Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9BUL8

- PDC10_HUMAN

UniProt

Q9BUL8 - PDC10_HUMAN

Protein

Programmed cell death protein 10

Gene

PDCD10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and MST4 activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Important for KDR/VEGFR2 signaling. Increases the stability of KDR/VEGFR2 and prevents its breakdown. Required for normal cardiovascular development. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB
    3. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. apoptotic process Source: UniProtKB-KW
    3. negative regulation of apoptotic process Source: UniProtKB
    4. positive regulation of cell proliferation Source: UniProtKB
    5. positive regulation of MAP kinase activity Source: UniProtKB

    Keywords - Biological processi

    Angiogenesis, Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Programmed cell death protein 10
    Alternative name(s):
    Cerebral cavernous malformations 3 protein
    TF-1 cell apoptosis-related protein 15
    Gene namesi
    Name:PDCD10
    Synonyms:CCM3, TFAR15
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:8761. PDCD10.

    Subcellular locationi

    Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Partially co-localizes with endogenous PXN at the leading edges of migrating cells.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi membrane Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Cerebral cavernous malformations 3 (CCM3) [MIM:603285]: A congenital vascular anomaly of the central nervous system that can result in hemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. The lesions are characterized by grossly enlarged blood vessels consisting of a single layer of endothelium and without any intervening neural tissue, ranging in diameter from a few millimeters to several centimeters.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi132 – 1321K → D: Loss of interaction with CCM2 and PXN; when associated with D-139; D-172 and D-179. 1 Publication
    Mutagenesisi135 – 1351A → D: Loss of interaction with CCM2. 1 Publication
    Mutagenesisi139 – 1391K → D: Loss of interaction with CCM2 and PXN; when associated with D-132; D-172 and D-179. 1 Publication
    Mutagenesisi172 – 1721K → D: Loss of interaction with CCM2 and PXN; when associated with D-132; D-139 and D-179. 1 Publication
    Mutagenesisi175 – 1751S → D: Loss of interaction with CCM2. 1 Publication
    Mutagenesisi179 – 1791K → D: Loss of interaction with CCM2 and PXN; when associated with D-132; D-139 and D-172. 1 Publication

    Organism-specific databases

    MIMi603285. phenotype.
    Orphaneti221061. Hereditary cerebral cavernous malformation.
    PharmGKBiPA33111.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 212212Programmed cell death protein 10PRO_0000187562Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei179 – 1791N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9BUL8.
    PaxDbiQ9BUL8.
    PRIDEiQ9BUL8.

    2D gel databases

    OGPiQ9BUL8.

    PTM databases

    PhosphoSiteiQ9BUL8.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9BUL8.
    BgeeiQ9BUL8.
    CleanExiHS_PDCD10.
    GenevestigatoriQ9BUL8.

    Organism-specific databases

    HPAiHPA027095.

    Interactioni

    Subunit structurei

    Homodimer. Interacts (via C-terminus) with CCM2 and PXN. Interacts (via N-terminus) with MST4, STK24 and STK25. Interacts with GOLGA2. Identified in a complex with CCM1 and CCM2. Interacts with KDR/VEGFR2. Interaction with KDR/VEGFR2 is enhanced by stimulation with VEGFA By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCM2Q9BSQ55EBI-740195,EBI-1573056
    PTPN13Q129233EBI-740195,EBI-355227
    STK24Q9Y6E07EBI-740195,EBI-740175
    STK25O005069EBI-740195,EBI-618295
    STRNO438153EBI-740195,EBI-1046642

    Protein-protein interaction databases

    BioGridi116400. 46 interactions.
    DIPiDIP-40607N.
    IntActiQ9BUL8. 25 interactions.
    MINTiMINT-5003501.
    STRINGi9606.ENSP00000338141.

    Structurei

    Secondary structure

    1
    212
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 193
    Helixi20 – 245
    Helixi26 – 349
    Helixi38 – 5417
    Helixi58 – 6912
    Helixi76 – 827
    Turni83 – 853
    Helixi88 – 914
    Helixi98 – 11518
    Helixi117 – 1204
    Beta strandi121 – 1233
    Helixi124 – 15128
    Turni152 – 1565
    Helixi157 – 18428
    Helixi187 – 20822

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3AJMX-ray2.30A/B8-212[»]
    3L8IX-ray2.50A/B/C/D1-212[»]
    3L8JX-ray3.05A14-212[»]
    3RQEX-ray2.80A/B/C/D1-212[»]
    3RQFX-ray2.70A/B/C/D1-212[»]
    3RQGX-ray2.50A/B/C/D1-212[»]
    3W8HX-ray2.43A8-212[»]
    3W8IX-ray2.40A8-212[»]
    4GEHX-ray1.95A/C9-212[»]
    ProteinModelPortaliQ9BUL8.
    SMRiQ9BUL8. Positions 11-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BUL8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PDCD10 family.Curated

    Phylogenomic databases

    eggNOGiNOG275788.
    HOGENOMiHOG000007888.
    HOVERGENiHBG052811.
    InParanoidiQ9BUL8.
    KOiK18269.
    OMAiRIRCHNA.
    OrthoDBiEOG7ZPNM3.
    PhylomeDBiQ9BUL8.
    TreeFamiTF105802.

    Family and domain databases

    InterProiIPR009652. DUF1241.
    [Graphical view]
    PANTHERiPTHR13250. PTHR13250. 1 hit.
    PfamiPF06840. DUF1241. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BUL8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRMTMEEMKN EAETTSMVSM PLYAVMYPVF NELERVNLSA AQTLRAAFIK    50
    AEKENPGLTQ DIIMKILEKK SVEVNFTESL LRMAADDVEE YMIERPEPEF 100
    QDLNEKARAL KQILSKIPDE INDRVRFLQT IKDIASAIKE LLDTVNNVFK 150
    KYQYQNRRAL EHQKKEFVKY SKSFSDTLKT YFKDGKAINV FVSANRLIHQ 200
    TNLILQTFKT VA 212
    Length:212
    Mass (Da):24,702
    Last modified:June 1, 2001 - v1
    Checksum:i5AA613F71FAAEF56
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti102 – 1021D → A.1 Publication
    Corresponds to variant rs1129087 [ dbSNP | Ensembl ].
    VAR_023578

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF022385 mRNA. Translation: AAB72225.1.
    CR457107 mRNA. Translation: CAG33388.1.
    AK291130 mRNA. Translation: BAF83819.1.
    AC079822 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78574.1.
    CH471052 Genomic DNA. Translation: EAW78575.1.
    CH471052 Genomic DNA. Translation: EAW78576.1.
    CH471052 Genomic DNA. Translation: EAW78577.1.
    CH471052 Genomic DNA. Translation: EAW78578.1.
    CH471052 Genomic DNA. Translation: EAW78580.1.
    CH471052 Genomic DNA. Translation: EAW78581.1.
    BC002506 mRNA. Translation: AAH02506.1.
    BC016353 mRNA. Translation: AAH16353.1.
    CCDSiCCDS3202.1.
    RefSeqiNP_009148.2. NM_007217.3.
    NP_665858.1. NM_145859.1.
    NP_665859.1. NM_145860.1.
    XP_005247143.1. XM_005247086.2.
    XP_005247144.1. XM_005247087.2.
    XP_005247145.1. XM_005247088.2.
    XP_006713548.1. XM_006713485.1.
    UniGeneiHs.478150.

    Genome annotation databases

    EnsembliENST00000392750; ENSP00000376506; ENSG00000114209.
    ENST00000461494; ENSP00000420021; ENSG00000114209.
    ENST00000470131; ENSP00000417202; ENSG00000114209.
    ENST00000473645; ENSP00000418317; ENSG00000114209.
    ENST00000497056; ENSP00000420553; ENSG00000114209.
    GeneIDi11235.
    KEGGihsa:11235.
    UCSCiuc003fex.3. human.

    Polymorphism databases

    DMDMi74733232.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF022385 mRNA. Translation: AAB72225.1 .
    CR457107 mRNA. Translation: CAG33388.1 .
    AK291130 mRNA. Translation: BAF83819.1 .
    AC079822 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78574.1 .
    CH471052 Genomic DNA. Translation: EAW78575.1 .
    CH471052 Genomic DNA. Translation: EAW78576.1 .
    CH471052 Genomic DNA. Translation: EAW78577.1 .
    CH471052 Genomic DNA. Translation: EAW78578.1 .
    CH471052 Genomic DNA. Translation: EAW78580.1 .
    CH471052 Genomic DNA. Translation: EAW78581.1 .
    BC002506 mRNA. Translation: AAH02506.1 .
    BC016353 mRNA. Translation: AAH16353.1 .
    CCDSi CCDS3202.1.
    RefSeqi NP_009148.2. NM_007217.3.
    NP_665858.1. NM_145859.1.
    NP_665859.1. NM_145860.1.
    XP_005247143.1. XM_005247086.2.
    XP_005247144.1. XM_005247087.2.
    XP_005247145.1. XM_005247088.2.
    XP_006713548.1. XM_006713485.1.
    UniGenei Hs.478150.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AJM X-ray 2.30 A/B 8-212 [» ]
    3L8I X-ray 2.50 A/B/C/D 1-212 [» ]
    3L8J X-ray 3.05 A 14-212 [» ]
    3RQE X-ray 2.80 A/B/C/D 1-212 [» ]
    3RQF X-ray 2.70 A/B/C/D 1-212 [» ]
    3RQG X-ray 2.50 A/B/C/D 1-212 [» ]
    3W8H X-ray 2.43 A 8-212 [» ]
    3W8I X-ray 2.40 A 8-212 [» ]
    4GEH X-ray 1.95 A/C 9-212 [» ]
    ProteinModelPortali Q9BUL8.
    SMRi Q9BUL8. Positions 11-211.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116400. 46 interactions.
    DIPi DIP-40607N.
    IntActi Q9BUL8. 25 interactions.
    MINTi MINT-5003501.
    STRINGi 9606.ENSP00000338141.

    PTM databases

    PhosphoSitei Q9BUL8.

    Polymorphism databases

    DMDMi 74733232.

    2D gel databases

    OGPi Q9BUL8.

    Proteomic databases

    MaxQBi Q9BUL8.
    PaxDbi Q9BUL8.
    PRIDEi Q9BUL8.

    Protocols and materials databases

    DNASUi 11235.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392750 ; ENSP00000376506 ; ENSG00000114209 .
    ENST00000461494 ; ENSP00000420021 ; ENSG00000114209 .
    ENST00000470131 ; ENSP00000417202 ; ENSG00000114209 .
    ENST00000473645 ; ENSP00000418317 ; ENSG00000114209 .
    ENST00000497056 ; ENSP00000420553 ; ENSG00000114209 .
    GeneIDi 11235.
    KEGGi hsa:11235.
    UCSCi uc003fex.3. human.

    Organism-specific databases

    CTDi 11235.
    GeneCardsi GC03M167381.
    GeneReviewsi PDCD10.
    HGNCi HGNC:8761. PDCD10.
    HPAi HPA027095.
    MIMi 603285. phenotype.
    609118. gene.
    neXtProti NX_Q9BUL8.
    Orphaneti 221061. Hereditary cerebral cavernous malformation.
    PharmGKBi PA33111.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG275788.
    HOGENOMi HOG000007888.
    HOVERGENi HBG052811.
    InParanoidi Q9BUL8.
    KOi K18269.
    OMAi RIRCHNA.
    OrthoDBi EOG7ZPNM3.
    PhylomeDBi Q9BUL8.
    TreeFami TF105802.

    Miscellaneous databases

    ChiTaRSi PDCD10. human.
    EvolutionaryTracei Q9BUL8.
    GeneWikii PDCD10.
    GenomeRNAii 11235.
    NextBioi 42758.
    PROi Q9BUL8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BUL8.
    Bgeei Q9BUL8.
    CleanExi HS_PDCD10.
    Genevestigatori Q9BUL8.

    Family and domain databases

    InterProi IPR009652. DUF1241.
    [Graphical view ]
    PANTHERi PTHR13250. PTHR13250. 1 hit.
    Pfami PF06840. DUF1241. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and expression of an apoptosis-related gene, human TFAR-15 gene."
      Wang Y.G., Liu H.T., Ma D.L., Zhang Y.M.
      Sci. China, Ser. C, Life Sci. 42:323-329(1999)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-102.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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].
      Tissue: Skin and Urinary bladder.
    7. Bienvenut W.V., Claeys D.
      Submitted (NOV-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 36-45 AND 117-124, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Platelet.
    8. Cited for: FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN CCM3.
    9. "PDCD10 interacts with Ste20-related kinase MST4 to promote cell growth and transformation via modulation of the ERK pathway."
      Ma X., Zhao H., Shan J., Long F., Chen Y., Chen Y., Zhang Y., Han X., Ma D.
      Mol. Biol. Cell 18:1965-1978(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MST4, FUNCTION, SUBCELLULAR LOCATION.
    10. "Functional analyses of human and zebrafish 18-amino acid in-frame deletion pave the way for domain mapping of the cerebral cavernous malformation 3 protein."
      Voss K., Stahl S., Hogan B.M., Reinders J., Schleider E., Schulte-Merker S., Felbor U.
      Hum. Mutat. 30:1003-1011(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STK25; CCM2 AND MST4, IDENTIFICATION IN A COMPLEX WITH CCM1 AND CCM2.
    11. "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-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and cell orientation."
      Fidalgo M., Fraile M., Pires A., Force T., Pombo C., Zalvide J.
      J. Cell Sci. 123:1274-1284(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GOLGA2; MST4; STK24 AND STK25, SUBCELLULAR LOCATION.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity."
      Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J.
      J. Biol. Chem. 285:24099-24107(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, INTERACTION WITH CCM2 AND PXN, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-132; ALA-135; LYS-139; LYS-172; SER-175 AND LYS-179.

    Entry informationi

    Entry nameiPDC10_HUMAN
    AccessioniPrimary (citable) accession number: Q9BUL8
    Secondary accession number(s): A8K515, D3DNN5, O14811
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 109 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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