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O76003

- GLRX3_HUMAN

UniProt

O76003 - GLRX3_HUMAN

Protein

Glutaredoxin-3

Gene

GLRX3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (26 Sep 2003)
      Previous versions | rss
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    Functioni

    Critical negative regulator of cardiac hypertrophy and a positive inotropic regulator By similarity. Crucial regulator of cellular iron homeostasis and hemoglobin maturation. May play a role in regulating the function of the thioredoxin system. Does not posses any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi159 – 1591Iron-sulfur (2Fe-2S); shared with dimeric partnerCurated
    Metal bindingi261 – 2611Iron-sulfur (2Fe-2S); shared with dimeric partnerCurated

    GO - Molecular functioni

    1. electron carrier activity Source: InterPro
    2. iron-sulfur cluster binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein disulfide oxidoreductase activity Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. negative regulation of cardiac muscle hypertrophy Source: UniProtKB
    3. regulation of the force of heart contraction Source: UniProtKB

    Keywords - Ligandi

    Iron, Iron-sulfur, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaredoxin-3
    Alternative name(s):
    PKC-interacting cousin of thioredoxin
    Short name:
    PICOT
    PKC-theta-interacting protein
    Short name:
    PKCq-interacting protein
    Thioredoxin-like protein 2
    Gene namesi
    Name:GLRX3
    Synonyms:PICOT, TXNL2
    ORF Names:HUSSY-22
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:15987. GLRX3.

    Subcellular locationi

    Cytoplasmcell cortex 1 Publication. CytoplasmmyofibrilsarcomereZ line By similarity
    Note: Under the plasma membrane. After PMA stimulation, GLRX3 and PRKCQ/PKC-theta translocate to a more extended submembrane area. In the Z line, found associated with CSRP3 By similarity.By similarity

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi159 – 1591C → S: Loss of 2Fe-2S-binding; when associated with S-261. 1 Publication
    Mutagenesisi261 – 2611C → S: Loss of 2Fe-2S-binding; when associated with S-159. 1 Publication

    Organism-specific databases

    PharmGKBiPA162389829.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 335334Glutaredoxin-3PRO_0000120019Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO76003.
    PaxDbiO76003.
    PeptideAtlasiO76003.
    PRIDEiO76003.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00008552.

    PTM databases

    PhosphoSiteiO76003.

    Miscellaneous databases

    PMAP-CutDBO76003.

    Expressioni

    Tissue specificityi

    Expressed in heart, spleen, testis and, to a lower extent, in thymus and peripheral blood leukocytes. Weakly expressed in lung, placenta, colon and small intestine.

    Gene expression databases

    BgeeiO76003.
    CleanExiHS_GLRX3.
    GenevestigatoriO76003.

    Organism-specific databases

    HPAiHPA028941.

    Interactioni

    Subunit structurei

    Monomer and homodimer; the homodimer is probably linked by 2 2Fe-2S clusters that may serve as a redox sensor. The monomer interacts with other proteins. Interacts (via N-terminus) with PRKCQ/PKC-theta. Interacts (via C-terminus) with CSRP3 By similarity. Interacts with CSRP2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CIAPIN1Q6FI813EBI-374781,EBI-750511
    PRKCQQ047595EBI-374781,EBI-374762

    Protein-protein interaction databases

    BioGridi115793. 29 interactions.
    IntActiO76003. 17 interactions.
    MINTiMINT-5002296.
    STRINGi9606.ENSP00000330836.

    Structurei

    Secondary structure

    1
    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 164
    Helixi19 – 2810
    Turni29 – 313
    Beta strandi34 – 396
    Helixi44 – 5916
    Beta strandi63 – 697
    Turni70 – 723
    Helixi74 – 796
    Beta strandi84 – 929
    Beta strandi95 – 1039
    Helixi105 – 11511
    Helixi133 – 1419
    Beta strandi143 – 15210
    Beta strandi154 – 1596
    Helixi160 – 17112
    Beta strandi177 – 1804
    Helixi181 – 1833
    Helixi185 – 19511
    Beta strandi202 – 2054
    Beta strandi208 – 2114
    Helixi213 – 2219
    Helixi225 – 2284
    Helixi233 – 24311
    Beta strandi245 – 25410
    Beta strandi256 – 2594
    Helixi263 – 27311
    Beta strandi279 – 2824
    Helixi283 – 2853
    Helixi287 – 29711
    Beta strandi304 – 3074
    Beta strandi310 – 3134
    Helixi315 – 3239
    Helixi327 – 3315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DIYNMR-A1-117[»]
    2WZ9X-ray1.55A1-125[»]
    2YANX-ray1.90A/B232-334[»]
    3ZYWX-ray1.84A/B130-232[»]
    ProteinModelPortaliO76003.
    SMRiO76003. Positions 11-125, 132-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO76003.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 117116ThioredoxinPROSITE-ProRule annotationAdd
    BLAST
    Domaini144 – 23693Glutaredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 33599Glutaredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The thioredoxin domain lacks the two redox-active cysteines. This strongly suggests that it lacks thioredoxin activity.

    Sequence similaritiesi

    Contains 2 glutaredoxin domains.PROSITE-ProRule annotation
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0526.
    HOVERGENiHBG054719.
    InParanoidiO76003.
    OMAiELPQVSF.
    OrthoDBiEOG7B5WX3.
    PhylomeDBiO76003.
    TreeFamiTF314151.

    Family and domain databases

    Gene3Di3.40.30.10. 3 hits.
    InterProiIPR002109. Glutaredoxin.
    IPR004480. Monothiol_GRX-rel.
    IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PANTHERiPTHR10293. PTHR10293. 1 hit.
    PfamiPF00462. Glutaredoxin. 2 hits.
    PF00085. Thioredoxin. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 3 hits.
    TIGRFAMsiTIGR00365. TIGR00365. 1 hit.
    PROSITEiPS51354. GLUTAREDOXIN_2. 2 hits.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O76003-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAGAAEAAV AAVEEVGSAG QFEELLRLKA KSLLVVHFWA PWAPQCAQMN    50
    EVMAELAKEL PQVSFVKLEA EGVPEVSEKY EISSVPTFLF FKNSQKIDRL 100
    DGAHAPELTK KVQRHASSGS FLPSANEHLK EDLNLRLKKL THAAPCMLFM 150
    KGTPQEPRCG FSKQMVEILH KHNIQFSSFD IFSDEEVRQG LKAYSSWPTY 200
    PQLYVSGELI GGLDIIKELE ASEELDTICP KAPKLEERLK VLTNKASVML 250
    FMKGNKQEAK CGFSKQILEI LNSTGVEYET FDILEDEEVR QGLKAYSNWP 300
    TYPQLYVKGE LVGGLDIVKE LKENGELLPI LRGEN 335
    Length:335
    Mass (Da):37,432
    Last modified:September 26, 2003 - v2
    Checksum:i46D644413D9EDFDA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → E in CAA09375. (PubMed:11124703)Curated
    Sequence conflicti67 – 671K → R in BAG51067. (PubMed:14702039)Curated
    Sequence conflicti210 – 2101I → T in BAG51059. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211Q → H.3 Publications
    Corresponds to variant rs13991 [ dbSNP | Ensembl ].
    VAR_016875
    Natural varianti123 – 1231P → S.3 Publications
    Corresponds to variant rs2274217 [ dbSNP | Ensembl ].
    VAR_016876

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF118649 mRNA. Translation: AAF28841.1.
    AF118652 mRNA. Translation: AAF28844.1.
    AJ010841 mRNA. Translation: CAA09375.1.
    AK022131 mRNA. Translation: BAG51067.1.
    AK021926 mRNA. Translation: BAG51059.1.
    AL139123 Genomic DNA. Translation: CAC40691.1.
    CH471066 Genomic DNA. Translation: EAW49152.1.
    CH471066 Genomic DNA. Translation: EAW49154.1.
    CH471066 Genomic DNA. Translation: EAW49155.1.
    BC005289 mRNA. Translation: AAH05289.1.
    BC014372 mRNA. Translation: AAH14372.2.
    CCDSiCCDS7661.1.
    RefSeqiNP_001186797.1. NM_001199868.1.
    NP_006532.2. NM_006541.4.
    UniGeneiHs.42644.

    Genome annotation databases

    EnsembliENST00000331244; ENSP00000330836; ENSG00000108010.
    ENST00000368644; ENSP00000357633; ENSG00000108010.
    ENST00000481034; ENSP00000435445; ENSG00000108010.
    GeneIDi10539.
    KEGGihsa:10539.
    UCSCiuc001lkm.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF118649 mRNA. Translation: AAF28841.1 .
    AF118652 mRNA. Translation: AAF28844.1 .
    AJ010841 mRNA. Translation: CAA09375.1 .
    AK022131 mRNA. Translation: BAG51067.1 .
    AK021926 mRNA. Translation: BAG51059.1 .
    AL139123 Genomic DNA. Translation: CAC40691.1 .
    CH471066 Genomic DNA. Translation: EAW49152.1 .
    CH471066 Genomic DNA. Translation: EAW49154.1 .
    CH471066 Genomic DNA. Translation: EAW49155.1 .
    BC005289 mRNA. Translation: AAH05289.1 .
    BC014372 mRNA. Translation: AAH14372.2 .
    CCDSi CCDS7661.1.
    RefSeqi NP_001186797.1. NM_001199868.1.
    NP_006532.2. NM_006541.4.
    UniGenei Hs.42644.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DIY NMR - A 1-117 [» ]
    2WZ9 X-ray 1.55 A 1-125 [» ]
    2YAN X-ray 1.90 A/B 232-334 [» ]
    3ZYW X-ray 1.84 A/B 130-232 [» ]
    ProteinModelPortali O76003.
    SMRi O76003. Positions 11-125, 132-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115793. 29 interactions.
    IntActi O76003. 17 interactions.
    MINTi MINT-5002296.
    STRINGi 9606.ENSP00000330836.

    PTM databases

    PhosphoSitei O76003.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00008552.

    Proteomic databases

    MaxQBi O76003.
    PaxDbi O76003.
    PeptideAtlasi O76003.
    PRIDEi O76003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331244 ; ENSP00000330836 ; ENSG00000108010 .
    ENST00000368644 ; ENSP00000357633 ; ENSG00000108010 .
    ENST00000481034 ; ENSP00000435445 ; ENSG00000108010 .
    GeneIDi 10539.
    KEGGi hsa:10539.
    UCSCi uc001lkm.2. human.

    Organism-specific databases

    CTDi 10539.
    GeneCardsi GC10P131934.
    HGNCi HGNC:15987. GLRX3.
    HPAi HPA028941.
    MIMi 612754. gene.
    neXtProti NX_O76003.
    PharmGKBi PA162389829.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOVERGENi HBG054719.
    InParanoidi O76003.
    OMAi ELPQVSF.
    OrthoDBi EOG7B5WX3.
    PhylomeDBi O76003.
    TreeFami TF314151.

    Miscellaneous databases

    ChiTaRSi GLRX3. human.
    EvolutionaryTracei O76003.
    GeneWikii GLRX3.
    GenomeRNAii 10539.
    NextBioi 39985.
    PMAP-CutDB O76003.
    PROi O76003.
    SOURCEi Search...

    Gene expression databases

    Bgeei O76003.
    CleanExi HS_GLRX3.
    Genevestigatori O76003.

    Family and domain databases

    Gene3Di 3.40.30.10. 3 hits.
    InterProi IPR002109. Glutaredoxin.
    IPR004480. Monothiol_GRX-rel.
    IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    PANTHERi PTHR10293. PTHR10293. 1 hit.
    Pfami PF00462. Glutaredoxin. 2 hits.
    PF00085. Thioredoxin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 3 hits.
    TIGRFAMsi TIGR00365. TIGR00365. 1 hit.
    PROSITEi PS51354. GLUTAREDOXIN_2. 2 hits.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain."
      Witte S., Villalba M., Bi K., Liu Y., Isakov N., Altman A.
      J. Biol. Chem. 275:1902-1909(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH PRKCQ, VARIANTS HIS-21 AND SER-123.
      Tissue: Liver, Spleen and T-cell lymphoma.
    2. "Characterization of 16 novel human genes showing high similarity to yeast sequences."
      Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G.
      Yeast 18:69-80(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Melanocyte.
    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], VARIANTS HIS-21 AND SER-123.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANTS HIS-21 AND SER-123.
      Tissue: Bone marrow and Urinary bladder.
    7. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 59-79; 115-130; 218-231; 246-253; 309-319 AND 323-332.
      Tissue: Fetal brain cortex.
    8. "Characterization of the human monothiol glutaredoxin 3 (PICOT) as iron-sulfur protein."
      Haunhorst P., Berndt C., Eitner S., Godoy J.R., Lillig C.H.
      Biochem. Biophys. Res. Commun. 394:372-376(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, MUTAGENESIS OF CYS-159 AND CYS-261, METAL.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation."
      Haunhorst P., Hanschmann E.M., Brautigam L., Stehling O., Hoffmann B., Muhlenhoff U., Lill R., Berndt C., Lillig C.H.
      Mol. Biol. Cell 24:1895-1903(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "The solution structure of the thioredoxin domain of human thioredoxin-like protein 2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-119.

    Entry informationi

    Entry nameiGLRX3_HUMAN
    AccessioniPrimary (citable) accession number: O76003
    Secondary accession number(s): B3KMP7
    , B3KMQ5, D3DRG2, Q5JV01, Q96CE0, Q9P1B0, Q9P1B1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: September 26, 2003
    Last modified: October 1, 2014
    This is version 145 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

    Miscellaneous

    Silencing of Grx3 in HeLa cells decreases the activities of several cytosolic Fe/S proteins, such as ACO1, a major component of post-transcriptional iron regulation. As a consequence, Grx3-depleted cells show decreased levels of ferritin and increased levels of transferrin receptor, features characteristic of cellular iron starvation (PubMed:23615448).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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