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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

Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone.1 Publication

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

  • cellular response to interleukin-1 Source: Ensembl
  • erythrocyte differentiation Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of erythrocyte differentiation Source: UniProtKB
  • protein export from nucleus Source: Ensembl
  • protein folding Source: InterPro
  • response to toxic substance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Organism-specific databases

PharmGKBiPA162391712.

Polymorphism and mutation databases

BioMutaiHSPA9.
DMDMi21264428.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646Mitochondrion3 PublicationsAdd
BLAST
Chaini47 – 679633Stress-70 protein, mitochondrialPRO_0000013563Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761N6-acetyllysineBy similarity
Modified residuei87 – 871PhosphothreonineCombined sources
Modified residuei135 – 1351N6-acetyllysine; alternateCombined sources
Modified residuei135 – 1351N6-succinyllysine; alternateBy similarity
Modified residuei138 – 1381N6-acetyllysine; alternateCombined sources
Modified residuei138 – 1381N6-succinyllysine; alternateBy similarity
Modified residuei143 – 1431N6-acetyllysineCombined sources
Modified residuei206 – 2061N6-acetyllysine; alternateBy similarity
Modified residuei206 – 2061N6-malonyllysine; alternate1 Publication
Modified residuei206 – 2061N6-succinyllysine; alternateBy similarity
Modified residuei234 – 2341N6-acetyllysineCombined sources
Modified residuei288 – 2881N6-acetyllysineCombined sources
Modified residuei300 – 3001N6-acetyllysine; alternateCombined sources
Modified residuei300 – 3001N6-succinyllysine; alternateBy similarity
Modified residuei368 – 3681N6-succinyllysineBy similarity
Modified residuei394 – 3941N6-succinyllysineBy similarity
Modified residuei408 – 4081PhosphoserineCombined sources
Modified residuei567 – 5671N6-acetyllysine; alternateCombined sources
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; alternateCombined sources
Modified residuei646 – 6461N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, 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.
PhosphoSiteiP38646.
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. 208 interactions.
IntActiP38646. 56 interactions.
MINTiMINT-1143092.
STRINGi9606.ENSP00000297185.

Structurei

Secondary structure

1
679
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi56 – 594Combined sources
Beta strandi62 – 7110Combined sources
Beta strandi74 – 774Combined sources
Beta strandi91 – 933Combined sources
Beta strandi99 – 1024Combined sources
Helixi103 – 1064Combined sources
Turni107 – 1115Combined sources
Helixi113 – 1153Combined sources
Helixi120 – 1223Combined sources
Turni123 – 1253Combined sources
Helixi131 – 1399Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi148 – 1569Combined sources
Beta strandi159 – 1613Combined sources
Helixi163 – 18220Combined sources
Beta strandi188 – 1936Combined sources
Helixi199 – 21113Combined sources
Beta strandi215 – 2217Combined sources
Helixi222 – 2298Combined sources
Helixi232 – 2343Combined sources
Beta strandi236 – 24510Combined sources
Beta strandi250 – 2589Combined sources
Beta strandi261 – 27010Combined sources
Helixi275 – 29420Combined sources
Helixi302 – 31817Combined sources
Turni319 – 3213Combined sources
Beta strandi323 – 33311Combined sources
Beta strandi340 – 3478Combined sources
Helixi348 – 3547Combined sources
Helixi356 – 3605Combined sources
Helixi363 – 37210Combined sources
Turni377 – 3793Combined sources
Beta strandi382 – 3876Combined sources
Helixi388 – 3914Combined sources
Helixi393 – 40311Combined sources
Turni413 – 4153Combined sources
Helixi416 – 42813Combined sources
Beta strandi445 – 4484Combined sources
Beta strandi452 – 4587Combined sources
Beta strandi463 – 47210Combined sources
Beta strandi482 – 4909Combined sources
Helixi494 – 4963Combined sources
Beta strandi497 – 5059Combined sources
Beta strandi518 – 5247Combined sources
Beta strandi530 – 5367Combined sources
Turni537 – 5393Combined sources
Beta strandi542 – 5487Combined sources
Helixi555 – 56713Combined sources
Helixi569 – 59022Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N8EX-ray2.80A/B439-597[»]
4KBOX-ray2.80A52-431[»]
ProteinModelPortaliP38646.
SMRiP38646. Positions 54-651.
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.
GeneTreeiENSGT00820000127001.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481S → P AA sequence (PubMed:7498169).Curated
Sequence conflicti66 – 661C → S AA sequence (PubMed:7498169).Curated
Sequence conflicti176 – 1761E → V in BAG37618 (PubMed:14702039).Curated
Sequence conflicti184 – 1841H → R in AAH00478 (PubMed:15489334).Curated
Sequence conflicti184 – 1841H → R in AAH24034 (PubMed:15489334).Curated
Sequence conflicti249 – 2491T → A in BAD96478 (Ref. 4) Curated
Sequence conflicti385 – 3851L → P in BAD96478 (Ref. 4) Curated
Sequence conflicti540 – 5401G → R in AAA67526 (PubMed:7829505).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741Q → R.1 Publication
Corresponds to variant rs17856004 [ dbSNP | Ensembl ].
VAR_046482
Natural varianti127 – 1271R → G.
Corresponds to variant rs35091799 [ dbSNP | Ensembl ].
VAR_049622
Natural varianti184 – 1841H → Y.1 Publication
VAR_046483
Natural varianti225 – 2251A → G.
Corresponds to variant rs34558740 [ dbSNP | Ensembl ].
VAR_049623

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3N8EX-ray2.80A/B439-597[»]
4KBOX-ray2.80A52-431[»]
ProteinModelPortaliP38646.
SMRiP38646. Positions 54-651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109545. 208 interactions.
IntActiP38646. 56 interactions.
MINTiMINT-1143092.
STRINGi9606.ENSP00000297185.

PTM databases

iPTMnetiP38646.
PhosphoSiteiP38646.
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.
GeneCardsiHSPA9.
HGNCiHGNC:5244. HSPA9.
HPAiCAB005219.
HPA000898.
MIMi600548. gene.
neXtProtiNX_P38646.
PharmGKBiPA162391712.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0102. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOVERGENiHBG051845.
InParanoidiP38646.
KOiK04043.
OMAiEKMAPPQ.
OrthoDBiEOG091G0386.
PhylomeDBiP38646.
TreeFamiTF105046.

Enzyme and pathway databases

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: September 7, 2016
This is version 181 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.