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P08758

- ANXA5_HUMAN

UniProt

P08758 - ANXA5_HUMAN

Protein

Annexin A5

Gene

ANXA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.

    GO - Molecular functioni

    1. calcium-dependent phospholipid binding Source: UniProtKB
    2. calcium ion binding Source: InterPro
    3. phospholipase inhibitor activity Source: ProtInc
    4. phospholipid binding Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: UniProtKB-KW
    2. negative regulation of apoptotic process Source: UniProtKB
    3. negative regulation of catalytic activity Source: GOC
    4. negative regulation of coagulation Source: InterPro
    5. response to organic substance Source: Ensembl
    6. signal transduction Source: UniProtKB

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium, Calcium/phospholipid-binding

    Enzyme and pathway databases

    SignaLinkiP08758.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Annexin A5
    Alternative name(s):
    Anchorin CII
    Annexin V
    Annexin-5
    Calphobindin I
    Short name:
    CBP-I
    Endonexin II
    Lipocortin V
    Placental anticoagulant protein 4
    Short name:
    PP4
    Placental anticoagulant protein I
    Short name:
    PAP-I
    Thromboplastin inhibitor
    Vascular anticoagulant-alpha
    Short name:
    VAC-alpha
    Gene namesi
    Name:ANXA5
    Synonyms:ANX5, ENX2, PP4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:543. ANXA5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endothelial microparticle Source: Ensembl
    3. external side of plasma membrane Source: Ensembl
    4. extracellular vesicular exosome Source: UniProtKB
    5. intracellular Source: LIFEdb
    6. membrane Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    Pregnancy loss, recurrent, 3 (RPRGL3) [MIM:614391]: A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi614391. phenotype.
    PharmGKBiPA24833.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 320319Annexin A5PRO_0000067487Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei70 – 701N6-acetyllysine1 Publication
    Modified residuei76 – 761N6-acetyllysine1 Publication
    Modified residuei79 – 791N6-acetyllysine1 Publication
    Modified residuei97 – 971N6-acetyllysine1 Publication
    Modified residuei101 – 1011N6-acetyllysine1 Publication
    Modified residuei290 – 2901N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP08758.
    PaxDbiP08758.
    PeptideAtlasiP08758.
    PRIDEiP08758.

    2D gel databases

    OGPiP08758.
    REPRODUCTION-2DPAGEIPI00329801.
    P08758.

    PTM databases

    PhosphoSiteiP08758.

    Expressioni

    Gene expression databases

    ArrayExpressiP08758.
    BgeeiP08758.
    CleanExiHS_ANXA5.
    GenevestigatoriP08758.

    Organism-specific databases

    HPAiCAB003677.
    HPA035330.

    Interactioni

    Subunit structurei

    Monomer. Binds ATRX and EIF5B By similarity. Interacts with hepatitis B virus (HBV).By similarity1 Publication

    Protein-protein interaction databases

    BioGridi106805. 31 interactions.
    IntActiP08758. 16 interactions.
    MINTiMINT-1382250.
    STRINGi9606.ENSP00000296511.

    Structurei

    Secondary structure

    1
    320
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 2812
    Beta strandi29 – 324
    Helixi35 – 439
    Helixi47 – 6115
    Helixi65 – 728
    Helixi75 – 8511
    Helixi88 – 10013
    Beta strandi102 – 1043
    Helixi107 – 11610
    Helixi119 – 13315
    Helixi137 – 1448
    Helixi147 – 15711
    Helixi169 – 18214
    Turni183 – 1853
    Beta strandi186 – 1883
    Helixi191 – 20010
    Helixi203 – 21715
    Helixi221 – 2288
    Helixi231 – 24515
    Helixi247 – 25610
    Helixi257 – 2593
    Beta strandi260 – 2634
    Helixi266 – 27611
    Turni277 – 2804
    Helixi281 – 29010
    Beta strandi292 – 2943
    Helixi296 – 3038
    Helixi306 – 31611

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ANWX-ray2.40A/B2-320[»]
    1ANXX-ray1.90A/B/C2-320[»]
    1AVHX-ray2.30A/B1-320[»]
    1AVRX-ray2.30A1-320[»]
    1HAKX-ray3.00A/B1-320[»]
    1HVDX-ray2.00A2-320[»]
    1HVEX-ray2.30A2-320[»]
    1HVFX-ray2.00A2-320[»]
    1HVGX-ray3.00A2-320[»]
    1SAVX-ray2.50A1-320[»]
    2XO2X-ray2.80A1-320[»]
    2XO3X-ray2.30A1-320[»]
    ProteinModelPortaliP08758.
    SMRiP08758. Positions 3-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08758.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati24 – 8461Annexin 1Add
    BLAST
    Repeati96 – 15661Annexin 2Add
    BLAST
    Repeati180 – 24061Annexin 3Add
    BLAST
    Repeati255 – 31561Annexin 4Add
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the annexin family.Curated
    Contains 4 annexin repeats.Curated

    Keywords - Domaini

    Annexin, Repeat

    Phylogenomic databases

    eggNOGiNOG281174.
    HOGENOMiHOG000158803.
    HOVERGENiHBG061815.
    InParanoidiP08758.
    KOiK16646.
    OMAiVRNIKQV.
    OrthoDBiEOG74XS72.
    PhylomeDBiP08758.
    TreeFamiTF105452.

    Family and domain databases

    Gene3Di1.10.220.10. 4 hits.
    InterProiIPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR015473. Annexins_V.
    IPR002392. AnnexinV.
    [Graphical view]
    PANTHERiPTHR10502:SF26. PTHR10502:SF26. 1 hit.
    PfamiPF00191. Annexin. 4 hits.
    [Graphical view]
    PRINTSiPR00196. ANNEXIN.
    PR00201. ANNEXINV.
    SMARTiSM00335. ANX. 4 hits.
    [Graphical view]
    PROSITEiPS00223. ANNEXIN. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08758-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR    50
    QEISAAFKTL FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL 100
    KGAGTNEKVL TEIIASRTPE ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ 150
    RMLVVLLQAN RDPDAGIDEA QVEQDAQALF QAGELKWGTD EEKFITIFGT 200
    RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV VKSIRSIPAY 250
    LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI 300
    KGDTSGDYKK ALLLLCGEDD 320
    Length:320
    Mass (Da):35,937
    Last modified:January 23, 2007 - v2
    Checksum:i45E14E3964BA4D1A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351S → L in CAG38759. 1 PublicationCurated
    Sequence conflicti279 – 2791I → T in AAH18671. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18366 mRNA. Translation: AAA35570.1.
    D00172 mRNA. Translation: BAA00122.1.
    X12454 mRNA. Translation: CAA30985.1.
    J03745 mRNA. Translation: AAA52386.1.
    M21731 mRNA. Translation: AAA36166.1.
    M19384 mRNA. Translation: AAB59545.1.
    U01691
    , U01681, U01682, U01683, U01685, U01686, U01687, U01689, U01690 Genomic DNA. Translation: AAB40047.1.
    U05770
    , U05760, U05761, U05762, U05764, U05765, U05766, U05767, U05768, U05769 Genomic DNA. Translation: AAB60648.1.
    AK312644 mRNA. Translation: BAG35528.1.
    CR536522 mRNA. Translation: CAG38759.1.
    CR541842 mRNA. Translation: CAG46640.1.
    AC096730 Genomic DNA. Translation: AAY40954.1.
    CH471056 Genomic DNA. Translation: EAX05257.1.
    CH471056 Genomic DNA. Translation: EAX05258.1.
    BC001429 mRNA. Translation: AAH01429.1.
    BC004993 mRNA. Translation: AAH04993.1.
    BC012804 mRNA. Translation: AAH12804.1.
    BC012822 mRNA. Translation: AAH12822.1.
    BC018671 mRNA. Translation: AAH18671.1.
    CCDSiCCDS3720.1.
    PIRiD29250. AQHUP.
    RefSeqiNP_001145.1. NM_001154.3.
    UniGeneiHs.480653.

    Genome annotation databases

    EnsembliENST00000296511; ENSP00000296511; ENSG00000164111.
    GeneIDi308.
    KEGGihsa:308.
    UCSCiuc003idu.4. human.

    Polymorphism databases

    DMDMi113960.

    Cross-referencesi

    Web resourcesi

    R&D Systems' cytokine source book: Annexin V

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18366 mRNA. Translation: AAA35570.1 .
    D00172 mRNA. Translation: BAA00122.1 .
    X12454 mRNA. Translation: CAA30985.1 .
    J03745 mRNA. Translation: AAA52386.1 .
    M21731 mRNA. Translation: AAA36166.1 .
    M19384 mRNA. Translation: AAB59545.1 .
    U01691
    , U01681 , U01682 , U01683 , U01685 , U01686 , U01687 , U01689 , U01690 Genomic DNA. Translation: AAB40047.1 .
    U05770
    , U05760 , U05761 , U05762 , U05764 , U05765 , U05766 , U05767 , U05768 , U05769 Genomic DNA. Translation: AAB60648.1 .
    AK312644 mRNA. Translation: BAG35528.1 .
    CR536522 mRNA. Translation: CAG38759.1 .
    CR541842 mRNA. Translation: CAG46640.1 .
    AC096730 Genomic DNA. Translation: AAY40954.1 .
    CH471056 Genomic DNA. Translation: EAX05257.1 .
    CH471056 Genomic DNA. Translation: EAX05258.1 .
    BC001429 mRNA. Translation: AAH01429.1 .
    BC004993 mRNA. Translation: AAH04993.1 .
    BC012804 mRNA. Translation: AAH12804.1 .
    BC012822 mRNA. Translation: AAH12822.1 .
    BC018671 mRNA. Translation: AAH18671.1 .
    CCDSi CCDS3720.1.
    PIRi D29250. AQHUP.
    RefSeqi NP_001145.1. NM_001154.3.
    UniGenei Hs.480653.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ANW X-ray 2.40 A/B 2-320 [» ]
    1ANX X-ray 1.90 A/B/C 2-320 [» ]
    1AVH X-ray 2.30 A/B 1-320 [» ]
    1AVR X-ray 2.30 A 1-320 [» ]
    1HAK X-ray 3.00 A/B 1-320 [» ]
    1HVD X-ray 2.00 A 2-320 [» ]
    1HVE X-ray 2.30 A 2-320 [» ]
    1HVF X-ray 2.00 A 2-320 [» ]
    1HVG X-ray 3.00 A 2-320 [» ]
    1SAV X-ray 2.50 A 1-320 [» ]
    2XO2 X-ray 2.80 A 1-320 [» ]
    2XO3 X-ray 2.30 A 1-320 [» ]
    ProteinModelPortali P08758.
    SMRi P08758. Positions 3-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106805. 31 interactions.
    IntActi P08758. 16 interactions.
    MINTi MINT-1382250.
    STRINGi 9606.ENSP00000296511.

    PTM databases

    PhosphoSitei P08758.

    Polymorphism databases

    DMDMi 113960.

    2D gel databases

    OGPi P08758.
    REPRODUCTION-2DPAGE IPI00329801.
    P08758.

    Proteomic databases

    MaxQBi P08758.
    PaxDbi P08758.
    PeptideAtlasi P08758.
    PRIDEi P08758.

    Protocols and materials databases

    DNASUi 308.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296511 ; ENSP00000296511 ; ENSG00000164111 .
    GeneIDi 308.
    KEGGi hsa:308.
    UCSCi uc003idu.4. human.

    Organism-specific databases

    CTDi 308.
    GeneCardsi GC04M122589.
    HGNCi HGNC:543. ANXA5.
    HPAi CAB003677.
    HPA035330.
    MIMi 131230. gene.
    614391. phenotype.
    neXtProti NX_P08758.
    PharmGKBi PA24833.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG281174.
    HOGENOMi HOG000158803.
    HOVERGENi HBG061815.
    InParanoidi P08758.
    KOi K16646.
    OMAi VRNIKQV.
    OrthoDBi EOG74XS72.
    PhylomeDBi P08758.
    TreeFami TF105452.

    Enzyme and pathway databases

    SignaLinki P08758.

    Miscellaneous databases

    ChiTaRSi ANXA5. human.
    EvolutionaryTracei P08758.
    GeneWikii Annexin_A5.
    GenomeRNAii 308.
    NextBioi 1243.
    PROi P08758.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08758.
    Bgeei P08758.
    CleanExi HS_ANXA5.
    Genevestigatori P08758.

    Family and domain databases

    Gene3Di 1.10.220.10. 4 hits.
    InterProi IPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR015473. Annexins_V.
    IPR002392. AnnexinV.
    [Graphical view ]
    PANTHERi PTHR10502:SF26. PTHR10502:SF26. 1 hit.
    Pfami PF00191. Annexin. 4 hits.
    [Graphical view ]
    PRINTSi PR00196. ANNEXIN.
    PR00201. ANNEXINV.
    SMARTi SM00335. ANX. 4 hits.
    [Graphical view ]
    PROSITEi PS00223. ANNEXIN. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of human placental anticoagulant protein."
      Funakoshi T., Hendrickson L.E., McMullen B.A., Fujikawa K.
      Biochemistry 26:8087-8092(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structure and expression of cDNA for an inhibitor of blood coagulation isolated from human placenta: a new lipocortin-like protein."
      Iwasaki A., Suda M., Nakao H., Nagoya T., Saino Y., Arai K., Mizoguchi T., Sato F., Yoshizaki H., Hirata M., Miyata T., Shidara Y., Murata M., Maki M.
      J. Biochem. 102:1261-1273(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-320.
    3. "Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+-dependent phospholipid-binding protein."
      Maurer-Fogy I., Reutelingsperger C.P.M., Pieters J., Bodo G., Stratowa C., Hauptmann R.
      Eur. J. Biochem. 174:585-592(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    4. "Cloning and expression of cDNA for human endonexin II, a Ca2+ and phospholipid binding protein."
      Kaplan R., Jaye M., Burgess W.H., Schlaepfer D.D., Haigler H.T.
      J. Biol. Chem. 263:8037-8043(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Five distinct calcium and phospholipid binding proteins share homology with lipocortin I."
      Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T., Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L., Hession C., Frey A.Z., Wallner B.P.
      J. Biol. Chem. 263:10799-10811(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Characterization of cDNA encoding human placental anticoagulant protein (PP4): homology with the lipocortin family."
      Grundmann U., Abel K.-J., Bohn H., Loebermann H., Lottspeich F., Kuepper H.
      Proc. Natl. Acad. Sci. U.S.A. 85:3708-3712(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    7. "The gene encoding human annexin V has a TATA-less promoter with a high G+C content."
      Fernandez M.-P., Morgan R.O., Fernandez M.R., Carcedo M.-T.
      Gene 149:253-260(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Lung.
    8. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    9. "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.
      , 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].
      Tissue: Neuroblastoma.
    10. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    11. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. "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].
      Tissue: Muscle, Ovary and Skin.
    14. "A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulation."
      Rothhut R., Comera C., Cortial S., Haumont P.-Y., Diep Le K.H., Cavadore J.-C., Conard J., Russo-Marie F., Lederer F.
      Biochem. J. 263:929-935(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    15. Quadroni M., Potts A., Barblan J., Bienvenut W.V.
      Submitted (JAN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 7-18; 30-45; 187-201 AND 277-286, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Melanoma.
    16. "Endonexin II, present on human liver plasma membranes, is a specific binding protein of small hepatitis B virus (HBV) envelope protein."
      Hertogs K., Leenders W.P., Depla E., De Bruin W.C., Meheus L., Raymackers J., Moshage H., Yap S.H.
      Virology 197:549-557(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-31; 93-108; 176-188 AND 304-319, INTERACTION WITH HBV.
    17. "Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein."
      Schlaepfer D.D., Mehlman T., Burgess W.H., Haigler H.T.
      Proc. Natl. Acad. Sci. U.S.A. 84:6078-6082(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 86-131; 259-297 AND 300-320.
    18. "Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor."
      Ahn N.G., Teller D.C., Bienkowski M.J., McMullen B.A., Lipkin E.W., de Haen C.
      J. Biol. Chem. 263:18657-18663(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 85-93.
      Tissue: Placenta.
    19. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
      Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
      Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 152-161 AND 246-260.
      Tissue: Adipocyte.
    20. "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
      Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
      Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "A common haplotype of the annexin A5 (ANXA5) gene promoter is associated with recurrent pregnancy loss."
      Bogdanova N., Horst J., Chlystun M., Croucher P.J., Nebel A., Bohring A., Todorova A., Schreiber S., Gerke V., Krawczak M., Markoff A.
      Hum. Mol. Genet. 16:573-578(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN RPRGL3.
    22. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    23. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-76; LYS-79 AND LYS-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes."
      Huber R., Roemisch J., Paques E.-P.
      EMBO J. 9:3867-3874(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    26. "The calcium binding sites in human annexin V by crystal structure analysis at 2.0-A resolution. Implications for membrane binding and calcium channel activity."
      Huber R., Schneider M., Mayr I., Roemisch J., Paques E.-P.
      FEBS Lett. 275:15-21(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    27. "Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins."
      Huber R., Berendes R., Burger A., Schneider M., Karshikov A., Luecke H., Roemisch J., Paques E.-P.
      J. Mol. Biol. 223:683-704(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    28. "Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor."
      Kaneko N., Ago H., Matsuda R., Inagaki E., Miyano M.
      J. Mol. Biol. 274:16-20(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    29. "Residue-specific bioincorporation of non-natural, biologically active amino acids into proteins as possible drug carriers: structure and stability of the per-thiaproline mutant of annexin V."
      Budisa N., Minks C., Medrano F.J., Lutz J., Huber R., Moroder L.
      Proc. Natl. Acad. Sci. U.S.A. 95:455-459(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiANXA5_HUMAN
    AccessioniPrimary (citable) accession number: P08758
    Secondary accession number(s): D3DNW7
    , Q6FHB3, Q6FI16, Q8WV69, Q9UDH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 172 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3