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Q96BI3 (APH1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-secretase subunit APH-1A

Short name=APH-1a
Alternative name(s):
Aph-1alpha
Presenilin-stabilization factor
Gene names
Name:APH1A
Synonyms:PSF
ORF Names:CGI-78, UNQ579/PRO1141
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.10 Ref.12

Subunit structure

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.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatusGolgi stack membrane; Multi-pass membrane protein. Note: Predominantly located in the endoplasmic reticulum and in the cis-Golgi. Ref.10 Ref.11 Ref.15

Tissue specificity

Widely expressed. Expressed in leukocytes, lung, placenta, small intestine, liver, kidney, spleen thymus, skeletal muscle, heart and brain. Isoform 1 and isoform 2 are nearly expressed at the same level. Ref.9

Sequence similarities

Belongs to the APH-1 family.

Sequence caution

The sequence AAD34072.1 differs from that shown. Reason: Frameshift at position 243.

The sequence AAN63816.1 differs from that shown. Reason: Frameshift at position 243.

Ontologies

Keywords
   Biological processNotch signaling pathway
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch receptor processing

Inferred from mutant phenotype Ref.1. Source: UniProtKB

Notch signaling pathway

Traceable author statement. Source: Reactome

amyloid precursor protein catabolic process

Inferred from mutant phenotype Ref.1. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement. Source: Reactome

membrane protein ectodomain proteolysis

Inferred from direct assay PubMed 15274632. Source: HGNC

membrane protein intracellular domain proteolysis

Inferred from mutant phenotype Ref.1. Source: UniProtKB

metanephros development

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of catalytic activity

Inferred from direct assay PubMed 15274632. Source: HGNC

protein processing

Inferred from direct assay PubMed 15274632. Source: HGNC

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 15274632. Source: HGNC

Golgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from direct assay PubMed 15274632. Source: HGNC

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from direct assay PubMed 15274632. Source: HGNC

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionendopeptidase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCSTNQ925423EBI-2606935,EBI-998440

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96BI3-1)

Also known as: L; Aph-alpha1;

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.
Isoform 2 (identifier: Q96BI3-2)

Also known as: S; Aph-alpha2;

The sequence of this isoform differs from the canonical sequence as follows:
     246-247: RR → KD
     248-265: Missing.
Isoform 3 (identifier: Q96BI3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     39-120: AFFWLVSLLL...PISIRQMAYV → RCSALPTTSCLI

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 265265Gamma-secretase subunit APH-1A
PRO_0000221050

Regions

Topological domain1 – 22Lumenal Potential
Transmembrane3 – 2321Helical; Name=1; Potential
Topological domain24 – 318Cytoplasmic Potential
Transmembrane32 – 5221Helical; Name=2; Potential
Topological domain53 – 6816Lumenal Potential
Transmembrane69 – 8921Helical; Name=3; Potential
Topological domain90 – 11829Cytoplasmic Potential
Transmembrane119 – 13921Helical; Name=4; Potential
Topological domain140 – 15819Lumenal Potential
Transmembrane159 – 17921Helical; Name=5; Potential
Topological domain180 – 1867Cytoplasmic Potential
Transmembrane187 – 20721Helical; Name=6; Potential
Topological domain208 – 2136Lumenal Potential
Transmembrane214 – 23421Helical; Name=7; Potential
Topological domain235 – 26531Cytoplasmic Potential

Natural variations

Alternative sequence39 – 12082AFFWL…QMAYV → RCSALPTTSCLI in isoform 3.
VSP_045424
Alternative sequence246 – 2472RR → KD in isoform 2.
VSP_008355
Alternative sequence248 – 26518Missing in isoform 2.
VSP_008356

Experimental info

Sequence conflict2361L → I in AAH01230. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (L) (Aph-alpha1) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 8E37984A1DECC263

FASTA26528,996
        10         20         30         40         50         60 
MGAAVFFGCT FVAFGPAFAL FLITVAGDPL RVIILVAGAF FWLVSLLLAS VVWFILVHVT 

        70         80         90        100        110        120 
DRSDARLQYG LLIFGAAVSV LLQEVFRFAY YKLLKKADEG LASLSEDGRS PISIRQMAYV 

       130        140        150        160        170        180 
SGLSFGIISG VFSVINILAD ALGPGVVGIH GDSPYYFLTS AFLTAAIILL HTFWGVVFFD 

       190        200        210        220        230        240 
ACERRRYWAL GLVVGSHLLT SGLTFLNPWY EASLLPIYAV TVSMGLWAFI TAGGSLRSIQ 

       250        260 
RSLLCRRQED SRVMVYSALR IPPED 

« Hide

Isoform 2 (S) (Aph-alpha2) [UniParc].

Checksum: 8EECF2236C1EA4A0
Show »

FASTA24726,840
Isoform 3 [UniParc].

Checksum: A6D104A120AEBFA2
Show »

FASTA19520,977

References

« Hide 'large scale' references
[1]"Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch."
Lee S.-F., Shah S., Li H., Yu C., Han W., Yu G.
J. Biol. Chem. 277:45013-45019(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH PSEN1; PSEN2 AND NCSTN.
Tissue: Glioblastoma.
[2]"PSF is essential for gamma-secretase activity and stabilization of presenilin and nicastrin."
Lee H.-J., Kim T.-W.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Retinoblastoma and Thyroid.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 1 AND 2).
Tissue: Adrenal gland, Brain, Cervix, Eye, Glial tumor and Lung.
[9]"aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation."
Francis R., McGrath G., Zhang J., Ruddy D.A., Sym M., Apfeld J., Nicoll M., Maxwell M., Hai B., Ellis M.C., Parks A.L., Xu W., Li J., Gurney M., Myers R.L., Himes C.S., Hiebsch R., Ruble C., Nye J.S., Curtis D.
Dev. Cell 3:85-97(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1."
Luo W.-J., Wang H., Li H., Kim B.S., Shah S., Lee H.-J., Thinakaran G., Kim T.-W., Yu G., Xu H.
J. Biol. Chem. 278:7850-7854(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[11]"APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin.nicastrin complexes."
Gu Y., Chen F., Sanjo N., Kawarai T., Hasegawa H., Duthie M., Li W., Ruan X., Luthra A., Mount H.T.J., Tandon A., Fraser P.E., St George-Hyslop P.H.
J. Biol. Chem. 278:7374-7380(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PSEN1.
[12]"APH1, PEN2, and nicastrin increase Abeta levels and gamma-secretase activity."
Marlow L., Canet R.M., Haugabook S.J., Hardy J.A., Lahiri D.K., Sambamurti K.
Biochem. Biophys. Res. Commun. 305:502-509(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE GAMMA-SECRETASE COMPLEX.
[13]"Gamma-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2."
Kimberly W.T., LaVoie M.J., Ostaszewski B.L., Ye W., Wolfe M.S., Selkoe D.J.
Proc. Natl. Acad. Sci. U.S.A. 100:6382-6387(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF A GAMMA-SECRETASE COMPLEX WITH PEN2; PSEN1/PSEN2 AND NCSTN.
[14]"Reconstitution of gamma-secretase activity."
Edbauer D., Winkler E., Regula J.T., Pesold B., Steiner H., Haass C.
Nat. Cell Biol. 5:486-488(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY OF A GAMMA-SECRETASE COMPLEX.
[15]"Membrane topology and nicastrin-enhanced endoproteolysis of APH-1, a component of the gamma-secretase complex."
Fortna R.R., Crystal A.S., Morais V.A., Pijak D.S., Lee V.M., Doms R.W.
J. Biol. Chem. 279:3685-3693(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF508787 mRNA. Translation: AAN63816.1. Frameshift.
AY113698 mRNA. Translation: AAM61955.1.
AY113699 mRNA. Translation: AAM61956.1.
AF151835 mRNA. Translation: AAD34072.1. Frameshift.
AY358951 mRNA. Translation: AAQ89310.1.
AK027879 mRNA. Translation: BAG51389.1.
AK075295 mRNA. Translation: BAC11529.1.
AK298832 mRNA. Translation: BAG60962.1.
AL138795 Genomic DNA. Translation: CAI22811.1.
AL138795 Genomic DNA. Translation: CAI22812.1.
CH471121 Genomic DNA. Translation: EAW53565.1.
CH471121 Genomic DNA. Translation: EAW53566.1.
CH471121 Genomic DNA. Translation: EAW53567.1.
BC001230 mRNA. Translation: AAH01230.1.
BC008732 mRNA. Translation: AAH08732.1.
BC009501 mRNA. Translation: AAH09501.1.
BC015568 mRNA. Translation: AAH15568.1.
BC017699 mRNA. Translation: AAH17699.1.
BC020590 mRNA. Translation: AAH20590.1.
RefSeqNP_001071096.1. NM_001077628.2.
NP_001230700.1. NM_001243771.1.
NP_001230701.1. NM_001243772.1.
NP_057106.2. NM_016022.3.
UniGeneHs.108408.
Hs.735911.

3D structure databases

ProteinModelPortalQ96BI3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119296. 17 interactions.
IntActQ96BI3. 16 interactions.
STRING9606.ENSP00000358105.

Chemistry

BindingDBQ96BI3.
ChEMBLCHEMBL2094135.

PTM databases

PhosphoSiteQ96BI3.

Polymorphism databases

DMDM37077707.

Proteomic databases

PaxDbQ96BI3.
PRIDEQ96BI3.

Protocols and materials databases

DNASU51107.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360244; ENSP00000353380; ENSG00000117362. [Q96BI3-2]
ENST00000369109; ENSP00000358105; ENSG00000117362. [Q96BI3-1]
ENST00000414276; ENSP00000397473; ENSG00000117362. [Q96BI3-3]
ENST00000581822; ENSP00000464062; ENSG00000266334. [Q96BI3-1]
ENST00000582205; ENSP00000463082; ENSG00000266334. [Q96BI3-3]
ENST00000584744; ENSP00000464506; ENSG00000266334. [Q96BI3-2]
GeneID51107.
KEGGhsa:51107.
UCSCuc001ety.2. human. [Q96BI3-1]
uc001etz.2. human. [Q96BI3-2]
uc010pbx.2. human.

Organism-specific databases

CTD51107.
GeneCardsGC01M150237.
HGNCHGNC:29509. APH1A.
HPACAB037272.
MIM607629. gene.
neXtProtNX_Q96BI3.
PharmGKBPA142672599.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300477.
HOGENOMHOG000007541.
HOVERGENHBG050541.
InParanoidQ96BI3.
KOK06172.
OMAFIAFGPP.
PhylomeDBQ96BI3.
TreeFamTF314362.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_691. A third proteolytic cleavage releases NICD.
SignaLinkQ96BI3.

Gene expression databases

ArrayExpressQ96BI3.
BgeeQ96BI3.
CleanExHS_APH1A.
GenevestigatorQ96BI3.

Family and domain databases

InterProIPR009294. Aph-1.
[Graphical view]
PANTHERPTHR12889. PTHR12889. 1 hit.
PfamPF06105. Aph-1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi51107.
NextBio53845.
PROQ96BI3.
SOURCESearch...

Entry information

Entry nameAPH1A_HUMAN
AccessionPrimary (citable) accession number: Q96BI3
Secondary accession number(s): B4DQK0 expand/collapse secondary AC list , Q5TB22, Q5TB23, Q969R6, Q9BVG0, Q9Y386
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 117 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM