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Q13371

- PHLP_HUMAN

UniProt

Q13371 - PHLP_HUMAN

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Protein

Phosducin-like protein

Gene

PDCL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. heterotrimeric G-protein complex assembly Source: Ensembl
  2. intracellular signal transduction Source: GOC
  3. negative regulation of protein refolding Source: Ensembl
  4. protein folding Source: Ensembl
  5. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
  6. signal transduction Source: UniProtKB
  7. visual perception Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

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

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. 21 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.
GeneTreeiENSGT00530000062970.
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

        10         20         30         40         50
MTTLDDKLLG EKLQYYYSSS EDEDSDHEDK DRGRCAPASS SVPAEAELAG
60 70 80 90 100
EGISVNTGPK GVINDWRRFK QLETEQREEQ CREMERLIKK LSMTCRSHLD
110 120 130 140 150
EEEEQQKQKD LQEKISGKMT LKEFAIMNED QDDEEFLQQY RKQRMEEMRQ
160 170 180 190 200
QLHKGPQFKQ VFEISSGEGF LDMIDKEQKS IVIMVHIYED GIPGTEAMNG
210 220 230 240 250
CMICLAAEYP AVKFCKVKSS VIGASSQFTR NALPALLIYK GGELIGNFVR
260 270 280 290 300
VTDQLGDDFF AVDLEAFLQE FGLLPEKEVL VLTSVRNSAT CHSEDSDLEI

D
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 21 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.
GeneTreei ENSGT00530000062970.
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

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

« Hide 'large scale' publications
  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 29, 2014
This is version 124 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