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P38646 (GRP75_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·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
Short name=MOT
Peptide-binding protein 74
Short name=PBP74
Gene names
Name:HSPA9
Synonyms:GRP75, HSPA9B, mt-HSP70
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. 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. Ref.13 Ref.15 Ref.18 Ref.20

Subcellular location

Mitochondrion. Nucleusnucleolus Ref.19.

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.8 Ref.9 Ref.10
Chain47 – 679633Stress-70 protein, mitochondrial HAMAP-Rule MF_00332
PRO_0000013563

Amino acid modifications

Modified residue761N6-acetyllysine By similarity
Modified residue1351N6-acetyllysine; alternate Ref.14
Modified residue1351N6-succinyllysine; alternate By similarity
Modified residue1381N6-acetyllysine; alternate Ref.14
Modified residue1381N6-succinyllysine; alternate By similarity
Modified residue1431N6-acetyllysine Ref.14
Modified residue2061N6-acetyllysine; alternate By similarity
Modified residue2061N6-malonyllysine; alternate Ref.17
Modified residue2061N6-succinyllysine; alternate By similarity
Modified residue2341N6-acetyllysine Ref.14
Modified residue2881N6-acetyllysine Ref.14
Modified residue3001N6-acetyllysine; alternate Ref.14
Modified residue3001N6-succinyllysine; alternate By similarity
Modified residue3681N6-succinyllysine By similarity
Modified residue3941N6-succinyllysine By similarity
Modified residue5671N6-acetyllysine; alternate Ref.14
Modified residue5671N6-succinyllysine; alternate By similarity
Modified residue6001N6-acetyllysine; alternate By similarity
Modified residue6001N6-succinyllysine; alternate By similarity
Modified residue6101N6-succinyllysine By similarity
Modified residue6121N6-acetyllysine By similarity
Modified residue6461N6-acetyllysine; alternate Ref.14
Modified residue6461N6-succinyllysine; alternate By similarity

Natural variations

Natural variant741Q → R. Ref.7
Corresponds to variant rs17856004 [ dbSNP | Ensembl ].
VAR_046482
Natural variant1271R → G.
Corresponds to variant rs35091799 [ dbSNP | Ensembl ].
VAR_049622
Natural variant1841H → Y. Ref.5
VAR_046483
Natural variant2251A → G.
Corresponds to variant rs34558740 [ dbSNP | Ensembl ].
VAR_049623

Experimental info

Sequence conflict481S → P AA sequence Ref.9
Sequence conflict661C → S AA sequence Ref.9
Sequence conflict1761E → V in BAG37618. Ref.3
Sequence conflict1841H → R in AAH00478. Ref.7
Sequence conflict1841H → R in AAH24034. Ref.7
Sequence conflict2491T → A in BAD96478. Ref.4
Sequence conflict3851L → P in BAD96478. Ref.4
Sequence conflict5401G → R in AAA67526. Ref.2

Secondary structure

....................... 679
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38646 [UniParc].

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

FASTA67973,680
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FXN.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-138; LYS-143; LYS-234; LYS-288; LYS-300; LYS-567 AND LYS-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis."
Uhrigshardt H., Singh A., Kovtunovych G., Ghosh M., Rouault T.A.
Hum. Mol. Genet. 19:3816-3834(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSCB.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-206.
[18]"MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization."
Alkhaja A.K., Jans D.C., Nikolov M., Vukotic M., Lytovchenko O., Ludewig F., Schliebs W., Riedel D., Urlaub H., Jakobs S., Deckers M.
Mol. Biol. Cell 23:247-257(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MINOS/MITOS COMPLEX.
[19]"Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[20]"Structural and stability studies of the human mtHsp70-escort protein 1: An essential mortalin co-chaperone."
Dores-Silva P.R., Minari K., Ramos C.H., Barbosa L.R., Borges J.C.
Int. J. Biol. Macromol. 56:140-148(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNLZ.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB48127.
RefSeqNP_004125.3. NM_004134.6.
UniGeneHs.184233.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3N8EX-ray2.80A/B439-597[»]
ProteinModelPortalP38646.
SMRP38646. Positions 55-651.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109545. 139 interactions.
IntActP38646. 42 interactions.
MINTMINT-1143092.

PTM databases

PhosphoSiteP38646.

Polymorphism databases

DMDM21264428.

2D gel databases

DOSAC-COBS-2DPAGEP38646.
OGPP38646.
REPRODUCTION-2DPAGEIPI00007765.
SWISS-2DPAGEP38646.
UCD-2DPAGEP38646.

Proteomic databases

PaxDbP38646.
PRIDEP38646.

Protocols and materials databases

DNASU3313.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297185; ENSP00000297185; ENSG00000113013.
GeneID3313.
KEGGhsa:3313.
UCSCuc003ldf.3. human.

Organism-specific databases

CTD3313.
GeneCardsGC05M137890.
HGNCHGNC:5244. HSPA9.
HPACAB005219.
HPA000898.
MIM600548. gene.
neXtProtNX_P38646.
PharmGKBPA162391712.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0443.
HOVERGENHBG051845.
InParanoidP38646.
KOK04043.
OMAMITKNTT.
OrthoDBEOG715Q3K.
PhylomeDBP38646.
TreeFamTF105046.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP38646.
BgeeP38646.
GenevestigatorP38646.

Family and domain databases

HAMAPMF_00332. DnaK.
InterProIPR012725. Chaperone_DnaK.
IPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
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. human.
EvolutionaryTraceP38646.
GeneWikiHSPA9.
GenomeRNAi3313.
NextBio13142.
PROP38646.
SOURCESearch...

Entry information

Entry nameGRP75_HUMAN
AccessionPrimary (citable) accession number: P38646
Secondary accession number(s): B2RCM1 expand/collapse secondary AC list , P30036, P31932, Q1HB43, Q53H23, Q6GU03, Q9BWB7, Q9UC56
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 27, 2002
Last modified: April 16, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM