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E5RHT1

- E5RHT1_HUMAN

UniProt

E5RHT1 - E5RHT1_HUMAN

Protein
Submitted name:

Presenilin-2 CTF subunit

Gene

PSEN2

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. anagen Source: Ensembl
    2. beta-amyloid metabolic process Source: Ensembl
    3. brain morphogenesis Source: Ensembl
    4. calcium ion transport Source: Ensembl
    5. cardiac muscle contraction Source: Ensembl
    6. cell fate specification Source: Ensembl
    7. cellular protein metabolic process Source: Ensembl
    8. dorsal/ventral neural tube patterning Source: Ensembl
    9. embryonic limb morphogenesis Source: Ensembl
    10. endoplasmic reticulum calcium ion homeostasis Source: Ensembl
    11. forebrain development Source: Ensembl
    12. hematopoietic progenitor cell differentiation Source: Ensembl
    13. intracellular signal transduction Source: InterPro
    14. locomotion Source: Ensembl
    15. lung alveolus development Source: Ensembl
    16. memory Source: Ensembl
    17. myeloid leukocyte differentiation Source: Ensembl
    18. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    19. negative regulation of protein binding Source: Ensembl
    20. negative regulation of protein complex assembly Source: Ensembl
    21. negative regulation of protein phosphorylation Source: Ensembl
    22. Notch signaling pathway Source: Ensembl
    23. positive regulation of apoptotic process Source: Ensembl
    24. positive regulation of coagulation Source: Ensembl
    25. positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    26. protein processing Source: Ensembl
    27. protein transport Source: Ensembl
    28. regulation of epidermal growth factor-activated receptor activity Source: Ensembl
    29. regulation of synaptic plasticity Source: Ensembl
    30. response to hypoxia Source: Ensembl
    31. somitogenesis Source: Ensembl
    32. T cell activation involved in immune response Source: Ensembl
    33. T cell receptor signaling pathway Source: Ensembl
    34. thymus development Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Presenilin-2 CTF subunitImported
    Gene namesi
    Name:PSEN2Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9509. PSEN2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. endoplasmic reticulum Source: Ensembl
    3. integral component of membrane Source: InterPro
    4. neuronal cell body Source: Ensembl
    5. Z disc Source: Ensembl

    Expressioni

    Gene expression databases

    ArrayExpressiE5RHT1.
    BgeeiE5RHT1.

    Structurei

    3D structure databases

    ProteinModelPortaliE5RHT1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Family and domain databases

    InterProiIPR001493. Pept_A22A_PS2.
    IPR001108. Peptidase_A22A.
    [Graphical view]
    PANTHERiPTHR10202. PTHR10202. 1 hit.
    PTHR10202:SF11. PTHR10202:SF11. 1 hit.
    PfamiPF01080. Presenilin. 1 hit.
    [Graphical view]
    PRINTSiPR01074. PRESENILIN2.

    Sequencei

    Sequence statusi: Fragment.

    E5RHT1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTFMASDSE EEVCDERTSL MSAESPTPRS CQEGRQGPED GENTAQWRSQ    50
    ENEEDGEEDP DRYVCSGVPG RPPGLEEELT LKYGAKHVIM LFVPVTLCMI 100
    VVVATIKSVR FYTEKNGQLI YTPFTEDTP 129
    Length:129
    Mass (Da):14,455
    Last modified:February 8, 2011 - v1
    Checksum:i09C4AB535E8B4F9D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei129 – 1291Imported

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL359732 Genomic DNA. No translation available.
    AL391628 Genomic DNA. No translation available.

    Genome annotation databases

    EnsembliENST00000495488; ENSP00000429682; ENSG00000143801.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL359732 Genomic DNA. No translation available.
    AL391628 Genomic DNA. No translation available.

    3D structure databases

    ProteinModelPortali E5RHT1.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000495488 ; ENSP00000429682 ; ENSG00000143801 .

    Organism-specific databases

    HGNCi HGNC:9509. PSEN2.
    GenAtlasi Search...

    Miscellaneous databases

    ChiTaRSi PSEN2. human.
    NextBioi 35498458.

    Gene expression databases

    ArrayExpressi E5RHT1.
    Bgeei E5RHT1.

    Family and domain databases

    InterProi IPR001493. Pept_A22A_PS2.
    IPR001108. Peptidase_A22A.
    [Graphical view ]
    PANTHERi PTHR10202. PTHR10202. 1 hit.
    PTHR10202:SF11. PTHR10202:SF11. 1 hit.
    Pfami PF01080. Presenilin. 1 hit.
    [Graphical view ]
    PRINTSi PR01074. PRESENILIN2.
    ProtoNeti Search...

    Publicationsi

    1. "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., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , 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., 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., 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., 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., McLaren S., Milne S., Mistry S., Moore M.J., 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., 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., Banerjee R., Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D., Porter K.M., Prigmore E.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    3. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. Ensembl
      Submitted (JUL-2011) to UniProtKB
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiE5RHT1_HUMAN
    AccessioniPrimary (citable) accession number: E5RHT1
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 8, 2011
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 29 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    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

    Caution

    The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3