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P08133

- ANXA6_HUMAN

UniProt

P08133 - ANXA6_HUMAN

Protein

Annexin A6

Gene

ANXA6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    May associate with CD21. May regulate the release of Ca2+ from intracellular stores.

    GO - Molecular functioni

    1. calcium-dependent phospholipid binding Source: UniProtKB
    2. calcium-dependent protein binding Source: AgBase
    3. calcium ion binding Source: InterPro
    4. cholesterol binding Source: UniProt
    5. GTP binding Source: UniProt
    6. ligand-gated ion channel activity Source: UniProt
    7. lipid binding Source: UniProt
    8. protein binding Source: UniProtKB
    9. protein homodimerization activity Source: UniProt

    GO - Biological processi

    1. calcium ion transport Source: Ensembl
    2. ion transmembrane transport Source: UniProt
    3. protein homooligomerization Source: UniProt
    4. regulation of muscle contraction Source: Ensembl

    Keywords - Ligandi

    Calcium, Calcium/phospholipid-binding

    Protein family/group databases

    TCDBi1.A.31.1.2. the annexin (annexin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Annexin A6
    Alternative name(s):
    67 kDa calelectrin
    Annexin VI
    Annexin-6
    Calphobindin-II
    Short name:
    CPB-II
    Chromobindin-20
    Lipocortin VI
    Protein III
    p68
    p70
    Gene namesi
    Name:ANXA6
    Synonyms:ANX6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:544. ANXA6.

    Subcellular locationi

    Cytoplasm By similarity. Melanosome 1 Publication
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProtKB
    2. late endosome membrane Source: UniProt
    3. lysosomal membrane Source: UniProt
    4. melanosome Source: UniProtKB-SubCell
    5. membrane Source: UniProtKB
    6. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24834.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 673672Annexin A6PRO_0000067494Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei30 – 301Phosphotyrosine1 Publication
    Modified residuei63 – 631N6-acetyllysine1 Publication
    Modified residuei68 – 681N6-acetyllysine1 Publication
    Modified residuei75 – 751N6-acetyllysine1 Publication
    Modified residuei81 – 811N6-acetyllysine1 Publication
    Modified residuei201 – 2011PhosphotyrosineBy similarity
    Modified residuei306 – 3061N6-acetyllysine1 Publication
    Modified residuei370 – 3701N6-acetyllysine1 Publication
    Modified residuei418 – 4181N6-acetyllysine1 Publication
    Modified residuei483 – 4831N6-acetyllysine1 Publication
    Modified residuei620 – 6201N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated in response to growth factor stimulation.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP08133.
    PaxDbiP08133.
    PRIDEiP08133.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00221226.
    UCD-2DPAGEP08133.

    PTM databases

    PhosphoSiteiP08133.

    Expressioni

    Inductioni

    By Epstein-Barr virus (EBV).

    Gene expression databases

    ArrayExpressiP08133.
    BgeeiP08133.
    CleanExiHS_ANXA6.
    GenevestigatoriP08133.

    Organism-specific databases

    HPAiCAB005077.
    HPA002462.
    HPA009650.

    Interactioni

    Protein-protein interaction databases

    BioGridi106806. 28 interactions.
    IntActiP08133. 10 interactions.
    MINTiMINT-4999263.
    STRINGi9606.ENSP00000346550.

    Structurei

    Secondary structure

    1
    673
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 3211
    Beta strandi34 – 374
    Helixi40 – 478
    Helixi52 – 6615
    Helixi70 – 778
    Helixi80 – 9011
    Helixi93 – 10513
    Beta strandi106 – 1094
    Helixi112 – 12110
    Helixi124 – 13714
    Helixi142 – 1498
    Helixi152 – 16312
    Helixi174 – 18714
    Turni188 – 1903
    Beta strandi191 – 1933
    Helixi196 – 20510
    Helixi208 – 22114
    Beta strandi222 – 2243
    Helixi226 – 2305
    Turni231 – 2333
    Helixi236 – 26227
    Beta strandi264 – 2685
    Helixi271 – 28010
    Turni281 – 2855
    Helixi286 – 29611
    Beta strandi297 – 2993
    Helixi301 – 3066
    Helixi311 – 32111
    Helixi333 – 34816
    Helixi365 – 37612
    Beta strandi377 – 3804
    Helixi383 – 3919
    Helixi395 – 40915
    Helixi413 – 4208
    Helixi424 – 43310
    Helixi436 – 44813
    Beta strandi449 – 4524
    Helixi455 – 46410
    Helixi467 – 48115
    Helixi485 – 4928
    Helixi495 – 50410
    Helixi516 – 53015
    Helixi535 – 5373
    Helixi546 – 5538
    Helixi556 – 56813
    Beta strandi569 – 5724
    Helixi574 – 5818
    Helixi584 – 61128
    Beta strandi613 – 6164
    Helixi619 – 62810
    Turni630 – 6334
    Helixi634 – 64512
    Helixi649 – 6568
    Helixi659 – 66810

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M9IX-ray2.65A2-673[»]
    ProteinModelPortaliP08133.
    SMRiP08133. Positions 10-673.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08133.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati29 – 8961Annexin 1Add
    BLAST
    Repeati101 – 16161Annexin 2Add
    BLAST
    Repeati185 – 24561Annexin 3Add
    BLAST
    Repeati260 – 32061Annexin 4Add
    BLAST
    Repeati372 – 43261Annexin 5Add
    BLAST
    Repeati444 – 50461Annexin 6Add
    BLAST
    Repeati533 – 59361Annexin 7Add
    BLAST
    Repeati608 – 66861Annexin 8Add
    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 8 annexin repeats.Curated

    Keywords - Domaini

    Annexin, Repeat

    Phylogenomic databases

    eggNOGiNOG267770.
    HOGENOMiHOG000158803.
    HOVERGENiHBG061815.
    InParanoidiP08133.
    KOiK17094.
    OMAiEKSLYSM.
    OrthoDBiEOG74XS72.
    PhylomeDBiP08133.
    TreeFamiTF105452.

    Family and domain databases

    Gene3Di1.10.220.10. 8 hits.
    InterProiIPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR002393. AnnexinVI.
    [Graphical view]
    PfamiPF00191. Annexin. 8 hits.
    [Graphical view]
    PRINTSiPR00196. ANNEXIN.
    PR00202. ANNEXINVI.
    SMARTiSM00335. ANX. 8 hits.
    [Graphical view]
    PROSITEiPS00223. ANNEXIN. 8 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: P08133-1) [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

    MAKPAQGAKY RGSIHDFPGF DPNQDAEALY TAMKGFGSDK EAILDIITSR    50
    SNRQRQEVCQ SYKSLYGKDL IADLKYELTG KFERLIVGLM RPPAYCDAKE 100
    IKDAISGIGT DEKCLIEILA SRTNEQMHQL VAAYKDAYER DLEADIIGDT 150
    SGHFQKMLVV LLQGTREEDD VVSEDLVQQD VQDLYEAGEL KWGTDEAQFI 200
    YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK LMLAVVKCIR 250
    STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS 300
    LYSMIKNDTS GEYKKTLLKL SGGDDDAAGQ FFPEAAQVAY QMWELSAVAR 350
    VELKGTVRPA NDFNPDADAK ALRKAMKGLG TDEDTIIDII THRSNVQRQQ 400
    IRQTFKSHFG RDLMTDLKSE ISGDLARLIL GLMMPPAHYD AKQLKKAMEG 450
    AGTDEKALIE ILATRTNAEI RAINEAYKED YHKSLEDALS SDTSGHFRRI 500
    LISLATGHRE EGGENLDQAR EDAQVAAEIL EIADTPSGDK TSLETRFMTI 550
    LCTRSYPHLR RVFQEFIKMT NYDVEHTIKK EMSGDVRDAF VAIVQSVKNK 600
    PLFFADKLYK SMKGAGTDEK TLTRIMVSRS EIDLLNIRRE FIEKYDKSLH 650
    QAIEGDTSGD FLKALLALCG GED 673
    Length:673
    Mass (Da):75,873
    Last modified:January 23, 2007 - v3
    Checksum:i90F47474F7F6D7B6
    GO
    Isoform 2 (identifier: P08133-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-32: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:641
    Mass (Da):72,423
    Checksum:i61E3E5CAF66A51E3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti221 – 2211T → A in BAH13893. (PubMed:14702039)Curated
    Sequence conflicti226 – 2272IE → MK in AAA35656. (PubMed:2963335)Curated
    Sequence conflicti248 – 2481C → R in BAC86715. (PubMed:14702039)Curated
    Sequence conflicti555 – 5551S → T in AAA35656. (PubMed:2963335)Curated
    Sequence conflicti619 – 6191E → D in CAA68286. (PubMed:3258820)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3232Missing in isoform 2. 1 PublicationVSP_045480Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00097 mRNA. Translation: CAA68286.1.
    J03578 mRNA. Translation: AAA35656.1.
    D00510 mRNA. Translation: BAA00400.1.
    AK126836 mRNA. Translation: BAC86715.1. Sequence problems.
    AK303078 mRNA. Translation: BAH13893.1.
    AC008641 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61684.1.
    CH471062 Genomic DNA. Translation: EAW61686.1.
    BC017046 mRNA. Translation: AAH17046.1.
    CCDSiCCDS47315.1. [P08133-1]
    CCDS54941.1. [P08133-2]
    PIRiJU0032. AQHU68.
    RefSeqiNP_001146.2. NM_001155.4. [P08133-1]
    NP_001180473.1. NM_001193544.1. [P08133-2]
    UniGeneiHs.412117.

    Genome annotation databases

    EnsembliENST00000354546; ENSP00000346550; ENSG00000197043. [P08133-1]
    ENST00000523714; ENSP00000430517; ENSG00000197043. [P08133-2]
    GeneIDi309.
    KEGGihsa:309.
    UCSCiuc003ltl.2. human. [P08133-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00097 mRNA. Translation: CAA68286.1 .
    J03578 mRNA. Translation: AAA35656.1 .
    D00510 mRNA. Translation: BAA00400.1 .
    AK126836 mRNA. Translation: BAC86715.1 . Sequence problems.
    AK303078 mRNA. Translation: BAH13893.1 .
    AC008641 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61684.1 .
    CH471062 Genomic DNA. Translation: EAW61686.1 .
    BC017046 mRNA. Translation: AAH17046.1 .
    CCDSi CCDS47315.1. [P08133-1 ]
    CCDS54941.1. [P08133-2 ]
    PIRi JU0032. AQHU68.
    RefSeqi NP_001146.2. NM_001155.4. [P08133-1 ]
    NP_001180473.1. NM_001193544.1. [P08133-2 ]
    UniGenei Hs.412117.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M9I X-ray 2.65 A 2-673 [» ]
    ProteinModelPortali P08133.
    SMRi P08133. Positions 10-673.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106806. 28 interactions.
    IntActi P08133. 10 interactions.
    MINTi MINT-4999263.
    STRINGi 9606.ENSP00000346550.

    Protein family/group databases

    TCDBi 1.A.31.1.2. the annexin (annexin) family.

    PTM databases

    PhosphoSitei P08133.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00221226.
    UCD-2DPAGE P08133.

    Proteomic databases

    MaxQBi P08133.
    PaxDbi P08133.
    PRIDEi P08133.

    Protocols and materials databases

    DNASUi 309.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354546 ; ENSP00000346550 ; ENSG00000197043 . [P08133-1 ]
    ENST00000523714 ; ENSP00000430517 ; ENSG00000197043 . [P08133-2 ]
    GeneIDi 309.
    KEGGi hsa:309.
    UCSCi uc003ltl.2. human. [P08133-1 ]

    Organism-specific databases

    CTDi 309.
    GeneCardsi GC05M150460.
    HGNCi HGNC:544. ANXA6.
    HPAi CAB005077.
    HPA002462.
    HPA009650.
    MIMi 114070. gene.
    neXtProti NX_P08133.
    PharmGKBi PA24834.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG267770.
    HOGENOMi HOG000158803.
    HOVERGENi HBG061815.
    InParanoidi P08133.
    KOi K17094.
    OMAi EKSLYSM.
    OrthoDBi EOG74XS72.
    PhylomeDBi P08133.
    TreeFami TF105452.

    Miscellaneous databases

    ChiTaRSi ANXA6. human.
    EvolutionaryTracei P08133.
    GeneWikii ANXA6.
    GenomeRNAii 309.
    NextBioi 1247.
    PROi P08133.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08133.
    Bgeei P08133.
    CleanExi HS_ANXA6.
    Genevestigatori P08133.

    Family and domain databases

    Gene3Di 1.10.220.10. 8 hits.
    InterProi IPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR002393. AnnexinVI.
    [Graphical view ]
    Pfami PF00191. Annexin. 8 hits.
    [Graphical view ]
    PRINTSi PR00196. ANNEXIN.
    PR00202. ANNEXINVI.
    SMARTi SM00335. ANX. 8 hits.
    [Graphical view ]
    PROSITEi PS00223. ANNEXIN. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the human, membrane-associated Ca2+-binding protein p68 a novel member of a protein family."
      Crompton M.R., Owens R.J., Totty N.F., Moss S.E., Waterfield M.D., Crumpton M.J.
      EMBO J. 7:21-27(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Human 67-kDa calelectrin contains a duplication of four repeats found in 35-kDa lipocortins."
      Suedhof T.C., Slaughter C.A., Leznicki I., Barjon P., Reynolds G.A.
      Proc. Natl. Acad. Sci. U.S.A. 85:664-668(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    3. "Structure and expression of cDNA for calphobindin II, a human placental coagulation inhibitor."
      Iwasaki A., Suda M., Watanabe M., Nakao H., Hattori Y., Nagoya T., Saino Y., Shidara Y., Maki M.
      J. Biochem. 106:43-49(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Amygdala and Thymus.
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
      Tissue: Uterus.
    8. "Structure and properties of calphobindin II, an anticoagulant protein from human placenta."
      Yoshizaki H., Mizoguchi T., Arai K., Shiratsuchi M., Shidara Y., Maki M.
      J. Biochem. 107:43-50(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-673.
    9. "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 485-499.
      Tissue: Adipocyte.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-63; LYS-68; LYS-75; LYS-81; LYS-306; LYS-370; LYS-418; LYS-483 AND LYS-620, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. "The structure of recombinant human annexin VI in crystals and membrane-bound."
      Benz J., Bergner A., Hofmann A., Demange P., Goettig P., Liemann S., Huber R., Voges D.
      J. Mol. Biol. 260:638-643(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).

    Entry informationi

    Entry nameiANXA6_HUMAN
    AccessioniPrimary (citable) accession number: P08133
    Secondary accession number(s): B7Z8A7
    , D3DQH4, E9PGK1, Q6ZT79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 165 of the entry and version 3 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

    Seems to bind one calcium ion with high affinity.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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