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UniProtKB/Swiss-Prot entry P38646


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GRP75_HUMAN
Primary accession number P38646
Secondary accession numbers B2RCM1 P30036 P31932 Q1HB43 Q53H23 Q6GU03 Q9BWB7 Q9UC56
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on May 27, 2002 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 98)
Name and origin of the protein
Protein name Stress-70 protein, mitochondrial [Precursor]
Synonyms 75 kDa glucose-regulated protein
GRP 75
Heat shock 70 kDa protein 9
Peptide-binding protein 74
PBP74
Mortalin
MOT
Gene name
Name: HSPA9
Synonyms: GRP75, HSPA9B
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=B-cell;
PubMed=7684501 [NCBI, ExPASy, EBI, Israel, Japan]
Domanico S.Z., Denagel D.C., Dahlseid J.N., Green J.M., Pierce S.K.;
"Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family.";
Mol. Cell. Biol. 13:3598-3610(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.270.4.1705; PubMed=7829505 [NCBI, ExPASy, EBI, Israel, Japan]
Bhattacharyya T., Karnezis A.N., Murphy S.P., Hoang T., Freeman B.C., Phillips B., Morimoto R.I.;
"Cloning and subcellular localization of human mitochondrial hsp70.";
J. Biol. Chem. 270:1705-1710(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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].
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-184.
NIEHS SNPs program;
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-74.
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
PROTEIN SEQUENCE OF 47-68.
TISSUE=Colon carcinoma;
DOI=10.1002/elps.1150180344; PubMed=9150948 [NCBI, ExPASy, EBI, Israel, Japan]
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[9]
PROTEIN SEQUENCE OF 47-66.
TISSUE=Mammary gland;
DOI=10.1002/elps.11501601202; PubMed=7498169 [NCBI, ExPASy, EBI, Israel, Japan]
Giometti C.S., Tollaksen S.L., Chubb C., Williams C., Huberman E.;
"Analysis of proteins from human breast epithelial cells using two-dimensional gel electrophoresis.";
Electrophoresis 16:1215-1224(1995).
[10]
PROTEIN SEQUENCE OF 47-56.
TISSUE=Liver;
DOI=10.1002/elps.11501301201; PubMed=1286669 [NCBI, ExPASy, EBI, Israel, Japan]
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[11]
SEQUENCE REVISION.
TISSUE=Liver;
DOI=10.1002/elps.11501401181; PubMed=8313870 [NCBI, ExPASy, EBI, Israel, Japan]
Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.;
"Human liver protein map: update 1993.";
Electrophoresis 14:1216-1222(1993).
[12]
PROTEIN SEQUENCE OF 86-99; 108-121; 160-173; 188-202; 207-234; 349-360; 378-391; 395-405; 469-485; 499-513 AND 542-555, AND MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-568, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[14]
INTERACTION WITH FXN.
DOI=10.1093/hmg/ddm038; PubMed=17331979 [NCBI, ExPASy, EBI, Israel, Japan]
Shan Y., Napoli E., Cortopassi G.;
"Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones.";
Hum. Mol. Genet. 16:929-941(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L11066; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
L15189; AAA67526.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK315177; BAG37618.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222758; BAD96478.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ531046; ABF50973.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471062; EAW62129.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000478; AAH00478.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024034; AAH24034.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00007765; -.
PIR B48127; B48127.
RefSeq NP_004125.3; -.
UniGene Hs.184233
3D structure databases
HSSP P04475; 1DG4. [HSSP ENTRY / PDB]
ModBase P38646.
Protein-protein interaction databases
IntAct P38646; 36.
PTM databases
PhosphoSite P38646; -.
2D gel databases
SWISS-2DPAGE P38646; -.
DOSAC-COBS-2DPAGE P38646; -.
HSC-2DPAGE P38646; -.
OGP P38646; -.
PHCI-2DPAGE P38646; -.
REPRODUCTION-2DPAGE IPI00007765; -.
Siena-2DPAGE P38646; -.
Organism-specific databases
GeneCards GC05M137920; -.
H-InvDB HIX0005214; -.
HGNC HGNC:5244; HSPA9.
GenAtlas HSPA9.
HPA CAB005219; -.
HPA000898; -.
MIM 600548; gene. [NCBI / EBI]
Gene expression databases
ArrayExpress P38646; -.
Bgee P38646; -.
GermOnline ENSG00000113013; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0042645; Cellular component: mitochondrial nucleoid (inferred from direct assay from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051082; Molecular function: unfolded protein binding (traceable author statement from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from UniProtKB).
GO:0006457; Biological process: protein folding (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR012725; DnaK_prok.
IPR018181; Heat_shock_70_CS.
IPR001023; Hsp70.
IPR013126; Hsp_70.
Graphical view of domain structure.
PANTHER PTHR19375; Hsp70; 1.
Pfam PF00012; HSP70; 1.
Pfam graphical view of domain structure.
PRINTS PR00301; HEATSHOCK70.
ProDom PD000089; Hsp70; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR02350; prok_dnaK; 1.
PROSITE PS00297; HSP70_1; 1.
PS00329; HSP70_2; 1.
PS01036; HSP70_3; 1.
Proteomic databases
PRIDE P38646; -.
Genome annotation databases
Ensembl ENSG00000113013; Homo sapiens. [Contig view]
GeneID 3313; -.
KEGG hsa:3313; -.
Phylogenomic databases
HOVERGEN P38646; -.
OMA P38646; ANNGDAW.
Other
NextBio 13142; -.
SOURCE HSPA9; Homo sapiens.
ProtoNet P38646.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; ATP-binding; Chaperone; Direct protein sequencing; Mitochondrion; Nucleotide-binding; Phosphoprotein; Polymorphism; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    46  46     Mitochondrion. 
CHAIN   47   679  633     Stress-70 protein, mitochondrial. PRO_0000013563
MOD_RES   200   200        Phosphoserine. 
MOD_RES   288   288        N6-acetyllysine (By similarity). 
MOD_RES   300   300        N6-acetyllysine (By similarity). 
MOD_RES   568   568        Phosphotyrosine. 
VARIANT   74    74  1     Q -> R (in dbSNP:rs17856004 [NCBI]). VAR_046482 
VARIANT   127   127  1     R -> G (in dbSNP:rs35091799 [NCBI]). VAR_049622 
VARIANT   184   184  1     H -> Y. VAR_046483 
VARIANT   225   225  1     A -> G (in dbSNP:rs34558740 [NCBI]). VAR_049623 
CONFLICT   48    48        S -> P (in Ref. 9; AA sequence). 
CONFLICT   66    66        C -> S (in Ref. 9; AA sequence). 
CONFLICT   176   176        E -> V (in Ref. 3; BAG37618). 
CONFLICT   184   184        H -> R (in Ref. 7; AAH00478/AAH24034). 
CONFLICT   249   249        T -> A (in Ref. 4; BAD96478). 
CONFLICT   385   385        L -> P (in Ref. 4; BAD96478). 
CONFLICT   540   540        G -> R (in Ref. 2; AAA67526). 
Sequence information
Length: 679 AA [This is the length of the unprocessed precursor] Molecular weight: 73680 Da [This is the MW of the unprocessed precursor] CRC64: 90969A8D06757753 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MISASRAAAA RLVGAAASRG PTAARHQDSW NGLSHEAFRL VSRRDYASEA IKGAVVGIDL 

        70         80         90        100        110        120 
GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL VGMPAKRQAV TNPNNTFYAT 

       130        140        150        160        170        180 
KRLIGRRYDD PEVQKDIKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN 

       190        200        210        220        230        240 
YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI 

       250        260        270        280        290        300 
AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK 

       310        320        330        340        350        360 
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDSSGPK HLNMKLTRAQ FEGIVTDLIR 

       370        380        390        400        410        420 
RTIAPCQKAM QDAEVSKSDI GEVILVGGMT RMPKVQQTVQ DLFGRAPSKA VNPDEAVAIG 

       430        440        450        460        470        480 
AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTKLINR NTTIPTKKSQ VFSTAADGQT 

       490        500        510        520        530        540 
QVEIKVCQGE REMAGDNKLL GQFTLIGIPP APRGVPQIEV TFDIDANGIV HVSAKDKGTG 

       550        560        570        580        590        600 
REQQIVIQSS GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK 

       610        620        630        640        650        660 
DQLPADECNK LKEEISKMRE LLARKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE 

       670 
GSGSSGTGEQ KEDQKEEKQ 

P38646 in FASTA format

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