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2025-05-09 18:54:51, GGRNA : RefSeq release 60 (20130726)
LOCUS NM_004134 3506 bp mRNA linear PRI 15-JUL-2013
DEFINITION Homo sapiens heat shock 70kDa protein 9 (mortalin) (HSPA9), mRNA.
ACCESSION NM_004134
VERSION NM_004134.6 GI:296080701
KEYWORDS RefSeq.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (bases 1 to 3506)
AUTHORS Rozenberg,P., Kocsis,J., Saar,M., Prohaszka,Z., Fust,G. and
Fishelson,Z.
TITLE Elevated levels of mitochondrial mortalin and cytosolic HSP70 in
blood as risk factors in patients with colorectal cancer
JOURNAL Int. J. Cancer 133 (2), 514-518 (2013)
PUBMED 23319326
REMARK GeneRIF: mortalin and cytosolic HSP70 may have roles in colorectal
cancer
REFERENCE 2 (bases 1 to 3506)
AUTHORS Tsuneki,M., Maruyama,S., Yamazaki,M., Xu,B., Essa,A., Abe,T.,
Babkair,H., Cheng,J., Yamamoto,T. and Saku,T.
TITLE Extracellular heat shock protein A9 is a novel interaction partner
of podoplanin in oral squamous cell carcinoma cells
JOURNAL Biochem. Biophys. Res. Commun. 434 (1), 124-130 (2013)
PUBMED 23541579
REMARK GeneRIF: HSPA9 secreted by oral squamous cell carcinoma cells
interacts with podoplanin (PDPN) on their cell surface in an
autocrine manner and regulates their growth and invasiveness
REFERENCE 3 (bases 1 to 3506)
AUTHORS Groleau,S.E., Lubarda,J., Thomas,N., Ferro,M.A., Pristupa,Z.B.,
Mishra,R.K. and Gabriele,J.P.
TITLE Human blood analysis reveals differences in gene expression of
catecholamine-regulated protein 40 (CRP40) in schizophrenia
JOURNAL Schizophr. Res. 143 (1), 203-206 (2013)
PUBMED 23182727
REMARK GeneRIF: These results suggest a possible functional role of CRP40
in the pathogenesis of schizophrenia.
REFERENCE 4 (bases 1 to 3506)
AUTHORS Gestl,E.E. and Anne Bottger,S.
TITLE Cytoplasmic sequestration of the tumor suppressor p53 by a heat
shock protein 70 family member, mortalin, in human colorectal
adenocarcinoma cell lines
JOURNAL Biochem. Biophys. Res. Commun. 423 (2), 411-416 (2012)
PUBMED 22683628
REMARK GeneRIF: these data reveal the characteristic cytoplasmic
sequestration of p53 by the heat shock protein mortalin in human
colorectal adenocarcinoma cell lines, as is the case for other
cancers, such as glioblastomas and hepatocellular carcinomas.
REFERENCE 5 (bases 1 to 3506)
AUTHORS Agostini,I., Popov,S., Li,J., Dubrovsky,L., Hao,T. and Bukrinsky,M.
TITLE Heat-shock protein 70 can replace viral protein R of HIV-1 during
nuclear import of the viral preintegration complex
JOURNAL Exp. Cell Res. 259 (2), 398-403 (2000)
PUBMED 10964507
REFERENCE 6 (bases 1 to 3506)
AUTHORS Kaula,S.C., Reddelb,R.R., Sugiharac,T., Mitsuia,Y. and Wadhwac,R.
TITLE Inactivation of p53 and life span extension of human diploid
fibroblasts by mot-2
JOURNAL FEBS Lett. 474 (2-3), 159-164 (2000)
PUBMED 10838077
REFERENCE 7 (bases 1 to 3506)
AUTHORS Mizukoshi,E., Suzuki,M., Loupatov,A., Uruno,T., Hayashi,H.,
Misono,T., Kaul,S.C., Wadhwa,R. and Imamura,T.
TITLE Fibroblast growth factor-1 interacts with the glucose-regulated
protein GRP75/mortalin
JOURNAL Biochem. J. 343 (PT 2), 461-466 (1999)
PUBMED 10510314
REFERENCE 8 (bases 1 to 3506)
AUTHORS Kaul,S.C., Wadhwa,R., Matsuda,Y., Hensler,P.J., Pereira-Smith,O.M.,
Komatsu,Y. and Mitsui,Y.
TITLE Mouse and human chromosomal assignments of mortalin, a novel member
of the murine hsp70 family of proteins
JOURNAL FEBS Lett. 361 (2-3), 269-272 (1995)
PUBMED 7698336
REFERENCE 9 (bases 1 to 3506)
AUTHORS Bhattacharyya,T., Karnezis,A.N., Murphy,S.P., Hoang,T.,
Freeman,B.C., Phillips,B. and Morimoto,R.I.
TITLE Cloning and subcellular localization of human mitochondrial hsp70
JOURNAL J. Biol. Chem. 270 (4), 1705-1710 (1995)
PUBMED 7829505
REFERENCE 10 (bases 1 to 3506)
AUTHORS Domanico,S.Z., DeNagel,D.C., Dahlseid,J.N., Green,J.M. and
Pierce,S.K.
TITLE Cloning of the gene encoding peptide-binding protein 74 shows that
it is a new member of the heat shock protein 70 family
JOURNAL Mol. Cell. Biol. 13 (6), 3598-3610 (1993)
PUBMED 7684501
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from DC356852.1, AC113340.2,
AK315177.1, AC011385.6 and AK225488.1.
This sequence is a reference standard in the RefSeqGene project.
On May 15, 2010 this sequence version replaced gi:156071496.
Summary: This gene encodes a member of the heat shock protein 70
gene family. The encoded protein is primarily localized to the
mitochondria but is also found in the endoplasmic reticulum, plasma
membrane and cytoplasmic vesicles. This protein is a heat-shock
cognate protein. This protein plays a role in cell proliferation,
stress response and maintenance of the mitochondria. A pseudogene
of this gene is found on chromosome 2.[provided by RefSeq, May
2010].
Sequence Note: This RefSeq record was created from transcript and
genomic sequence data to make the sequence consistent with the
reference genome assembly. The genomic coordinates used for the
transcript record were based on transcript alignments.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: L11066.1, BC000478.2 [ECO:0000332]
RNAseq introns :: mixed/partial sample support
ERS025081, ERS025082 [ECO:0000350]
##Evidence-Data-END##
##RefSeq-Attributes-START##
gene product(s) localized to mito. :: reported by MitoCarta
##RefSeq-Attributes-END##
COMPLETENESS: complete on the 3' end.
PRIMARY REFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP
1-163 DC356852.1 1-163
164-212 AC113340.2 77983-78031
213-837 AK315177.1 1-625
838-838 AC011385.6 79577-79577
839-1066 AK315177.1 627-854
1067-1067 AC011385.6 81386-81386
1068-2351 AK315177.1 856-2139
2352-3053 AK225488.1 1699-2400
3054-3506 AC011385.6 93176-93628
FEATURES Location/Qualifiers
source 1..3506
/organism="Homo sapiens"
/mol_type="mRNA"
/db_xref="taxon:9606"
/chromosome="5"
/map="5q31.1"
gene 1..3506
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/note="heat shock 70kDa protein 9 (mortalin)"
/db_xref="GeneID:3313"
/db_xref="HGNC:5244"
/db_xref="HPRD:02770"
/db_xref="MIM:600548"
exon 1..392
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
misc_feature 21..23
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/note="upstream in-frame stop codon"
variation 106
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="g"
/db_xref="dbSNP:41294550"
variation 297
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="g"
/db_xref="dbSNP:17523658"
CDS 312..2351
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/note="p66-mortalin; peptide-binding protein 74; mortalin,
perinuclear; heat shock 70kD protein 9B; stress-70
protein, mitochondrial; mortalin-2; 75 kDa
glucose-regulated protein"
/codon_start=1
/product="stress-70 protein, mitochondrial precursor"
/protein_id="NP_004125.3"
/db_xref="GI:24234688"
/db_xref="CCDS:CCDS4208.1"
/db_xref="GeneID:3313"
/db_xref="HGNC:5244"
/db_xref="HPRD:02770"
/db_xref="MIM:600548"
/translation="
MISASRAAAARLVGAAASRGPTAARHQDSWNGLSHEAFRLVSRRDYASEAIKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDSSGPKHLNMKLTRAQFEGIVTDLIRRTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLKEEISKMRELLARKDSETGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSGTGEQKEDQKEEKQ
"
transit_peptide 312..449
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
mat_peptide 450..2348
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/product="stress-70 protein, mitochondrial"
misc_feature 465..2279
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/note="molecular chaperone DnaK; Provisional; Region:
dnaK; PRK00290"
/db_xref="CDD:178963"
misc_feature 465..1556
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/note="Nucleotide-binding domain of human HSPA9,
Escherichia coli DnaK, and similar proteins; Region:
HSPA9-like_NBD; cd11733"
/db_xref="CDD:212683"
misc_feature order(492..503,672..674,975..977,1047..1052,1056..1058,
1134..1136,1248..1250,1257..1259,1269..1271,1470..1478,
1482..1484)
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/note="nucleotide binding site [chemical binding]; other
site"
/db_xref="CDD:212683"
misc_feature order(546..548,555..557,609..611,621..623,630..635,
639..644,849..860,1218..1220,1227..1232,1239..1241,
1293..1295,1299..1304)
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/note="NEF interaction site [polypeptide binding]; other
site"
/db_xref="CDD:212683"
misc_feature 714..716
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-acetyllysine; propagated from
UniProtKB/Swiss-Prot (P38646.2); acetylation site"
misc_feature 723..725
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-acetyllysine; propagated from
UniProtKB/Swiss-Prot (P38646.2); acetylation site"
misc_feature 738..740
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-acetyllysine; propagated from
UniProtKB/Swiss-Prot (P38646.2); acetylation site"
misc_feature order(906..911,915..920,963..968,972..974,1095..1106)
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/note="SBD interface [polypeptide binding]; other site"
/db_xref="CDD:212683"
misc_feature 909..911
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="phosphorylation site"
misc_feature 927..929
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-malonyllysine; propagated from
UniProtKB/Swiss-Prot (P38646.2); modified site"
misc_feature 1011..1013
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-acetyllysine; propagated from
UniProtKB/Swiss-Prot (P38646.2); acetylation site"
misc_feature 1173..1175
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-acetyllysine; propagated from
UniProtKB/Swiss-Prot (P38646.2); acetylation site"
misc_feature 1209..1211
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-acetyllysine; propagated from
UniProtKB/Swiss-Prot (P38646.2); acetylation site"
misc_feature 1770..1772
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="S-nitrosylation site; modified site"
misc_feature 2010..2012
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-acetyllysine; propagated from
UniProtKB/Swiss-Prot (P38646.2); acetylation site"
misc_feature 2013..2015
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="phosphorylation site"
misc_feature 2247..2249
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/experiment="experimental evidence, no additional details
recorded"
/note="N6-acetyllysine; propagated from
UniProtKB/Swiss-Prot (P38646.2); acetylation site"
variation 332
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="g"
/replace="t"
/db_xref="dbSNP:36043650"
variation 387
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="t"
/db_xref="dbSNP:41294552"
exon 393..451
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
exon 452..539
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
STS 455..698
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/standard_name="BARC0023"
/db_xref="UniSTS:255309"
exon 540..721
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
variation 554
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="t"
/db_xref="dbSNP:34916633"
variation 690
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="g"
/db_xref="dbSNP:35091799"
exon 722..846
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
exon 847..920
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
exon 921..1027
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
variation 985
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="g"
/db_xref="dbSNP:34558740"
STS 987..1124
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/standard_name="GDB:451580"
/db_xref="UniSTS:157317"
exon 1028..1190
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
variation 1085
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="a"
/replace="g"
/db_xref="dbSNP:41295717"
exon 1191..1283
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
variation 1259
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="a"
/replace="g"
/db_xref="dbSNP:1042665"
exon 1284..1493
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
exon 1494..1721
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
exon 1722..1826
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
variation 1748
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="a"
/replace="g"
/db_xref="dbSNP:41296451"
exon 1827..1944
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
exon 1945..2039
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
exon 2040..2132
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
STS 2120..2305
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/standard_name="RH69016"
/db_xref="UniSTS:9454"
exon 2133..2273
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
variation 2192
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="t"
/db_xref="dbSNP:1042686"
variation 2244
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="t"
/db_xref="dbSNP:10117"
exon 2274..3506
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/inference="alignment:Splign:1.39.8"
STS 2293..2436
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/standard_name="RH67940"
/db_xref="UniSTS:91334"
STS 2442..3221
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/standard_name="HSPA9B_1300"
/db_xref="UniSTS:280768"
variation 2550
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="a"
/replace="c"
/db_xref="dbSNP:1042803"
polyA_site 2560
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
STS 2654..3002
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/standard_name="D5S2414"
/db_xref="UniSTS:11900"
STS 2733..2828
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/standard_name="Bda02f10"
/db_xref="UniSTS:88698"
STS 2767..2905
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/standard_name="A002P41"
/db_xref="UniSTS:40617"
variation 2961
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="t"
/db_xref="dbSNP:1042981"
variation 2971
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="t"
/db_xref="dbSNP:41296457"
polyA_signal 3031..3036
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
polyA_site 3053
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
STS 3208..3398
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/standard_name="D5S1564E"
/db_xref="UniSTS:10884"
variation 3342
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace="c"
/replace="t"
/db_xref="dbSNP:41296461"
variation 3360
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
/replace=""
/replace="gtttttagatctctaacatgaaa"
/db_xref="dbSNP:41296459"
polyA_signal 3478..3483
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
polyA_site 3506
/gene="HSPA9"
/gene_synonym="CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2;
MTHSP75; PBP74"
ORIGIN
ttcctcccctggactctttctgagctcagagccgccgcagccgggacaggagggcaggctttctccaaccatcatgctgcggagcatattacctgtacgccctggctccgggagcggcagtcgagtatcctctggtcaggcggcgcgggcggcgcctcagcggaagagcgggcctctgggccgcagtgaccaacccccgcccctcaccccacgtggttggaggtttccagaagcgctgccgccaccgcatcgcgcagctctttgccgtcggagcgcttgtttgctgcctcgtactcctccatttatccgccatgataagtgccagccgagctgcagcagcccgtctcgtgggcgccgcagcctcccggggccctacggccgcccgccaccaggatagctggaatggccttagtcatgaggcttttagacttgtttcaaggcgggattatgcatcagaagcaatcaagggagcagttgttggtattgatttgggtactaccaactcctgcgtggcagttatggaaggtaaacaagcaaaggtgctggagaatgccgaaggtgccagaaccaccccttcagttgtggcctttacagcagatggtgagcgacttgttggaatgccggccaagcgacaggctgtcaccaacccaaacaatacattttatgctaccaagcgtctcattggccggcgatatgatgatcctgaagtacagaaagacattaaaaatgttccctttaaaattgtccgtgcctccaatggtgatgcctgggttgaggctcatgggaaattgtattctccgagtcagattggagcatttgtgttgatgaagatgaaagagactgcagaaaattacttggggcacacagcaaaaaatgctgtgatcacagtcccagcttatttcaatgactcgcagagacaggccactaaagatgctggccagatatctggactgaatgtgcttcgggtgattaatgagcccacagctgctgctcttgcctatggtctagacaaatcagaagacaaagtcattgctgtatatgatttaggtggtggaacttttgatatttctatcctggaaattcagaaaggagtatttgaggtgaaatccacaaatggggataccttcttaggtggggaagactttgaccaggccttgctacggcacattgtgaaggagttcaagagagagacaggggttgatttgactaaagacaacatggcacttcagagggtacgggaagctgctgaaaaggctaaatgtgaactctcctcatctgtgcagactgacatcaatttgccctatcttacaatggattcttctggacccaagcatttgaatatgaagttgacccgtgctcaatttgaagggattgtcactgatctaatcagaaggactatcgctccatgccaaaaagctatgcaagatgcagaagtcagcaagagtgacataggagaagtgattcttgtgggtggcatgactaggatgcccaaggttcagcagactgtacaggatctttttggcagagccccaagtaaagctgtcaatcctgatgaggctgtggccattggagctgccattcagggaggtgtgttggccggcgatgtcacggatgtgctgctccttgatgtcactcccctgtctctgggtattgaaactctaggaggtgtctttaccaaacttattaataggaataccactattccaaccaagaagagccaggtattctctactgccgctgatggtcaaacgcaagtggaaattaaagtgtgtcagggtgaaagagagatggctggagacaacaaactccttggacagtttactttgattggaattccaccagcccctcgtggagttcctcagattgaagttacatttgacattgatgccaatgggatagtacatgtttctgctaaagataaaggcacaggacgtgagcagcagattgtaatccagtcttctggtggattaagcaaagatgatattgaaaatatggttaaaaatgcagagaaatatgctgaagaagaccggcgaaagaaggaacgagttgaagcagttaatatggctgaaggaatcattcacgacacagaaaccaagatggaagaattcaaggaccaattacctgctgatgagtgcaacaagctgaaagaagagatttccaaaatgagggagctcctggctagaaaagacagcgaaacaggagaaaatattagacaggcagcatcctctcttcagcaggcatcactgaagctgttcgaaatggcatacaaaaagatggcatctgagcgagaaggctctggaagttctggcactggggaacaaaaggaagatcaaaaggaggaaaaacagtaataatagcagaaattttgaagccagaaggacaacatatgaagcttaggagtgaagagacttcctgagcagaaatgggcgaacttcagtctttttactgtgtttttgcagtattctatatataatttccttaatttgtaaatttagtgaccattagctagtgatcatttaatggacagtgattctaacagtataaagttcacaatattctatgtccctagcctgtcatttttcagctgcatgtaaaaggaggtaggatgaattgatcattataaagatttaactattttatgctgaagtgaccatattttcaaggggtgaaaccatctcgcacacagcaatgaaggtagtcatccatagacttgaaatgagaccacatatggggatgagatccttctagttagcctagtactgctgtactggcctgtatgtacatggggtccttcaactgaggccttgcaagtcaagctggctgtgccatgtttgtagatggggcagaggaatctagaacaatgggaaacttagctatttatattaggtacagctattaaaacaaggtaggaatgaggctagacctttaacttccctaaggcatacttttctagctaccttctgccctgtgtctggcacctacatccttgatgattgttctcttacccattctggaatttttttttttttaaataaatacagaaagcatcttgatctcttgtttgtgaggggtgatgccctgagatttagcttcaagaatatgccatggctcatgcttcccatatttcccaaagagggaaatacaggatttgctaacactggttaaaaatgcaaattcaagatttggaagggctgttataatgaaataatgagcagtatcagcatgtgcaaatcttgtttgaaggattttattttctccccttagacctttggtacatttagaatcttgaaagtttctagatctctaacatgaaagtttctagatctctaacatgaaagtttttagatctctaacatgaaaaccaaggtggctattttcaggttgctttcagctccaagtagaaataaccagaattggcttacattaaagaaactgcatctagaaataagtcctaagatactatttctatggctcaaaaataaaaggaacccagatttctttcccta
//
ANNOTATIONS from NCBI Entrez Gene (20130726):
GeneID:3313 -> Molecular function: GO:0005515 [protein binding] evidence: IPI
GeneID:3313 -> Molecular function: GO:0005524 [ATP binding] evidence: IEA
GeneID:3313 -> Molecular function: GO:0019899 [enzyme binding] evidence: IEA
GeneID:3313 -> Molecular function: GO:0051082 [unfolded protein binding] evidence: TAS
GeneID:3313 -> Biological process: GO:0006457 [protein folding] evidence: IEA
GeneID:3313 -> Biological process: GO:0006611 [protein export from nucleus] evidence: IEA
GeneID:3313 -> Biological process: GO:0006626 [protein targeting to mitochondrion] evidence: TAS
GeneID:3313 -> Biological process: GO:0043066 [negative regulation of apoptotic process] evidence: TAS
GeneID:3313 -> Biological process: GO:0044267 [cellular protein metabolic process] evidence: TAS
GeneID:3313 -> Cellular component: GO:0005730 [nucleolus] evidence: IEA
GeneID:3313 -> Cellular component: GO:0005737 [cytoplasm] evidence: TAS
GeneID:3313 -> Cellular component: GO:0005739 [mitochondrion] evidence: IDA
GeneID:3313 -> Cellular component: GO:0005739 [mitochondrion] evidence: TAS
GeneID:3313 -> Cellular component: GO:0009986 [cell surface] evidence: IDA
GeneID:3313 -> Cellular component: GO:0042645 [mitochondrial nucleoid] evidence: IDA
by
@meso_cacase at
DBCLS
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