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Protein

Proenkephalin-B

Gene

PDYN

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

Functioni

Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity).By similarity
Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin (By similarity).By similarity
Leumorphin has a typical opiod activity and may have anti-apoptotic effect.By similarity

GO - Biological processi

  1. neuropeptide signaling pathway Source: UniProtKB-KW
  2. synaptic transmission Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endorphin, Neuropeptide, Neurotransmitter, Opioid peptide

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_15295. Opioid Signalling.
REACT_15457. G-protein activation.
REACT_19231. G alpha (i) signalling events.

Protein family/group databases

TCDBi1.C.89.1.1. the dynorphin channel-forming neuropeptide (dynorphin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Proenkephalin-B
Alternative name(s):
Beta-neoendorphin-dynorphin
Preprodynorphin
Cleaved into the following 9 chains:
Big dynorphin
Short name:
Big Dyn
Dynorphin A(1-17)
Short name:
Dyn-A17
Short name:
Dynorphin A
Alternative name(s):
Dynorphin B
Short name:
Dyn-B
Dynorphin B(1-13)
Alternative name(s):
Dynorphin B-29
Gene namesi
Name:PDYN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:8820. PDYN.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 23 (SCA23)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionSpinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA23 is an adult-onset autosomal dominant form characterized by slowly progressive gait and limb ataxia, with variable additional features, including peripheral neuropathy and dysarthria.

See also OMIM:610245
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221C → Y in SCA23. 1 Publication
VAR_072266
Natural varianti138 – 1381R → S in SCA23; PDYN, dynorphin A and dynorphin B are located in Purkinje cells as observed in control cerebellum, but cerebellar tissue with the mutation has decreased levels of SLC1A6 and CALB1, both of which are markers of Purkinje cells; SLC1A6 accumulates and aggregates in patient cerebellar tissue. 1 Publication
VAR_064913
Natural varianti206 – 2061R → C in SCA23. 1 Publication
VAR_072268
Natural varianti206 – 2061R → H in SCA23. 1 Publication
VAR_072269
Natural varianti211 – 2111L → S in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; these results suggest slow conversion of dynorphin A to short enkephalins; mutant S-211 dynorphin A is not neurotoxic to cultured striatal neurons; no effect on membrane property. 2 Publications
VAR_064914
Natural varianti212 – 2121R → W in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property. 2 Publications
Corresponds to variant rs201486601 [ dbSNP | Ensembl ].
VAR_064915
Natural varianti215 – 2151R → C in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, resulting in an approximately 2-fold decreased level of dynorphin B compared to dynorphin A; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property. 2 Publications
VAR_064916
Natural varianti227 – 2271G → D in SCA23. 1 Publication
VAR_072270

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

MIMi610245. phenotype.
Orphaneti101108. Spinocerebellar ataxia type 23.
PharmGKBiPA33163.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Propeptidei21 – 172152PRO_0000008176Add
BLAST
Peptidei175 – 18410Alpha-neoendorphinPRO_0000306347
Peptidei175 – 1839Beta-neoendorphinPRO_0000008177
Peptidei175 – 1795Leu-enkephalinBy similarityPRO_0000306348
Propeptidei186 – 20419PRO_0000008178Add
BLAST
Peptidei207 – 23832Big dynorphinPRO_0000306349Add
BLAST
Peptidei207 – 22317Dynorphin A(1-17)PRO_0000008179Add
BLAST
Peptidei207 – 21913Dynorphin A(1-13)By similarityPRO_0000306350Add
BLAST
Peptidei207 – 2148Dynorphin A(1-8)By similarityPRO_0000306351
Peptidei207 – 2115Leu-enkephalinBy similarityPRO_0000306352
Peptidei226 – 25429LeumorphinPRO_0000008180Add
BLAST
Peptidei226 – 23813RimorphinPRO_0000008181Add
BLAST
Peptidei226 – 2305Leu-enkephalinPRO_0000008182

Post-translational modificationi

The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiP01213.
PeptideAtlasiP01213.
PRIDEiP01213.

PTM databases

PhosphoSiteiP01213.

Miscellaneous databases

PMAP-CutDBP01213.

Expressioni

Gene expression databases

BgeeiP01213.
CleanExiHS_PDYN.
ExpressionAtlasiP01213. baseline.
GenevestigatoriP01213.

Organism-specific databases

HPAiHPA049841.
HPA053342.

Interactioni

Protein-protein interaction databases

BioGridi111199. 9 interactions.
STRINGi9606.ENSP00000217305.

Structurei

3D structure databases

ProteinModelPortaliP01213.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG46156.
GeneTreeiENSGT00530000063761.
HOGENOMiHOG000013003.
HOVERGENiHBG000063.
InParanoidiP01213.
KOiK15840.
OMAiRRQFKVV.
OrthoDBiEOG7BW0K5.
PhylomeDBiP01213.
TreeFamiTF332620.

Family and domain databases

InterProiIPR006024. Opioid_neupept.
IPR000750. Proenkphlin_B.
[Graphical view]
PANTHERiPTHR11438. PTHR11438. 1 hit.
PTHR11438:SF4. PTHR11438:SF4. 1 hit.
PfamiPF01160. Opiods_neuropep. 1 hit.
[Graphical view]
PRINTSiPR01028. OPIOIDPRCRSR.
PR01030. PENKBPRCRSR.
PROSITEiPS01252. OPIOIDS_PRECURSOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01213-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWQGLVLAA CLLMFPSTTA DCLSRCSLCA VKTQDGPKPI NPLICSLQCQ
60 70 80 90 100
AALLPSEEWE RCQSFLSFFT PSTLGLNDKE DLGSKSVGEG PYSELAKLSG
110 120 130 140 150
SFLKELEKSK FLPSISTKEN TLSKSLEEKL RGLSDGFREG AESELMRDAQ
160 170 180 190 200
LNDGAMETGT LYLAEEDPKE QVKRYGGFLR KYPKRSSEVA GEGDGDSMGH
210 220 230 240 250
EDLYKRYGGF LRRIRPKLKW DNQKRYGGFL RRQFKVVTRS QEDPNAYSGE

LFDA
Length:254
Mass (Da):28,385
Last modified:July 20, 1986 - v1
Checksum:i783E7D6AC068CE68
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221C → Y in SCA23. 1 Publication
VAR_072266
Natural varianti25 – 251R → Q Very rare neutral polymorphism. 1 Publication
VAR_072267
Natural varianti138 – 1381R → S in SCA23; PDYN, dynorphin A and dynorphin B are located in Purkinje cells as observed in control cerebellum, but cerebellar tissue with the mutation has decreased levels of SLC1A6 and CALB1, both of which are markers of Purkinje cells; SLC1A6 accumulates and aggregates in patient cerebellar tissue. 1 Publication
VAR_064913
Natural varianti206 – 2061R → C in SCA23. 1 Publication
VAR_072268
Natural varianti206 – 2061R → H in SCA23. 1 Publication
VAR_072269
Natural varianti211 – 2111L → S in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; these results suggest slow conversion of dynorphin A to short enkephalins; mutant S-211 dynorphin A is not neurotoxic to cultured striatal neurons; no effect on membrane property. 2 Publications
VAR_064914
Natural varianti212 – 2121R → W in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property. 2 Publications
Corresponds to variant rs201486601 [ dbSNP | Ensembl ].
VAR_064915
Natural varianti215 – 2151R → C in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, resulting in an approximately 2-fold decreased level of dynorphin B compared to dynorphin A; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property. 2 Publications
VAR_064916
Natural varianti227 – 2271G → D in SCA23. 1 Publication
VAR_072270

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02536 Genomic DNA. No translation available.
K02267 Genomic DNA. No translation available.
AH002816 Genomic DNA. Translation: AAA58456.2.
X00176 Genomic DNA. Translation: CAA24999.1.
AK289618 mRNA. Translation: BAF82307.1.
AL034562 Genomic DNA. Translation: CAB38875.1.
CH471133 Genomic DNA. Translation: EAX10604.1.
BC026334 mRNA. Translation: AAH26334.1.
CCDSiCCDS13023.1.
PIRiA01478. DFHU.
RefSeqiNP_001177821.1. NM_001190892.1.
NP_001177827.1. NM_001190898.2.
NP_001177828.1. NM_001190899.2.
NP_001177829.1. NM_001190900.1.
NP_077722.1. NM_024411.4.
UniGeneiHs.22584.

Genome annotation databases

EnsembliENST00000217305; ENSP00000217305; ENSG00000101327.
ENST00000539905; ENSP00000440185; ENSG00000101327.
ENST00000540134; ENSP00000442259; ENSG00000101327.
GeneIDi5173.
KEGGihsa:5173.
UCSCiuc002wfv.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02536 Genomic DNA. No translation available.
K02267 Genomic DNA. No translation available.
AH002816 Genomic DNA. Translation: AAA58456.2.
X00176 Genomic DNA. Translation: CAA24999.1.
AK289618 mRNA. Translation: BAF82307.1.
AL034562 Genomic DNA. Translation: CAB38875.1.
CH471133 Genomic DNA. Translation: EAX10604.1.
BC026334 mRNA. Translation: AAH26334.1.
CCDSiCCDS13023.1.
PIRiA01478. DFHU.
RefSeqiNP_001177821.1. NM_001190892.1.
NP_001177827.1. NM_001190898.2.
NP_001177828.1. NM_001190899.2.
NP_001177829.1. NM_001190900.1.
NP_077722.1. NM_024411.4.
UniGeneiHs.22584.

3D structure databases

ProteinModelPortaliP01213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111199. 9 interactions.
STRINGi9606.ENSP00000217305.

Chemistry

BindingDBiP01213.
ChEMBLiCHEMBL2227.

Protein family/group databases

TCDBi1.C.89.1.1. the dynorphin channel-forming neuropeptide (dynorphin) family.

PTM databases

PhosphoSiteiP01213.

Proteomic databases

PaxDbiP01213.
PeptideAtlasiP01213.
PRIDEiP01213.

Protocols and materials databases

DNASUi5173.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217305; ENSP00000217305; ENSG00000101327.
ENST00000539905; ENSP00000440185; ENSG00000101327.
ENST00000540134; ENSP00000442259; ENSG00000101327.
GeneIDi5173.
KEGGihsa:5173.
UCSCiuc002wfv.3. human.

Organism-specific databases

CTDi5173.
GeneCardsiGC20M001907.
HGNCiHGNC:8820. PDYN.
HPAiHPA049841.
HPA053342.
MIMi131340. gene.
610245. phenotype.
neXtProtiNX_P01213.
Orphaneti101108. Spinocerebellar ataxia type 23.
PharmGKBiPA33163.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG46156.
GeneTreeiENSGT00530000063761.
HOGENOMiHOG000013003.
HOVERGENiHBG000063.
InParanoidiP01213.
KOiK15840.
OMAiRRQFKVV.
OrthoDBiEOG7BW0K5.
PhylomeDBiP01213.
TreeFamiTF332620.

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_15295. Opioid Signalling.
REACT_15457. G-protein activation.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

GenomeRNAii5173.
NextBioi20018.
PMAP-CutDBP01213.
PROiP01213.
SOURCEiSearch...

Gene expression databases

BgeeiP01213.
CleanExiHS_PDYN.
ExpressionAtlasiP01213. baseline.
GenevestigatoriP01213.

Family and domain databases

InterProiIPR006024. Opioid_neupept.
IPR000750. Proenkphlin_B.
[Graphical view]
PANTHERiPTHR11438. PTHR11438. 1 hit.
PTHR11438:SF4. PTHR11438:SF4. 1 hit.
PfamiPF01160. Opiods_neuropep. 1 hit.
[Graphical view]
PRINTSiPR01028. OPIOIDPRCRSR.
PR01030. PENKBPRCRSR.
PROSITEiPS01252. OPIOIDS_PRECURSOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and structural organization of the human preproenkephalin B gene."
    Horikawa S., Takai T., Toyosato M., Takahashi H., Noda M., Kakidani H., Kubo T., Hirose T., Inayama S., Hayashida H., Miyata T., Numa S.
    Nature 306:611-614(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Amygdala.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "NMR and structural model of dynorphin A (1-17) bound to dodecylphosphocholine micelles."
    Tessmer M.R., Kallick D.A.
    Biochemistry 36:1971-1981(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF DYNORPHIN A(1-17).
  7. "Dynorphin peptides differentially regulate the human kappa opioid receptor."
    Chen Y., Chen C., Liu-Chen L.-Y.
    Life Sci. 80:1439-1448(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Big dynorphin as a putative endogenous ligand for the kappa-opioid receptor."
    Merg F., Filliol D., Usynin I., Bazov I., Bark N., Hurd Y.L., Yakovleva T., Kieffer B.L., Bakalkin G.
    J. Neurochem. 97:292-301(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: VARIANTS SCA23 SER-138; SER-211; TRP-212 AND CYS-215, CHARACTERIZATION OF VARIANTS SCA23 SER-138; SER-211; TRP-212 AND CYS-215.
  10. "Perturbations of model membranes induced by pathogenic dynorphin A mutants causing neurodegeneration in human brain."
    Madani F., Taqi M.M., Warmlander S.K., Verbeek D.S., Bakalkin G., Graslund A.
    Biochem. Biophys. Res. Commun. 411:111-114(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCA23 SER-211; TRP-212 AND CYS-215, CHARACTERIZATION OF VARIANTS SCA23 SER-211; TRP-212 AND CYS-215.
  11. Cited for: VARIANT SCA23 TYR-22, VARIANT GLN-25.
  12. "Identification and characterization of novel PDYN mutations in dominant cerebellar ataxia cases."
    Jezierska J., Stevanin G., Watanabe H., Fokkens M.R., Zagnoli F., Kok J., Goas J.Y., Bertrand P., Robin C., Brice A., Bakalkin G., Durr A., Verbeek D.S.
    J. Neurol. 260:1807-1812(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCA23 CYS-206; HIS-206 AND ASP-227.

Entry informationi

Entry nameiPDYN_HUMAN
AccessioniPrimary (citable) accession number: P01213
Secondary accession number(s): A8K0Q3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: July 20, 1986
Last modified: February 3, 2015
This is version 135 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 20
    Human chromosome 20: 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

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.