MINTi MINT-1207318.
STRINGi 9606.ENSP00000315136.

PTM databases

PhosphoSitei O96018.

Proteomic databases

MaxQBi O96018.
PaxDbi O96018.
PRIDEi O96018.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316757 ; ENSP00000315136 ; ENSG00000011132 .
GeneIDi 9546.
KEGGi hsa:9546.
UCSCi uc002lyo.1. human.

Organism-specific databases

CTDi 9546.
GeneCardsi GC19M003750.
HGNCi HGNC:580. APBA3.
HPAi HPA045577.
MIMi 604262. gene.
neXtProti NX_O96018.
PharmGKBi PA24872.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG283022.
GeneTreei ENSGT00390000013578.
HOGENOMi HOG000033981.
HOVERGENi HBG050523.
InParanoidi O96018.
OMAi ALHTISY.
OrthoDBi EOG78PV8H.
PhylomeDBi O96018.
TreeFami TF315245.

Miscellaneous databases

ChiTaRSi APBA3. human.
EvolutionaryTracei O96018.
GeneWikii APBA3.
GenomeRNAii 9546.
NextBioi 35799.
PROi O96018.
SOURCEi Search...

Gene expression databases

Bgeei O96018.
CleanExi HS_APBA3.
ExpressionAtlasi O96018. baseline and differential.
Genevestigatori O96018.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
2.30.42.10. 2 hits.
InterProi IPR001478. PDZ.
IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
[Graphical view ]
Pfami PF00595. PDZ. 2 hits.
PF00640. PID. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 2 hits.
SM00462. PTB. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 2 hits.
PROSITEi PS50106. PDZ. 2 hits.
PS01179. PID. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "X11L2, a new member of X11 protein family interacts with Alzheimer's beta-amyloid precursor protein."
    Tanahashi H., Tabira T.
    Biochem. Biophys. Res. Commun. 255:663-667(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. "Genomic organization of the human X11L2 gene (APBA3), a third member of the X11 protein family interacting with Alzheimer's beta-amyloid precursor protein."
    Tanahashi H., Tabira T.
    NeuroReport 10:2575-2578(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 207-575.
  5. "Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2."
    Okamoto M., Suedhof T.C.
    Eur. J. Cell Biol. 77:161-165(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 472-575.
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, VARIANT [LARGE SCALE ANALYSIS] ARG-376, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Mint3 enhances the activity of hypoxia-inducible factor-1 (HIF-1) in macrophages by suppressing the activity of factor inhibiting HIF-1."
    Sakamoto T., Seiki M.
    J. Biol. Chem. 284:30350-30359(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIF1AN, SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Solution structure of the PDZ domain of amyloid beta A4 precursor protein-binding family A member 3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 387-569.

Entry informationi

Entry nameiAPBA3_HUMAN
AccessioniPrimary (citable) accession number: O96018
Secondary accession number(s): O60483, Q9UPZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3