SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O76003

- GLRX3_HUMAN

UniProt

O76003 - GLRX3_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glutaredoxin-3
Gene
GLRX3, PICOT, TXNL2, HUSSY-22
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Sites

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

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
Complete GO annotation...

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
Complete GO annotation...

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. 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.1 Publication

GO - Cellular componenti

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

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 – 11Removed1 Publication
Chaini2 – 335334Glutaredoxin-3
PRO_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.2 Publications

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

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.

Miscellaneous databases

EvolutionaryTraceiO76003.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 117116Thioredoxin
Add
BLAST
Domaini144 – 23693Glutaredoxin 1
Add
BLAST
Domaini237 – 33599Glutaredoxin 2
Add
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.
Contains 1 thioredoxin domain.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → E in CAA09375. 1 Publication
Sequence conflicti67 – 671K → R in BAG51067. 1 Publication
Sequence conflicti210 – 2101I → T in BAG51059. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 144 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 (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

Similar proteinsi