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Q5T3N0

- Q5T3N0_HUMAN

UniProt

Q5T3N0 - Q5T3N0_HUMAN

Protein

Annexin

Gene

ANXA1

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

    GO - Molecular functioni

    1. calcium-dependent phospholipid binding Source: UniProtKB-KW
    2. calcium ion binding Source: InterPro
    3. phospholipase A2 inhibitor activity Source: Ensembl

    GO - Biological processi

    1. alpha-beta T cell differentiation Source: Ensembl
    2. arachidonic acid secretion Source: Ensembl
    3. cell surface receptor signaling pathway Source: Ensembl
    4. cellular response to glucocorticoid stimulus Source: Ensembl
    5. cellular response to hydrogen peroxide Source: Ensembl
    6. endocrine pancreas development Source: Ensembl
    7. estrous cycle phase Source: Ensembl
    8. gliogenesis Source: Ensembl
    9. hepatocyte differentiation Source: Ensembl
    10. insulin secretion Source: Ensembl
    11. negative regulation of acute inflammatory response Source: Ensembl
    12. negative regulation of apoptotic process Source: Ensembl
    13. negative regulation of protein secretion Source: Ensembl
    14. neutrophil homeostasis Source: Ensembl
    15. positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
    16. positive regulation of neutrophil apoptotic process Source: Ensembl
    17. positive regulation of prostaglandin biosynthetic process Source: Ensembl
    18. regulation of cell proliferation Source: Ensembl
    19. response to drug Source: Ensembl
    20. response to estradiol Source: Ensembl
    21. response to interleukin-1 Source: Ensembl
    22. response to peptide hormone Source: Ensembl
    23. response to X-ray Source: Ensembl

    Keywords - Ligandi

    Calcium, Calcium/phospholipid-bindingUniRule annotation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AnnexinUniRule annotation
    Gene namesi
    Name:ANXA1Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:533. ANXA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular space Source: Ensembl
    3. mitochondrial membrane Source: Ensembl
    4. nucleus Source: Ensembl
    5. plasma membrane Source: HPA
    6. protein complex Source: Ensembl
    7. sarcolemma Source: Ensembl

    PTM / Processingi

    Proteomic databases

    PRIDEiQ5T3N0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5T3N0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5T3N0.
    SMRiQ5T3N0. Positions 2-115.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    A pair of annexin repeats may form one binding site for calcium and phospholipid.UniRule annotation

    Sequence similaritiesi

    Belongs to the annexin family.UniRule annotation
    Contains 1 annexin repeat.UniRule annotation

    Keywords - Domaini

    AnnexinUniRule annotationSAAS annotation, RepeatUniRule annotationSAAS annotation

    Phylogenomic databases

    HOGENOMiHOG000158803.
    HOVERGENiHBG061815.

    Family and domain databases

    Gene3Di1.10.220.10. 1 hit.
    InterProiIPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR002388. AnnexinI.
    [Graphical view]
    PfamiPF00191. Annexin. 1 hit.
    [Graphical view]
    PRINTSiPR00196. ANNEXIN.
    PR00197. ANNEXINI.
    SMARTiSM00335. ANX. 1 hit.
    [Graphical view]
    PROSITEiPS00223. ANNEXIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Q5T3N0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA    50
    LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK PLDETLKKAL 100
    TGHLEEVVLA LLKTP 115
    Length:115
    Mass (Da):12,643
    Last modified:December 21, 2004 - v1
    Checksum:iEF00F9FFBD3C7875
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei115 – 1151Imported

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL359997 Genomic DNA. No translation available.

    Genome annotation databases

    EnsembliENST00000415424; ENSP00000414013; ENSG00000135046.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL359997 Genomic DNA. No translation available.

    3D structure databases

    ProteinModelPortali Q5T3N0.
    SMRi Q5T3N0. Positions 2-115.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5T3N0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000415424 ; ENSP00000414013 ; ENSG00000135046 .

    Organism-specific databases

    HGNCi HGNC:533. ANXA1.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000158803.
    HOVERGENi HBG061815.

    Miscellaneous databases

    ChiTaRSi ANXA1. human.

    Gene expression databases

    ArrayExpressi Q5T3N0.

    Family and domain databases

    Gene3Di 1.10.220.10. 1 hit.
    InterProi IPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR002388. AnnexinI.
    [Graphical view ]
    Pfami PF00191. Annexin. 1 hit.
    [Graphical view ]
    PRINTSi PR00196. ANNEXIN.
    PR00197. ANNEXINI.
    SMARTi SM00335. ANX. 1 hit.
    [Graphical view ]
    PROSITEi PS00223. ANNEXIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    3. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Ensembl
      Submitted (JUL-2011) to UniProtKB
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiQ5T3N0_HUMAN
    AccessioniPrimary (citable) accession number: Q5T3N0
    Entry historyi
    Integrated into UniProtKB/TrEMBL: December 21, 2004
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 73 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