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O75340

- PDCD6_HUMAN

UniProt

O75340 - PDCD6_HUMAN

Protein

Programmed cell death protein 6

Gene

PDCD6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Calcium-binding protein required for T-cell receptor-, Fas-, and glucocorticoid-induced cell death. May mediate Ca2+-regulated signals along the death pathway By similarity. Calcium-dependent adapter necessary for the association between PDCD6IP and TSG101. Interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity. May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphoprylation of the Akt signaling pathway. Seems to play a role in the regulation of the distribution and function of MCOLN1 in the endosomal pathway. Isoform 2 has a lower Ca2+ affinity than isoform 1. Isoform 1 and, to a lesser extend, isoform 2, can stabilize SHISA5.By similarity5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi36 – 47121Add
    BLAST
    Calcium bindingi73 – 84122PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi103 – 114123Add
    BLAST
    Calcium bindingi169 – 181134Add
    BLAST

    GO - Molecular functioni

    1. binding, bridging Source: UniProtKB
    2. calcium-dependent cysteine-type endopeptidase activity Source: RefGenome
    3. calcium-dependent protein binding Source: UniProtKB
    4. calcium ion binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein dimerization activity Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    2. angiogenesis Source: UniProtKB-KW
    3. apoptotic signaling pathway Source: ProtInc
    4. cellular response to heat Source: UniProtKB
    5. intracellular protein transport Source: UniProtKB
    6. negative regulation of protein kinase B signaling Source: UniProtKB
    7. negative regulation of TOR signaling Source: UniProtKB
    8. negative regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
    9. positive regulation of angiogenesis Source: UniProtKB
    10. positive regulation of endothelial cell migration Source: UniProtKB
    11. positive regulation of endothelial cell proliferation Source: UniProtKB
    12. proteolysis Source: RefGenome
    13. response to calcium ion Source: UniProtKB
    14. vascular endothelial growth factor receptor-2 signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Angiogenesis, Apoptosis

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Programmed cell death protein 6
    Alternative name(s):
    Apoptosis-linked gene 2 protein
    Probable calcium-binding protein ALG-2
    Gene namesi
    Name:PDCD6
    Synonyms:ALG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:8765. PDCD6.

    Subcellular locationi

    Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Nucleus. Endosome
    Note: Interaction with RBM22 induces relocalization from the cytoplasm to the nucleus. Translocated from the cytoplasm to the nucleus after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic vesicle Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB
    4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    5. endosome Source: UniProtKB-SubCell
    6. extracellular vesicular exosome Source: UniProt
    7. nuclear membrane Source: UniProtKB-SubCell
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi47 – 471E → A: Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-114. 2 Publications
    Mutagenesisi57 – 571W → A: Reduces the interaction with PDCD6IP and ANXA7. 1 Publication
    Mutagenesisi60 – 601F → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. 1 Publication
    Mutagenesisi91 – 911Y → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. 1 Publication
    Mutagenesisi95 – 951W → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. 1 Publication
    Mutagenesisi114 – 1141E → A: Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-47. 2 Publications
    Mutagenesisi122 – 1221F → A: Increases interaction with PDCD6IP and ANXA7. Impairs interaction with ANXA11. Augments stauroporine-induced cell death. 1 Publication
    Mutagenesisi122 – 1221F → G: Increases interaction with PDCD6IP. Impairs interaction with ANXA11. 1 Publication
    Mutagenesisi122 – 1221F → S: Increases interaction with PDCD6IP. Impairs interaction with ANAX7 and ANXA11. 1 Publication
    Mutagenesisi122 – 1221F → W: Impairs interaction with ANXA11. 1 Publication
    Mutagenesisi180 – 1801Y → A: Abolishes the interaction with PDCD6IP, TSG101, ANXA7 and ANXA11. 1 Publication

    Organism-specific databases

    PharmGKBiPA33115.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 191190Programmed cell death protein 6PRO_0000073729Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO75340.
    PRIDEiO75340.

    PTM databases

    PhosphoSiteiO75340.

    Expressioni

    Gene expression databases

    ArrayExpressiO75340.
    BgeeiO75340.
    CleanExiHS_ALG2.
    HS_PDCD6.
    GenevestigatoriO75340.

    Organism-specific databases

    HPAiHPA047221.

    Interactioni

    Subunit structurei

    Isoform 1 and isoform 2 self-associate; probably forming homodimers. Interacts with SHISA5, PEF1, RBM22, PLSCR4, ANXA7, TSG101 and DAPK1. Interacts with PDCD6IP, SEC31A, ANXA11 (via N-terminus), PLSCR3 (via N-terminus) and MCOLN1; the interactions are calcium-dependent. Isoform 2 does not interact with SHISA5, PDCD6IP, TSG101, ANXA7 and ANXA11.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DAPK1P533553EBI-352915,EBI-358616
    KDRP359684EBI-352915,EBI-1005487
    PDCD6IPQ8WUM45EBI-352915,EBI-310624
    PLSCR3Q9NRY69EBI-352915,EBI-750734
    PTPN23Q9H3S73EBI-352915,EBI-724478
    SEC31AO949796EBI-352915,EBI-1767898

    Protein-protein interaction databases

    BioGridi115333. 35 interactions.
    DIPiDIP-33217N.
    IntActiO75340. 30 interactions.
    MINTiMINT-5000341.
    STRINGi9606.ENSP00000323816.

    Structurei

    Secondary structure

    1
    191
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 3510
    Beta strandi36 – 405
    Beta strandi41 – 433
    Helixi45 – 517
    Beta strandi55 – 584
    Helixi62 – 7211
    Beta strandi74 – 807
    Helixi82 – 10221
    Beta strandi107 – 1104
    Helixi112 – 12110
    Helixi128 – 13811
    Beta strandi143 – 1475
    Helixi148 – 16821
    Beta strandi172 – 1743
    Helixi180 – 1889

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZN8X-ray2.70A2-191[»]
    2ZN9X-ray2.40A/B20-191[»]
    2ZNDX-ray1.70A20-191[»]
    2ZNEX-ray2.20A/B24-191[»]
    2ZRSX-ray3.10A/B/C/D/E/F/G/H24-191[»]
    2ZRTX-ray3.30A/B/C/D/E/F/G/H24-191[»]
    3AAJX-ray2.40A/B24-191[»]
    3AAKX-ray2.70A20-191[»]
    ProteinModelPortaliO75340.
    SMRiO75340. Positions 24-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75340.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 5836EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini59 – 8931EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini90 – 12536EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini126 – 16136EF-hand 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini162 – 19130EF-hand 5PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 5 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    HOGENOMiHOG000231984.
    HOVERGENiHBG004492.
    OMAiFLWNIFQ.
    OrthoDBiEOG7RV9FM.
    PhylomeDBiO75340.
    TreeFamiTF314682.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF13499. EF-hand_7. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 5 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75340-1) [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

    MAAYSYRPGP GAGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDTELQQ    50
    ALSNGTWTPF NPVTVRSIIS MFDRENKAGV NFSEFTGVWK YITDWQNVFR 100
    TYDRDNSGMI DKNELKQALS GFGYRLSDQF HDILIRKFDR QGRGQIAFDD 150
    FIQGCIVLQR LTDIFRRYDT DQDGWIQVSY EQYLSMVFSI V 191
    Length:191
    Mass (Da):21,868
    Last modified:November 1, 1998 - v1
    Checksum:iD0B5944CF3C696AD
    GO
    Isoform 2 (identifier: O75340-2) [UniParc]FASTAAdd to Basket

    Also known as: ALG-2(delta)GF122

    The sequence of this isoform differs from the canonical sequence as follows:
         121-122: Missing.

    Show »
    Length:189
    Mass (Da):21,664
    Checksum:i8F93724C044DD93A
    GO
    Isoform 3 (identifier: O75340-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         70-191: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:69
    Mass (Da):7,349
    Checksum:i8410709B76C52B47
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti123 – 1231G → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035459

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei70 – 191122Missing in isoform 3. 1 PublicationVSP_045542Add
    BLAST
    Alternative sequencei121 – 1222Missing in isoform 2. 1 PublicationVSP_045113

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035606 mRNA. Translation: AAC27697.1.
    U58773 mRNA. Translation: AAF14336.1.
    AK315370 mRNA. Translation: BAG37763.1.
    BT020072 mRNA. Translation: AAV38875.1.
    AC010442 Genomic DNA. No translation available.
    AC021087 Genomic DNA. No translation available.
    AC118458 Genomic DNA. No translation available.
    CH471235 Genomic DNA. Translation: EAW50991.1.
    BC012384 mRNA. Translation: AAH12384.1.
    BC106706 mRNA. Translation: AAI06707.1.
    BC110291 mRNA. Translation: AAI10292.1.
    CB991882 mRNA. No translation available.
    CCDSiCCDS3854.1. [O75340-1]
    CCDS58940.1. [O75340-2]
    CCDS58941.1. [O75340-3]
    RefSeqiNP_001254485.1. NM_001267556.1. [O75340-2]
    NP_001254486.1. NM_001267557.1.
    NP_001254487.1. NM_001267558.1.
    NP_001254488.1. NM_001267559.1. [O75340-3]
    NP_037364.1. NM_013232.3. [O75340-1]
    UniGeneiHs.50823.

    Genome annotation databases

    EnsembliENST00000264933; ENSP00000264933; ENSG00000249915. [O75340-1]
    ENST00000505221; ENSP00000422085; ENSG00000249915. [O75340-3]
    ENST00000507528; ENSP00000423815; ENSG00000249915. [O75340-2]
    GeneIDi10016.
    KEGGihsa:10016.
    UCSCiuc003jat.1. human. [O75340-1]
    uc003jau.2. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035606 mRNA. Translation: AAC27697.1 .
    U58773 mRNA. Translation: AAF14336.1 .
    AK315370 mRNA. Translation: BAG37763.1 .
    BT020072 mRNA. Translation: AAV38875.1 .
    AC010442 Genomic DNA. No translation available.
    AC021087 Genomic DNA. No translation available.
    AC118458 Genomic DNA. No translation available.
    CH471235 Genomic DNA. Translation: EAW50991.1 .
    BC012384 mRNA. Translation: AAH12384.1 .
    BC106706 mRNA. Translation: AAI06707.1 .
    BC110291 mRNA. Translation: AAI10292.1 .
    CB991882 mRNA. No translation available.
    CCDSi CCDS3854.1. [O75340-1 ]
    CCDS58940.1. [O75340-2 ]
    CCDS58941.1. [O75340-3 ]
    RefSeqi NP_001254485.1. NM_001267556.1. [O75340-2 ]
    NP_001254486.1. NM_001267557.1.
    NP_001254487.1. NM_001267558.1.
    NP_001254488.1. NM_001267559.1. [O75340-3 ]
    NP_037364.1. NM_013232.3. [O75340-1 ]
    UniGenei Hs.50823.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZN8 X-ray 2.70 A 2-191 [» ]
    2ZN9 X-ray 2.40 A/B 20-191 [» ]
    2ZND X-ray 1.70 A 20-191 [» ]
    2ZNE X-ray 2.20 A/B 24-191 [» ]
    2ZRS X-ray 3.10 A/B/C/D/E/F/G/H 24-191 [» ]
    2ZRT X-ray 3.30 A/B/C/D/E/F/G/H 24-191 [» ]
    3AAJ X-ray 2.40 A/B 24-191 [» ]
    3AAK X-ray 2.70 A 20-191 [» ]
    ProteinModelPortali O75340.
    SMRi O75340. Positions 24-191.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115333. 35 interactions.
    DIPi DIP-33217N.
    IntActi O75340. 30 interactions.
    MINTi MINT-5000341.
    STRINGi 9606.ENSP00000323816.

    PTM databases

    PhosphoSitei O75340.

    Proteomic databases

    MaxQBi O75340.
    PRIDEi O75340.

    Protocols and materials databases

    DNASUi 10016.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264933 ; ENSP00000264933 ; ENSG00000249915 . [O75340-1 ]
    ENST00000505221 ; ENSP00000422085 ; ENSG00000249915 . [O75340-3 ]
    ENST00000507528 ; ENSP00000423815 ; ENSG00000249915 . [O75340-2 ]
    GeneIDi 10016.
    KEGGi hsa:10016.
    UCSCi uc003jat.1. human. [O75340-1 ]
    uc003jau.2. human.

    Organism-specific databases

    CTDi 10016.
    GeneCardsi GC05P000258.
    HGNCi HGNC:8765. PDCD6.
    HPAi HPA047221.
    MIMi 601057. gene.
    neXtProti NX_O75340.
    PharmGKBi PA33115.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000231984.
    HOVERGENi HBG004492.
    OMAi FLWNIFQ.
    OrthoDBi EOG7RV9FM.
    PhylomeDBi O75340.
    TreeFami TF314682.

    Miscellaneous databases

    ChiTaRSi PDCD6. human.
    EvolutionaryTracei O75340.
    GeneWikii PDCD6.
    GenomeRNAii 10016.
    NextBioi 37841.
    PROi O75340.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75340.
    Bgeei O75340.
    CleanExi HS_ALG2.
    HS_PDCD6.
    Genevestigatori O75340.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF13499. EF-hand_7. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 5 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Ganjei J.K., D'Adamio L.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Urcelay E., Ibarreta D., Parrilla R., Ayuso M.S.
      Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "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] (ISOFORM 1).
      Tissue: Cerebellum.
    4. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORMS 1; 2 AND 3).
      Tissue: Colon, Ovary and Placenta.
    8. "Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner."
      Kitaura Y., Matsumoto S., Satoh H., Hitomi K., Maki M.
      J. Biol. Chem. 276:14053-14058(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PEF1.
    9. "Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized by dimerization through their fifth EF-hand regions."
      Kitaura Y., Satoh H., Takahashi H., Shibata H., Maki M.
      Arch. Biochem. Biophys. 399:12-18(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PEF1.
    10. "ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner."
      Satoh H., Shibata H., Nakano Y., Kitaura Y., Maki M.
      Biochem. Biophys. Res. Commun. 291:1166-1172(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANXA11.
    11. "Programmed cell death 6 (PDCD6) protein interacts with death-associated protein kinase 1 (DAPk1): additive effect on apoptosis via caspase-3 dependent pathway."
      Lee J.H., Rho S.B., Chun T.
      Biotechnol. Lett. 27:1011-1015(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DAPK1.
    12. "Nuclear translocation of the calcium-binding protein ALG-2 induced by the RNA-binding protein RBM22."
      Montaville P., Dai Y., Cheung C.Y., Giller K., Becker S., Michalak M., Webb S.E., Miller A.L., Krebs J.
      Biochim. Biophys. Acta 1763:1335-1343(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBM22.
    13. "The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A."
      Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.
      Mol. Biol. Cell 17:4876-4887(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEC31A AND PDCD6IP, MUTAGENESIS OF GLU-47 AND GLU-114, SUBCELLULAR LOCATION.
    14. "The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane."
      Draeby I., Woods Y.L., la Cour J.M., Mollerup J., Bourdon J.C., Berchtold M.W.
      Arch. Biochem. Biophys. 467:87-94(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH WITH SHISA5.
    15. "Identification of Alix-type and non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants."
      Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., Maki M.
      J. Biol. Chem. 283:9623-9632(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLSCR3; PLSCR4; PDCD6IP; ANXA7; ANXA11; SEC31A AND TSG101, MUTAGENESIS OF GLU-47; TRP-57; PHE-60; TYR-91; TRP-95; GLU-114 AND TYR-180.
    16. "Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that bridges Alix and TSG101."
      Okumura M., Ichioka F., Kobayashi R., Suzuki H., Yoshida H., Shibata H., Maki M.
      Biochem. Biophys. Res. Commun. 386:237-241(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Identification of the penta-EF-hand protein ALG-2 as a Ca2+-dependent interactor of mucolipin-1."
      Vergarajauregui S., Martina J.A., Puertollano R.
      J. Biol. Chem. 284:36357-36366(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MCOLN1.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7."
      Janowicz A., Michalak M., Krebs J.
      Biochim. Biophys. Acta 1813:1045-1049(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    20. "Programmed cell death 6 (PDCD6) inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of VEGFR-2."
      Rho S.B., Song Y.J., Lim M.C., Lee S.H., Kim B.R., Park S.Y.
      Cell. Signal. 24:131-139(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KDR.
    21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [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].
    22. "Structural basis for Ca2+ -dependent formation of ALG-2/Alix peptide complex: Ca2+/EF3-driven arginine switch mechanism."
      Suzuki H., Kawasaki M., Inuzuka T., Okumura M., Kakiuchi T., Shibata H., Wakatsuki S., Maki M.
      Structure 16:1562-1573(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 24-191 IN COMPLEXES WITH CALCIUM; ZINC AND PDCD6IP, SUBUNIT, INTERACTION WITH PDCD6IP.
    23. "Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2DeltaGF122) and structural roles of F122 in target recognition."
      Inuzuka T., Suzuki H., Kawasaki M., Shibata H., Wakatsuki S., Maki M.
      BMC Struct. Biol. 10:25-25(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-191, INTERACTION WITH PDCD6IP; TSG101; ANXA7 AND ANXA11, MUTAGENESIS OF PHE-122.
    24. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-123.

    Entry informationi

    Entry nameiPDCD6_HUMAN
    AccessioniPrimary (citable) accession number: O75340
    Secondary accession number(s): B2RD16
    , E7ESR3, Q2YDC2, Q5TZS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3