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Q9DBX2

- PHLP_MOUSE

UniProt

Q9DBX2 - PHLP_MOUSE

Protein

Phosducin-like protein

Gene

Pdcl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitates the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers.1 Publication

    GO - Biological processi

    1. heterotrimeric G-protein complex assembly Source: MGI
    2. negative regulation of protein refolding Source: Ensembl
    3. protein folding Source: Ensembl
    4. response to stimulus Source: UniProtKB-KW
    5. visual perception Source: MGI

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Sensory transduction, Vision

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosducin-like protein
    Short name:
    PHLP
    Gene namesi
    Name:Pdcl
    Synonyms:PhLP1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1914716. Pdcl.

    Pathology & Biotechi

    Disruption phenotypei

    Conditional deletion in photoreceptor cells leads to 50-fold decrease in Gbeta-Ggamma dimer formation and more than 10-fold decrease in light sensitivity. A 20-fold reduction in Gbeta5 and RGS9-1 expression is also observed, causing a 15-fold delay in the shutoff of light responses.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 301300Phosducin-like proteinPRO_0000163756Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonineBy similarity
    Modified residuei25 – 251Phosphoserine1 Publication
    Modified residuei293 – 2931PhosphoserineBy similarity
    Modified residuei296 – 2961PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9DBX2.
    PaxDbiQ9DBX2.
    PRIDEiQ9DBX2.

    PTM databases

    PhosphoSiteiQ9DBX2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9DBX2.
    BgeeiQ9DBX2.
    CleanExiMM_PDCL.
    GenevestigatoriQ9DBX2.

    Interactioni

    Subunit structurei

    Forms a complex with the beta and gamma subunits of the GTP-binding protein, transducin. Interacts with the CCT chaperonin complex By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBX2.
    SMRiQ9DBX2. Positions 51-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni158 – 301144Thioredoxin foldBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the phosducin family.Curated

    Phylogenomic databases

    eggNOGiNOG262340.
    GeneTreeiENSGT00530000062970.
    HOGENOMiHOG000232010.
    HOVERGENiHBG003456.
    InParanoidiQ9DBX2.
    OMAiMQEYNML.
    OrthoDBiEOG7H4DVC.
    PhylomeDBiQ9DBX2.
    TreeFamiTF315179.

    Family and domain databases

    Gene3Di1.10.168.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR001200. Phosducin.
    IPR023196. Phosducin_N_dom.
    IPR024253. Phosducin_thioredoxin-like_dom.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF02114. Phosducin. 1 hit.
    [Graphical view]
    PRINTSiPR00677. PHOSDUCIN.
    SUPFAMiSSF52833. SSF52833. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9DBX2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTLDDKLLG EKLQYYYSTS EDEDSDHEDK DRGRGAPAIS STPAEAELAG    50
    EGISINTGPK GVINDWRRFK QLETEQREEQ CREMERLIKK LSMSCRSHLD 100
    EEEEQQKQKD LQEKISGKMT LKEFGTKDKN LDDEEFLQQY RKQRMEEMRQ 150
    QFHKGPQFKQ VFEIPSGEGF LDMIDKEQKS TLIMVHIYED GVPGTEAMNG 200
    CMICLATEYP AVKFCRVRSS VIGASSRFTR NALPALLIYK AGELIGNFVR 250
    VTDQLGEDFF AVDLEAFLQE FGLLPEKEVL VLTSVRNSAT CHSEDSDLEI 300
    D 301
    Length:301
    Mass (Da):34,407
    Last modified:June 1, 2001 - v1
    Checksum:iFE0A130521AD4CFC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004704 mRNA. Translation: BAB23489.1.
    AK028668 mRNA. Translation: BAC26056.1.
    AK028814 mRNA. Translation: BAC26133.1.
    AK166983 mRNA. Translation: BAE39165.1.
    CCDSiCCDS15998.1.
    RefSeqiNP_080452.2. NM_026176.3.
    XP_006498314.1. XM_006498251.1.
    XP_006498315.1. XM_006498252.1.
    UniGeneiMm.30709.

    Genome annotation databases

    EnsembliENSMUST00000009174; ENSMUSP00000009174; ENSMUSG00000009030.
    ENSMUST00000112940; ENSMUSP00000108562; ENSMUSG00000009030.
    GeneIDi67466.
    KEGGimmu:67466.
    UCSCiuc008jmp.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004704 mRNA. Translation: BAB23489.1 .
    AK028668 mRNA. Translation: BAC26056.1 .
    AK028814 mRNA. Translation: BAC26133.1 .
    AK166983 mRNA. Translation: BAE39165.1 .
    CCDSi CCDS15998.1.
    RefSeqi NP_080452.2. NM_026176.3.
    XP_006498314.1. XM_006498251.1.
    XP_006498315.1. XM_006498252.1.
    UniGenei Mm.30709.

    3D structure databases

    ProteinModelPortali Q9DBX2.
    SMRi Q9DBX2. Positions 51-277.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9DBX2.

    Proteomic databases

    MaxQBi Q9DBX2.
    PaxDbi Q9DBX2.
    PRIDEi Q9DBX2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000009174 ; ENSMUSP00000009174 ; ENSMUSG00000009030 .
    ENSMUST00000112940 ; ENSMUSP00000108562 ; ENSMUSG00000009030 .
    GeneIDi 67466.
    KEGGi mmu:67466.
    UCSCi uc008jmp.2. mouse.

    Organism-specific databases

    CTDi 5082.
    MGIi MGI:1914716. Pdcl.

    Phylogenomic databases

    eggNOGi NOG262340.
    GeneTreei ENSGT00530000062970.
    HOGENOMi HOG000232010.
    HOVERGENi HBG003456.
    InParanoidi Q9DBX2.
    OMAi MQEYNML.
    OrthoDBi EOG7H4DVC.
    PhylomeDBi Q9DBX2.
    TreeFami TF315179.

    Miscellaneous databases

    ChiTaRSi PDCL. mouse.
    NextBioi 324658.
    PROi Q9DBX2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DBX2.
    Bgeei Q9DBX2.
    CleanExi MM_PDCL.
    Genevestigatori Q9DBX2.

    Family and domain databases

    Gene3Di 1.10.168.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR001200. Phosducin.
    IPR023196. Phosducin_N_dom.
    IPR024253. Phosducin_thioredoxin-like_dom.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF02114. Phosducin. 1 hit.
    [Graphical view ]
    PRINTSi PR00677. PHOSDUCIN.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Lung and Skin.
    2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    3. "Phosducin-like protein 1 is essential for G-protein assembly and signaling in retinal rod photoreceptors."
      Lai C.W., Kolesnikov A.V., Frederick J.M., Blake D.R., Jiang L., Stewart J.S., Chen C.K., Barrow J.R., Baehr W., Kefalov V.J., Willardson B.M.
      J. Neurosci. 33:7941-7951(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiPHLP_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBX2
    Secondary accession number(s): Q3TKI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 17, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3