Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01408
Entry Name
UniProt Accession
Theoretical PI
7.74
Molecular Weight
28996.08
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Gamma-secretase subunit APH-1A
Protein Synonyms/Alias
APH-1a; Aph-1alpha; Presenilin-stabilization factor;
Gene Name
APH1A
Gene Synonyms/Alias
PSF; CGI-78; UNQ579/PRO1141;
Created Date
26-SEP-2003
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
182
Canonical
GVVFFDACERRRYWA
[1]
S-Palmitoylation
245
Canonical
SIQRSLLCRRQEDSR
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Cheng H, Vetrivel KS, Drisdel RC, Meckler X, Gong P, Leem JY, Li T, Carter M, Chen Y, Nguyen P, Iwatsubo T, Tomita T, Wong PC, Green WN, Kounnas MZ, ThinakaranG. S-palmitoylation of gamma-secretase subunits nicastrin and APH-1. J Biol Chem.2009 Jan 16;284(3):1373-84. doi: 10.1074/jbc.M806380200. Epub 2008 Nov 20. PubMedPMID: 19028695; PubMed Central PMCID: PMC2615504.[PMID:19028695]
Functional Description
Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (beta-amyloid precursor protein). It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex.
Sequence Annotation
Topological domain: 1 2 Lumenal.
Transmembrane: 3 23 Helical; Name=1.
Topological domain: 24 31 Cytoplasmic.
Transmembrane: 32 52 Helical; Name=2.
Topological domain: 53 68 Lumenal.
Transmembrane: 69 89 Helical; Name=3.
Topological domain: 90 118 Cytoplasmic.
Transmembrane: 119 139 Helical; Name=4.
Topological domain: 140 158 Lumenal.
Transmembrane: 159 179 Helical; Name=5.
Topological domain: 180 186 Cytoplasmic.
Transmembrane: 187 207 Helical; Name=6.
Topological domain: 208 213 Lumenal.
Transmembrane: 214 234 Helical; Name=7.
Topological domain: 235 265 Cytoplasmic.
Protein Length
265 AA.
Protein Sequence
(Canonical)
MGAAVFFGCT FVAFGPAFAL FLITVAGDPL RVIILVAGAF FWLVSLLLAS VVWFILVHVT  60
DRSDARLQYG LLIFGAAVSV LLQEVFRFAY YKLLKKADEG LASLSEDGRS PISIRQMAYV  120
SGLSFGIISG VFSVINILAD ALGPGVVGIH GDSPYYFLTS AFLTAAIILL HTFWGVVFFD  180
ACERRRYWAL GLVVGSHLLT SGLTFLNPWY EASLLPIYAV TVSMGLWAFI TAGGSLRSIQ  240
RSLLCRRQED SRVMVYSALR IPPED                                        265
FASTA
(Canonical)
>LipidDB-9606-01408|Q96BI3
MGAAVFFGCTFVAFGPAFALFLITVAGDPLRVIILVAGAFFWLVSLLLASVVWFILVHVT
DRSDARLQYGLLIFGAAVSVLLQEVFRFAYYKLLKKADEGLASLSEDGRSPISIRQMAYV
SGLSFGIISGVFSVINILADALGPGVVGIHGDSPYYFLTSAFLTAAIILLHTFWGVVFFD
ACERRRYWALGLVVGSHLLTSGLTFLNPWYEASLLPIYAVTVSMGLWAFITAGGSLRSIQ
RSLLCRRQEDSRVMVYSALRIPPED
Gene Ontology
GO:0005783; C:endoplasmic reticulum; IDA:HGNC
GO:0005794; C:Golgi apparatus; IDA:HGNC
GO:0005887; C:integral component of plasma membrane; IDA:HGNC
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0004175; F:endopeptidase activity; IEA:Ensembl
GO:0042987; P:amyloid precursor protein catabolic process; IMP:UniProtKB
GO:0097190; P:apoptotic signaling pathway; TAS:Reactome
GO:0006509; P:membrane protein ectodomain proteolysis; IDA:HGNC
GO:0031293; P:membrane protein intracellular domain proteolysis; IMP:UniProtKB
GO:0001656; P:metanephros development; IEA:Ensembl
GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome
GO:0007220; P:Notch receptor processing; IMP:UniProtKB
GO:0007219; P:Notch signaling pathway; TAS:Reactome
GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome
GO:0043085; P:positive regulation of catalytic activity; IDA:HGNC
GO:0016485; P:protein processing; IDA:HGNC
Interpro
InterPro; IPR009294; Aph-1
Pfam
Pfam; PF06105; Aph-1;
SMART
PROSITE
PRINTS