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Q969G5

- PRDBP_HUMAN

UniProt

Q969G5 - PRDBP_HUMAN

Protein

Protein kinase C delta-binding protein

Gene

PRKCDBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Seems to have an immune potentiation function.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C delta-binding protein
    Alternative name(s):
    Cavin-3
    Serum deprivation response factor-related gene product that binds to C-kinase
    Short name:
    hSRBC
    Gene namesi
    Name:PRKCDBP
    Synonyms:SRBC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9400. PRKCDBP.

    Subcellular locationi

    GO - Cellular componenti

    1. caveola Source: MGI
    2. protein complex Source: MGI

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA33764.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261Protein kinase C delta-binding proteinPRO_0000331412Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei165 – 1651Phosphoserine3 Publications
    Modified residuei166 – 1661Phosphoserine3 Publications

    Post-translational modificationi

    In vitro, phosphorylated by PRKCD.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ969G5.
    PaxDbiQ969G5.
    PeptideAtlasiQ969G5.
    PRIDEiQ969G5.

    PTM databases

    PhosphoSiteiQ969G5.

    Expressioni

    Tissue specificityi

    Strongly expressed in mammary and epithelial cells.1 Publication

    Inductioni

    Down-regulated in breast and lung cancer cell lines.1 Publication

    Gene expression databases

    ArrayExpressiQ969G5.
    BgeeiQ969G5.
    CleanExiHS_PRKCDBP.
    GenevestigatoriQ969G5.

    Organism-specific databases

    HPAiHPA055136.

    Interactioni

    Subunit structurei

    Interacts with PRKCD and with phosphatidylserine. Phosphatidylserine may form a bridge between PKC and PKC-binding partners and stabilize the binding By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EPS15L1Q9UBC22EBI-3893101,EBI-2556746

    Protein-protein interaction databases

    BioGridi125187. 25 interactions.
    DIPiDIP-60484N.
    IntActiQ969G5. 5 interactions.
    STRINGi9606.ENSP00000307292.

    Structurei

    3D structure databases

    ProteinModelPortaliQ969G5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PTRF/SDPR family.Curated

    Phylogenomic databases

    eggNOGiNOG43715.
    HOGENOMiHOG000115686.
    HOVERGENiHBG108288.
    InParanoidiQ969G5.
    OrthoDBiEOG7GTT5J.
    PhylomeDBiQ969G5.
    TreeFamiTF331031.

    Family and domain databases

    InterProiIPR026752. Cavin_fam.
    [Graphical view]
    PANTHERiPTHR15240. PTHR15240. 1 hit.
    PfamiPF15237. PTRF_SDPR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q969G5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRESALERGP VPEAPAGGPV HAVTVVTLLE KLASMLETLR ERQGGLARRQ    50
    GGLAGSVRRI QSGLGALSRS HDTTSNTLAQ LLAKAERVSS HANAAQERAV 100
    RRAAQVQRLE ANHGLLVARG KLHVLLFKEE GEVPASAFQK APEPLGPADQ 150
    SELGPEQLEA EVGESSDEEP VESRAQRLRR TGLQKVQSLR RALSGRKGPA 200
    APPPTPVKPP RLGPGRSAEA QPEAQPALEP TLEPEPPQDT EEDPGRPGAA 250
    EEALLQMESV A 261
    Length:261
    Mass (Da):27,701
    Last modified:January 11, 2011 - v3
    Checksum:iE806A01DA992C53B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81R → P.3 Publications
    Corresponds to variant rs2682123 [ dbSNP | Ensembl ].
    VAR_042851
    Natural varianti104 – 1041A → T.
    Corresponds to variant rs10839551 [ dbSNP | Ensembl ].
    VAR_042852
    Natural varianti158 – 1581L → P.
    Corresponds to variant rs1051992 [ dbSNP | Ensembl ].
    VAR_042853
    Natural varianti255 – 2551L → F.
    Corresponds to variant rs12294600 [ dbSNP | Ensembl ].
    VAR_042854

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF339881 mRNA. Translation: AAK97572.1.
    AF408198 Genomic DNA. Translation: AAK97528.1.
    AC068733 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68733.1.
    BC011585 mRNA. Translation: AAH11585.1.
    CCDSiCCDS7762.1.
    RefSeqiNP_659477.2. NM_145040.2.
    UniGeneiHs.434044.

    Genome annotation databases

    EnsembliENST00000303927; ENSP00000307292; ENSG00000170955.
    GeneIDi112464.
    KEGGihsa:112464.
    UCSCiuc001mcu.1. human.

    Polymorphism databases

    DMDMi317373527.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF339881 mRNA. Translation: AAK97572.1 .
    AF408198 Genomic DNA. Translation: AAK97528.1 .
    AC068733 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68733.1 .
    BC011585 mRNA. Translation: AAH11585.1 .
    CCDSi CCDS7762.1.
    RefSeqi NP_659477.2. NM_145040.2.
    UniGenei Hs.434044.

    3D structure databases

    ProteinModelPortali Q969G5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125187. 25 interactions.
    DIPi DIP-60484N.
    IntActi Q969G5. 5 interactions.
    STRINGi 9606.ENSP00000307292.

    PTM databases

    PhosphoSitei Q969G5.

    Polymorphism databases

    DMDMi 317373527.

    Proteomic databases

    MaxQBi Q969G5.
    PaxDbi Q969G5.
    PeptideAtlasi Q969G5.
    PRIDEi Q969G5.

    Protocols and materials databases

    DNASUi 112464.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303927 ; ENSP00000307292 ; ENSG00000170955 .
    GeneIDi 112464.
    KEGGi hsa:112464.
    UCSCi uc001mcu.1. human.

    Organism-specific databases

    CTDi 112464.
    GeneCardsi GC11M006340.
    HGNCi HGNC:9400. PRKCDBP.
    HPAi HPA055136.
    neXtProti NX_Q969G5.
    PharmGKBi PA33764.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43715.
    HOGENOMi HOG000115686.
    HOVERGENi HBG108288.
    InParanoidi Q969G5.
    OrthoDBi EOG7GTT5J.
    PhylomeDBi Q969G5.
    TreeFami TF331031.

    Miscellaneous databases

    ChiTaRSi PRKCDBP. human.
    GenomeRNAii 112464.
    NextBioi 78586.
    PROi Q969G5.

    Gene expression databases

    ArrayExpressi Q969G5.
    Bgeei Q969G5.
    CleanExi HS_PRKCDBP.
    Genevestigatori Q969G5.

    Family and domain databases

    InterProi IPR026752. Cavin_fam.
    [Graphical view ]
    PANTHERi PTHR15240. PTHR15240. 1 hit.
    Pfami PF15237. PTRF_SDPR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Inactivation of human SRBC, located within the 11p15.5-p15.4 tumor suppressor region, in breast and lung cancers."
      Xu X.L., Wu L.C., Du F., Davis A., Peyton M., Tomizawa Y., Maitra A., Tomlinson G., Gazdar A.F., Weissman B.E., Bowcock A.M., Baer R., Minna J.D.
      Cancer Res. 61:7943-7949(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INDUCTION, TISSUE SPECIFICITY, VARIANT PRO-8.
      Tissue: Epithelium.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-8.
    4. "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], VARIANT PRO-8.
      Tissue: Skin.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPRDBP_HUMAN
    AccessioniPrimary (citable) accession number: Q969G5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 87 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3