Stress-70 protein, mitochondrial precursor

Names and origin

Protein names

Recommended name:
    Stress-70 protein, mitochondrial
Alternative name(s):
    75 kDa glucose-regulated protein
    GRP 75
    Heat shock 70 kDa protein 9
    Peptide-binding protein 74
      Short name=PBP74
    Mortalin
      Short name=MOT

Gene names

Name:	HSPA9
Synonyms:	GRP75, HSPA9B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	679 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone.
Subunit structure	Interacts with FXN. Ref.14
Subcellular location	Mitochondrion.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.13 Ref.15
Sequence similarities	Belongs to the heat shock protein 70 family.

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Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: UniProtKB protein folding Inferred from electronic annotation. Source: InterPro
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB mitochondrial nucleoid Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW unfolded protein binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 46

46

Mitochondrion Ref.8 Ref.9 Ref.10

Chain

47 – 679

633

Stress-70 protein, mitochondrial

PRO_0000013563

Amino acid modifications

Modified residue

135

1

N6-acetyllysine Ref.17

Modified residue

138

1

N6-acetyllysine Ref.17

Modified residue

143

1

N6-acetyllysine Ref.17

Modified residue

200

1

Phosphoserine Ref.15

Modified residue

234

1

N6-acetyllysine Ref.17

Modified residue

288

1

N6-acetyllysine Ref.17

Modified residue

300

1

N6-acetyllysine Ref.17

Modified residue

345

1

N6-acetyllysine Ref.17

Modified residue

567

1

N6-acetyllysine Ref.17

Modified residue

568

1

Phosphotyrosine Ref.13

Modified residue

646

1

N6-acetyllysine Ref.17

Natural variations

Natural variant

74

1

Q → R: dbSNP rs17856004. Ref.7

VAR_046482

Natural variant

127

1

R → G: dbSNP rs35091799.

VAR_049622

Natural variant

184

1

H → Y

VAR_046483

Natural variant

225

1

A → G: dbSNP rs34558740.

VAR_049623

Experimental info

Sequence conflict

48

1

S → P AA sequence Ref.9

Sequence conflict

66

1

C → S AA sequence Ref.9

Sequence conflict

176

1

E → V in BAG37618. Ref.3

Sequence conflict

184

1

H → R in AAH00478. Ref.7

Sequence conflict

184

1

H → R in AAH24034. Ref.7

Sequence conflict

249

1

T → A in BAD96478. Ref.4

Sequence conflict

385

1

L → P in BAD96478. Ref.4

Sequence conflict

540

1

G → R in AAA67526. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P38646-1 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: 90969A8D06757753
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FASTA

679

73,680

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 7684501] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: B-cell.
[2]	"Cloning and subcellular localization of human mitochondrial hsp70." Bhattacharyya T., Karnezis A.N., Murphy S.P., Hoang T., Freeman B.C., Phillips B., Morimoto R.I. J. Biol. Chem. 270:1705-1710(1995) [PubMed: 7829505] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Teratocarcinoma.
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[5]	NIEHS SNPs program Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-184.
[6]	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. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-74. Tissue: Muscle.
[8]	"A two-dimensional gel database of human colon carcinoma proteins." Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J. Electrophoresis 18:605-613(1997) [PubMed: 9150948] [Abstract] Cited for: PROTEIN SEQUENCE OF 47-68. Tissue: Colon carcinoma.
[9]	"Analysis of proteins from human breast epithelial cells using two-dimensional gel electrophoresis." Giometti C.S., Tollaksen S.L., Chubb C., Williams C., Huberman E. Electrophoresis 16:1215-1224(1995) [PubMed: 7498169] [Abstract] Cited for: PROTEIN SEQUENCE OF 47-66. Tissue: Mammary gland.
[10]	"Human liver protein map: a reference database established by microsequencing and gel comparison." 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. Electrophoresis 13:992-1001(1992) [PubMed: 1286669] [Abstract] Cited for: PROTEIN SEQUENCE OF 47-56. Tissue: Liver.
[11]	"Human liver protein map: update 1993." Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F. Electrophoresis 14:1216-1222(1993) [PubMed: 8313870] [Abstract] Cited for: SEQUENCE REVISION. Tissue: Liver.
[12]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: 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, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[13]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." 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. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-568, MASS SPECTROMETRY.
[14]	"Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones." Shan Y., Napoli E., Cortopassi G. Hum. Mol. Genet. 16:929-941(2007) [PubMed: 17331979] [Abstract] Cited for: INTERACTION WITH FXN.
[15]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." 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. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, MASS SPECTROMETRY.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-138; LYS-143; LYS-234; LYS-288; LYS-300; LYS-345; LYS-567 AND LYS-646, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases
	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.
IPI	IPI00007765.
PIR	B48127.
RefSeq	NP_004125.3.
UniGene	Hs.184233
3D structure databases
HSSP	HSSP built from PDB template 1DG4 based on UniProtKB P04475.
ModBase	Search...
Protein-protein interaction databases
IntAct	P38646. 39 interactions.
STRING	P38646.
PTM databases
PhosphoSite	P38646.
2-D gel databases
SWISS-2DPAGE	P38646.
DOSAC-COBS-2DPAGE	P38646.
HSC-2DPAGE	P38646.
OGP	P38646.
PHCI-2DPAGE	P38646.
REPRODUCTION-2DPAGE	IPI00007765.
Siena-2DPAGE	P38646.
Proteomic databases
PRIDE	P38646.
Genome annotation databases
Ensembl	ENST00000297185; ENSP00000297185; ENSG00000113013; Homo sapiens. [Genome view]
GeneID	3313.
KEGG	hsa:3313.
UCSC	uc003ldf.1. human.
Organism-specific databases
CTD	3313.
GeneCards	GC05M137920.
H-InvDB	HIX0005214.
HGNC	HGNC:5244. HSPA9.
HPA	CAB005219. HPA000898.
MIM	600548. gene.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P38646.
OMA	ANNGDAW.
Gene expression databases
ArrayExpress	P38646.
Bgee	P38646.
Genevestigator	P38646.
GermOnline	ENSG00000113013. Homo sapiens.
Family and domain databases
InterPro	IPR012725. Chaperone_DnaK. IPR018181. Heat_shock_70_CS. IPR001023. Hsp70. IPR013126. Hsp_70. [Graphical view]
PANTHER	PTHR19375. Hsp70. 1 hit.
Pfam	PF00012. HSP70. 1 hit. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
ProDom	PD000089. Hsp70. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02350. prok_dnaK. 1 hit.
PROSITE	PS00297. HSP70_1. 1 hit. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	13142.
SOURCE	Search...

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Entry information

Entry name

GRP75_HUMAN

Accession

Primary (citable) accession number: P38646
Secondary accession number(s): B2RCM1

Q9UC56

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	May 27, 2002
Last modified:	November 3, 2009
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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Index of human polymorphisms and disease mutations

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents