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P38647

- GRP75_MOUSE

UniProt

P38647 - GRP75_MOUSE

Protein

Stress-70 protein, mitochondrial

Gene

Hspa9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (03 Oct 2012)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. enzyme binding Source: UniProtKB
    3. protein binding Source: MGI

    GO - Biological processi

    1. protein export from nucleus Source: MGI
    2. protein folding Source: InterPro

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_199101. 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
    Peptide-binding protein 74
    Short name:
    PBP74
    p66 MOT
    Gene namesi
    Name:Hspa9
    Synonyms:Grp75, Hsp74, Hspa9a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:96245. Hspa9.

    Subcellular locationi

    Mitochondrion 1 Publication. Nucleusnucleolus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. mitochondrial nucleoid Source: Ensembl
    3. mitochondrion Source: MGI
    4. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4646Mitochondrion1 PublicationAdd
    BLAST
    Chaini47 – 679633Stress-70 protein, mitochondrialPRO_0000013564Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 761N6-acetyllysine1 Publication
    Modified residuei135 – 1351N6-acetyllysine; alternate2 Publications
    Modified residuei135 – 1351N6-succinyllysine; alternate1 Publication
    Modified residuei138 – 1381N6-acetyllysine; alternate1 Publication
    Modified residuei138 – 1381N6-succinyllysine; alternate1 Publication
    Modified residuei143 – 1431N6-acetyllysineBy similarity
    Modified residuei206 – 2061N6-acetyllysine; alternate1 Publication
    Modified residuei206 – 2061N6-malonyllysine; alternateBy similarity
    Modified residuei206 – 2061N6-succinyllysine; alternate1 Publication
    Modified residuei234 – 2341N6-acetyllysine1 Publication
    Modified residuei288 – 2881N6-acetyllysine1 Publication
    Modified residuei300 – 3001N6-acetyllysine; alternate2 Publications
    Modified residuei300 – 3001N6-succinyllysine; alternate1 Publication
    Modified residuei360 – 3601N6-acetyllysine; alternate2 Publications
    Modified residuei360 – 3601N6-succinyllysine; alternate1 Publication
    Modified residuei368 – 3681N6-succinyllysine1 Publication
    Modified residuei394 – 3941N6-succinyllysine1 Publication
    Modified residuei567 – 5671N6-acetyllysine; alternate2 Publications
    Modified residuei567 – 5671N6-succinyllysine; alternate1 Publication
    Modified residuei600 – 6001N6-acetyllysine; alternate1 Publication
    Modified residuei600 – 6001N6-succinyllysine; alternate1 Publication
    Modified residuei610 – 6101N6-succinyllysine1 Publication
    Modified residuei612 – 6121N6-acetyllysine1 Publication
    Modified residuei646 – 6461N6-acetyllysine; alternate1 Publication
    Modified residuei646 – 6461N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP38647.
    PRIDEiP38647.

    2D gel databases

    COMPLUYEAST-2DPAGEP38647.
    REPRODUCTION-2DPAGEIPI00133903.
    P38647.
    SWISS-2DPAGEP38647.

    PTM databases

    PhosphoSiteiP38647.

    Expressioni

    Tissue specificityi

    Found in all the cell types examined.

    Inductioni

    Not induced by heat shock, instead protein level is decreased.

    Gene expression databases

    CleanExiMM_HSPA9.
    GenevestigatoriP38647.

    Interactioni

    Subunit structurei

    Interacts with FXN. Interacts with HSCB By similarity. 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 By similarity. Interacts with TESPA1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi200457. 20 interactions.
    IntActiP38647. 16 interactions.
    MINTiMINT-1860030.
    STRINGi10090.ENSMUSP00000025217.

    Structurei

    3D structure databases

    ProteinModelPortaliP38647.
    SMRiP38647. Positions 54-651.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0443.
    GeneTreeiENSGT00750000117237.
    HOGENOMiHOG000228136.
    HOVERGENiHBG051845.
    InParanoidiP38647.
    KOiK04043.
    OMAiQRDVAIM.
    OrthoDBiEOG715Q3K.
    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.

    P38647-1 [UniParc]FASTAAdd to Basket

    « Hide

    MISASRAAAA RLVGTAASRS PAAARPQDGW NGLSHEAFRF VSRRDYASEA    50
    IKGAVVGIDL GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL 100
    VGMPAKRQAV TNPNNTFYAT KRLIGRRYDD PEVQKDTKNV PFKIVRASNG 150
    DAWVEAHGKL YSPSQIGAFV LMKMKETAEN YLGHTAKNAV ITVPAYFNDS 200
    QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI AVYDLGGGTF 250
    DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK 300
    DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDASGPK HLNMKLTRAQ 350
    FEGIVTDLIK 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 LKEEISKMRA LLAGKDSETG ENIRQAASSL QQASLKLFEM 650
    AYKKMASERE GSGSSGTGEQ KEDQKEEKQ 679
    Length:679
    Mass (Da):73,461
    Last modified:October 3, 2012 - v3
    Checksum:iDF1C997775627928
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51S → T AA sequence (PubMed:7684501)Curated
    Sequence conflicti78 – 781L → Q in BAE21690. (PubMed:16141072)Curated
    Sequence conflicti106 – 1061K → R AA sequence (PubMed:7684501)Curated
    Sequence conflicti150 – 1501G → S in BAE35373. (PubMed:16141072)Curated
    Sequence conflicti522 – 5221F → S AA sequence (PubMed:7684501)Curated

    Polymorphismi

    Two forms of the protein have been found, MOT-1, found in mortal cells and MOT-2, found in immortal cells. The sequence of MOT-2 is shown here.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti618 – 6181M → V in MOT-1.
    Natural varianti624 – 6241G → R in MOT-1.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11089 mRNA. Translation: BAA01862.2.
    L06896 mRNA. No translation available.
    D17666 Genomic DNA. Translation: BAA04548.1.
    D17556 mRNA. Translation: BAA04493.1.
    AK004946 mRNA. Translation: BAB23690.1.
    AK002634 mRNA. Translation: BAB22248.1.
    AK133501 mRNA. Translation: BAE21690.1.
    AK137109 mRNA. Translation: BAE23238.1.
    AK145965 mRNA. Translation: BAE26790.1.
    AK159791 mRNA. Translation: BAE35373.1.
    AK165958 mRNA. Translation: BAE38486.1.
    AK167856 mRNA. Translation: BAE39874.1.
    AC114820 Genomic DNA. No translation available.
    AC131675 Genomic DNA. No translation available.
    CH466557 Genomic DNA. Translation: EDK97122.1.
    BC052727 mRNA. Translation: AAH52727.1.
    BC057343 mRNA. Translation: AAH57343.1.
    CCDSiCCDS29138.1.
    PIRiS39839. A48127.
    RefSeqiNP_034611.2. NM_010481.2.
    UniGeneiMm.209419.

    Genome annotation databases

    EnsembliENSMUST00000025217; ENSMUSP00000025217; ENSMUSG00000024359.
    GeneIDi15526.
    KEGGimmu:15526.
    UCSCiuc008elv.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11089 mRNA. Translation: BAA01862.2 .
    L06896 mRNA. No translation available.
    D17666 Genomic DNA. Translation: BAA04548.1 .
    D17556 mRNA. Translation: BAA04493.1 .
    AK004946 mRNA. Translation: BAB23690.1 .
    AK002634 mRNA. Translation: BAB22248.1 .
    AK133501 mRNA. Translation: BAE21690.1 .
    AK137109 mRNA. Translation: BAE23238.1 .
    AK145965 mRNA. Translation: BAE26790.1 .
    AK159791 mRNA. Translation: BAE35373.1 .
    AK165958 mRNA. Translation: BAE38486.1 .
    AK167856 mRNA. Translation: BAE39874.1 .
    AC114820 Genomic DNA. No translation available.
    AC131675 Genomic DNA. No translation available.
    CH466557 Genomic DNA. Translation: EDK97122.1 .
    BC052727 mRNA. Translation: AAH52727.1 .
    BC057343 mRNA. Translation: AAH57343.1 .
    CCDSi CCDS29138.1.
    PIRi S39839. A48127.
    RefSeqi NP_034611.2. NM_010481.2.
    UniGenei Mm.209419.

    3D structure databases

    ProteinModelPortali P38647.
    SMRi P38647. Positions 54-651.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200457. 20 interactions.
    IntActi P38647. 16 interactions.
    MINTi MINT-1860030.
    STRINGi 10090.ENSMUSP00000025217.

    PTM databases

    PhosphoSitei P38647.

    2D gel databases

    COMPLUYEAST-2DPAGE P38647.
    REPRODUCTION-2DPAGE IPI00133903.
    P38647.
    SWISS-2DPAGE P38647.

    Proteomic databases

    PaxDbi P38647.
    PRIDEi P38647.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025217 ; ENSMUSP00000025217 ; ENSMUSG00000024359 .
    GeneIDi 15526.
    KEGGi mmu:15526.
    UCSCi uc008elv.2. mouse.

    Organism-specific databases

    CTDi 3313.
    MGIi MGI:96245. Hspa9.

    Phylogenomic databases

    eggNOGi COG0443.
    GeneTreei ENSGT00750000117237.
    HOGENOMi HOG000228136.
    HOVERGENi HBG051845.
    InParanoidi P38647.
    KOi K04043.
    OMAi QRDVAIM.
    OrthoDBi EOG715Q3K.
    TreeFami TF105046.

    Enzyme and pathway databases

    Reactomei REACT_199101. Mitochondrial protein import.

    Miscellaneous databases

    ChiTaRSi HSPA9. mouse.
    NextBioi 288444.
    PROi P38647.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_HSPA9.
    Genevestigatori P38647.

    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. "Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype."
      Wadhwa R., Kaul S.C., Ikawa Y., Sugimoto Y.
      J. Biol. Chem. 268:6615-6621(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: CD-1-ICR.
      Tissue: Embryonic fibroblast.
    2. Wadhwa R.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 123.
    3. "Induction of cellular senescence by transfection of cytosolic mortalin cDNA in NIH 3T3 cells."
      Wadhwa R., Kaul S.C., Sugimoto Y., Mitsui Y.
      J. Biol. Chem. 268:22239-22242(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: CD-1-ICR.
      Tissue: Embryonic fibroblast.
    4. "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], PARTIAL PROTEIN SEQUENCE.
      Tissue: B-cell.
    5. "Structure and organization of the gene encoding a mouse mitochondrial stress-70 protein."
      Michikawa Y., Baba T., Arai Y., Sakakura T., Kusakabe M.
      FEBS Lett. 336:27-33(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
      Tissue: Liver.
    6. "Antigenic protein specific for C3H strain mouse is a mitochondrial stress-70 protein."
      Michikawa Y., Baba T., Arai Y., Sakakura T., Tanaka M., Kusakabe M.
      Biochem. Biophys. Res. Commun. 196:223-232(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C3H/HeN.
      Tissue: Kidney.
    7. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and DBA/2.
      Tissue: Embryo, Kidney and Liver.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    9. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    11. "Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
      Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
      Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 47-70.
      Tissue: Fibroblast.
    12. Lubec G., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 188-202; 266-284; 349-360; 395-405 AND 499-513, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Hippocampus.
    13. "PBP74, a new member of the mammalian 70-kDa heat shock protein family, is a mitochondrial protein."
      Dahlseid J.N., Lill R., Green J.M., Xu X., Qiu Y., Pierce S.K.
      Mol. Biol. Cell 5:1265-1275(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-300; LYS-360 AND LYS-567, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-138; LYS-206; LYS-300; LYS-360; LYS-368; LYS-394; LYS-567; LYS-600; LYS-610 AND LYS-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    15. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-135; LYS-138; LYS-206; LYS-234; LYS-288; LYS-300; LYS-360; LYS-567; LYS-600; LYS-612 AND LYS-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiGRP75_MOUSE
    AccessioniPrimary (citable) accession number: P38647
    Secondary accession number(s): Q3TW93
    , Q3UVN1, Q3V015, Q7TSZ0, Q9CQ05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3