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Protein

Phosducin

Gene

PDC

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

Functioni

May participate in the regulation of visual phototransduction or in the integration of photoreceptor metabolism. Inhibits the transcriptional activation activity of the cone-rod homeobox CRX.1 Publication

GO - Molecular functioni

  1. phospholipase inhibitor activity Source: ProtInc

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: ProtInc
  2. negative regulation of catalytic activity Source: GOC
  3. phototransduction Source: ProtInc
  4. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Enzyme and pathway databases

SignaLinkiP20941.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosducin
Short name:
PHD
Alternative name(s):
33 kDa phototransducing protein
Protein MEKA
Gene namesi
Name:PDC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:8759. PDC.

Subcellular locationi

Cytoplasmcytosol 1 Publication. Cell projectionciliumphotoreceptor outer segment 1 Publication. Photoreceptor inner segment 1 Publication. Nucleus 1 Publication
Note: Outer and inner segments of the rod cells.

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. photoreceptor inner segment Source: UniProtKB-SubCell
  4. photoreceptor outer segment Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33109.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246PhosducinPRO_0000163752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731Phosphoserine; by PKABy similarity

Post-translational modificationi

Light-induced changes in cyclic nucleotide levels modulate the phosphorylation of this protein by cAMP kinase.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP20941.
PRIDEiP20941.

PTM databases

PhosphoSiteiP20941.

Expressioni

Gene expression databases

BgeeiP20941.
CleanExiHS_PDC.
ExpressionAtlasiP20941. baseline.
GenevestigatoriP20941.

Organism-specific databases

HPAiHPA028432.

Interactioni

Subunit structurei

Forms a complex with the beta and gamma subunits of the GTP-binding protein, transducin. Interacts with CRX.1 Publication

Protein-protein interaction databases

BioGridi111159. 3 interactions.
STRINGi9606.ENSP00000375855.

Structurei

3D structure databases

ProteinModelPortaliP20941.
SMRiP20941. Positions 14-230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 246136Thioredoxin foldBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the phosducin family.Curated

Phylogenomic databases

eggNOGiNOG262340.
GeneTreeiENSGT00530000062970.
HOGENOMiHOG000232010.
HOVERGENiHBG003456.
InParanoidiP20941.
KOiK08327.
OMAiCMQDMHQ.
OrthoDBiEOG7H4DVC.
PhylomeDBiP20941.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P20941-1) [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
MEEAKSQSLE EDFEGQATHT GPKGVINDWR KFKLESQDSD SIPPSKKEIL
60 70 80 90 100
RQMSSPQSRN GKDSKERVSR KMSIQEYELI HKEKEDENCL RKYRRQCMQD
110 120 130 140 150
MHQKLSFGPR YGFVYELETG KQFLETIEKE LKITTIVVHI YEDGIKGCDA
160 170 180 190 200
LNSSLTCLAA EYPIVKFCKI KASNTGAGDR FSLDVLPTLL IYKGGELISN
210 220 230 240
FISVAEQFAE EFFAGDVESF LNEYGLLPER EVHVLEHTKI EEEDVE
Length:246
Mass (Da):28,246
Last modified:February 1, 1991 - v1
Checksum:iDF59C2C7C3308C90
GO
Isoform 2 (identifier: P20941-2) [UniParc]FASTAAdd to Basket

Also known as: PhLOP1

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Show »
Length:194
Mass (Da):22,317
Checksum:i228ADD7757825F29
GO
Isoform 3 (identifier: P20941-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPESLDSPTSGRPGVTTHSTRTPGTEIQTIISNPVPKM

Show »
Length:283
Mass (Da):32,118
Checksum:iB9637E3DF21C470D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401I → L in AAA36210. (PubMed:2383274)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5252Missing in isoform 2. 1 PublicationVSP_043880Add
BLAST
Alternative sequencei1 – 11M → MPESLDSPTSGRPGVTTHST RTPGTEIQTIISNPVPKM in isoform 3. 1 PublicationVSP_053778

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33478 mRNA. Translation: AAA35486.1.
M38059, M60720, M38058 Genomic DNA. Translation: AAA36210.1.
AF076463 mRNA. Translation: AAD43141.1.
AF076464 mRNA. Translation: AAD43142.1.
AL596220 Genomic DNA. Translation: CAI13122.1.
AL663036 Genomic DNA. No translation available.
CH471067 Genomic DNA. Translation: EAW91212.1.
CCDSiCCDS1370.1. [P20941-1]
CCDS41447.1. [P20941-2]
PIRiA35422.
RefSeqiNP_002588.3. NM_002597.4. [P20941-1]
NP_072098.1. NM_022576.3. [P20941-2]
UniGeneiHs.654381.

Genome annotation databases

EnsembliENST00000391997; ENSP00000375855; ENSG00000116703. [P20941-1]
ENST00000497198; ENSP00000422775; ENSG00000116703. [P20941-2]
GeneIDi5132.
KEGGihsa:5132.
UCSCiuc001grz.3. human. [P20941-1]

Polymorphism databases

DMDMi130134.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Mutations of the PDC gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33478 mRNA. Translation: AAA35486.1.
M38059, M60720, M38058 Genomic DNA. Translation: AAA36210.1.
AF076463 mRNA. Translation: AAD43141.1.
AF076464 mRNA. Translation: AAD43142.1.
AL596220 Genomic DNA. Translation: CAI13122.1.
AL663036 Genomic DNA. No translation available.
CH471067 Genomic DNA. Translation: EAW91212.1.
CCDSiCCDS1370.1. [P20941-1]
CCDS41447.1. [P20941-2]
PIRiA35422.
RefSeqiNP_002588.3. NM_002597.4. [P20941-1]
NP_072098.1. NM_022576.3. [P20941-2]
UniGeneiHs.654381.

3D structure databases

ProteinModelPortaliP20941.
SMRiP20941. Positions 14-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111159. 3 interactions.
STRINGi9606.ENSP00000375855.

PTM databases

PhosphoSiteiP20941.

Polymorphism databases

DMDMi130134.

Proteomic databases

PaxDbiP20941.
PRIDEiP20941.

Protocols and materials databases

DNASUi5132.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000391997; ENSP00000375855; ENSG00000116703. [P20941-1]
ENST00000497198; ENSP00000422775; ENSG00000116703. [P20941-2]
GeneIDi5132.
KEGGihsa:5132.
UCSCiuc001grz.3. human. [P20941-1]

Organism-specific databases

CTDi5132.
GeneCardsiGC01M186412.
HGNCiHGNC:8759. PDC.
HPAiHPA028432.
MIMi171490. gene.
neXtProtiNX_P20941.
PharmGKBiPA33109.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG262340.
GeneTreeiENSGT00530000062970.
HOGENOMiHOG000232010.
HOVERGENiHBG003456.
InParanoidiP20941.
KOiK08327.
OMAiCMQDMHQ.
OrthoDBiEOG7H4DVC.
PhylomeDBiP20941.
TreeFamiTF315179.

Enzyme and pathway databases

SignaLinkiP20941.

Miscellaneous databases

GeneWikiiPhosducin.
GenomeRNAii5132.
NextBioi19786.
PROiP20941.
SOURCEiSearch...

Gene expression databases

BgeeiP20941.
CleanExiHS_PDC.
ExpressionAtlasiP20941. baseline.
GenevestigatoriP20941.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the human, bovine and rat 33-kDa proteins and cDNA in retina and pineal gland."
    Abe T., Nakabayashi H., Tamada H., Takagi T., Sakuragi S., Yamaki K., Shinohara T.
    Gene 91:209-215(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Pineal gland and Retina.
  2. "Isolation and analysis of the human MEKA gene encoding a retina-specific protein."
    Watanabe Y., Kawasaki K., Miki N., Kuo C.H.
    Biochem. Biophys. Res. Commun. 170:951-956(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Modulation of CRX transactivation activity by phosducin isoforms."
    Zhu X., Craft C.M.
    Mol. Cell. Biol. 20:5216-5226(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION WITH CRX, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
    Tissue: Retina.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiPHOS_HUMAN
AccessioniPrimary (citable) accession number: P20941
Secondary accession number(s): Q14816, Q9UP22, Q9UP23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: January 7, 2015
This is version 131 of the entry and version 1 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.