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Q13371

- PHLP_HUMAN

UniProt

Q13371 - PHLP_HUMAN

Protein

Phosducin-like protein

Gene

PDCL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 3 (17 Jan 2003)
      Previous versions | rss
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    Functioni

    Isoform 1: 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.
    Isoform 2: Acts as a negative regulator of heterotrimeric G proteins assembly by trapping the preloaded G beta subunits inside the CCT chaperonin.

    GO - Molecular functioni

    1. receptor signaling protein activity Source: ProtInc

    GO - Biological processi

    1. intracellular signal transduction Source: GOC
    2. negative regulation of protein refolding Source: Ensembl
    3. protein folding Source: Ensembl
    4. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
    5. signal transduction Source: UniProtKB
    6. visual perception Source: UniProtKB-KW

    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:PHLOP1, PhLP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:8770. PDCL.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33119.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 301300Phosducin-like proteinPRO_0000163755Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei25 – 251PhosphoserineBy similarity
    Modified residuei293 – 2931Phosphoserine1 Publication
    Modified residuei296 – 2961Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13371.
    PaxDbiQ13371.
    PRIDEiQ13371.

    PTM databases

    PhosphoSiteiQ13371.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13371.
    BgeeiQ13371.
    CleanExiHS_PDCL.
    GenevestigatoriQ13371.

    Organism-specific databases

    HPAiCAB026473.
    HPA021571.
    HPA021647.

    Interactioni

    Subunit structurei

    Forms a complex with the beta and gamma subunits of the GTP-binding protein, transducin. Interacts with the CCT chaperonin complex.2 Publications

    Protein-protein interaction databases

    BioGridi111116. 11 interactions.
    IntActiQ13371. 3 interactions.
    MINTiMINT-2806359.
    STRINGi9606.ENSP00000259467.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13371.
    SMRiQ13371. Positions 51-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosducin family.Curated

    Phylogenomic databases

    eggNOGiNOG262340.
    HOGENOMiHOG000232010.
    HOVERGENiHBG003456.
    InParanoidiQ13371.
    OMAiMQEYNML.
    PhylomeDBiQ13371.
    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.

    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: Q13371-1) [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

    MTTLDDKLLG EKLQYYYSSS EDEDSDHEDK DRGRCAPASS SVPAEAELAG    50
    EGISVNTGPK GVINDWRRFK QLETEQREEQ CREMERLIKK LSMTCRSHLD 100
    EEEEQQKQKD LQEKISGKMT LKEFAIMNED QDDEEFLQQY RKQRMEEMRQ 150
    QLHKGPQFKQ VFEISSGEGF LDMIDKEQKS IVIMVHIYED GIPGTEAMNG 200
    CMICLAAEYP AVKFCKVKSS VIGASSQFTR NALPALLIYK GGELIGNFVR 250
    VTDQLGDDFF AVDLEAFLQE FGLLPEKEVL VLTSVRNSAT CHSEDSDLEI 300
    D 301
    Length:301
    Mass (Da):34,282
    Last modified:January 17, 2003 - v3
    Checksum:i717675FF869760D5
    GO
    Isoform 2 (identifier: Q13371-2) [UniParc]FASTAAdd to Basket

    Also known as: PhLPs

    The sequence of this isoform differs from the canonical sequence as follows:
         1-83: Missing.

    Note: Expressed ubiquitously, highest levels are found in neural tissues amounting to 10% of total PDCL mRNA.

    Show »
    Length:218
    Mass (Da):24,902
    Checksum:i5B7D4109656A481B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti151 – 1511Q → E in AAD01930. 1 PublicationCurated
    Sequence conflicti218 – 2181K → E in CAB56011. (PubMed:11230166)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti218 – 2181K → N.
    Corresponds to variant rs4466466 [ dbSNP | Ensembl ].
    VAR_050525

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8383Missing in isoform 2. CuratedVSP_053571Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF031463 mRNA. Translation: AAD01930.1.
    AL117602 mRNA. Translation: CAB56011.1.
    AK313429 mRNA. Translation: BAG36221.1.
    AL359512 Genomic DNA. Translation: CAI94958.1.
    CH471090 Genomic DNA. Translation: EAW87546.1.
    BC017227 mRNA. Translation: AAH17227.1.
    AF083324 Genomic DNA. Translation: AAC78848.1.
    AF083325 Genomic DNA. Translation: AAC78849.1.
    U38236 Genomic DNA. Translation: AAA79724.1.
    CCDSiCCDS6845.1. [Q13371-1]
    PIRiT17321.
    RefSeqiNP_005379.3. NM_005388.4. [Q13371-1]
    UniGeneiHs.271749.
    Hs.620774.

    Genome annotation databases

    EnsembliENST00000259467; ENSP00000259467; ENSG00000136940. [Q13371-1]
    GeneIDi5082.
    KEGGihsa:5082.
    UCSCiuc004bmz.2. human. [Q13371-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF031463 mRNA. Translation: AAD01930.1 .
    AL117602 mRNA. Translation: CAB56011.1 .
    AK313429 mRNA. Translation: BAG36221.1 .
    AL359512 Genomic DNA. Translation: CAI94958.1 .
    CH471090 Genomic DNA. Translation: EAW87546.1 .
    BC017227 mRNA. Translation: AAH17227.1 .
    AF083324 Genomic DNA. Translation: AAC78848.1 .
    AF083325 Genomic DNA. Translation: AAC78849.1 .
    U38236 Genomic DNA. Translation: AAA79724.1 .
    CCDSi CCDS6845.1. [Q13371-1 ]
    PIRi T17321.
    RefSeqi NP_005379.3. NM_005388.4. [Q13371-1 ]
    UniGenei Hs.271749.
    Hs.620774.

    3D structure databases

    ProteinModelPortali Q13371.
    SMRi Q13371. Positions 51-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111116. 11 interactions.
    IntActi Q13371. 3 interactions.
    MINTi MINT-2806359.
    STRINGi 9606.ENSP00000259467.

    PTM databases

    PhosphoSitei Q13371.

    Proteomic databases

    MaxQBi Q13371.
    PaxDbi Q13371.
    PRIDEi Q13371.

    Protocols and materials databases

    DNASUi 5082.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259467 ; ENSP00000259467 ; ENSG00000136940 . [Q13371-1 ]
    GeneIDi 5082.
    KEGGi hsa:5082.
    UCSCi uc004bmz.2. human. [Q13371-1 ]

    Organism-specific databases

    CTDi 5082.
    GeneCardsi GC09M125560.
    HGNCi HGNC:8770. PDCL.
    HPAi CAB026473.
    HPA021571.
    HPA021647.
    MIMi 604421. gene.
    neXtProti NX_Q13371.
    PharmGKBi PA33119.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262340.
    HOGENOMi HOG000232010.
    HOVERGENi HBG003456.
    InParanoidi Q13371.
    OMAi MQEYNML.
    PhylomeDBi Q13371.
    TreeFami TF315179.

    Miscellaneous databases

    ChiTaRSi PDCL. human.
    GeneWikii Phosducin-like.
    GenomeRNAii 5082.
    NextBioi 19608.
    PROi Q13371.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13371.
    Bgeei Q13371.
    CleanExi HS_PDCL.
    Genevestigatori Q13371.

    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. "Molecular cloning and functional analysis of human phosducin-like protein."
      Lazarov M.E., Martin M.M., Savage J.R., Willardson B.M., Elton T.S.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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] (ISOFORM 1).
      Tissue: Ovary.
    7. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12 AND 278-286, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    8. "Cloning and characterization of the rat and human phosducin-like protein genes: structure, expression and chromosomal localization."
      Thibault C., Wang J.-F., Charnas R., Mirel D., Barhite S., Miles M.F.
      Biochim. Biophys. Acta 1444:346-354(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-264 (ISOFORM 1).
    9. "Identification of phosphorylation sites on phosducin-like protein by QTOF mass spectrometry."
      Carter M.D., Southwick K., Lukov G., Willardson B.M., Thulin C.D.
      J. Biomol. Tech. 15:257-264(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-296.
    10. "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.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Role of molecular chaperones in G protein beta5/regulator of G protein signaling dimer assembly and G protein betagamma dimer specificity."
      Howlett A.C., Gray A.J., Hunter J.M., Willardson B.M.
      J. Biol. Chem. 284:16386-16399(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 1), SUBUNIT.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Splice isoforms of phosducin-like protein control the expression of heterotrimeric G proteins."
      Gao X., Sinha S., Belcastro M., Woodard C., Ramamurthy V., Stoilov P., Sokolov M.
      J. Biol. Chem. 288:25760-25768(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, SUBUNIT.

    Entry informationi

    Entry nameiPHLP_HUMAN
    AccessioniPrimary (citable) accession number: Q13371
    Secondary accession number(s): Q4VXB6
    , Q96AF1, Q9UEW7, Q9UFL0, Q9UNX1, Q9UNX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 17, 2003
    Last modified: October 1, 2014
    This is version 123 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3