PHLP_HUMAN
ID PHLP_HUMAN Reviewed; 301 AA.
AC Q13371; Q4VXB6; Q96AF1; Q9UEW7; Q9UFL0; Q9UNX1; Q9UNX2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Phosducin-like protein;
DE Short=PHLP;
GN Name=PDCL; Synonyms=PHLOP1, PhLP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lazarov M.E., Martin M.M., Savage J.R., Willardson B.M., Elton T.S.;
RT "Molecular cloning and functional analysis of human phosducin-like
RT protein.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-12 AND 278-286, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-264 (ISOFORM 1).
RX PubMed=10095058; DOI=10.1016/s0167-4781(99)00006-8;
RA Thibault C., Wang J.-F., Charnas R., Mirel D., Barhite S., Miles M.F.;
RT "Cloning and characterization of the rat and human phosducin-like protein
RT genes: structure, expression and chromosomal localization.";
RL Biochim. Biophys. Acta 1444:346-354(1999).
RN [9]
RP PHOSPHORYLATION AT SER-296.
RX PubMed=15585822;
RA Carter M.D., Southwick K., Lukov G., Willardson B.M., Thulin C.D.;
RT "Identification of phosphorylation sites on phosducin-like protein by QTOF
RT mass spectrometry.";
RL J. Biomol. Tech. 15:257-264(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-296, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP FUNCTION (ISOFORM 1), AND SUBUNIT.
RX PubMed=19376773; DOI=10.1074/jbc.m900800200;
RA Howlett A.C., Gray A.J., Hunter J.M., Willardson B.M.;
RT "Role of molecular chaperones in G protein beta5/regulator of G protein
RT signaling dimer assembly and G protein betagamma dimer specificity.";
RL J. Biol. Chem. 284:16386-16399(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, AND SUBUNIT.
RX PubMed=23888055; DOI=10.1074/jbc.m113.486258;
RA Gao X., Sinha S., Belcastro M., Woodard C., Ramamurthy V., Stoilov P.,
RA Sokolov M.;
RT "Splice isoforms of phosducin-like protein control the expression of
RT heterotrimeric G proteins.";
RL J. Biol. Chem. 288:25760-25768(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-296, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Acts as a positive regulator of hedgehog signaling and
CC regulates ciliary function. {ECO:0000250|UniProtKB:Q9DBX2}.
CC -!- FUNCTION: [Isoform 1]: Functions as a co-chaperone for CCT in the
CC assembly of heterotrimeric G protein complexes, facilitates the
CC assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers.
CC -!- FUNCTION: [Isoform 2]: Acts as a negative regulator of heterotrimeric G
CC proteins assembly by trapping the preloaded G beta subunits inside the
CC CCT chaperonin.
CC -!- SUBUNIT: Forms a complex with the beta and gamma subunits of the GTP-
CC binding protein, transducin. Interacts with the CCT chaperonin complex.
CC {ECO:0000269|PubMed:19376773, ECO:0000269|PubMed:23888055}.
CC -!- INTERACTION:
CC Q13371; Q86V38: ATN1; NbExp=3; IntAct=EBI-5772890, EBI-11954292;
CC Q13371; P49368: CCT3; NbExp=6; IntAct=EBI-5772890, EBI-356673;
CC Q13371; Q92876: KLK6; NbExp=3; IntAct=EBI-5772890, EBI-2432309;
CC Q13371; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-5772890, EBI-5453723;
CC Q13371; P62195: PSMC5; NbExp=16; IntAct=EBI-5772890, EBI-357745;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9DBX2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13371-1; Sequence=Displayed;
CC Name=2; Synonyms=PhLPs;
CC IsoId=Q13371-2; Sequence=VSP_053571;
CC -!- MISCELLANEOUS: [Isoform 2]: Expressed ubiquitously, highest levels are
CC found in neural tissues amounting to 10% of total PDCL mRNA.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR EMBL; AF031463; AAD01930.1; -; mRNA.
DR EMBL; AL117602; CAB56011.1; -; mRNA.
DR EMBL; AK313429; BAG36221.1; -; mRNA.
DR EMBL; AL359512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87546.1; -; Genomic_DNA.
DR EMBL; BC017227; AAH17227.1; -; mRNA.
DR EMBL; AF083324; AAC78848.1; -; Genomic_DNA.
DR EMBL; AF083325; AAC78849.1; -; Genomic_DNA.
DR EMBL; U38236; AAA79724.1; -; Genomic_DNA.
DR CCDS; CCDS6845.1; -. [Q13371-1]
DR PIR; T17321; T17321.
DR RefSeq; NP_005379.3; NM_005388.4. [Q13371-1]
DR AlphaFoldDB; Q13371; -.
DR SMR; Q13371; -.
DR BioGRID; 111116; 145.
DR CORUM; Q13371; -.
DR IntAct; Q13371; 45.
DR MINT; Q13371; -.
DR STRING; 9606.ENSP00000259467; -.
DR GlyGen; Q13371; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13371; -.
DR PhosphoSitePlus; Q13371; -.
DR BioMuta; PDCL; -.
DR EPD; Q13371; -.
DR jPOST; Q13371; -.
DR MassIVE; Q13371; -.
DR MaxQB; Q13371; -.
DR PaxDb; Q13371; -.
DR PeptideAtlas; Q13371; -.
DR PRIDE; Q13371; -.
DR ProteomicsDB; 59355; -. [Q13371-1]
DR Antibodypedia; 16148; 166 antibodies from 31 providers.
DR DNASU; 5082; -.
DR Ensembl; ENST00000259467.9; ENSP00000259467.4; ENSG00000136940.14. [Q13371-1]
DR GeneID; 5082; -.
DR KEGG; hsa:5082; -.
DR MANE-Select; ENST00000259467.9; ENSP00000259467.4; NM_005388.5; NP_005379.3.
DR UCSC; uc004bmz.3; human. [Q13371-1]
DR CTD; 5082; -.
DR DisGeNET; 5082; -.
DR GeneCards; PDCL; -.
DR HGNC; HGNC:8770; PDCL.
DR HPA; ENSG00000136940; Low tissue specificity.
DR MIM; 604421; gene.
DR neXtProt; NX_Q13371; -.
DR OpenTargets; ENSG00000136940; -.
DR PharmGKB; PA33119; -.
DR VEuPathDB; HostDB:ENSG00000136940; -.
DR eggNOG; KOG3171; Eukaryota.
DR GeneTree; ENSGT00940000159569; -.
DR HOGENOM; CLU_085598_0_0_1; -.
DR InParanoid; Q13371; -.
DR OMA; RQTGHNQ; -.
DR OrthoDB; 1324495at2759; -.
DR PhylomeDB; Q13371; -.
DR TreeFam; TF315179; -.
DR PathwayCommons; Q13371; -.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR SignaLink; Q13371; -.
DR SIGNOR; Q13371; -.
DR BioGRID-ORCS; 5082; 226 hits in 1083 CRISPR screens.
DR ChiTaRS; PDCL; human.
DR GeneWiki; Phosducin-like; -.
DR GenomeRNAi; 5082; -.
DR Pharos; Q13371; Tbio.
DR PRO; PR:Q13371; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q13371; protein.
DR Bgee; ENSG00000136940; Expressed in buccal mucosa cell and 200 other tissues.
DR ExpressionAtlas; Q13371; baseline and differential.
DR Genevisible; Q13371; HS.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:1902605; P:heterotrimeric G-protein complex assembly; IBA:GO_Central.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd02987; Phd_like_Phd; 1.
DR Gene3D; 1.10.168.10; -; 1.
DR InterPro; IPR001200; Phosducin.
DR InterPro; IPR023196; Phosducin_N_dom_sf.
DR InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF02114; Phosducin; 1.
DR PRINTS; PR00677; PHOSDUCIN.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Chaperone;
KW Cilium biogenesis/degradation; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 2..301
FT /note="Phosducin-like protein"
FT /id="PRO_0000163755"
FT REGION 18..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63737"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBX2"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15585822,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053571"
FT VARIANT 218
FT /note="K -> N (in dbSNP:rs4466466)"
FT /id="VAR_050525"
FT CONFLICT 151
FT /note="Q -> E (in Ref. 1; AAD01930)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="K -> E (in Ref. 2; CAB56011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 34282 MW; 717675FF869760D5 CRC64;
MTTLDDKLLG EKLQYYYSSS EDEDSDHEDK DRGRCAPASS SVPAEAELAG EGISVNTGPK
GVINDWRRFK QLETEQREEQ CREMERLIKK LSMTCRSHLD EEEEQQKQKD LQEKISGKMT
LKEFAIMNED QDDEEFLQQY RKQRMEEMRQ QLHKGPQFKQ VFEISSGEGF LDMIDKEQKS
IVIMVHIYED GIPGTEAMNG CMICLAAEYP AVKFCKVKSS VIGASSQFTR NALPALLIYK
GGELIGNFVR VTDQLGDDFF AVDLEAFLQE FGLLPEKEVL VLTSVRNSAT CHSEDSDLEI
D
