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P38646

- GRP75_HUMAN

UniProt

P38646 - GRP75_HUMAN

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Protein
Stress-70 protein, mitochondrial
Gene
HSPA9, GRP75, HSPA9B, mt-HSP70
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. ATP binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. negative regulation of apoptotic process Source: UniProtKB
  3. protein export from nucleus Source: Ensembl
  4. protein folding Source: InterPro
  5. protein targeting to mitochondrion Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

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
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:5244. HSPA9.

Subcellular locationi

Mitochondrion. Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrial nucleoid Source: BHF-UCL
  4. mitochondrion Source: UniProtKB
  5. nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162391712.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646Mitochondrion3 Publications
Add
BLAST
Chaini47 – 679633Stress-70 protein, mitochondrialUniRule annotation
PRO_0000013563Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761N6-acetyllysine By similarity
Modified residuei135 – 1351N6-acetyllysine; alternate1 Publication
Modified residuei135 – 1351N6-succinyllysine; alternate By similarity
Modified residuei138 – 1381N6-acetyllysine; alternate1 Publication
Modified residuei138 – 1381N6-succinyllysine; alternate By similarity
Modified residuei143 – 1431N6-acetyllysine1 Publication
Modified residuei206 – 2061N6-acetyllysine; alternate By similarity
Modified residuei206 – 2061N6-malonyllysine; alternate1 Publication
Modified residuei206 – 2061N6-succinyllysine; alternate By similarity
Modified residuei234 – 2341N6-acetyllysine1 Publication
Modified residuei288 – 2881N6-acetyllysine1 Publication
Modified residuei300 – 3001N6-acetyllysine; alternate1 Publication
Modified residuei300 – 3001N6-succinyllysine; alternate By similarity
Modified residuei368 – 3681N6-succinyllysine By similarity
Modified residuei394 – 3941N6-succinyllysine By similarity
Modified residuei567 – 5671N6-acetyllysine; alternate1 Publication
Modified residuei567 – 5671N6-succinyllysine; alternate By similarity
Modified residuei600 – 6001N6-acetyllysine; alternate By similarity
Modified residuei600 – 6001N6-succinyllysine; alternate By similarity
Modified residuei610 – 6101N6-succinyllysine By similarity
Modified residuei612 – 6121N6-acetyllysine By similarity
Modified residuei646 – 6461N6-acetyllysine; alternate1 Publication
Modified residuei646 – 6461N6-succinyllysine; alternate By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP38646.
PaxDbiP38646.
PRIDEiP38646.

2D gel databases

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

PTM databases

PhosphoSiteiP38646.

Expressioni

Gene expression databases

ArrayExpressiP38646.
BgeeiP38646.
GenevestigatoriP38646.

Organism-specific databases

HPAiCAB005219.
HPA000898.

Interactioni

Subunit structurei

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. 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

Protein-protein interaction databases

BioGridi109545. 110 interactions.
IntActiP38646. 42 interactions.
MINTiMINT-1143092.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N8EX-ray2.80A/B439-597[»]
4KBOX-ray2.80A52-431[»]
ProteinModelPortaliP38646.
SMRiP38646. Positions 54-651.

Miscellaneous databases

EvolutionaryTraceiP38646.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0443.
HOVERGENiHBG051845.
InParanoidiP38646.
KOiK04043.
OMAiMSEHKKS.
OrthoDBiEOG715Q3K.
PhylomeDBiP38646.
TreeFamiTF105046.

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.

P38646-1 [UniParc]FASTAAdd to Basket

« Hide

MISASRAAAA RLVGAAASRG PTAARHQDSW NGLSHEAFRL VSRRDYASEA    50
IKGAVVGIDL GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL 100
VGMPAKRQAV TNPNNTFYAT KRLIGRRYDD PEVQKDIKNV PFKIVRASNG 150
DAWVEAHGKL YSPSQIGAFV LMKMKETAEN YLGHTAKNAV ITVPAYFNDS 200
QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI AVYDLGGGTF 250
DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK 300
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDSSGPK HLNMKLTRAQ 350
FEGIVTDLIR RTIAPCQKAM QDAEVSKSDI GEVILVGGMT RMPKVQQTVQ 400
DLFGRAPSKA VNPDEAVAIG AAIQGGVLAG DVTDVLLLDV TPLSLGIETL 450
GGVFTKLINR NTTIPTKKSQ VFSTAADGQT QVEIKVCQGE REMAGDNKLL 500
GQFTLIGIPP APRGVPQIEV TFDIDANGIV HVSAKDKGTG REQQIVIQSS 550
GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK 600
DQLPADECNK LKEEISKMRE LLARKDSETG ENIRQAASSL QQASLKLFEM 650
AYKKMASERE GSGSSGTGEQ KEDQKEEKQ 679
Length:679
Mass (Da):73,680
Last modified:May 27, 2002 - v2
Checksum:i90969A8D06757753
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481S → P AA sequence 1 Publication
Sequence conflicti66 – 661C → S AA sequence 1 Publication
Sequence conflicti176 – 1761E → V in BAG37618. 1 Publication
Sequence conflicti184 – 1841H → R in AAH00478. 1 Publication
Sequence conflicti184 – 1841H → R in AAH24034. 1 Publication
Sequence conflicti249 – 2491T → A in BAD96478. 1 Publication
Sequence conflicti385 – 3851L → P in BAD96478. 1 Publication
Sequence conflicti540 – 5401G → R in AAA67526. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi21264428.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4208.1.
PIRi B48127.
RefSeqi NP_004125.3. NM_004134.6.
UniGenei Hs.184233.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3N8E X-ray 2.80 A/B 439-597 [» ]
4KBO X-ray 2.80 A 52-431 [» ]
ProteinModelPortali P38646.
SMRi P38646. Positions 54-651.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109545. 110 interactions.
IntActi P38646. 42 interactions.
MINTi MINT-1143092.

PTM databases

PhosphoSitei P38646.

Polymorphism databases

DMDMi 21264428.

2D gel databases

DOSAC-COBS-2DPAGE P38646.
OGPi P38646.
REPRODUCTION-2DPAGE IPI00007765.
SWISS-2DPAGE P38646.
UCD-2DPAGE P38646.

Proteomic databases

MaxQBi P38646.
PaxDbi P38646.
PRIDEi P38646.

Protocols and materials databases

DNASUi 3313.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297185 ; ENSP00000297185 ; ENSG00000113013 .
GeneIDi 3313.
KEGGi hsa:3313.
UCSCi uc003ldf.3. human.

Organism-specific databases

CTDi 3313.
GeneCardsi GC05M137890.
HGNCi HGNC:5244. HSPA9.
HPAi CAB005219.
HPA000898.
MIMi 600548. gene.
neXtProti NX_P38646.
PharmGKBi PA162391712.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0443.
HOVERGENi HBG051845.
InParanoidi P38646.
KOi K04043.
OMAi MSEHKKS.
OrthoDBi EOG715Q3K.
PhylomeDBi P38646.
TreeFami TF105046.

Enzyme and pathway databases

Reactomei REACT_118595. Mitochondrial protein import.

Miscellaneous databases

ChiTaRSi HSPA9. human.
EvolutionaryTracei P38646.
GeneWikii HSPA9.
GenomeRNAii 3313.
NextBioi 13142.
PROi P38646.
SOURCEi Search...

Gene expression databases

ArrayExpressi P38646.
Bgeei P38646.
Genevestigatori P38646.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPi MF_00332. DnaK.
InterProi IPR012725. Chaperone_DnaK.
IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
TIGRFAMsi TIGR02350. prok_dnaK. 1 hit.
PROSITEi PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. 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. "Tespa1 is a novel component of mitochondria-associated endoplasmic reticulum membranes and affects mitochondrial calcium flux."
    Matsuzaki H., Fujimoto T., Tanaka M., Shirasawa S.
    Biochem. Biophys. Res. Commun. 433:322-326(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TESPA.
  21. "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.

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 3, 2014
This is version 158 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

External Data

Dasty 3

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