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Histidine--tRNA ligase, cytoplasmic (EC 6.1.1.21) (Histidyl-tRNA synthetase) (HisRS)

 SYHC_HUMAN              Reviewed;         509 AA.
P12081; B4DHQ1; B4DY73; D6REN6; J3KNE5;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 2.
23-MAY-2018, entry version 194.
RecName: Full=Histidine--tRNA ligase, cytoplasmic;
EC=6.1.1.21;
AltName: Full=Histidyl-tRNA synthetase;
Short=HisRS;
Name=HARS; Synonyms=HRS;
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 1).
PubMed=1549469; DOI=10.1093/nar/20.5.1075;
Raben N., Borriello F., Amin J., Horwitz R., Fraser D., Plotz P.;
"Human histidyl-tRNA synthetase: recognition of amino acid signature
regions in class 2a aminoacyl-tRNA synthetases.";
Nucleic Acids Res. 20:1075-1081(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3554142; DOI=10.1093/nar/15.8.3349;
Tsui F.W.L., Siminovitch L.;
"Isolation, structure and expression of mammalian genes for histidyl-
tRNA synthetase.";
Nucleic Acids Res. 15:3349-3367(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Caudate nucleus, and Testis;
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] (ISOFORM 4).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
"Homo sapiens protein coding cDNA.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Uterus;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
PubMed=8406012; DOI=10.1016/0378-1119(93)90294-D;
Tsui H.W., Mok S., de Souza L., Martin A., Tsui F.W.L.;
"Transcriptional analyses of the gene region that encodes human
histidyl-tRNA synthetase: identification of a novel bidirectional
regulatory element.";
Gene 131:201-208(1993).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
PubMed=7755634; DOI=10.1006/bbrc.1995.1696;
O'Hanlon T.P., Raben N., Miller F.W.;
"A novel gene oriented in a head-to-head configuration with the human
histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a
polypeptide homologous to HRS.";
Biochem. Biophys. Res. Commun. 210:556-566(1995).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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]
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).
[11]
INVOLVEMENT IN CMT2W, VARIANTS GLU-5; ASP-205 AND ARG-376, VARIANTS
CMT2W GLN-137; ALA-238 AND SER-505, AND CHARACTERIZATION OF VARIANT
CMT2W GLN-137.
PubMed=22930593; DOI=10.1002/humu.22210;
NISC comparative sequencing program;
Vester A., Velez-Ruiz G., McLaughlin H.M., Lupski J.R., Talbot K.,
Vance J.M., Zuchner S., Roda R.H., Fischbeck K.H., Biesecker L.G.,
Nicholson G., Beg A.A., Antonellis A.;
"A loss-of-function variant in the human histidyl-tRNA synthetase
(HARS) gene is neurotoxic in vivo.";
Hum. Mutat. 34:191-199(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND 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).
[13]
FUNCTION, INVOLVEMENT IN CMT2W, VARIANTS CMT2W ILE-132; HIS-134;
GLU-175 AND TYR-364, AND CHARACTERIZATION OF VARIANTS CMT2W ILE-132;
HIS-134; GLU-175 AND TYR-364.
PubMed=26072516; DOI=10.1093/brain/awv158;
Safka Brozkova D., Deconinck T., Griffin L.B., Ferbert A.,
Haberlova J., Mazanec R., Lassuthova P., Roth C., Pilunthanakul T.,
Rautenstrauss B., Janecke A.R., Zavadakova P., Chrast R., Rivolta C.,
Zuchner S., Antonellis A., Beg A.A., De Jonghe P., Senderek J.,
Seeman P., Baets J.;
"Loss of function mutations in HARS cause a spectrum of inherited
peripheral neuropathies.";
Brain 138:2161-2172(2015).
[14]
STRUCTURE BY NMR OF 1-60.
RIKEN structural genomics initiative (RSGI);
"Solution structures of the WHEP-TRS domain of human histidyl-tRNA
synthetase.";
Submitted (NOV-2005) to the PDB data bank.
[15] {ECO:0000244|PDB:4PHC}
X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) IN COMPLEX WITH L-HISTIDINE,
AND SUBUNIT.
PubMed=25151410; DOI=10.1016/j.biochi.2014.08.005;
Koh C.Y., Wetzel A.B., de van der Schueren W.J., Hol W.G.;
"Comparison of histidine recognition in human and trypanosomatid
histidyl-tRNA synthetases.";
Biochimie 106:111-120(2014).
[16] {ECO:0000244|PDB:4X5O}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND SUBUNIT.
Kim Y.K., Chang J.E., Kim S., Jeon Y.H.;
"Structural characteristics of human histidyl-tRNA synthetase.";
Biodesign 2:142-148(2015).
[17]
VARIANT USH3B SER-454.
PubMed=22279524; DOI=10.1371/journal.pone.0028936;
Puffenberger E.G., Jinks R.N., Sougnez C., Cibulskis K., Willert R.A.,
Achilly N.P., Cassidy R.P., Fiorentini C.J., Heiken K.F.,
Lawrence J.J., Mahoney M.H., Miller C.J., Nair D.T., Politi K.A.,
Worcester K.N., Setton R.A., Dipiazza R., Sherman E.A., Eastman J.T.,
Francklyn C., Robey-Bond S., Rider N.L., Gabriel S., Morton D.H.,
Strauss K.A.;
"Genetic mapping and exome sequencing identify variants associated
with five novel diseases.";
PLoS ONE 7:E28936-E28936(2012).
-!- FUNCTION: Cytoplasmic histidine--tRNA ligase (Probable). Plays a
role in axon guidance. {ECO:0000269|PubMed:26072516, ECO:0000305}.
-!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP +
diphosphate + L-histidyl-tRNA(His).
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25151410,
ECO:0000269|Ref.16}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1057566, EBI-1057566;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P12081-1; Sequence=Displayed;
Name=2;
IsoId=P12081-2; Sequence=VSP_045118;
Name=3;
IsoId=P12081-3; Sequence=VSP_045118, VSP_046662;
Name=4;
IsoId=P12081-4; Sequence=VSP_046662;
-!- TISSUE SPECIFICITY: Brain, heart, liver and kidney.
-!- DISEASE: Usher syndrome 3B (USH3B) [MIM:614504]: A syndrome
characterized by progressive vision and hearing loss during early
childhood. Some patients have the so-called 'Charles Bonnet
syndrome,' involving decreased visual acuity and vivid visual
hallucinations. USH is a genetically heterogeneous condition
characterized by the association of retinitis pigmentosa with
sensorineural deafness. Age at onset and differences in auditory
and vestibular function distinguish Usher syndrome type 1 (USH1),
Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3).
USH3 is characterized by postlingual, progressive hearing loss,
variable vestibular dysfunction, and onset of retinitis pigmentosa
symptoms, including nyctalopia, constriction of the visual fields,
and loss of central visual acuity, usually by the second decade of
life. {ECO:0000269|PubMed:22279524}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Charcot-Marie-Tooth disease 2W (CMT2W) [MIM:616625]: An
autosomal dominant, axonal 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. Charcot-
Marie-Tooth disease is classified in two main groups on the basis
of electrophysiologic properties and histopathology: primary
peripheral demyelinating neuropathies (designated CMT1 when they
are dominantly inherited) and primary peripheral axonal
neuropathies (CMT2). Neuropathies of the CMT2 group are
characterized by signs of axonal degeneration in the absence of
obvious myelin alterations, normal or slightly reduced nerve
conduction velocities, and progressive distal muscle weakness and
atrophy. CMT2W patients manifest a peripheral neuropathy mainly
affecting the lower limbs and resulting in gait difficulties and
distal sensory impairment. Most patients also have upper limb
involvement. {ECO:0000269|PubMed:22930593,
ECO:0000269|PubMed:26072516}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA28956.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; Z11518; CAA77607.1; -; mRNA.
EMBL; X05345; CAA28956.1; ALT_FRAME; mRNA.
EMBL; AK295219; BAG58213.1; -; mRNA.
EMBL; AK302295; BAG63635.1; -; mRNA.
EMBL; AK225776; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC116353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011807; AAH11807.1; -; mRNA.
EMBL; BC080514; AAH80514.1; -; mRNA.
EMBL; M96646; AAA58668.1; -; Genomic_DNA.
EMBL; U18936; AAA73973.1; -; Genomic_DNA.
CCDS; CCDS4237.1; -. [P12081-1]
CCDS; CCDS58976.1; -. [P12081-2]
CCDS; CCDS58977.1; -. [P12081-3]
CCDS; CCDS58978.1; -. [P12081-4]
PIR; I37559; SYHUHT.
RefSeq; NP_001244969.1; NM_001258040.2. [P12081-2]
RefSeq; NP_001244970.1; NM_001258041.2. [P12081-4]
RefSeq; NP_001244971.1; NM_001258042.2. [P12081-3]
RefSeq; NP_002100.2; NM_002109.5. [P12081-1]
UniGene; Hs.528050; -.
PDB; 1X59; NMR; -; A=1-60.
PDB; 2LW7; NMR; -; A=2-60, A=399-509.
PDB; 4G84; X-ray; 2.40 A; A/B=54-506.
PDB; 4G85; X-ray; 3.11 A; A/B=1-506.
PDB; 4PHC; X-ray; 2.84 A; A/B/C/D=1-509.
PDB; 4X5O; X-ray; 2.80 A; A/B=1-509.
PDBsum; 1X59; -.
PDBsum; 2LW7; -.
PDBsum; 4G84; -.
PDBsum; 4G85; -.
PDBsum; 4PHC; -.
PDBsum; 4X5O; -.
ProteinModelPortal; P12081; -.
SMR; P12081; -.
BioGrid; 109285; 51.
DIP; DIP-37596N; -.
IntAct; P12081; 4.
MINT; P12081; -.
STRING; 9606.ENSP00000425634; -.
BindingDB; P12081; -.
ChEMBL; CHEMBL4002; -.
DrugBank; DB00117; L-Histidine.
iPTMnet; P12081; -.
PhosphoSitePlus; P12081; -.
SwissPalm; P12081; -.
BioMuta; HARS; -.
DMDM; 135123; -.
EPD; P12081; -.
MaxQB; P12081; -.
PaxDb; P12081; -.
PeptideAtlas; P12081; -.
PRIDE; P12081; -.
Ensembl; ENST00000307633; ENSP00000304668; ENSG00000170445. [P12081-3]
Ensembl; ENST00000438307; ENSP00000411511; ENSG00000170445. [P12081-2]
Ensembl; ENST00000457527; ENSP00000387893; ENSG00000170445. [P12081-4]
Ensembl; ENST00000504156; ENSP00000425634; ENSG00000170445. [P12081-1]
GeneID; 3035; -.
KEGG; hsa:3035; -.
UCSC; uc003lgv.6; human. [P12081-1]
CTD; 3035; -.
DisGeNET; 3035; -.
EuPathDB; HostDB:ENSG00000170445.12; -.
GeneCards; HARS; -.
HGNC; HGNC:4816; HARS.
HPA; HPA036539; -.
MalaCards; HARS; -.
MIM; 142810; gene.
MIM; 614504; phenotype.
MIM; 616625; phenotype.
neXtProt; NX_P12081; -.
OpenTargets; ENSG00000170445; -.
Orphanet; 231183; Usher syndrome type 3.
PharmGKB; PA29191; -.
eggNOG; KOG1936; Eukaryota.
eggNOG; COG0124; LUCA.
GeneTree; ENSGT00390000005922; -.
HOGENOM; HOG000018075; -.
HOVERGEN; HBG002731; -.
InParanoid; P12081; -.
KO; K01892; -.
OMA; CDFDFIG; -.
OrthoDB; EOG091G05P3; -.
PhylomeDB; P12081; -.
TreeFam; TF300652; -.
BRENDA; 6.1.1.21; 2681.
Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
ChiTaRS; HARS; human.
EvolutionaryTrace; P12081; -.
GeneWiki; HARS; -.
GenomeRNAi; 3035; -.
PRO; PR:P12081; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000170445; -.
CleanEx; HS_HARS; -.
ExpressionAtlas; P12081; baseline and differential.
Genevisible; P12081; HS.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004821; F:histidine-tRNA ligase activity; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
GO; GO:0006412; P:translation; NAS:UniProtKB.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
CDD; cd00859; HisRS_anticodon; 1.
Gene3D; 3.40.50.800; -; 1.
HAMAP; MF_00127; His_tRNA_synth; 1.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004154; Anticodon-bd.
InterPro; IPR036621; Anticodon-bd_dom_sf.
InterPro; IPR015807; His-tRNA-ligase.
InterPro; IPR004516; HisRS/HisZ.
InterPro; IPR033656; HisRS_anticodon.
InterPro; IPR009068; S15_NS1_RNA-bd.
InterPro; IPR000738; WHEP-TRS_dom.
PANTHER; PTHR11476; PTHR11476; 1.
Pfam; PF03129; HGTP_anticodon; 1.
Pfam; PF00458; WHEP-TRS; 1.
PIRSF; PIRSF001549; His-tRNA_synth; 1.
SMART; SM00991; WHEP-TRS; 1.
SUPFAM; SSF47060; SSF47060; 1.
TIGRFAMs; TIGR00442; hisS; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE; PS00762; WHEP_TRS_1; 1.
PROSITE; PS51185; WHEP_TRS_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Aminoacyl-tRNA synthetase; ATP-binding; Charcot-Marie-Tooth disease;
Complete proteome; Cytoplasm; Deafness; Disease mutation; Ligase;
Neurodegeneration; Neuropathy; Nucleotide-binding; Phosphoprotein;
Polymorphism; Protein biosynthesis; Reference proteome;
Retinitis pigmentosa; Usher syndrome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 509 Histidine--tRNA ligase, cytoplasmic.
/FTId=PRO_0000136332.
DOMAIN 3 59 WHEP-TRS.
REGION 130 132 L-histidine binding.
{ECO:0000244|PDB:4PHC,
ECO:0000269|PubMed:25151410}.
REGION 330 331 L-histidine binding.
{ECO:0000244|PDB:4PHC,
ECO:0000269|PubMed:25151410}.
BINDING 157 157 L-histidine. {ECO:0000244|PDB:4PHC,
ECO:0000269|PubMed:25151410}.
BINDING 173 173 L-histidine. {ECO:0000244|PDB:4PHC,
ECO:0000269|PubMed:25151410}.
BINDING 177 177 L-histidine. {ECO:0000244|PDB:4PHC,
ECO:0000269|PubMed:25151410}.
BINDING 326 326 L-histidine. {ECO:0000244|PDB:4PHC,
ECO:0000269|PubMed:25151410}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 60 99 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045118.
VAR_SEQ 155 174 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.4}.
/FTId=VSP_046662.
VARIANT 5 5 A -> E (in dbSNP:rs78741041).
{ECO:0000269|PubMed:22930593}.
/FTId=VAR_069021.
VARIANT 132 132 T -> I (in CMT2W; loss-of-function
mutation; dbSNP:rs143473232).
{ECO:0000269|PubMed:26072516}.
/FTId=VAR_075064.
VARIANT 134 134 P -> H (in CMT2W; loss-of-function
mutation; dbSNP:rs863225122).
{ECO:0000269|PubMed:26072516}.
/FTId=VAR_075065.
VARIANT 137 137 R -> Q (in CMT2W; has a neurotoxic effect
in an animal model; results in loss of
function; dbSNP:rs191391414).
{ECO:0000269|PubMed:22930593}.
/FTId=VAR_069022.
VARIANT 175 175 D -> E (in CMT2W; hypomorphic mutation;
dbSNP:rs863225123).
{ECO:0000269|PubMed:26072516}.
/FTId=VAR_075066.
VARIANT 205 205 G -> D (in dbSNP:rs147288996).
{ECO:0000269|PubMed:22930593}.
/FTId=VAR_069023.
VARIANT 238 238 V -> A (in CMT2W; unknown pathological
significance; dbSNP:rs536175170).
{ECO:0000269|PubMed:22930593}.
/FTId=VAR_069024.
VARIANT 364 364 D -> Y (in CMT2W; loss-of-function
mutation; dbSNP:rs863225124).
{ECO:0000269|PubMed:26072516}.
/FTId=VAR_075067.
VARIANT 376 376 K -> R (in dbSNP:rs139447495).
{ECO:0000269|PubMed:22930593}.
/FTId=VAR_069025.
VARIANT 399 399 A -> V (in dbSNP:rs34732372).
/FTId=VAR_061908.
VARIANT 454 454 Y -> S (in USH3B; dbSNP:rs387906639).
{ECO:0000269|PubMed:22279524}.
/FTId=VAR_067918.
VARIANT 505 505 P -> S (in CMT2W; unknown pathological
significance; dbSNP:rs747156884).
{ECO:0000269|PubMed:22930593}.
/FTId=VAR_069026.
CONFLICT 6 6 A -> P (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 126 126 S -> P (in Ref. 3; BAG58213).
{ECO:0000305}.
CONFLICT 165 165 R -> G (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 181 181 N -> Q (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 186 186 I -> N (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 191 191 C -> S (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 206 206 D -> N (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 223 223 I -> V (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 227 227 S -> P (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 284 284 L -> V (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 347 347 A -> E (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 373 374 KG -> QR (in Ref. 2; CAA28956).
{ECO:0000305}.
CONFLICT 375 375 R -> L (in Ref. 3; BAG58213).
{ECO:0000305}.
CONFLICT 493 493 D -> E (in Ref. 2; CAA28956).
{ECO:0000305}.
HELIX 2 23 {ECO:0000244|PDB:1X59}.
HELIX 28 45 {ECO:0000244|PDB:1X59}.
HELIX 67 86 {ECO:0000244|PDB:4G84}.
STRAND 96 99 {ECO:0000244|PDB:4G84}.
HELIX 100 103 {ECO:0000244|PDB:4G84}.
TURN 104 106 {ECO:0000244|PDB:4PHC}.
HELIX 109 113 {ECO:0000244|PDB:4PHC}.
STRAND 120 122 {ECO:0000244|PDB:4X5O}.
STRAND 125 127 {ECO:0000244|PDB:4G84}.
HELIX 132 141 {ECO:0000244|PDB:4G84}.
STRAND 147 156 {ECO:0000244|PDB:4G84}.
STRAND 163 165 {ECO:0000244|PDB:4X5O}.
STRAND 169 180 {ECO:0000244|PDB:4G84}.
HELIX 186 202 {ECO:0000244|PDB:4G84}.
STRAND 207 213 {ECO:0000244|PDB:4G84}.
HELIX 214 224 {ECO:0000244|PDB:4G84}.
HELIX 228 238 {ECO:0000244|PDB:4G84}.
HELIX 239 242 {ECO:0000244|PDB:4G84}.
HELIX 246 255 {ECO:0000244|PDB:4G84}.
HELIX 261 271 {ECO:0000244|PDB:4G84}.
STRAND 274 276 {ECO:0000244|PDB:4G84}.
HELIX 277 283 {ECO:0000244|PDB:4G84}.
HELIX 287 290 {ECO:0000244|PDB:4G84}.
HELIX 293 311 {ECO:0000244|PDB:4G84}.
HELIX 315 317 {ECO:0000244|PDB:4G84}.
STRAND 318 321 {ECO:0000244|PDB:4G84}.
TURN 328 330 {ECO:0000244|PDB:4G84}.
STRAND 332 342 {ECO:0000244|PDB:4G84}.
STRAND 352 362 {ECO:0000244|PDB:4G84}.
HELIX 367 369 {ECO:0000244|PDB:4G84}.
STRAND 371 373 {ECO:0000244|PDB:4G85}.
STRAND 379 384 {ECO:0000244|PDB:4G84}.
HELIX 386 398 {ECO:0000244|PDB:4G84}.
TURN 399 401 {ECO:0000244|PDB:4G84}.
STRAND 411 414 {ECO:0000244|PDB:4G84}.
STRAND 416 419 {ECO:0000244|PDB:4G84}.
HELIX 421 433 {ECO:0000244|PDB:4G84}.
STRAND 438 440 {ECO:0000244|PDB:4G85}.
STRAND 442 445 {ECO:0000244|PDB:4X5O}.
HELIX 448 458 {ECO:0000244|PDB:4G84}.
STRAND 462 465 {ECO:0000244|PDB:4G84}.
HELIX 468 473 {ECO:0000244|PDB:4G84}.
STRAND 475 480 {ECO:0000244|PDB:4G84}.
TURN 481 483 {ECO:0000244|PDB:4G84}.
STRAND 486 490 {ECO:0000244|PDB:4G84}.
HELIX 491 493 {ECO:0000244|PDB:4G84}.
HELIX 494 502 {ECO:0000244|PDB:4G84}.
SEQUENCE 509 AA; 57411 MW; 65D8BB71CE79B1FF CRC64;
MAERAALEEL VKLQGERVRG LKQQKASAEL IEEEVAKLLK LKAQLGPDES KQKFVLKTPK
GTRDYSPRQM AVREKVFDVI IRCFKRHGAE VIDTPVFELK ETLMGKYGED SKLIYDLKDQ
GGELLSLRYD LTVPFARYLA MNKLTNIKRY HIAKVYRRDN PAMTRGRYRE FYQCDFDIAG
NFDPMIPDAE CLKIMCEILS SLQIGDFLVK VNDRRILDGM FAICGVSDSK FRTICSSVDK
LDKVSWEEVK NEMVGEKGLA PEVADRIGDY VQQHGGVSLV EQLLQDPKLS QNKQALEGLG
DLKLLFEYLT LFGIDDKISF DLSLARGLDY YTGVIYEAVL LQTPAQAGEE PLGVGSVAAG
GRYDGLVGMF DPKGRKVPCV GLSIGVERIF SIVEQRLEAL EEKIRTTETQ VLVASAQKKL
LEERLKLVSE LWDAGIKAEL LYKKNPKLLN QLQYCEEAGI PLVAIIGEQE LKDGVIKLRS
VTSREEVDVR REDLVEEIKR RTGQPLCIC


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