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P38647 (GRP75_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stress-70 protein, mitochondrial
Alternative name(s):
75 kDa glucose-regulated protein
Short name=GRP-75
Heat shock 70 kDa protein 9
Mortalin
Peptide-binding protein 74
Short name=PBP74
p66 MOT
Gene names
Name:Hspa9
Synonyms:Grp75, Hsp74, Hspa9a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length679 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone. HAMAP-Rule MF_00332

Subunit structure

Interacts with FXN. Interacts with HSCB By similarity. Component of the MINOS/MitOS complex, that includes IMMT, HSPA9 and CHCHD3 and associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2. Interacts with DNLZ, the interaction is required to prevent self-aggregation By similarity. Interacts with TESPA1 By similarity. HAMAP-Rule MF_00332

Subcellular location

Mitochondrion. Nucleusnucleolus By similarity Ref.13.

Tissue specificity

Found in all the cell types examined.

Induction

Not induced by heat shock, instead protein level is decreased. HAMAP-Rule MF_00332

Polymorphism

Two forms of the protein have been found, MOT-1, found in mortal cells and MOT-2, found in immortal cells. The sequence of MOT-2 is shown here. HAMAP-Rule MF_00332

Sequence similarities

Belongs to the heat shock protein 70 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion Ref.11
Chain47 – 679633Stress-70 protein, mitochondrial HAMAP-Rule MF_00332
PRO_0000013564

Amino acid modifications

Modified residue761N6-acetyllysine Ref.15
Modified residue1351N6-acetyllysine; alternate Ref.14 Ref.15
Modified residue1351N6-succinyllysine; alternate Ref.14
Modified residue1381N6-acetyllysine; alternate Ref.15
Modified residue1381N6-succinyllysine; alternate Ref.14
Modified residue1431N6-acetyllysine By similarity
Modified residue2061N6-acetyllysine; alternate Ref.15
Modified residue2061N6-malonyllysine; alternate By similarity
Modified residue2061N6-succinyllysine; alternate Ref.14
Modified residue2341N6-acetyllysine Ref.15
Modified residue2881N6-acetyllysine Ref.15
Modified residue3001N6-acetyllysine; alternate Ref.14 Ref.15
Modified residue3001N6-succinyllysine; alternate Ref.14
Modified residue3601N6-acetyllysine; alternate Ref.14 Ref.15
Modified residue3601N6-succinyllysine; alternate Ref.14
Modified residue3681N6-succinyllysine Ref.14
Modified residue3941N6-succinyllysine Ref.14
Modified residue5671N6-acetyllysine; alternate Ref.14 Ref.15
Modified residue5671N6-succinyllysine; alternate Ref.14
Modified residue6001N6-acetyllysine; alternate Ref.15
Modified residue6001N6-succinyllysine; alternate Ref.14
Modified residue6101N6-succinyllysine Ref.14
Modified residue6121N6-acetyllysine Ref.15
Modified residue6461N6-acetyllysine; alternate Ref.15
Modified residue6461N6-succinyllysine; alternate Ref.14

Natural variations

Natural variant6181M → V in MOT-1.
Natural variant6241G → R in MOT-1.

Experimental info

Sequence conflict51S → T AA sequence Ref.4
Sequence conflict781L → Q in BAE21690. Ref.7
Sequence conflict1061K → R AA sequence Ref.4
Sequence conflict1501G → S in BAE35373. Ref.7
Sequence conflict5221F → S AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
P38647 [UniParc].

Last modified October 3, 2012. Version 3.
Checksum: DF1C997775627928

FASTA67973,461
        10         20         30         40         50         60 
MISASRAAAA RLVGTAASRS PAAARPQDGW NGLSHEAFRF VSRRDYASEA IKGAVVGIDL 

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

       130        140        150        160        170        180 
KRLIGRRYDD PEVQKDTKNV 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 YLTMDASGPK HLNMKLTRAQ FEGIVTDLIK 

       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 LKEEISKMRA LLAGKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE 

       670 
GSGSSGTGEQ KEDQKEEKQ 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype."
Wadhwa R., Kaul S.C., Ikawa Y., Sugimoto Y.
J. Biol. Chem. 268:6615-6621(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD-1-ICR.
Tissue: Embryonic fibroblast.
[2]Wadhwa R.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 123.
[3]"Induction of cellular senescence by transfection of cytosolic mortalin cDNA in NIH 3T3 cells."
Wadhwa R., Kaul S.C., Sugimoto Y., Mitsui Y.
J. Biol. Chem. 268:22239-22242(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CD-1-ICR.
Tissue: Embryonic fibroblast.
[4]"Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family."
Domanico S.Z., Denagel D.C., Dahlseid J.N., Green J.M., Pierce S.K.
Mol. Cell. Biol. 13:3598-3610(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: B-cell.
[5]"Structure and organization of the gene encoding a mouse mitochondrial stress-70 protein."
Michikawa Y., Baba T., Arai Y., Sakakura T., Kusakabe M.
FEBS Lett. 336:27-33(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
Tissue: Liver.
[6]"Antigenic protein specific for C3H strain mouse is a mitochondrial stress-70 protein."
Michikawa Y., Baba T., Arai Y., Sakakura T., Tanaka M., Kusakabe M.
Biochem. Biophys. Res. Commun. 196:223-232(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H/HeN.
Tissue: Kidney.
[7]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and DBA/2.
Tissue: Embryo, Kidney and Liver.
[8]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[9]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[11]"Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 47-70.
Tissue: Fibroblast.
[12]Lubec G., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 188-202; 266-284; 349-360; 395-405 AND 499-513, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
[13]"PBP74, a new member of the mammalian 70-kDa heat shock protein family, is a mitochondrial protein."
Dahlseid J.N., Lill R., Green J.M., Xu X., Qiu Y., Pierce S.K.
Mol. Biol. Cell 5:1265-1275(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-300; LYS-360 AND LYS-567, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-138; LYS-206; LYS-300; LYS-360; LYS-368; LYS-394; LYS-567; LYS-600; LYS-610 AND LYS-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[15]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-135; LYS-138; LYS-206; LYS-234; LYS-288; LYS-300; LYS-360; LYS-567; LYS-600; LYS-612 AND LYS-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D11089 mRNA. Translation: BAA01862.2.
L06896 mRNA. No translation available.
D17666 Genomic DNA. Translation: BAA04548.1.
D17556 mRNA. Translation: BAA04493.1.
AK004946 mRNA. Translation: BAB23690.1.
AK002634 mRNA. Translation: BAB22248.1.
AK133501 mRNA. Translation: BAE21690.1.
AK137109 mRNA. Translation: BAE23238.1.
AK145965 mRNA. Translation: BAE26790.1.
AK159791 mRNA. Translation: BAE35373.1.
AK165958 mRNA. Translation: BAE38486.1.
AK167856 mRNA. Translation: BAE39874.1.
AC114820 Genomic DNA. No translation available.
AC131675 Genomic DNA. No translation available.
CH466557 Genomic DNA. Translation: EDK97122.1.
BC052727 mRNA. Translation: AAH52727.1.
BC057343 mRNA. Translation: AAH57343.1.
CCDSCCDS29138.1.
PIRA48127. S39839.
RefSeqNP_034611.2. NM_010481.2.
UniGeneMm.209419.

3D structure databases

ProteinModelPortalP38647.
SMRP38647. Positions 54-651.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200457. 20 interactions.
IntActP38647. 16 interactions.
MINTMINT-1860030.
STRING10090.ENSMUSP00000025217.

PTM databases

PhosphoSiteP38647.

2D gel databases

COMPLUYEAST-2DPAGEP38647.
REPRODUCTION-2DPAGEIPI00133903.
P38647.
SWISS-2DPAGEP38647.

Proteomic databases

PaxDbP38647.
PRIDEP38647.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025217; ENSMUSP00000025217; ENSMUSG00000024359.
GeneID15526.
KEGGmmu:15526.
UCSCuc008elv.2. mouse.

Organism-specific databases

CTD3313.
MGIMGI:96245. Hspa9.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00750000117237.
HOGENOMHOG000228136.
HOVERGENHBG051845.
InParanoidP38647.
KOK04043.
OMAQRDVAIM.
OrthoDBEOG715Q3K.
TreeFamTF105046.

Gene expression databases

CleanExMM_HSPA9.
GenevestigatorP38647.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPMF_00332. DnaK.
InterProIPR012725. Chaperone_DnaK.
IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100920. SSF100920. 1 hit.
TIGRFAMsTIGR02350. prok_dnaK. 1 hit.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSPA9. mouse.
NextBio288444.
PROP38647.
SOURCESearch...

Entry information

Entry nameGRP75_MOUSE
AccessionPrimary (citable) accession number: P38647
Secondary accession number(s): Q3TW93 expand/collapse secondary AC list , Q3UVN1, Q3V015, Q7TSZ0, Q9CQ05
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot