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E5RHT1

- E5RHT1_HUMAN

UniProt

E5RHT1 - E5RHT1_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

Expressioni

Gene expression databases

ArrayExpressiE5RHT1.
BgeeiE5RHT1.

Structurei

3D structure databases

ProteinModelPortaliE5RHT1.

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

Non-terminal residue

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 28 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 proteome

External Data

Dasty 3

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