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Tyrosine--tRNA ligase, cytoplasmic (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) [Cleaved into: Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed]

 SYYC_HUMAN              Reviewed;         528 AA.
P54577; B3KWK4; D3DPQ4; O43276; Q53EN1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
28-MAR-2018, entry version 192.
RecName: Full=Tyrosine--tRNA ligase, cytoplasmic;
EC=6.1.1.1;
AltName: Full=Tyrosyl-tRNA synthetase;
Short=TyrRS;
Contains:
RecName: Full=Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed;
Name=YARS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8552597; DOI=10.1073/pnas.93.1.166;
Ribas de Pouplana L., Frugier M., Quinn C.L., Schimmel P.;
"Evidence that two present-day components needed for the genetic code
appeared after nucleated cells separated from eubacteria.";
Proc. Natl. Acad. Sci. U.S.A. 93:166-170(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9162081; DOI=10.1074/jbc.272.22.14420;
Kleeman T.A., Wei D., Simpson K.L., First E.A.;
"Human tyrosyl-tRNA synthetase shares amino acid sequence homology
with a putative cytokine.";
J. Biol. Chem. 272:14420-14425(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone, and Lung;
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).
[7]
PROTEIN SEQUENCE OF 2-16.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
PROTEIN SEQUENCE OF 2-16, ACETYLATION AT GLY-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND GLY-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197; LYS-206; LYS-474;
LYS-482 AND LYS-490, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-386, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF 1-342, AND SUBUNIT.
PubMed=12427973; DOI=10.1073/pnas.242611799;
Yang X.-L., Skene R.J., McRee D.E., Schimmel P.;
"Crystal structure of a human aminoacyl-tRNA synthetase cytokine.";
Proc. Natl. Acad. Sci. U.S.A. 99:15369-15374(2002).
[16]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-364 IN COMPLEX WITH
TYROSINE.
PubMed=14671330; DOI=10.1073/pnas.2136794100;
Yang X.-L., Otero F.J., Skene R.J., McRee D.E., Schimmel P.,
Ribas de Pouplana L.;
"Crystal structures that suggest late development of genetic code
components for differentiating aromatic side chains.";
Proc. Natl. Acad. Sci. U.S.A. 100:15376-15380(2003).
[17]
SUBCELLULAR LOCATION, VARIANTS CMTDIC 153-VAL--VAL-156 DEL; ARG-41 AND
LYS-196, AND CHARACTERIZATION OF VARIANTS CMTDIC ARG-41 AND LYS-196.
PubMed=16429158; DOI=10.1038/ng1727;
Jordanova A., Irobi J., Thomas F.P., Van Dijck P., Meerschaert K.,
Dewil M., Dierick I., Jacobs A., De Vriendt E., Guergueltcheva V.,
Rao C.V., Tournev I., Gondim F.A.A., D'Hooghe M., Van Gerwen V.,
Callaerts P., Van Den Bosch L., Timmermans J.-P., Robberecht W.,
Gettemans J., Thevelein J.M., De Jonghe P., Kremensky I.,
Timmerman V.;
"Disrupted function and axonal distribution of mutant tyrosyl-tRNA
synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy.";
Nat. Genet. 38:197-202(2006).
[18]
VARIANT LYS-274.
PubMed=24627108; DOI=10.1007/s00415-014-7289-8;
Schabhuettl M., Wieland T., Senderek J., Baets J., Timmerman V.,
De Jonghe P., Reilly M.M., Stieglbauer K., Laich E., Windhager R.,
Erwa W., Trajanoski S., Strom T.M., Auer-Grumbach M.;
"Whole-exome sequencing in patients with inherited neuropathies:
outcome and challenges.";
J. Neurol. 261:970-982(2014).
-!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a
two-step reaction: tyrosine is first activated by ATP to form Tyr-
AMP and then transferred to the acceptor end of tRNA(Tyr).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP +
diphosphate + L-tyrosyl-tRNA(Tyr).
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12427973,
ECO:0000269|PubMed:14671330}.
-!- INTERACTION:
P09874:PARP1; NbExp=5; IntAct=EBI-1048893, EBI-355676;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16429158}.
-!- DISEASE: Charcot-Marie-Tooth disease, dominant, intermediate type,
C (CMTDIC) [MIM:608323]: A form of Charcot-Marie-Tooth disease, a
disorder of the peripheral nervous system, characterized by
progressive weakness and atrophy, initially of the peroneal
muscles and later of the distal muscles of the arms. The dominant
intermediate type C is characterized by clinical and pathologic
features intermediate between demyelinating and axonal peripheral
neuropathies, and motor median nerve conduction velocities ranging
from 25 to 45 m/sec. {ECO:0000269|PubMed:16429158}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB39406.1; Type=Frameshift; Positions=354; Evidence={ECO:0000305};
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EMBL; U40714; AAB39406.1; ALT_FRAME; mRNA.
EMBL; U89436; AAB88409.1; -; mRNA.
EMBL; AK125213; BAG54166.1; -; mRNA.
EMBL; AK223608; BAD97328.1; -; mRNA.
EMBL; CH471059; EAX07506.1; -; Genomic_DNA.
EMBL; CH471059; EAX07507.1; -; Genomic_DNA.
EMBL; BC001933; AAH01933.1; -; mRNA.
EMBL; BC004151; AAH04151.1; -; mRNA.
EMBL; BC016689; AAH16689.1; -; mRNA.
CCDS; CCDS368.1; -.
RefSeq; NP_003671.1; NM_003680.3.
UniGene; Hs.213264; -.
PDB; 1N3L; X-ray; 1.18 A; A=1-364.
PDB; 1NTG; X-ray; 2.21 A; A/B/C/D=359-528.
PDB; 1Q11; X-ray; 1.60 A; A=1-364.
PDB; 4Q93; X-ray; 2.10 A; A=1-364.
PDB; 4QBT; X-ray; 2.10 A; A=1-364.
PDB; 5THH; X-ray; 1.96 A; A=4-342.
PDB; 5THL; X-ray; 1.60 A; A=1-364.
PDBsum; 1N3L; -.
PDBsum; 1NTG; -.
PDBsum; 1Q11; -.
PDBsum; 4Q93; -.
PDBsum; 4QBT; -.
PDBsum; 5THH; -.
PDBsum; 5THL; -.
ProteinModelPortal; P54577; -.
SMR; P54577; -.
BioGrid; 114134; 58.
DIP; DIP-50415N; -.
IntAct; P54577; 25.
MINT; P54577; -.
STRING; 9606.ENSP00000362576; -.
BindingDB; P54577; -.
ChEMBL; CHEMBL3179; -.
DrugBank; DB01766; Beta-(2-Naphthyl)-Alanine.
DrugBank; DB00135; L-Tyrosine.
DrugBank; DB07205; N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE.
DrugBank; DB08371; PARA-(BENZOYL)-PHENYLALANINE.
DrugBank; DB03978; Tyrosinal.
CarbonylDB; P54577; -.
iPTMnet; P54577; -.
PhosphoSitePlus; P54577; -.
SwissPalm; P54577; -.
BioMuta; YARS; -.
DMDM; 13638438; -.
REPRODUCTION-2DPAGE; IPI00007074; -.
EPD; P54577; -.
MaxQB; P54577; -.
PaxDb; P54577; -.
PeptideAtlas; P54577; -.
PRIDE; P54577; -.
DNASU; 8565; -.
Ensembl; ENST00000373477; ENSP00000362576; ENSG00000134684.
GeneID; 8565; -.
KEGG; hsa:8565; -.
UCSC; uc001bvy.2; human.
CTD; 8565; -.
DisGeNET; 8565; -.
EuPathDB; HostDB:ENSG00000134684.10; -.
GeneCards; YARS; -.
HGNC; HGNC:12840; YARS.
HPA; HPA017936; -.
HPA; HPA018950; -.
HPA; HPA018954; -.
MalaCards; YARS; -.
MIM; 603623; gene.
MIM; 608323; phenotype.
neXtProt; NX_P54577; -.
OpenTargets; ENSG00000134684; -.
Orphanet; 100045; Autosomal dominant intermediate Charcot-Marie-Tooth disease type C.
PharmGKB; PA37431; -.
eggNOG; KOG2144; Eukaryota.
eggNOG; KOG2241; Eukaryota.
eggNOG; COG0073; LUCA.
eggNOG; COG0162; LUCA.
GeneTree; ENSGT00790000123100; -.
HOGENOM; HOG000228237; -.
HOVERGEN; HBG080113; -.
InParanoid; P54577; -.
KO; K01866; -.
OMA; YIGFEIS; -.
OrthoDB; EOG091G03XO; -.
PhylomeDB; P54577; -.
TreeFam; TF300898; -.
BRENDA; 6.1.1.1; 2681.
Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
ChiTaRS; YARS; human.
EvolutionaryTrace; P54577; -.
GeneWiki; YARS; -.
GenomeRNAi; 8565; -.
PMAP-CutDB; P54577; -.
PRO; PR:P54577; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134684; -.
CleanEx; HS_YARS; -.
ExpressionAtlas; P54577; baseline and differential.
Genevisible; P54577; HS.
GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IBA:GO_Central.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005153; F:interleukin-8 receptor binding; TAS:ProtInc.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0004871; F:signal transducer activity; NAS:ProtInc.
GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
GO; GO:0004831; F:tyrosine-tRNA ligase activity; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; IBA:GO_Central.
GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; TAS:ProtInc.
CDD; cd00805; TyrRS_core; 1.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR002305; aa-tRNA-synth_Ic.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR002547; tRNA-bd_dom.
InterPro; IPR002307; Tyr-tRNA-ligase.
Pfam; PF00579; tRNA-synt_1b; 1.
Pfam; PF01588; tRNA_bind; 1.
PRINTS; PR01040; TRNASYNTHTYR.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR00234; tyrS; 1.
PROSITE; PS50886; TRBD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
Charcot-Marie-Tooth disease; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Ligase;
Neurodegeneration; Neuropathy; Nucleotide-binding; Phosphoprotein;
Polymorphism; Protein biosynthesis; Reference proteome; RNA-binding;
tRNA-binding.
CHAIN 1 528 Tyrosine--tRNA ligase, cytoplasmic.
/FTId=PRO_0000423285.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.8}.
CHAIN 2 528 Tyrosine--tRNA ligase, cytoplasmic, N-
terminally processed.
/FTId=PRO_0000055673.
DOMAIN 364 468 tRNA-binding. {ECO:0000255|PROSITE-
ProRule:PRU00209}.
MOTIF 44 52 "HIGH" region.
MOTIF 222 226 "KMSKS" region.
BINDING 39 39 Tyrosine. {ECO:0000244|PDB:4QBT,
ECO:0000269|PubMed:14671330}.
BINDING 166 166 Tyrosine. {ECO:0000244|PDB:4QBT,
ECO:0000269|PubMed:14671330}.
BINDING 170 170 Tyrosine. {ECO:0000244|PDB:4QBT,
ECO:0000269|PubMed:14671330}.
BINDING 173 173 Tyrosine. {ECO:0000244|PDB:4QBT,
ECO:0000269|PubMed:14671330}.
BINDING 188 188 Tyrosine. {ECO:0000244|PDB:4QBT,
ECO:0000269|PubMed:14671330}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 2 2 N-acetylglycine; in Tyrosine--tRNA
ligase, cytoplasmic, N-terminally
processed. {ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.8}.
MOD_RES 197 197 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 206 206 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 386 386 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 474 474 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 482 482 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 490 490 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 41 41 G -> R (in CMTDIC; partial loss of
activity; dbSNP:rs121908833).
{ECO:0000269|PubMed:16429158}.
/FTId=VAR_026681.
VARIANT 153 156 Missing (in CMTDIC).
{ECO:0000269|PubMed:16429158}.
/FTId=VAR_026682.
VARIANT 170 170 Q -> H (in dbSNP:rs2128600).
/FTId=VAR_026683.
VARIANT 196 196 E -> K (in CMTDIC; partial loss of
activity; dbSNP:rs121908834).
{ECO:0000269|PubMed:16429158}.
/FTId=VAR_026684.
VARIANT 274 274 E -> K (found in a patient with
hereditary motor and sensory neuropathy;
unknown pathological significance;
dbSNP:rs758897498).
{ECO:0000269|PubMed:24627108}.
/FTId=VAR_073292.
CONFLICT 143 143 H -> R (in Ref. 4; BAD97328).
{ECO:0000305}.
HELIX 7 15 {ECO:0000244|PDB:1N3L}.
STRAND 19 22 {ECO:0000244|PDB:1N3L}.
HELIX 24 31 {ECO:0000244|PDB:1N3L}.
STRAND 37 42 {ECO:0000244|PDB:1N3L}.
HELIX 50 52 {ECO:0000244|PDB:1N3L}.
HELIX 53 64 {ECO:0000244|PDB:1N3L}.
STRAND 68 73 {ECO:0000244|PDB:1N3L}.
HELIX 75 80 {ECO:0000244|PDB:1N3L}.
TURN 81 84 {ECO:0000244|PDB:1N3L}.
HELIX 87 108 {ECO:0000244|PDB:1N3L}.
STRAND 115 119 {ECO:0000244|PDB:1N3L}.
HELIX 120 122 {ECO:0000244|PDB:1N3L}.
TURN 123 125 {ECO:0000244|PDB:1N3L}.
HELIX 127 137 {ECO:0000244|PDB:1N3L}.
HELIX 142 148 {ECO:0000244|PDB:1N3L}.
TURN 149 152 {ECO:0000244|PDB:1N3L}.
HELIX 161 176 {ECO:0000244|PDB:1N3L}.
STRAND 180 185 {ECO:0000244|PDB:1N3L}.
HELIX 186 188 {ECO:0000244|PDB:1N3L}.
HELIX 189 198 {ECO:0000244|PDB:1N3L}.
HELIX 199 202 {ECO:0000244|PDB:1N3L}.
STRAND 208 212 {ECO:0000244|PDB:1N3L}.
HELIX 238 246 {ECO:0000244|PDB:1N3L}.
STRAND 247 249 {ECO:0000244|PDB:1Q11}.
HELIX 259 266 {ECO:0000244|PDB:1N3L}.
TURN 267 273 {ECO:0000244|PDB:1N3L}.
STRAND 275 277 {ECO:0000244|PDB:1N3L}.
HELIX 281 283 {ECO:0000244|PDB:1N3L}.
STRAND 287 291 {ECO:0000244|PDB:1N3L}.
HELIX 292 300 {ECO:0000244|PDB:1N3L}.
HELIX 306 327 {ECO:0000244|PDB:1N3L}.
HELIX 331 340 {ECO:0000244|PDB:1N3L}.
HELIX 365 367 {ECO:0000244|PDB:1NTG}.
STRAND 370 380 {ECO:0000244|PDB:1NTG}.
STRAND 388 393 {ECO:0000244|PDB:1NTG}.
STRAND 395 398 {ECO:0000244|PDB:1NTG}.
STRAND 400 405 {ECO:0000244|PDB:1NTG}.
TURN 407 409 {ECO:0000244|PDB:1NTG}.
HELIX 412 414 {ECO:0000244|PDB:1NTG}.
TURN 415 417 {ECO:0000244|PDB:1NTG}.
STRAND 419 423 {ECO:0000244|PDB:1NTG}.
STRAND 429 431 {ECO:0000244|PDB:1NTG}.
STRAND 434 436 {ECO:0000244|PDB:1NTG}.
STRAND 442 454 {ECO:0000244|PDB:1NTG}.
STRAND 466 469 {ECO:0000244|PDB:1NTG}.
STRAND 479 481 {ECO:0000244|PDB:1NTG}.
HELIX 483 485 {ECO:0000244|PDB:1NTG}.
HELIX 487 492 {ECO:0000244|PDB:1NTG}.
STRAND 495 497 {ECO:0000244|PDB:1NTG}.
STRAND 501 505 {ECO:0000244|PDB:1NTG}.
STRAND 508 512 {ECO:0000244|PDB:1NTG}.
STRAND 526 528 {ECO:0000244|PDB:1NTG}.
SEQUENCE 528 AA; 59143 MW; 00C7E88843905780 CRC64;
MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKIYW GTATTGKPHV AYFVPMSKIA
DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRVSYYENV IKAMLESIGV PLEKLKFIKG
TDYQLSKEYT LDVYRLSSVV TQHDSKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD
AQFGGIDQRK IFTFAEKYLP ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED
VKKKLKKAFC EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT AYVDLEKDFA
AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPM AKGPAKNSEP
EEVIPSRLDI RVGKIITVEK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV
VVLCNLKPQK MRGVESQGML LCASIEGINR QVEPLDPPAG SAPGEHVFVK GYEKGQPDEE
LKPKKKVFEK LQADFKISEE CIAQWKQTNF MTKLGSISCK SLKGGNIS


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