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Protein

Stress-70 protein, mitochondrial

Gene

Hspa9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • fibroblast growth factor binding Source: RGD
  • heat shock protein binding Source: RGD

GO - Biological processi

  • cellular response to interleukin-1 Source: RGD
  • hemopoiesis Source: UniProtKB
  • protein folding Source: InterPro
  • response to folic acid Source: RGD
  • response to thyroxine Source: RGD
  • response to toxic substance Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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
mtHSP70
Gene namesi
Name:Hspa9
Synonyms:Grp75, Hspa9a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1311806. Hspa9.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • mitochondrion Source: RGD
  • nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionBy similarityAdd
BLAST
Chaini47 – 679633Stress-70 protein, mitochondrialPRO_0000013565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761N6-acetyllysineBy similarity
Modified residuei87 – 871PhosphothreonineBy similarity
Modified residuei135 – 1351N6-acetyllysine; alternateBy similarity
Modified residuei135 – 1351N6-succinyllysine; alternateBy similarity
Modified residuei138 – 1381N6-acetyllysine; alternateBy similarity
Modified residuei138 – 1381N6-succinyllysine; alternateBy similarity
Modified residuei143 – 1431N6-acetyllysineBy similarity
Modified residuei206 – 2061N6-acetyllysine; alternateBy similarity
Modified residuei206 – 2061N6-malonyllysine; alternateBy similarity
Modified residuei206 – 2061N6-succinyllysine; alternateBy similarity
Modified residuei234 – 2341N6-acetyllysineBy similarity
Modified residuei288 – 2881N6-acetyllysineBy similarity
Modified residuei300 – 3001N6-acetyllysine; alternateBy similarity
Modified residuei300 – 3001N6-succinyllysine; alternateBy similarity
Modified residuei360 – 3601N6-acetyllysine; alternateBy similarity
Modified residuei360 – 3601N6-succinyllysine; alternateBy similarity
Modified residuei368 – 3681N6-succinyllysineBy similarity
Modified residuei394 – 3941N6-succinyllysineBy similarity
Modified residuei408 – 4081PhosphoserineBy similarity
Modified residuei567 – 5671N6-acetyllysine; alternateBy similarity
Modified residuei567 – 5671N6-succinyllysine; alternateBy similarity
Modified residuei600 – 6001N6-acetyllysine; alternateBy similarity
Modified residuei600 – 6001N6-succinyllysine; alternateBy similarity
Modified residuei610 – 6101N6-succinyllysineBy similarity
Modified residuei612 – 6121N6-acetyllysineBy similarity
Modified residuei646 – 6461N6-acetyllysine; alternateBy similarity
Modified residuei646 – 6461N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP48721.
PRIDEiP48721.

2D gel databases

World-2DPAGE0004:P48721.

PTM databases

iPTMnetiP48721.
PhosphoSiteiP48721.

Interactioni

Subunit structurei

Interacts with FXN. Interacts with HSCB (By similarity). Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1, MTX2 and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. Interacts with DNLZ, the interaction is required to prevent self-aggregation (By similarity). Interacts with TESPA1 (By similarity).By similarity

GO - Molecular functioni

  • fibroblast growth factor binding Source: RGD
  • heat shock protein binding Source: RGD

Protein-protein interaction databases

IntActiP48721. 3 interactions.
MINTiMINT-4592308.
STRINGi10116.ENSRNOP00000026696.

Structurei

3D structure databases

ProteinModelPortaliP48721.
SMRiP48721. Positions 55-580.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0102. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228136.
HOVERGENiHBG051845.
InParanoidiP48721.
PhylomeDBiP48721.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK.
InterProiIPR012725. Chaperone_DnaK.
IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
TIGRFAMsiTIGR02350. prok_dnaK. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P48721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISASRAAAA RLVGTTASRS PAAARHQDGW NGLSHEVFRF VSRRDYASEA
60 70 80 90 100
IKGAVVGIDL GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTPDGERL
110 120 130 140 150
VGMPAKRQAV TNPNNTFYAT KRLIGRRYDD PEVQKDTKNV PFKIVRASNG
160 170 180 190 200
DAWVEAHGKL YSPSQIGAFV LMKMKETAEN YLGHTAKNAV ITVPAYFNDS
210 220 230 240 250
QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI AVYDLGGGTF
260 270 280 290 300
DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK
310 320 330 340 350
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDASGPK HLNMKLTRAQ
360 370 380 390 400
FEGIVTDLIK RTIAPCQKAM QDREVSKSDI GEVILVGGMT RMPKVQQTVQ
410 420 430 440 450
DLFGRAPSKA VNPDEAVAIG AAIQGGVLAG DVTDVLLLDV TPLSLGIETL
460 470 480 490 500
GGVFTKLINR NTTIPTKKSQ VFSTAADGQT QVEIKVCQGE REMAGDNKLL
510 520 530 540 550
GQFTLIGIPP APRGVPQIEV TFDIDANGIV HVSAKDKGTG REQQIVIQSS
560 570 580 590 600
GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK
610 620 630 640 650
DQLPADECNK LKEEISKMRE LLARKDSETG ENIRQAASSL QQASLKLFEM
660 670
AYKKMASERE GSGSSSTGEQ KEDQKEEKQ
Length:679
Mass (Da):73,858
Last modified:October 17, 2006 - v3
Checksum:i4616EDE5307691A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371V → A in AAB34982 (PubMed:7629893).Curated
Sequence conflicti81 – 811A → S in AAB33049 (PubMed:7811387).Curated
Sequence conflicti373 – 3731R → A in AAB34982 (PubMed:7629893).Curated
Sequence conflicti487 – 4871C → T AA sequence (PubMed:2372296).Curated
Sequence conflicti493 – 4931M → Q AA sequence (PubMed:2372296).Curated
Sequence conflicti589 – 5891I → V in AAB33049 (PubMed:7811387).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S75280 mRNA. Translation: AAB33049.1.
S78556 mRNA. Translation: AAB34982.1.
PIRiI56581.
UniGeneiRn.7535.

Genome annotation databases

UCSCiRGD:1311806. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S75280 mRNA. Translation: AAB33049.1.
S78556 mRNA. Translation: AAB34982.1.
PIRiI56581.
UniGeneiRn.7535.

3D structure databases

ProteinModelPortaliP48721.
SMRiP48721. Positions 55-580.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP48721. 3 interactions.
MINTiMINT-4592308.
STRINGi10116.ENSRNOP00000026696.

PTM databases

iPTMnetiP48721.
PhosphoSiteiP48721.

2D gel databases

World-2DPAGE0004:P48721.

Proteomic databases

PaxDbiP48721.
PRIDEiP48721.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:1311806. rat.

Organism-specific databases

RGDi1311806. Hspa9.

Phylogenomic databases

eggNOGiKOG0102. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228136.
HOVERGENiHBG051845.
InParanoidiP48721.
PhylomeDBiP48721.

Miscellaneous databases

PROiP48721.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK.
InterProiIPR012725. Chaperone_DnaK.
IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
TIGRFAMsiTIGR02350. prok_dnaK. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "cDNA cloning and efficient mitochondrial import of pre-mtHSP70 from rat liver."
    Webster T.J., Naylor D.J., Hartman D.J., Hoej P.B., Hoogenraad N.J.
    DNA Cell Biol. 13:1213-1220(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of rat grp75, an hsp70-family member, and its expression in normal and ischemic brain."
    Massa S.M., Longo F.M., Zuo J., Wang S., Chen J., Sharp F.R.
    J. Neurosci. Res. 40:807-819(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "A microsequencing approach to identify proteins which appear to interact with thyrotropin in rat FRTL-5 thyroid cells."
    Akamizu T., Saji M., Kohn L.D.
    Biochem. Biophys. Res. Commun. 170:351-358(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 80-98 AND 484-503.
  4. Lubec G., Vishwanath V., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 188-202; 266-284; 499-513 AND 577-595, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.

Entry informationi

Entry nameiGRP75_RAT
AccessioniPrimary (citable) accession number: P48721
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 17, 2006
Last modified: July 6, 2016
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.