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P38646

- GRP75_HUMAN

UniProt

P38646 - GRP75_HUMAN

Protein

Stress-70 protein, mitochondrial

Gene

HSPA9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (27 May 2002)
      Previous versions | rss
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    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

    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 1 Publication. 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

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162391712.

    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 residuei135 – 1351N6-acetyllysine; alternate1 Publication
    Modified residuei135 – 1351N6-succinyllysine; alternateBy similarity
    Modified residuei138 – 1381N6-acetyllysine; alternate1 Publication
    Modified residuei138 – 1381N6-succinyllysine; alternateBy similarity
    Modified residuei143 – 1431N6-acetyllysine1 Publication
    Modified residuei206 – 2061N6-acetyllysine; alternateBy similarity
    Modified residuei206 – 2061N6-malonyllysine; alternate1 Publication
    Modified residuei206 – 2061N6-succinyllysine; alternateBy similarity
    Modified residuei234 – 2341N6-acetyllysine1 Publication
    Modified residuei288 – 2881N6-acetyllysine1 Publication
    Modified residuei300 – 3001N6-acetyllysine; alternate1 Publication
    Modified residuei300 – 3001N6-succinyllysine; alternateBy similarity
    Modified residuei368 – 3681N6-succinyllysineBy similarity
    Modified residuei394 – 3941N6-succinyllysineBy similarity
    Modified residuei567 – 5671N6-acetyllysine; alternate1 Publication
    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; alternate1 Publication
    Modified residuei646 – 6461N6-succinyllysine; alternateBy 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. 43 interactions.
    MINTiMINT-1143092.

    Structurei

    Secondary structure

    1
    679
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38646.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    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

    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. 1 PublicationCurated
    Sequence conflicti385 – 3851L → P in BAD96478. 1 PublicationCurated
    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:
    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. 43 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

    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: October 1, 2014
    This is version 159 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