Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Probable hydrolase PNKD (EC 3.-.-.-) (Myofibrillogenesis regulator 1) (MR-1) (Paroxysmal nonkinesiogenic dyskinesia protein) (Trans-activated by hepatitis C virus core protein 2)

 PNKD_HUMAN              Reviewed;         385 AA.
Q8N490; A8K1F2; Q96A48; Q9BU26; Q9NSX4; Q9ULN6; Q9Y4T1;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
23-MAY-2018, entry version 123.
RecName: Full=Probable hydrolase PNKD;
EC=3.-.-.-;
AltName: Full=Myofibrillogenesis regulator 1;
Short=MR-1;
AltName: Full=Paroxysmal nonkinesiogenic dyskinesia protein;
AltName: Full=Trans-activated by hepatitis C virus core protein 2;
Name=PNKD; Synonyms=KIAA1184, MR1, TAHCCP2;
ORFNames=FKSG19, UNQ2491/PRO5778;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
INTERACTION WITH MRLC2; MYOM1 AND ENO3.
PubMed=15188056; DOI=10.1093/abbs/36.6.412;
Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G.,
Gong L.-M.;
"Characterization of MR-1, a novel myofibrillogenesis regulator in
human muscle.";
Acta Biochim. Biophys. Sin. 36:412-418(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION.
PubMed=15188498; DOI=10.3748/wjg.v10.i12.1746;
Liu M., Liu Y., Cheng J., Zhang S.-L., Wang L., Shao Q., Zhang J.,
Yang Q.;
"Transactivating effect of hepatitis C virus core protein: a
suppression subtractive hybridization study.";
World J. Gastroenterol. 10:1746-1749(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Wang Y.-G., Gong L.;
"Cloning of FKSG19, a novel gene expressed in ovarian tumour tissue.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
Liu Y., Cheng J., Wang G., Li K., Dong J., Li L., Chen J., Zhang L.;
"Identification of human genomic DNA structure of the gene trans-
activated by hepatitis C virus core protein 2.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Caudate nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-385 (ISOFORM 1).
TISSUE=Brain;
PubMed=10574461; DOI=10.1093/dnares/6.5.329;
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
"Characterization of cDNA clones selected by the GeneMark analysis
from size-fractionated cDNA libraries from human brain.";
DNA Res. 6:329-336(1999).
[11]
INVOLVEMENT IN DYT8.
PubMed=16717228; DOI=10.1212/01.wnl.0000217332.51740.7c;
Spacey S.D., Adams P.J., Lam P.C., Materek L.A., Stoessl A.J.,
Snutch T.P., Hsiung G.Y.;
"Genetic heterogeneity in paroxysmal nonkinesigenic dyskinesia.";
Neurology 66:1588-1590(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
VARIANTS DYT8 VAL-7 AND VAL-9, AND TISSUE SPECIFICITY.
PubMed=15262732; DOI=10.1001/archneur.61.7.1025;
Rainier S., Thomas D., Tokarz D., Ming L., Bui M., Plein E., Zhao X.,
Lemons R., Albin R., Delaney C., Alvarado D., Fink J.K.;
"Myofibrillogenesis regulator 1 gene mutations cause paroxysmal
dystonic choreoathetosis.";
Arch. Neurol. 61:1025-1029(2004).
[17]
TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
PubMed=15496428; DOI=10.1093/hmg/ddh330;
Lee H.-Y., Xu Y., Huang Y., Ahn A.H., Auburger G.W., Pandolfo M.,
Kwiecinski H., Grimes D.A., Lang A.E., Nielsen J.E., Averyanov Y.,
Servidei S., Friedman A., Van Bogaert P., Abramowicz M.J., Bruno M.K.,
Sorensen B.F., Tang L., Fu Y.-H., Ptacek L.J.;
"The gene for paroxysmal non-kinesigenic dyskinesia encodes an enzyme
in a stress response pathway.";
Hum. Mol. Genet. 13:3161-3170(2004).
[18]
VARIANTS DYT8 VAL-7 AND VAL-9.
PubMed=15824259; DOI=10.1001/archneur.62.4.597;
Chen D.-H., Matsushita M., Rainier S., Meaney B., Tisch L., Feleke A.,
Wolff J., Lipe H., Fink J., Bird T.D., Raskind W.H.;
"Presence of alanine-to-valine substitutions in myofibrillogenesis
regulator 1 in paroxysmal nonkinesigenic dyskinesia: confirmation in 2
kindreds.";
Arch. Neurol. 62:597-600(2005).
[19]
VARIANT DYT8 VAL-9.
PubMed=16972263; DOI=10.1002/mds.21095;
Stefanova E., Djarmati A., Momcilovic D., Dragasevic N., Svetel M.,
Klein C., Kostic V.S.;
"Clinical characteristics of paroxysmal nonkinesigenic dyskinesia in
Serbian family with Myofibrillogenesis regulator 1 gene mutation.";
Mov. Disord. 21:2010-2015(2006).
[20]
VARIANT DYT8 VAL-7.
PubMed=16632198; DOI=10.1016/j.neulet.2006.03.048;
Hempelmann A., Kumar S., Muralitharan S., Sander T.;
"Myofibrillogenesis regulator 1 gene (MR-1) mutation in an Omani
family with paroxysmal nonkinesigenic dyskinesia.";
Neurosci. Lett. 402:118-120(2006).
-!- FUNCTION: Probable hydrolase that plays an aggravative role in the
development of cardiac hypertrophy via activation of the NF-kappa-
B signaling pathway. {ECO:0000250}.
-!- SUBUNIT: Isoform 2 interacts with the sarcomeric proteins, MRLC2,
MYOM1 and ENO3. {ECO:0000269|PubMed:15188056}.
-!- INTERACTION:
Q7L273:KCTD9; NbExp=3; IntAct=EBI-746368, EBI-4397613;
G5E962:MAGEA11; NbExp=3; IntAct=EBI-746368, EBI-11525615;
P43364-2:MAGEA11; NbExp=3; IntAct=EBI-746368, EBI-10178634;
P27361:MAPK3; NbExp=4; IntAct=EBI-746368, EBI-73995;
-!- SUBCELLULAR LOCATION: Isoform 1: Membrane; Peripheral membrane
protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 3: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=MR-1L;
IsoId=Q8N490-1; Sequence=Displayed;
Name=2; Synonyms=MR-1S;
IsoId=Q8N490-2; Sequence=VSP_027739, VSP_027740;
Name=3; Synonyms=MR-1M;
IsoId=Q8N490-3; Sequence=VSP_027736;
Name=4;
IsoId=Q8N490-4; Sequence=VSP_027737, VSP_027738;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 is only expressed in the brain.
Isoform 2 is ubiquitously detected with highest expression in
skeletal muscle and detected in myocardial myofibrils. Variant
Val-7 and Val-9 are detected in the brain only.
{ECO:0000269|PubMed:15188056, ECO:0000269|PubMed:15262732,
ECO:0000269|PubMed:15496428}.
-!- INDUCTION: By Hepatitis C virus core protein.
{ECO:0000269|PubMed:15188498}.
-!- DISEASE: Dystonia 8 (DYT8) [MIM:118800]: A paroxysmal non-
kinesigenic dystonia/dyskinesia. Dystonia is defined by the
presence of sustained involuntary muscle contractions, often
leading to abnormal postures. Dystonia type 8 is characterized by
attacks of involuntary movements brought on by stress, alcohol,
fatigue or caffeine. The attacks generally last between a few
seconds and four hours or longer. The attacks may begin in one
limb and spread throughout the body, including the face.
{ECO:0000269|PubMed:15262732, ECO:0000269|PubMed:15824259,
ECO:0000269|PubMed:16632198, ECO:0000269|PubMed:16717228,
ECO:0000269|PubMed:16972263}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
Glyoxalase II family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF417001; AAL08573.1; -; mRNA.
EMBL; AY039043; AAK83449.1; -; mRNA.
EMBL; AF318057; AAL25716.1; -; mRNA.
EMBL; AF390031; AAM73649.1; -; Genomic_DNA.
EMBL; AY358753; AAQ89113.1; -; mRNA.
EMBL; AK289867; BAF82556.1; -; mRNA.
EMBL; AL080092; CAB45707.2; -; mRNA.
EMBL; AL137675; CAB70870.2; -; mRNA.
EMBL; CH471063; EAW70602.1; -; Genomic_DNA.
EMBL; CH471063; EAW70604.1; -; Genomic_DNA.
EMBL; BC002937; AAH02937.1; -; mRNA.
EMBL; BC021118; AAH21118.1; -; mRNA.
EMBL; BC036457; AAH36457.1; -; mRNA.
EMBL; AB033010; BAA86498.1; -; mRNA.
CCDS; CCDS2411.1; -. [Q8N490-1]
CCDS; CCDS2413.1; -. [Q8N490-3]
CCDS; CCDS42816.1; -. [Q8N490-2]
PIR; T46495; T46495.
RefSeq; NP_001070867.1; NM_001077399.2. [Q8N490-2]
RefSeq; NP_056303.3; NM_015488.4. [Q8N490-1]
RefSeq; NP_072094.1; NM_022572.4. [Q8N490-3]
UniGene; Hs.98475; -.
ProteinModelPortal; Q8N490; -.
SMR; Q8N490; -.
BioGrid; 117446; 99.
IntAct; Q8N490; 20.
MINT; Q8N490; -.
STRING; 9606.ENSP00000273077; -.
iPTMnet; Q8N490; -.
PhosphoSitePlus; Q8N490; -.
BioMuta; PNKD; -.
DMDM; 158563846; -.
EPD; Q8N490; -.
MaxQB; Q8N490; -.
PaxDb; Q8N490; -.
PeptideAtlas; Q8N490; -.
PRIDE; Q8N490; -.
DNASU; 25953; -.
Ensembl; ENST00000248451; ENSP00000248451; ENSG00000127838. [Q8N490-2]
Ensembl; ENST00000258362; ENSP00000258362; ENSG00000127838. [Q8N490-3]
Ensembl; ENST00000273077; ENSP00000273077; ENSG00000127838. [Q8N490-1]
Ensembl; ENST00000436005; ENSP00000414400; ENSG00000127838. [Q8N490-4]
GeneID; 25953; -.
KEGG; hsa:25953; -.
UCSC; uc002vhm.2; human. [Q8N490-1]
CTD; 25953; -.
DisGeNET; 25953; -.
EuPathDB; HostDB:ENSG00000127838.13; -.
GeneCards; PNKD; -.
GeneReviews; PNKD; -.
HGNC; HGNC:9153; PNKD.
HPA; HPA010134; -.
HPA; HPA017068; -.
MalaCards; PNKD; -.
MIM; 118800; phenotype.
MIM; 609023; gene.
neXtProt; NX_Q8N490; -.
OpenTargets; ENSG00000127838; -.
Orphanet; 98810; Paroxysmal non-kinesigenic dyskinesia.
PharmGKB; PA33476; -.
eggNOG; KOG0813; Eukaryota.
eggNOG; COG0491; LUCA.
GeneTree; ENSGT00530000063033; -.
HOVERGEN; HBG001152; -.
InParanoid; Q8N490; -.
OMA; HTVGHMI; -.
OrthoDB; EOG091G08UZ; -.
PhylomeDB; Q8N490; -.
TreeFam; TF105273; -.
ChiTaRS; PNKD; human.
GeneWiki; PNKD; -.
GenomeRNAi; 25953; -.
PRO; PR:Q8N490; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000127838; -.
CleanEx; HS_MR1; -.
CleanEx; HS_PNKD; -.
ExpressionAtlas; Q8N490; baseline and differential.
Genevisible; Q8N490; HS.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro.
GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IMP:SynGO-UCL.
GO; GO:0050884; P:neuromuscular process controlling posture; IEA:Ensembl.
GO; GO:0042053; P:regulation of dopamine metabolic process; IEA:Ensembl.
GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; IEA:Ensembl.
CDD; cd07723; hydroxyacylglutathione_hydrola; 1.
Gene3D; 3.60.15.10; -; 1.
HAMAP; MF_01374; Glyoxalase_2; 1.
InterPro; IPR035680; Clx_II_MBL.
InterPro; IPR032282; HAGH_C.
InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
Pfam; PF16123; HAGH_C; 1.
Pfam; PF00753; Lactamase_B; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF56281; SSF56281; 1.
TIGRFAMs; TIGR03413; GSH_gloB; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Disease mutation;
Dystonia; Hydrolase; Membrane; Metal-binding; Mitochondrion; Nucleus;
Reference proteome; Zinc.
CHAIN 1 385 Probable hydrolase PNKD.
/FTId=PRO_0000299549.
REGION 291 293 Substrate binding. {ECO:0000250}.
REGION 376 379 Substrate binding. {ECO:0000250}.
METAL 172 172 Zinc 1. {ECO:0000250}.
METAL 174 174 Zinc 1. {ECO:0000250}.
METAL 176 176 Zinc 2. {ECO:0000250}.
METAL 177 177 Zinc 2. {ECO:0000250}.
METAL 229 229 Zinc 1. {ECO:0000250}.
METAL 253 253 Zinc 1. {ECO:0000250}.
METAL 253 253 Zinc 2. {ECO:0000250}.
METAL 291 291 Zinc 2. {ECO:0000250}.
VAR_SEQ 1 79 MAAVVAATALKGRGARNARVLRGILAGATANKASHNRTRAL
QSHSSPEGKEEPEPLSPELEYIPRKRGKNPMKAVGLAW ->
MAWQGWPAAWQWVAGCWLLLVLVLVLLVSPRGCRARRGLRG
LLMAHSQRLLFRIG (in isoform 3).
{ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_027736.
VAR_SEQ 1 60 Missing (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_027737.
VAR_SEQ 61 78 EYIPRKRGKNPMKAVGLA -> MPSSVHHTKRQMMSIYCY
(in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_027738.
VAR_SEQ 80 142 YSLYTRTWLGYLFYRQQLRRARNRYPKGHSKTQPRLFNGVK
VLPIPVLSDNYSYLIIDTQAQL -> AIGFPCGILLFILTK
REVDKDRVKQMKARQNMRLSNTGEYESQRFRASSQSAPSPD
VGSGVQT (in isoform 2).
{ECO:0000303|PubMed:15188056,
ECO:0000303|PubMed:15188498,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.3}.
/FTId=VSP_027739.
VAR_SEQ 143 385 Missing (in isoform 2).
{ECO:0000303|PubMed:15188056,
ECO:0000303|PubMed:15188498,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.3}.
/FTId=VSP_027740.
VARIANT 7 7 A -> V (in DYT8; dbSNP:rs121434512).
{ECO:0000269|PubMed:15262732,
ECO:0000269|PubMed:15824259,
ECO:0000269|PubMed:16632198}.
/FTId=VAR_034844.
VARIANT 9 9 A -> V (in DYT8; dbSNP:rs121434511).
{ECO:0000269|PubMed:15262732,
ECO:0000269|PubMed:15824259,
ECO:0000269|PubMed:16972263}.
/FTId=VAR_034845.
CONFLICT 12 12 G -> S (in Ref. 9; AAH36457).
{ECO:0000305}.
CONFLICT 33 33 A -> V (in Ref. 9; AAH36457).
{ECO:0000305}.
CONFLICT 47 47 P -> S (in Ref. 9; AAH36457).
{ECO:0000305}.
CONFLICT 377 377 R -> L (in Ref. 7; CAB70870).
{ECO:0000305}.
SEQUENCE 385 AA; 42876 MW; A4D631D3A4319A2C CRC64;
MAAVVAATAL KGRGARNARV LRGILAGATA NKASHNRTRA LQSHSSPEGK EEPEPLSPEL
EYIPRKRGKN PMKAVGLAWY SLYTRTWLGY LFYRQQLRRA RNRYPKGHSK TQPRLFNGVK
VLPIPVLSDN YSYLIIDTQA QLAVAVDPSD PRAVQASIEK EGVTLVAILC THKHWDHSGG
NRDLSRRHRD CRVYGSPQDG IPYLTHPLCH QDVVSVGRLQ IRALATPGHT QGHLVYLLDG
EPYKGPSCLF SGDLLFLSGC GRTFEGNAET MLSSLDTVLG LGDDTLLWPG HEYAEENLGF
AGVVEPENLA RERKMQWVQR QRLERKGTCP STLGEERSYN PFLRTHCLAL QEALGPGPGP
TGDDDYSRAQ LLEELRRLKD MHKSK


Related products :

Catalog number Product name Quantity
EIAAB31679 FKSG19,Homo sapiens,Human,KIAA1184,MR1,MR-1,Myofibrillogenesis regulator 1,Paroxysmal nonkinesiogenic dyskinesia protein,PNKD,Probable hydrolase PNKD,TAHCCP2,Trans-activated by hepatitis C virus core
EIAAB31680 Brp17,Fksg19,Kiaa1184,MNCb-5687,Mouse,Mr1,MR-1,Mus musculus,Myofibrillogenesis regulator 1,Paroxysmal nonkinesiogenic dyskinesia protein,Pnkd,Probable hydrolase PNKD,Tahccp2
E3165h Human Paroxysmal Nonkinesiogenic Dyskinesia ELISA 96T
PNKP PNKD Gene paroxysmal nonkinesigenic dyskinesia
EIAAB39538 Homo sapiens,Human,KIAA0610,Spartin,Spastic paraplegia 20 protein,SPG20,TAHCCP1,Trans-activated by hepatitis C virus core protein 1
CSB-EL018260MO Mouse paroxysmal nonkinesigenic dyskinesia (PNKD) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL018260HU Human paroxysmal nonkinesigenic dyskinesia (PNKD) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL018260BO Bovine paroxysmal nonkinesigenic dyskinesia (PNKD) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
PNKD_MOUSE ELISA Kit FOR Probable hydrolase PNKD; organism: Mouse; gene name: Pnkd 96T
PNKD_HUMAN ELISA Kit FOR Probable hydrolase PNKD; organism: Human; gene name: PNKD 96T
CSB-EL018260BO Bovine Probable hydrolase PNKD(PNKD) ELISA kit SpeciesBovine 96T
CSB-EL018260MO Mouse Probable hydrolase PNKD(PNKD) ELISA kit SpeciesMouse 96T
CSB-EL018260HU Human Probable hydrolase PNKD(PNKD) ELISA kit SpeciesHuman 96T
CSB-EL018260MO Mouse Probable hydrolase PNKD(PNKD) ELISA kit 96T
G1257 Probable hydrolase PNKD (PNKD), Mouse, ELISA Kit 96T
G1256 Probable hydrolase PNKD (PNKD), Human, ELISA Kit 96T
CSB-EL018260HU Human Probable hydrolase PNKD(PNKD) ELISA kit 96T
G1255 Probable hydrolase PNKD (PNKD), Bovine, ELISA Kit 96T
EIAAB31681 Bos taurus,Bovine,PNKD,Probable hydrolase PNKD
CSB-EL018260BO Bovine Probable hydrolase PNKD(PNKD) ELISA kit 96T
orb81568 Hepatitis Virus Nucleocapsid (core) 24 protein The HCV Core 24 genotype-1b, E.coli derived recombinant protein, contains the HCV core nucleocapsid immunodominant regions. The protein is fused with b-g 100
orb81633 Hepatitis B Virus Core (1-183) protein The E.coli derived 18 kDa recombinant protein contains the HBV core ayw immunodominant region, amino acids 1-183. For research use only. 100
orb81632 Hepatitis B Virus Core (1-186) protein The E.coli derived recombinant protein contains the HBV core immunodominant region amino acids 1-186, and fused to His tag. For research use only. 100
orb81556 Hepatitis Virus Nucleocapsid (core) Genotype-1b protein The E.coli derived recombinant multimer protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fus 100
orb81558 Hepatitis Virus Nucleocapsid (core) Genotype-2b protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur