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Protein

Gamma-secretase subunit APH-1B

Gene

Aph1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Probable 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. Probably present in a minority of gamma-secretase complexes compared to APH1A (By similarity).By similarity

GO - Molecular functioni

  • endopeptidase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Notch signaling pathway

Enzyme and pathway databases

ReactomeiR-MMU-1251985. Nuclear signaling by ERBB4.
R-MMU-193692. Regulated proteolysis of p75NTR.
R-MMU-1980148. Signaling by NOTCH3.
R-MMU-1980150. Signaling by NOTCH4.
R-MMU-205043. NRIF signals cell death from the nucleus.
R-MMU-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-secretase subunit APH-1B
Short name:
APH-1b
Alternative name(s):
Aph-1beta
Gene namesi
Name:Aph1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:3522097. Aph1b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei5 – 2521Helical; Name=1Sequence analysisAdd
BLAST
Transmembranei32 – 5221Helical; Name=2Sequence analysisAdd
BLAST
Transmembranei66 – 8621Helical; Name=3Sequence analysisAdd
BLAST
Transmembranei115 – 13521Helical; Name=4Sequence analysisAdd
BLAST
Transmembranei160 – 18021Helical; Name=5Sequence analysisAdd
BLAST
Transmembranei186 – 20621Helical; Name=6Sequence analysisAdd
BLAST
Transmembranei213 – 23321Helical; Name=7Sequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257Gamma-secretase subunit APH-1BPRO_0000221053Add
BLAST

Proteomic databases

MaxQBiQ8C7N7.
PaxDbiQ8C7N7.
PRIDEiQ8C7N7.

PTM databases

PhosphoSiteiQ8C7N7.

Expressioni

Gene expression databases

BgeeiQ8C7N7.
ExpressionAtlasiQ8C7N7. baseline and differential.
GenevisibleiQ8C7N7. MM.

Interactioni

Subunit structurei

Probable component of the gamma-secretase complex, a complex composed of a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal complex is sufficient for secretase activity, although other components may exist (By similarity). Interacts with PSEN1 and PSEN2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi228950. 13 interactions.
STRINGi10090.ENSMUSP00000034934.

Family & Domainsi

Sequence similaritiesi

Belongs to the APH-1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3972. Eukaryota.
ENOG4111FIJ. LUCA.
GeneTreeiENSGT00390000002049.
HOGENOMiHOG000007541.
HOVERGENiHBG050541.
InParanoidiQ8C7N7.
KOiK06172.
OMAiFRFGYYK.
OrthoDBiEOG7TF7B1.
PhylomeDBiQ8C7N7.
TreeFamiTF314362.

Family and domain databases

InterProiIPR009294. Aph-1.
[Graphical view]
PANTHERiPTHR12889. PTHR12889. 1 hit.
PfamiPF06105. Aph-1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8C7N7-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTAAVFFGCA FIAFGPALAL YVFTIATDPL RVIFLIAGAF FWLVSLLLSS
60 70 80 90 100
VFWFLVRVIT DNRDGPVQNY LLIFGVLLSV CIQELFRLAY YKLLKKASEG
110 120 130 140 150
LKSINPEETA PSMRLLAYVS GLGFGIMSGV FSFVNTLSNS LGPGTVGIHG
160 170 180 190 200
DSPQFFLNSA FMTLVVIMLH VFWGVVFFDG CEKNKWYTLL TVLLTHLVVS
210 220 230 240 250
TQTFLSPYYE VNLVTAYIIM VLMGIWAFYV AGGSCRSLKL CLLCQDKDFL

LYNQRSR
Length:257
Mass (Da):28,703
Last modified:March 1, 2003 - v1
Checksum:i52D39310695ED96A
GO
Isoform 2 (identifier: Q8C7N7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     160-212: AFMTLVVIML...TFLSPYYEVN → VRISASPMDI...SSDYLTPALS
     213-257: Missing.

Note: No experimental confirmation available.
Show »
Length:212
Mass (Da):23,043
Checksum:i8B533C4390833A11
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei160 – 21253AFMTL…YYEVN → VRISASPMDINSVSHSREPV LCAASKLVFPVGKVFDFLRP AAYSSDYLTPALS in isoform 2. 1 PublicationVSP_008359Add
BLAST
Alternative sequencei213 – 25745Missing in isoform 2. 1 PublicationVSP_008360Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028521 mRNA. Translation: BAC25988.1.
AK049828 mRNA. Translation: BAC33940.1.
AK154847 mRNA. Translation: BAE32873.1.
BC079659 mRNA. Translation: AAH79659.1.
CCDSiCCDS23307.1. [Q8C7N7-1]
RefSeqiNP_808251.1. NM_177583.4. [Q8C7N7-1]
UniGeneiMm.41291.

Genome annotation databases

EnsembliENSMUST00000034934; ENSMUSP00000034934; ENSMUSG00000032375. [Q8C7N7-1]
ENSMUST00000168309; ENSMUSP00000125816; ENSMUSG00000032375. [Q8C7N7-2]
GeneIDi208117.
KEGGimmu:208117.
UCSCiuc009qfe.1. mouse. [Q8C7N7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028521 mRNA. Translation: BAC25988.1.
AK049828 mRNA. Translation: BAC33940.1.
AK154847 mRNA. Translation: BAE32873.1.
BC079659 mRNA. Translation: AAH79659.1.
CCDSiCCDS23307.1. [Q8C7N7-1]
RefSeqiNP_808251.1. NM_177583.4. [Q8C7N7-1]
UniGeneiMm.41291.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228950. 13 interactions.
STRINGi10090.ENSMUSP00000034934.

PTM databases

PhosphoSiteiQ8C7N7.

Proteomic databases

MaxQBiQ8C7N7.
PaxDbiQ8C7N7.
PRIDEiQ8C7N7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034934; ENSMUSP00000034934; ENSMUSG00000032375. [Q8C7N7-1]
ENSMUST00000168309; ENSMUSP00000125816; ENSMUSG00000032375. [Q8C7N7-2]
GeneIDi208117.
KEGGimmu:208117.
UCSCiuc009qfe.1. mouse. [Q8C7N7-1]

Organism-specific databases

CTDi83464.
MGIiMGI:3522097. Aph1b.

Phylogenomic databases

eggNOGiKOG3972. Eukaryota.
ENOG4111FIJ. LUCA.
GeneTreeiENSGT00390000002049.
HOGENOMiHOG000007541.
HOVERGENiHBG050541.
InParanoidiQ8C7N7.
KOiK06172.
OMAiFRFGYYK.
OrthoDBiEOG7TF7B1.
PhylomeDBiQ8C7N7.
TreeFamiTF314362.

Enzyme and pathway databases

ReactomeiR-MMU-1251985. Nuclear signaling by ERBB4.
R-MMU-193692. Regulated proteolysis of p75NTR.
R-MMU-1980148. Signaling by NOTCH3.
R-MMU-1980150. Signaling by NOTCH4.
R-MMU-205043. NRIF signals cell death from the nucleus.
R-MMU-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

PROiQ8C7N7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C7N7.
ExpressionAtlasiQ8C7N7. baseline and differential.
GenevisibleiQ8C7N7. MM.

Family and domain databases

InterProiIPR009294. Aph-1.
[Graphical view]
PANTHERiPTHR12889. PTHR12889. 1 hit.
PfamiPF06105. Aph-1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Hippocampus and Skin.
  2. "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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Brain.

Entry informationi

Entry nameiAPH1B_MOUSE
AccessioniPrimary (citable) accession number: Q8C7N7
Secondary accession number(s): Q3U3B5, Q8CEC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.