P00390 (GSHR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione reductase, mitochondrial
Short name=GR
Short name=GRase
EC=1.8.1.7

Gene names

Name:	GSR
Synonyms:	GLUR, GRD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Maintains high levels of reduced glutathione in the cytosol.
Catalytic activity	2 glutathione + NADP+ = glutathione disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Homodimer; disulfide-linked. Ref.14
Subcellular location	Isoform Mitochondrial: Mitochondrion. Isoform Cytoplasmic: Cytoplasm.
Domain	Each subunit can be divided into 4 domains that are consecutive along the polypeptide chain. Domains 1 and 2 bind FAD and NADPH, respectively. Domain 4 forms the interface.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Sequence caution	The sequence AAP88037.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
Domain	Redox-active center Transit peptide
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic process Inferred from electronic annotation. Source: InterPro nucleobase-containing small molecule interconversion Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro electron carrier activity Traceable author statement PubMed 947404. Source: UniProtKB flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Isoform Mitochondrial (identifier: P00390-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Cytoplasmic (identifier: P00390-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.

Note: Produced by alternative initiation of isoform Mitochondrial. Initiator Met-1 is removed. Acetylated at Ala-2.

Isoform 2 (identifier: P00390-3)

Also known as: delta8;

The sequence of this isoform differs from the canonical sequence as follows:
     266-294: Missing.

Isoform 3 (identifier: P00390-4)

Also known as: delta9;

The sequence of this isoform differs from the canonical sequence as follows:
     295-347: Missing.

Note: Expressed at very high levels in peripheral blood.

Isoform 4 (identifier: P00390-5)

Also known as: delta8+9;

The sequence of this isoform differs from the canonical sequence as follows:
     266-294: Missing.
     295-347: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 43

43

Mitochondrion Potential

Chain

44 – 522

479

Glutathione reductase, mitochondrial

PRO_0000030276

Regions

Nucleotide binding

94 – 102

9

FAD

Sites

Active site

511

1

Proton acceptor

Amino acid modifications

Disulfide bond

102 ↔ 107

Redox-active Ref.14

Disulfide bond

134

Interchain Ref.14

Natural variations

Alternative sequence

1 – 43

43

Missing in isoform Cytoplasmic.

VSP_018972

Alternative sequence

266 – 294

29

Missing in isoform 2 and isoform 4.

VSP_042908

Alternative sequence

295 – 347

53

Missing in isoform 3 and isoform 4.

VSP_042909

Natural variant

153

1

R → C. Ref.3
Corresponds to variant rs8190955 [ dbSNP | Ensembl ].

VAR_019079

Natural variant

232

1

G → R.
Corresponds to variant rs8190976 [ dbSNP | Ensembl ].

VAR_051775

Natural variant

232

1

G → S. Ref.3
Corresponds to variant rs8190976 [ dbSNP | Ensembl ].

VAR_019080

Natural variant

261

1

I → V. Ref.3
Corresponds to variant rs8190997 [ dbSNP | Ensembl ].

VAR_019081

Natural variant

297

1

E → D. Ref.3
Corresponds to variant rs8191004 [ dbSNP | Ensembl ].

VAR_019082

Natural variant

314

1

P → H.
Corresponds to variant rs2020916 [ dbSNP | Ensembl ].

VAR_014554

Secondary structure

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522

Helix Strand Turn

Details...

Beta strand

62 – 64

3

Beta strand

66 – 70

5

Helix

74 – 85

12

Beta strand

90 – 96

7

Helix

100 – 105

6

Helix

107 – 123

17

Turn

124 – 130

7

Helix

140 – 164

25

Beta strand

168 – 172

5

Beta strand

174 – 176

3

Beta strand

183 – 186

4

Beta strand

189 – 192

4

Beta strand

196 – 198

3

Beta strand

202 – 204

3

Turn

209 – 211

3

Helix

215 – 217

3

Helix

221 – 224

4

Beta strand

232 – 237

6

Helix

241 – 252

12

Beta strand

256 – 260

5

Beta strand

262 – 266

5

Helix

272 – 284

13

Beta strand

288 – 290

3

Beta strand

293 – 300

8

Beta strand

302 – 311

10

Beta strand

319 – 331

13

Beta strand

335 – 338

4

Turn

340 – 343

4

Helix

344 – 347

4

Beta strand

370 – 372

3

Helix

374 – 377

4

Helix

383 – 398

16

Beta strand

413 – 415

3

Beta strand

417 – 419

3

Beta strand

421 – 425

5

Helix

428 – 435

8

Helix

437 – 439

3

Beta strand

440 – 447

8

Helix

450 – 454

5

Beta strand

461 – 468

8

Turn

469 – 472

4

Beta strand

473 – 481

9

Helix

484 – 496

13

Helix

501 – 505

5

Beta strand

511 – 514

4

Helix

515 – 519

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mitochondrial [UniParc]. Last modified July 11, 2001. Version 2. Checksum: DD8E2BA9D6E3757B	FASTA	522	56,257
	10 20 30 40 50 60 MALLPRALSA GAGPSWRRAA RAFRGFLLLL PEPAALTRAL SRAMACRQEP QPQGPPPAAG 70 80 90 100 110 120 AVASYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG TCVNVGCVPK KVMWNTAVHS 130 140 150 160 170 180 EFMHDHADYG FPSCEGKFNW RVIKEKRDAY VSRLNAIYQN NLTKSHIEII RGHAAFTSDP 190 200 210 220 230 240 KPTIEVSGKK YTAPHILIAT GGMPSTPHES QIPGASLGIT SDGFFQLEEL PGRSVIVGAG 250 260 270 280 290 300 YIAVEMAGIL SALGSKTSLM IRHDKVLRSF DSMISTNCTE ELENAGVEVL KFSQVKEVKK 310 320 330 340 350 360 TLSGLEVSMV TAVPGRLPVM TMIPDVDCLL WAIGRVPNTK DLSLNKLGIQ TDDKGHIIVD 370 380 390 400 410 420 EFQNTNVKGI YAVGDVCGKA LLTPVAIAAG RKLAHRLFEY KEDSKLDYNN IPTVVFSHPP 430 440 450 460 470 480 IGTVGLTEDE AIHKYGIENV KTYSTSFTPM YHAVTKRKTK CVMKMVCANK EEKVVGIHMQ 490 500 510 520 GLGCDEMLQG FAVAVKMGAT KADFDNTVAI HPTSSEELVT LR
	Isoform Cytoplasmic [UniParc]. Checksum: 3C0A194C96E880E7	FASTA	479	51,701
	10 20 30 40 50 60 MACRQEPQPQ GPPPAAGAVA SYDYLVIGGG SGGLASARRA AELGARAAVV ESHKLGGTCV 70 80 90 100 110 120 NVGCVPKKVM WNTAVHSEFM HDHADYGFPS CEGKFNWRVI KEKRDAYVSR LNAIYQNNLT 130 140 150 160 170 180 KSHIEIIRGH AAFTSDPKPT IEVSGKKYTA PHILIATGGM PSTPHESQIP GASLGITSDG 190 200 210 220 230 240 FFQLEELPGR SVIVGAGYIA VEMAGILSAL GSKTSLMIRH DKVLRSFDSM ISTNCTEELE 250 260 270 280 290 300 NAGVEVLKFS QVKEVKKTLS GLEVSMVTAV PGRLPVMTMI PDVDCLLWAI GRVPNTKDLS 310 320 330 340 350 360 LNKLGIQTDD KGHIIVDEFQ NTNVKGIYAV GDVCGKALLT PVAIAAGRKL AHRLFEYKED 370 380 390 400 410 420 SKLDYNNIPT VVFSHPPIGT VGLTEDEAIH KYGIENVKTY STSFTPMYHA VTKRKTKCVM 430 440 450 460 470 KMVCANKEEK VVGIHMQGLG CDEMLQGFAV AVKMGATKAD FDNTVAIHPT SSEELVTLR
	Isoform 2 (delta8) [UniParc]. Checksum: EFBA71DCDCFF1529	FASTA	493	53,027
	10 20 30 40 50 60 MALLPRALSA GAGPSWRRAA RAFRGFLLLL PEPAALTRAL SRAMACRQEP QPQGPPPAAG 70 80 90 100 110 120 AVASYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG TCVNVGCVPK KVMWNTAVHS 130 140 150 160 170 180 EFMHDHADYG FPSCEGKFNW RVIKEKRDAY VSRLNAIYQN NLTKSHIEII RGHAAFTSDP 190 200 210 220 230 240 KPTIEVSGKK YTAPHILIAT GGMPSTPHES QIPGASLGIT SDGFFQLEEL PGRSVIVGAG 250 260 270 280 290 300 YIAVEMAGIL SALGSKTSLM IRHDKVKEVK KTLSGLEVSM VTAVPGRLPV MTMIPDVDCL 310 320 330 340 350 360 LWAIGRVPNT KDLSLNKLGI QTDDKGHIIV DEFQNTNVKG IYAVGDVCGK ALLTPVAIAA 370 380 390 400 410 420 GRKLAHRLFE YKEDSKLDYN NIPTVVFSHP PIGTVGLTED EAIHKYGIEN VKTYSTSFTP 430 440 450 460 470 480 MYHAVTKRKT KCVMKMVCAN KEEKVVGIHM QGLGCDEMLQ GFAVAVKMGA TKADFDNTVA 490 IHPTSSEELV TLR
	Isoform 3 (delta9) [UniParc]. Checksum: 0AD475B02A87C63E	FASTA	469	50,497
	10 20 30 40 50 60 MALLPRALSA GAGPSWRRAA RAFRGFLLLL PEPAALTRAL SRAMACRQEP QPQGPPPAAG 70 80 90 100 110 120 AVASYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG TCVNVGCVPK KVMWNTAVHS 130 140 150 160 170 180 EFMHDHADYG FPSCEGKFNW RVIKEKRDAY VSRLNAIYQN NLTKSHIEII RGHAAFTSDP 190 200 210 220 230 240 KPTIEVSGKK YTAPHILIAT GGMPSTPHES QIPGASLGIT SDGFFQLEEL PGRSVIVGAG 250 260 270 280 290 300 YIAVEMAGIL SALGSKTSLM IRHDKVLRSF DSMISTNCTE ELENAGVEVL KFSQGIQTDD 310 320 330 340 350 360 KGHIIVDEFQ NTNVKGIYAV GDVCGKALLT PVAIAAGRKL AHRLFEYKED SKLDYNNIPT 370 380 390 400 410 420 VVFSHPPIGT VGLTEDEAIH KYGIENVKTY STSFTPMYHA VTKRKTKCVM KMVCANKEEK 430 440 450 460 VVGIHMQGLG CDEMLQGFAV AVKMGATKAD FDNTVAIHPT SSEELVTLR
	Isoform 4 (delta8+9) [UniParc]. Checksum: 793E0A9F8706B1B5	FASTA	440	47,267
	10 20 30 40 50 60 MALLPRALSA GAGPSWRRAA RAFRGFLLLL PEPAALTRAL SRAMACRQEP QPQGPPPAAG 70 80 90 100 110 120 AVASYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG TCVNVGCVPK KVMWNTAVHS 130 140 150 160 170 180 EFMHDHADYG FPSCEGKFNW RVIKEKRDAY VSRLNAIYQN NLTKSHIEII RGHAAFTSDP 190 200 210 220 230 240 KPTIEVSGKK YTAPHILIAT GGMPSTPHES QIPGASLGIT SDGFFQLEEL PGRSVIVGAG 250 260 270 280 290 300 YIAVEMAGIL SALGSKTSLM IRHDKGIQTD DKGHIIVDEF QNTNVKGIYA VGDVCGKALL 310 320 330 340 350 360 TPVAIAAGRK LAHRLFEYKE DSKLDYNNIP TVVFSHPPIG TVGLTEDEAI HKYGIENVKT 370 380 390 400 410 420 YSTSFTPMYH AVTKRKTKCV MKMVCANKEE KVVGIHMQGL GCDEMLQGFA VAVKMGATKA 430 440 DFDNTVAIHP TSSEELVTLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of mammalian glutathione reductase cDNA." Tutic M., Lu X.A., Schirmer R.H., Werner D. Eur. J. Biochem. 188:523-528(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC). Tissue: Placenta.
[2]	"Structural organization of the human glutathione reductase (GSR) gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence." Kelner M.J., Montoya M.A. Biochem. Biophys. Res. Commun. 269:366-368(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM MITOCHONDRIAL), ALTERNATIVE INITIATION.
[3]	NIEHS SNPs program Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-153; SER-232; VAL-261 AND ASP-297.
[4]	"Expression of glutathione reductase splice variants in human tissues." Satoh N., Watanabe N., Kanda A., Sugaya-Fukazawa M., Hisatomi H. Biochem. Genet. 48:816-821(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[5]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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] (ISOFORM MITOCHONDRIAL). Tissue: Lung.
[8]	"Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain." Krauth-Siegel R.L., Blatterspiel R., Saleh M., Schiltz E., Schirmer R.H., Untucht-Grau R. Eur. J. Biochem. 121:259-267(1982) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 45-522.
[9]	"Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide." Krohne-Ehrich G., Schirmer R.H., Untucht-Grau R. Eur. J. Biochem. 80:65-71(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 98-110. Tissue: Erythrocyte.
[10]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Three-dimensional structure of glutathione reductase at 2-A resolution." Thieme R., Pai E.F., Schirmer R.H., Schulz G.E. J. Mol. Biol. 152:763-782(1981) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS) OF 45-522.
[13]	"Refined structure of glutathione reductase at 1.54-A resolution." Karplus P.A., Schulz G.E. J. Mol. Biol. 195:701-729(1987) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 45-522.
[14]	"Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor." Savvides S.N., Karplus P.A. J. Biol. Chem. 271:8101-8107(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 62-522, DISULFIDE BONDS.
[15]	"Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity." Stoll V.S., Simpson S.J., Krauth-Siegel R.L., Walsh C.T., Pai E.F. Biochemistry 36:6437-6447(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 62-522.
[16]	"Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers." Becker K., Savvides S.N., Keese M., Schirmer R.H., Karplus P.A. Nat. Struct. Biol. 5:267-271(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 62-522.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Wikipedia

Glutathione reductase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X15722 mRNA. Translation: CAA33744.1.
AF228703 Genomic DNA. Translation: AAF37572.1.
AF228703 Genomic DNA. Translation: AAF37573.1.
AF228704 mRNA. Translation: AAF37574.1.
AY338490 Genomic DNA. Translation: AAP88037.1. Different initiation.
AB519179 mRNA. Translation: BAI43437.1.
AB519180 mRNA. Translation: BAI43438.1.
AB519181 mRNA. Translation: BAI43439.1.
AC009314 Genomic DNA. No translation available.
AC103959 Genomic DNA. No translation available.
AF215848 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63443.1.
CH471080 Genomic DNA. Translation: EAW63445.1.
BC069244 mRNA. Translation: AAH69244.1.

IPI

IPI00016862.
IPI00759575.
IPI00953236.
IPI00953696.
IPI00978634.

PIR

RDHUU. S08979.

RefSeq

NP_000628.2. NM_000637.3.
NP_001182031.1. NM_001195102.1.
NP_001182032.1. NM_001195103.1.
NP_001182033.1. NM_001195104.1.

UniGene

Hs.271510.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ALG	NMR	-	A	480-503	[»]
1BWC	X-ray	2.10	A	45-522	[»]
1DNC	X-ray	1.70	A	45-522	[»]
1GRA	X-ray	2.00	A	45-522	[»]
1GRB	X-ray	1.85	A	45-522	[»]
1GRE	X-ray	2.00	A	45-522	[»]
1GRF	X-ray	2.00	A	45-522	[»]
1GRG	X-ray	2.00	A	45-522	[»]
1GRH	X-ray	3.00	A	45-522	[»]
1GRT	X-ray	2.30	A	45-522	[»]
1GSN	X-ray	1.70	A	45-522	[»]
1K4Q	X-ray	1.90	A	62-522	[»]
1XAN	X-ray	2.00	A	62-522	[»]
2AAQ	X-ray	2.60	A	44-522	[»]
2GH5	X-ray	1.70	A/B	45-522	[»]
2GRT	X-ray	2.70	A	62-522	[»]
3DJG	X-ray	1.80	X	62-522	[»]
3DJJ	X-ray	1.10	A	45-522	[»]
3DK4	X-ray	1.20	A	45-522	[»]
3DK8	X-ray	1.10	A	62-522	[»]
3DK9	X-ray	0.95	A	45-522	[»]
3GRS	X-ray	1.54	A	45-522	[»]
3GRT	X-ray	2.50	A	62-522	[»]
3SQP	X-ray	2.21	A/B	45-522	[»]
4GR1	X-ray	2.40	A	45-522	[»]
4GRT	X-ray	2.80	A	62-522	[»]
5GRT	X-ray	2.40	A	62-522	[»]

ProteinModelPortal

P00390.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00390. 4 interactions.

MINT

MINT-5000460.

STRING

9606.ENSP00000221130.

PTM databases

PhosphoSite

P00390.

Polymorphism databases

DMDM

14916998.

2D gel databases

REPRODUCTION-2DPAGE

IPI00759575.

Proteomic databases

PaxDb

P00390.

PRIDE

P00390.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221130; ENSP00000221130; ENSG00000104687.
ENST00000414019; ENSP00000390065; ENSG00000104687.
ENST00000537535; ENSP00000438845; ENSG00000104687.
ENST00000541648; ENSP00000444559; ENSG00000104687.
ENST00000546342; ENSP00000445516; ENSG00000104687.

GeneID

2936.

KEGG

hsa:2936.

UCSC

uc003xih.2. human.

Organism-specific databases

CTD

2936.

GeneCards

GC08M030535.

HGNC

HGNC:4623. GSR.

HPA

CAB008632.
HPA001538.

MIM

138300. gene+phenotype.

neXtProt

NX_P00390.

Orphanet

90030. Hemolytic anemia due to glutathione reductase deficiency.

PharmGKB

PA29014.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1249.

HOGENOM

HOG000276712.

HOVERGEN

HBG004959.

InParanoid

P00390.

KO

K00383.

OMA

PHESQIP.

OrthoDB

EOG42BX8H.

PhylomeDB

P00390.

Enzyme and pathway databases

BioCyc

MetaCyc:HS02602-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P00390.

Gene expression databases

ArrayExpress

P00390.

Bgee

P00390.

CleanEx

HS_GSR.

Genevestigator

P00390.

GermOnline

ENSG00000104687. Homo sapiens.

Family and domain databases

Gene3D

3.30.390.30. 1 hit.

InterPro

IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

SUPFAM

SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.

TIGRFAMs

TIGR01421. gluta_reduc_1. 1 hit.

PROSITE

PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00390.

ChEMBL

CHEMBL2755.

DrugBank

DB00262. Carmustine.
DB00143. Glutathione.
DB00157. NADH.

EvolutionaryTrace

P00390.

GenomeRNAi

2936.

NextBio

11635.

SOURCE

Search...

Entry information

Entry name

GSHR_HUMAN

Accession

Primary (citable) accession number: P00390
Secondary accession number(s): C8KIL8 , C8KIL9, C8KIM0, D3DSV3, Q7Z5C9, Q9NP63

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 11, 2001
Last modified:	May 1, 2013
This is version 182 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.