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Protein

Stress-70 protein, mitochondrial

Gene

HSPA9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Chaperone protein which is implicated in the control of cell proliferation and cellular aging. Plays a role in the erythropoiesis process.2 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • erythrocyte differentiation Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of erythrocyte differentiation Source: UniProtKB
  • negative regulation of hematopoietic stem cell differentiation Source: Ensembl
  • protein export from nucleus Source: Ensembl
  • protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113013-MONOMER.
ReactomeiR-HSA-1268020. Mitochondrial protein import.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
SIGNORiP38646.

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
Short name:
MOT
Peptide-binding protein 74
Short name:
PBP74
Gene namesi
Name:HSPA9
Synonyms:GRP75, HSPA9B, mt-HSP70
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:5244. HSPA9.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • mitochondrial nucleoid Source: BHF-UCL
  • mitochondrion Source: UniProtKB
  • myelin sheath Source: Ensembl
  • nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Anemia, sideroblastic, 4 (SIDBA4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of sideroblastic anemia, a bone marrow disorder defined by the presence of pathologic iron deposits in erythroblast mitochondria. Sideroblastic anemia is characterized by anemia of varying severity, hypochromic peripheral erythrocytes, systemic iron overload secondary to chronic ineffective erythropoiesis, and the presence of bone marrow ringed sideroblasts. Sideroblasts are characterized by iron-loaded mitochondria clustered around the nucleus. SIDBA4 has been reported to be inherited as an autosomal recessive disease, with a pseudodominant pattern of inheritance in some families.
See also OMIM:182170
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076665212S → P in SIDBA4; unknown pathological significance. 1 Publication1
Natural variantiVAR_076666388G → S in SIDBA4; unknown pathological significance. 1 Publication1
Natural variantiVAR_076667415E → K in SIDBA4; unknown pathological significance. 1 Publication1
Natural variantiVAR_076668458 – 459Missing in SIDBA4. 1 Publication2
Even-plus syndrome (EVPLS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive syndrome characterized by epiphyseal and vertebral dysplasia, prenatal-onset short stature, a distinct craniofacial phenotype with microtia, a flat facial profile with flat nose and triangular nares, cardiac malformations, and additional findings such as anal atresia, hypodontia, aplasia cutis, and others.
See also OMIM:616854
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076662126R → W in EVPLS. 1 Publication1
Natural variantiVAR_076663128Y → C in EVPLS. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi3313.
MIMi182170. phenotype.
616854. phenotype.
OpenTargetsiENSG00000113013.
PharmGKBiPA162391712.

Polymorphism and mutation databases

BioMutaiHSPA9.
DMDMi21264428.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 46Mitochondrion3 PublicationsAdd BLAST46
ChainiPRO_000001356347 – 679Stress-70 protein, mitochondrialAdd BLAST633

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei76N6-acetyllysineBy similarity1
Modified residuei87PhosphothreonineCombined sources1
Modified residuei135N6-acetyllysine; alternateCombined sources1
Modified residuei135N6-succinyllysine; alternateBy similarity1
Modified residuei138N6-acetyllysine; alternateCombined sources1
Modified residuei138N6-succinyllysine; alternateBy similarity1
Modified residuei143N6-acetyllysineCombined sources1
Modified residuei206N6-acetyllysine; alternateBy similarity1
Modified residuei206N6-malonyllysine; alternate1 Publication1
Modified residuei206N6-succinyllysine; alternateBy similarity1
Modified residuei234N6-acetyllysineCombined sources1
Modified residuei288N6-acetyllysineCombined sources1
Modified residuei300N6-acetyllysine; alternateCombined sources1
Modified residuei300N6-succinyllysine; alternateBy similarity1
Modified residuei368N6-succinyllysineBy similarity1
Modified residuei394N6-succinyllysineBy similarity1
Modified residuei408PhosphoserineCombined sources1
Modified residuei513Omega-N-methylarginineCombined sources1
Modified residuei567N6-acetyllysine; alternateCombined sources1
Modified residuei567N6-succinyllysine; alternateBy similarity1
Modified residuei600N6-acetyllysine; alternateBy similarity1
Modified residuei600N6-succinyllysine; alternateBy similarity1
Modified residuei610N6-succinyllysineBy similarity1
Modified residuei612N6-acetyllysineBy similarity1
Modified residuei646N6-acetyllysine; alternateCombined sources1
Modified residuei646N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP38646.
MaxQBiP38646.
PaxDbiP38646.
PeptideAtlasiP38646.
PRIDEiP38646.
TopDownProteomicsiP38646.

2D gel databases

DOSAC-COBS-2DPAGEP38646.
OGPiP38646.
REPRODUCTION-2DPAGEIPI00007765.
SWISS-2DPAGEP38646.
UCD-2DPAGEP38646.

PTM databases

iPTMnetiP38646.
PhosphoSitePlusiP38646.
SwissPalmiP38646.

Expressioni

Gene expression databases

BgeeiENSG00000113013.
ExpressionAtlasiP38646. baseline and differential.
GenevisibleiP38646. HS.

Organism-specific databases

HPAiCAB005219.
HPA000898.

Interactioni

Subunit structurei

Interacts with FXN. Interacts with HSCB. 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. Interacts with TESPA1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005334EBI-354932,EBI-297353
NELFBQ8WX922EBI-354932,EBI-347721
TP53P046376EBI-354932,EBI-366083
TP73O1535011EBI-354932,EBI-389606
YKT6A4D2J03EBI-354932,EBI-10173443

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109545. 210 interactors.
IntActiP38646. 58 interactors.
MINTiMINT-1143092.
STRINGi9606.ENSP00000297185.

Structurei

Secondary structure

1679
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi56 – 59Combined sources4
Beta strandi62 – 71Combined sources10
Beta strandi74 – 77Combined sources4
Beta strandi91 – 93Combined sources3
Beta strandi99 – 102Combined sources4
Helixi103 – 106Combined sources4
Turni107 – 111Combined sources5
Helixi113 – 115Combined sources3
Helixi120 – 122Combined sources3
Turni123 – 125Combined sources3
Helixi131 – 139Combined sources9
Beta strandi141 – 146Combined sources6
Beta strandi148 – 156Combined sources9
Beta strandi159 – 161Combined sources3
Helixi163 – 182Combined sources20
Beta strandi188 – 193Combined sources6
Helixi199 – 211Combined sources13
Beta strandi215 – 221Combined sources7
Helixi222 – 229Combined sources8
Helixi232 – 234Combined sources3
Beta strandi236 – 245Combined sources10
Beta strandi250 – 258Combined sources9
Beta strandi261 – 270Combined sources10
Helixi275 – 294Combined sources20
Helixi302 – 318Combined sources17
Turni319 – 321Combined sources3
Beta strandi323 – 333Combined sources11
Beta strandi340 – 347Combined sources8
Helixi348 – 354Combined sources7
Helixi356 – 360Combined sources5
Helixi363 – 372Combined sources10
Turni377 – 379Combined sources3
Beta strandi382 – 387Combined sources6
Helixi388 – 391Combined sources4
Helixi393 – 403Combined sources11
Turni413 – 415Combined sources3
Helixi416 – 428Combined sources13
Beta strandi445 – 448Combined sources4
Beta strandi452 – 458Combined sources7
Beta strandi463 – 472Combined sources10
Beta strandi482 – 490Combined sources9
Helixi494 – 496Combined sources3
Beta strandi497 – 505Combined sources9
Beta strandi518 – 524Combined sources7
Beta strandi530 – 536Combined sources7
Turni537 – 539Combined sources3
Beta strandi542 – 548Combined sources7
Helixi555 – 567Combined sources13
Helixi569 – 590Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N8EX-ray2.80A/B439-597[»]
4KBOX-ray2.80A52-431[»]
ProteinModelPortaliP38646.
SMRiP38646.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38646.

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0102. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00860000133890.
HOVERGENiHBG051845.
InParanoidiP38646.
KOiK04043.
OMAiEKMAPPQ.
OrthoDBiEOG091G0386.
PhylomeDBiP38646.
TreeFamiTF105046.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK. 1 hit.
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.

P38646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISASRAAAA RLVGAAASRG PTAARHQDSW NGLSHEAFRL VSRRDYASEA
60 70 80 90 100
IKGAVVGIDL GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL
110 120 130 140 150
VGMPAKRQAV TNPNNTFYAT KRLIGRRYDD PEVQKDIKNV 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 YLTMDSSGPK HLNMKLTRAQ
360 370 380 390 400
FEGIVTDLIR RTIAPCQKAM QDAEVSKSDI 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 GSGSSGTGEQ KEDQKEEKQ
Length:679
Mass (Da):73,680
Last modified:May 27, 2002 - v2
Checksum:i90969A8D06757753
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti48S → P AA sequence (PubMed:7498169).Curated1
Sequence conflicti66C → S AA sequence (PubMed:7498169).Curated1
Sequence conflicti176E → V in BAG37618 (PubMed:14702039).Curated1
Sequence conflicti184H → R in AAH00478 (PubMed:15489334).Curated1
Sequence conflicti184H → R in AAH24034 (PubMed:15489334).Curated1
Sequence conflicti249T → A in BAD96478 (Ref. 4) Curated1
Sequence conflicti385L → P in BAD96478 (Ref. 4) Curated1
Sequence conflicti540G → R in AAA67526 (PubMed:7829505).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04648274Q → R.1 PublicationCorresponds to variant rs17856004dbSNPEnsembl.1
Natural variantiVAR_076662126R → W in EVPLS. 1 Publication1
Natural variantiVAR_049622127R → G.Corresponds to variant rs35091799dbSNPEnsembl.1
Natural variantiVAR_076663128Y → C in EVPLS. 1 Publication1
Natural variantiVAR_046483184H → Y.1 Publication1
Natural variantiVAR_076664200S → L.1 Publication1
Natural variantiVAR_076665212S → P in SIDBA4; unknown pathological significance. 1 Publication1
Natural variantiVAR_049623225A → G.Corresponds to variant rs34558740dbSNPEnsembl.1
Natural variantiVAR_076666388G → S in SIDBA4; unknown pathological significance. 1 Publication1
Natural variantiVAR_076667415E → K in SIDBA4; unknown pathological significance. 1 Publication1
Natural variantiVAR_076668458 – 459Missing in SIDBA4. 1 Publication2
Natural variantiVAR_076669539T → K.1 Publication1
Natural variantiVAR_076670573R → W.1 Publication1
Natural variantiVAR_076671577E → K.1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11066 mRNA. No translation available.
L15189 mRNA. Translation: AAA67526.1.
AK315177 mRNA. Translation: BAG37618.1.
AK222758 mRNA. Translation: BAD96478.1.
DQ531046 Genomic DNA. Translation: ABF50973.1.
CH471062 Genomic DNA. Translation: EAW62129.1.
BC000478 mRNA. Translation: AAH00478.1.
BC024034 mRNA. Translation: AAH24034.1.
CCDSiCCDS4208.1.
PIRiB48127.
RefSeqiNP_004125.3. NM_004134.6.
UniGeneiHs.184233.

Genome annotation databases

EnsembliENST00000297185; ENSP00000297185; ENSG00000113013.
GeneIDi3313.
KEGGihsa:3313.
UCSCiuc003ldf.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11066 mRNA. No translation available.
L15189 mRNA. Translation: AAA67526.1.
AK315177 mRNA. Translation: BAG37618.1.
AK222758 mRNA. Translation: BAD96478.1.
DQ531046 Genomic DNA. Translation: ABF50973.1.
CH471062 Genomic DNA. Translation: EAW62129.1.
BC000478 mRNA. Translation: AAH00478.1.
BC024034 mRNA. Translation: AAH24034.1.
CCDSiCCDS4208.1.
PIRiB48127.
RefSeqiNP_004125.3. NM_004134.6.
UniGeneiHs.184233.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N8EX-ray2.80A/B439-597[»]
4KBOX-ray2.80A52-431[»]
ProteinModelPortaliP38646.
SMRiP38646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109545. 210 interactors.
IntActiP38646. 58 interactors.
MINTiMINT-1143092.
STRINGi9606.ENSP00000297185.

PTM databases

iPTMnetiP38646.
PhosphoSitePlusiP38646.
SwissPalmiP38646.

Polymorphism and mutation databases

BioMutaiHSPA9.
DMDMi21264428.

2D gel databases

DOSAC-COBS-2DPAGEP38646.
OGPiP38646.
REPRODUCTION-2DPAGEIPI00007765.
SWISS-2DPAGEP38646.
UCD-2DPAGEP38646.

Proteomic databases

EPDiP38646.
MaxQBiP38646.
PaxDbiP38646.
PeptideAtlasiP38646.
PRIDEiP38646.
TopDownProteomicsiP38646.

Protocols and materials databases

DNASUi3313.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297185; ENSP00000297185; ENSG00000113013.
GeneIDi3313.
KEGGihsa:3313.
UCSCiuc003ldf.4. human.

Organism-specific databases

CTDi3313.
DisGeNETi3313.
GeneCardsiHSPA9.
HGNCiHGNC:5244. HSPA9.
HPAiCAB005219.
HPA000898.
MIMi182170. phenotype.
600548. gene.
616854. phenotype.
neXtProtiNX_P38646.
OpenTargetsiENSG00000113013.
PharmGKBiPA162391712.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0102. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00860000133890.
HOVERGENiHBG051845.
InParanoidiP38646.
KOiK04043.
OMAiEKMAPPQ.
OrthoDBiEOG091G0386.
PhylomeDBiP38646.
TreeFamiTF105046.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113013-MONOMER.
ReactomeiR-HSA-1268020. Mitochondrial protein import.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
SIGNORiP38646.

Miscellaneous databases

ChiTaRSiHSPA9. human.
EvolutionaryTraceiP38646.
GeneWikiiHSPA9.
GenomeRNAii3313.
PROiP38646.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113013.
ExpressionAtlasiP38646. baseline and differential.
GenevisibleiP38646. HS.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK. 1 hit.
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...

Entry informationi

Entry nameiGRP75_HUMAN
AccessioniPrimary (citable) accession number: P38646
Secondary accession number(s): B2RCM1
, P30036, P31932, Q1HB43, Q53H23, Q6GU03, Q9BWB7, Q9UC56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 27, 2002
Last modified: November 30, 2016
This is version 184 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.