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P07355

- ANXA2_HUMAN

UniProt

P07355 - ANXA2_HUMAN

Protein

Annexin A2

Gene

ANXA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 183 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response.

    GO - Molecular functioni

    1. calcium-dependent phospholipid binding Source: UniProtKB
    2. calcium-dependent protein binding Source: AgBase
    3. calcium ion binding Source: InterPro
    4. phosphatidylinositol-4,5-bisphosphate binding Source: UniProt
    5. phospholipase A2 inhibitor activity Source: UniProt
    6. poly(A) RNA binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. S100 protein binding Source: UniProt

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. body fluid secretion Source: Ensembl
    3. cellular response to acid chemical Source: Ensembl
    4. collagen fibril organization Source: Ensembl
    5. fibrinolysis Source: Ensembl
    6. membrane budding Source: UniProt
    7. membrane raft assembly Source: UniProt
    8. negative regulation of catalytic activity Source: GOC
    9. osteoclast development Source: UniProt
    10. positive regulation of binding Source: Ensembl
    11. positive regulation of fibroblast proliferation Source: Ensembl
    12. positive regulation of protein phosphorylation Source: Ensembl
    13. positive regulation of vesicle fusion Source: UniProtKB
    14. protein heterotetramerization Source: UniProt
    15. protein targeting to plasma membrane Source: Ensembl

    Keywords - Ligandi

    Calcium, Calcium/phospholipid-binding

    Protein family/group databases

    TCDBi1.A.31.1.4. the annexin (annexin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Annexin A2
    Alternative name(s):
    Annexin II
    Annexin-2
    Calpactin I heavy chain
    Calpactin-1 heavy chain
    Chromobindin-8
    Lipocortin II
    Placental anticoagulant protein IV
    Short name:
    PAP-IV
    Protein I
    p36
    Gene namesi
    Name:ANXA2
    Synonyms:ANX2, ANX2L4, CAL1H, LPC2D
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:537. ANXA2.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrixbasement membrane 1 Publication. Melanosome 1 Publication
    Note: In the lamina beneath the plasma membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Translocated from the cytoplasm to the cell surface through a Golgi-independent mechanism.

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB-SubCell
    2. cell cortex Source: Ensembl
    3. cell surface Source: UniProt
    4. early endosome Source: Ensembl
    5. extracellular space Source: UniProt
    6. extracellular vesicular exosome Source: UniProtKB
    7. extrinsic component of plasma membrane Source: Ensembl
    8. late endosome membrane Source: UniProt
    9. lipid particle Source: UniProtKB
    10. lysosomal membrane Source: UniProt
    11. macropinosome Source: Ensembl
    12. melanosome Source: UniProtKB-SubCell
    13. membrane Source: UniProtKB
    14. midbody Source: UniProtKB
    15. myelin sheath adaxonal region Source: Ensembl
    16. nucleus Source: UniProt
    17. perinuclear region of cytoplasm Source: Ensembl
    18. plasma membrane Source: BHF-UCL
    19. protein complex Source: Ensembl
    20. ruffle Source: Ensembl
    21. sarcolemma Source: Ensembl
    22. Schmidt-Lanterman incisure Source: Ensembl
    23. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 241Y → A: Abolishes heat stress-induced cell surface localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA24827.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 339338Annexin A2PRO_0000067470Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei24 – 241Phosphotyrosine; by SRC1 Publication
    Modified residuei26 – 261Phosphoserine; by PKC1 Publication
    Modified residuei49 – 491N6-acetyllysineBy similarity
    Modified residuei152 – 1521N6-acetyllysineBy similarity
    Modified residuei199 – 1991PhosphotyrosineBy similarity
    Modified residuei227 – 2271N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylation of Tyr-24 enhances heat stress-induced translocation to the cell surface.2 Publications
    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP07355.
    PaxDbiP07355.
    PRIDEiP07355.

    2D gel databases

    DOSAC-COBS-2DPAGEP07355.
    REPRODUCTION-2DPAGEIPI00455315.
    P07355.
    UCD-2DPAGEP07355.

    PTM databases

    PhosphoSiteiP07355.

    Expressioni

    Gene expression databases

    ArrayExpressiP07355.
    BgeeiP07355.
    CleanExiHS_ANXA2.
    GenevestigatoriP07355.

    Organism-specific databases

    HPAiCAB004311.
    HPA046964.

    Interactioni

    Subunit structurei

    Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36. Interacts with ATP1B1 and DYSF By similarity. Interacts with human cytomegalovirus (HCMV). Interacts with COCH.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q99IB85EBI-352622,EBI-6927873From a different organism.
    MLH1P406927EBI-352622,EBI-744248
    PCSK9Q8NBP77EBI-352622,EBI-7539251

    Protein-protein interaction databases

    BioGridi106799. 70 interactions.
    IntActiP07355. 31 interactions.
    MINTiMINT-1213203.
    STRINGi9606.ENSP00000346032.

    Structurei

    Secondary structure

    1
    339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 97
    Helixi35 – 4713
    Helixi53 – 608
    Helixi65 – 7915
    Helixi83 – 908
    Helixi93 – 10311
    Helixi106 – 11712
    Beta strandi120 – 1223
    Helixi125 – 13410
    Helixi137 – 15115
    Helixi155 – 1617
    Helixi165 – 17511
    Helixi188 – 20013
    Turni201 – 2044
    Beta strandi205 – 2073
    Helixi210 – 21910
    Helixi222 – 23211
    Turni233 – 2353
    Helixi240 – 2478
    Helixi250 – 26415
    Helixi266 – 27813
    Beta strandi279 – 2824
    Helixi285 – 29511
    Turni296 – 2983
    Helixi300 – 31112
    Helixi315 – 3228
    Helixi325 – 33511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W7BX-ray1.52A1-339[»]
    1XJLX-ray2.59A/B21-339[»]
    2HYUX-ray1.86A32-339[»]
    2HYVX-ray1.42A32-339[»]
    2HYWX-ray2.10A/B32-339[»]
    4DRWX-ray3.50A/B/C/D2-16[»]
    4HRHX-ray3.00A/B2-16[»]
    ProteinModelPortaliP07355.
    SMRiP07355. Positions 32-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07355.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati42 – 10261Annexin 1Add
    BLAST
    Repeati114 – 17461Annexin 2Add
    BLAST
    Repeati199 – 25961Annexin 3Add
    BLAST
    Repeati274 – 33461Annexin 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 2423S100A10-binding siteSequence AnalysisAdd
    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

    eggNOGiNOG259189.
    HOGENOMiHOG000158803.
    HOVERGENiHBG061815.
    InParanoidiP07355.
    KOiK17092.
    OMAiFIQQDTK.
    OrthoDBiEOG74XS72.
    TreeFamiTF105452.

    Family and domain databases

    Gene3Di1.10.220.10. 4 hits.
    InterProiIPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR002389. AnnexinII.
    [Graphical view]
    PANTHERiPTHR10502:SF18. PTHR10502:SF18. 1 hit.
    PfamiPF00191. Annexin. 4 hits.
    [Graphical view]
    PRINTSiPR00196. ANNEXIN.
    PR00198. ANNEXINII.
    SMARTiSM00335. ANX. 4 hits.
    [Graphical view]
    PROSITEiPS00223. ANNEXIN. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P07355-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG    50
    VDEVTIVNIL TNRSNAQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL 100
    GLLKTPAQYD ASELKASMKG LGTDEDSLIE IICSRTNQEL QEINRVYKEM 150
    YKTDLEKDII SDTSGDFRKL MVALAKGRRA EDGSVIDYEL IDQDARDLYD 200
    AGVKRKGTDV PKWISIMTER SVPHLQKVFD RYKSYSPYDM LESIRKEVKG 250
    DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM 300
    LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD 339
    Length:339
    Mass (Da):38,604
    Last modified:January 23, 2007 - v2
    Checksum:i5126E1337A0CBEA1
    GO
    Isoform 2 (identifier: P07355-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGRQLAGCGDAGKKASFKM

    Show »
    Length:357
    Mass (Da):40,411
    Checksum:i2AA081CB4E7AC75C
    GO

    Sequence cautioni

    The sequence AAH66955.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291A → P AA sequence (PubMed:8110754)Curated
    Sequence conflicti166 – 1661D → G in CAE45704. (PubMed:17974005)Curated
    Sequence conflicti293 – 2931V → A in AAH23990. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti98 – 981V → L.1 Publication
    Corresponds to variant rs17845226 [ dbSNP | Ensembl ].
    VAR_012982

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGRQLAGCGDAGKKASFKM in isoform 2. 1 PublicationVSP_038091

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00017 mRNA. Translation: BAA00013.1.
    BT007432 mRNA. Translation: AAP36100.1.
    BX640598 mRNA. Translation: CAE45704.1.
    AC087385 Genomic DNA. No translation available.
    BC001388 mRNA. Translation: AAH01388.1.
    BC009564 mRNA. Translation: AAH09564.1.
    BC015834 mRNA. Translation: AAH15834.1.
    BC016774 mRNA. Translation: AAH16774.1.
    BC021114 mRNA. Translation: AAH21114.1.
    BC023990 mRNA. Translation: AAH23990.1.
    BC052558 mRNA. Translation: AAH52558.1.
    BC052567 mRNA. Translation: AAH52567.1.
    BC066955 mRNA. Translation: AAH66955.2. Different initiation.
    BC068065 mRNA. Translation: AAH68065.1.
    BC093056 mRNA. Translation: AAH93056.1.
    CCDSiCCDS10175.1. [P07355-1]
    CCDS32256.1. [P07355-2]
    PIRiA23942. LUHU36.
    RefSeqiNP_001002857.1. NM_001002857.1. [P07355-1]
    NP_001002858.1. NM_001002858.2. [P07355-2]
    NP_001129487.1. NM_001136015.2. [P07355-1]
    NP_004030.1. NM_004039.2. [P07355-1]
    UniGeneiHs.511605.

    Genome annotation databases

    EnsembliENST00000332680; ENSP00000346032; ENSG00000182718. [P07355-2]
    ENST00000396024; ENSP00000379342; ENSG00000182718. [P07355-1]
    ENST00000421017; ENSP00000411352; ENSG00000182718. [P07355-1]
    ENST00000451270; ENSP00000387545; ENSG00000182718. [P07355-1]
    GeneIDi302.
    KEGGihsa:302.
    UCSCiuc002agk.3. human. [P07355-1]
    uc002agm.3. human. [P07355-2]

    Polymorphism databases

    DMDMi113950.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Red velvet - Issue 86 of September 2007

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00017 mRNA. Translation: BAA00013.1 .
    BT007432 mRNA. Translation: AAP36100.1 .
    BX640598 mRNA. Translation: CAE45704.1 .
    AC087385 Genomic DNA. No translation available.
    BC001388 mRNA. Translation: AAH01388.1 .
    BC009564 mRNA. Translation: AAH09564.1 .
    BC015834 mRNA. Translation: AAH15834.1 .
    BC016774 mRNA. Translation: AAH16774.1 .
    BC021114 mRNA. Translation: AAH21114.1 .
    BC023990 mRNA. Translation: AAH23990.1 .
    BC052558 mRNA. Translation: AAH52558.1 .
    BC052567 mRNA. Translation: AAH52567.1 .
    BC066955 mRNA. Translation: AAH66955.2 . Different initiation.
    BC068065 mRNA. Translation: AAH68065.1 .
    BC093056 mRNA. Translation: AAH93056.1 .
    CCDSi CCDS10175.1. [P07355-1 ]
    CCDS32256.1. [P07355-2 ]
    PIRi A23942. LUHU36.
    RefSeqi NP_001002857.1. NM_001002857.1. [P07355-1 ]
    NP_001002858.1. NM_001002858.2. [P07355-2 ]
    NP_001129487.1. NM_001136015.2. [P07355-1 ]
    NP_004030.1. NM_004039.2. [P07355-1 ]
    UniGenei Hs.511605.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W7B X-ray 1.52 A 1-339 [» ]
    1XJL X-ray 2.59 A/B 21-339 [» ]
    2HYU X-ray 1.86 A 32-339 [» ]
    2HYV X-ray 1.42 A 32-339 [» ]
    2HYW X-ray 2.10 A/B 32-339 [» ]
    4DRW X-ray 3.50 A/B/C/D 2-16 [» ]
    4HRH X-ray 3.00 A/B 2-16 [» ]
    ProteinModelPortali P07355.
    SMRi P07355. Positions 32-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106799. 70 interactions.
    IntActi P07355. 31 interactions.
    MINTi MINT-1213203.
    STRINGi 9606.ENSP00000346032.

    Chemistry

    BindingDBi P07355.
    ChEMBLi CHEMBL2111435.
    DrugBanki DB00031. Tenecteplase.

    Protein family/group databases

    TCDBi 1.A.31.1.4. the annexin (annexin) family.

    PTM databases

    PhosphoSitei P07355.

    Polymorphism databases

    DMDMi 113950.

    2D gel databases

    DOSAC-COBS-2DPAGE P07355.
    REPRODUCTION-2DPAGE IPI00455315.
    P07355.
    UCD-2DPAGE P07355.

    Proteomic databases

    MaxQBi P07355.
    PaxDbi P07355.
    PRIDEi P07355.

    Protocols and materials databases

    DNASUi 302.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332680 ; ENSP00000346032 ; ENSG00000182718 . [P07355-2 ]
    ENST00000396024 ; ENSP00000379342 ; ENSG00000182718 . [P07355-1 ]
    ENST00000421017 ; ENSP00000411352 ; ENSG00000182718 . [P07355-1 ]
    ENST00000451270 ; ENSP00000387545 ; ENSG00000182718 . [P07355-1 ]
    GeneIDi 302.
    KEGGi hsa:302.
    UCSCi uc002agk.3. human. [P07355-1 ]
    uc002agm.3. human. [P07355-2 ]

    Organism-specific databases

    CTDi 302.
    GeneCardsi GC15M060639.
    HGNCi HGNC:537. ANXA2.
    HPAi CAB004311.
    HPA046964.
    MIMi 151740. gene.
    neXtProti NX_P07355.
    PharmGKBi PA24827.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259189.
    HOGENOMi HOG000158803.
    HOVERGENi HBG061815.
    InParanoidi P07355.
    KOi K17092.
    OMAi FIQQDTK.
    OrthoDBi EOG74XS72.
    TreeFami TF105452.

    Miscellaneous databases

    ChiTaRSi ANXA2. human.
    EvolutionaryTracei P07355.
    GeneWikii Annexin_A2.
    GenomeRNAii 302.
    NextBioi 1217.
    PROi P07355.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07355.
    Bgeei P07355.
    CleanExi HS_ANXA2.
    Genevestigatori P07355.

    Family and domain databases

    Gene3Di 1.10.220.10. 4 hits.
    InterProi IPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR002389. AnnexinII.
    [Graphical view ]
    PANTHERi PTHR10502:SF18. PTHR10502:SF18. 1 hit.
    Pfami PF00191. Annexin. 4 hits.
    [Graphical view ]
    PRINTSi PR00196. ANNEXIN.
    PR00198. ANNEXINII.
    SMARTi SM00335. ANX. 4 hits.
    [Graphical view ]
    PROSITEi PS00223. ANNEXIN. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase."
      Huang K.-S., Wallner B.P., Mattaliano R.J., Tizard R., Burne C., Frey A., Hession C., McGray P., Sinclair L.K., Chow E.P., Browning J.L., Ramachandran K.L., Tang J., Smart J.E., Pepinsky R.B.
      Cell 46:191-199(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication."
      Spano F., Raugei G., Palla E., Colella C., Melli M.
      Gene 95:243-251(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Colon endothelium.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1), VARIANT LEU-98.
      Tissue: Brain, Colon, Pancreas, Prostate, Skin, Testis and Urinary bladder.
    7. Cited for: PROTEIN SEQUENCE OF 2-10; 38-47; 50-63; 69-77; 89-115; 153-169 AND 213-220, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon adenocarcinoma and Osteosarcoma.
    8. "The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha."
      Jindal H.K., Chaney W.G., Anderson C.W., Davis R.G., Vishwanatha J.K.
      J. Biol. Chem. 266:5169-5176(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 11-27; 49-62; 68-77; 120-135; 314-323 AND 329-339.
    9. "Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells."
      Hyatt S.L., Liao L., Chapline C., Jaken S.
      Biochemistry 33:1223-1228(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 15-40 AND 50-63.
    10. "An endothelial cell-surface form of annexin II binds human cytomegalovirus."
      Wright J.F., Kurosky A., Wasi S.
      Biochem. Biophys. Res. Commun. 198:983-989(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-37; 119-126; 172-191 AND 301-307, INTERACTION WITH HCMV.
      Tissue: Umbilical vein endothelial cell.
    11. "Annexin II is a major component of fusogenic endosomal vesicles."
      Emans N., Gorvel J.P., Walter C., Gerke V., Kellner R., Griffiths G., Gruenberg J.
      J. Cell Biol. 120:1357-1369(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 234-241 AND 252-261.
    12. "The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo."
      Gould K.L., Woodgett J.R., Isacke C.M., Hunter T.
      Mol. Cell. Biol. 6:2738-2744(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-26.
    13. "An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface."
      Deora A.B., Kreitzer G., Jacovina A.T., Hajjar K.A.
      J. Biol. Chem. 279:43411-43418(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-24, MUTAGENESIS OF TYR-24.
    14. Cited for: ISGYLATION.
    15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Cochlin induced TREK-1 co-expression and annexin A2 secretion: role in trabecular meshwork cell elongation and motility."
      Goel M., Sienkiewicz A.E., Picciani R., Lee R.K., Bhattacharya S.K.
      PLoS ONE 6:E23070-E23070(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COCH.
    18. "The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein."
      Burger A., Berendes R., Liemann S., Benz J., Hofmann A., Goettig P., Huber R., Gerke V., Tiel C., Roemisch J., Weber K.
      J. Mol. Biol. 257:839-847(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiANXA2_HUMAN
    AccessioniPrimary (citable) accession number: P07355
    Secondary accession number(s): Q567R4
    , Q6N0B3, Q8TBV2, Q96DD5, Q9UDH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 183 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

    Miscellaneous

    It may cross-link plasma membrane phospholipids with actin and the cytoskeleton and be involved with exocytosis.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3