B7Z904 (B7Z904_HUMAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Thioredoxin reductase 1 EMBL EAW97745.1

Submitted name:
Thioredoxin reductase 1, cytoplasmic Ensembl ENSP00000412045
Submitted name:
cDNA FLJ56205, highly similar to Thioredoxin reductase 1, cytoplasmic (EC 1.8.1.9) EMBL BAH14140.1

Gene names

Name:	TXNRD1 EMBL EAW97745.1 Ensembl ENSP00000412045
ORF Names:	hCG_1812757 EMBL EAW97745.1

Organism

Homo sapiens (Human) [Reference proteome] EMBL BAH14140.1

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	647 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. RuleBase RU003691

Ontologies

Keywords
Domain	Redox-active center RuleBase RU003691
Ligand	FAD RuleBase RU003691 Flavoprotein RuleBase RU003691
Molecular function	Oxidoreductase RuleBase RU003691
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NADPH oxidation Inferred from electronic annotation. Source: Compara benzene-containing compound metabolic process Inferred from electronic annotation. Source: Compara cell proliferation Inferred from electronic annotation. Source: Compara cell redox homeostasis Inferred from electronic annotation. Source: InterPro cellular response to copper ion Inferred from electronic annotation. Source: Compara cellular response to hyperoxia Inferred from electronic annotation. Source: Compara glutathione metabolic process Inferred from electronic annotation. Source: Compara halogen metabolic process Inferred from electronic annotation. Source: Compara hydrogen peroxide catabolic process Inferred from electronic annotation. Source: Compara mesoderm formation Inferred from electronic annotation. Source: Compara methylmercury metabolic process Inferred from electronic annotation. Source: Compara placenta development Inferred from electronic annotation. Source: Compara positive regulation of cell death Inferred from electronic annotation. Source: Compara protein tetramerization Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to selenium ion Inferred from electronic annotation. Source: Compara selenocysteine metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA cytosol Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara nucleolus Inferred from direct assay. Source: HPA
Molecular_function	NAD(P)H oxidase activity Inferred from electronic annotation. Source: Compara NADP binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro mercury ion binding Inferred from electronic annotation. Source: Compara protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro selenate reductase activity Inferred from electronic annotation. Source: Compara thioredoxin-disulfide reductase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	B7Z904 [UniParc]. Last modified March 3, 2009. Version 1. Checksum: 83F77EB03EFE2739	FASTA	647	70,699
	10 20 30 40 50 60 MGCAEGKAVA AAAPTELQTK GKNGDGRRRS AKDHHPGKTL PENPAGFTST ATADSRALLQ 70 80 90 100 110 120 AYIDGHSVVI FSRSTCTRCT EVKKLFKSLC VPYFVLELDQ TEDGRALEGT LSELAAETDL 130 140 150 160 170 180 PVVFVKQRKI GGHGPTLKAY QEGRLQKLLK MNGPEDLPKS YDYDLIIIGG GSGGLAAAKE 190 200 210 220 230 240 AAQYGKKVMV LDFVTPTPLG TRWGLGGTCV NVGCIPKKLM HQAALLGQAL QDSRNYGWKV 250 260 270 280 290 300 EETVKHDWDR MIEAVQNHIG SLNWGYRVAL REKKVVYENA YGQFIGPHRI KATNNKGKEK 310 320 330 340 350 360 IYSAERFLIA TGERPRYLGI PGDKEYCISS DDLFSLPYCP GKTLVVGASY VALECAGFLA 370 380 390 400 410 420 GIGLDVTVMV RSILLRGFDQ DMANKIGEHM EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV 430 440 450 460 470 480 AQSTNSEEII EGEYNTVMLA IGRDACTRKI GLETVGVKIN EKTGKIPVTD EEQTNVPYIY 490 500 510 520 530 540 AIGDILEDKV ELTPVAIQAG RLLAQRLYAG STVKCDYENV PTTVFTPLEY GACGLSEEKA 550 560 570 580 590 600 VEKFGEENIE VYHSYFWPLE WTIPSRDNNK CYAKIICNTK DNERVVGFHV LGPNAGEVTQ 610 620 630 640 GFAAALKCGL TKKQLDSTIG IHPVCAEVFT TLSVTKRSGA SILQAGC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The finished DNA sequence of human chromosome 12." Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A., null. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"NEDO human cDNA sequencing project focused on splicing variants." Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T. , Sugano S., Nomura N., Isogai T. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Tissue: Trachea EMBL BAH14140.1.
[4]	Ensembl Submitted (AUG-2012) to UniProtKB Cited for: IDENTIFICATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC089983 Genomic DNA. No translation available. AC090107 Genomic DNA. No translation available. AK304241 mRNA. Translation: BAH14140.1. CH471054 Genomic DNA. Translation: EAW97745.1.
IPI	IPI00983068.
UniGene	Hs.654922.
3D structure databases
SMR	B7Z904. Positions 59-646.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000429002; ENSP00000412045; ENSG00000198431.
Organism-specific databases
HGNC	HGNC:12437. TXNRD1.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG004959.
Gene expression databases
ArrayExpress	B7Z904.
Family and domain databases
Gene3D	3.30.390.30. 1 hit. 3.40.30.10. 1 hit.
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR002109. Glutaredoxin. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR012336. Thioredoxin-like_fold. IPR006338. Thioredoxin/glutathione_Rdtase. [Graphical view]
PANTHER	PTHR22912:SF23. PTHR22912:SF23. 1 hit.
Pfam	PF00462. Glutaredoxin. 1 hit. 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. SSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMs	TIGR01438. TGR. 1 hit.
PROSITE	PS51354. GLUTAREDOXIN_2. 1 hit. PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TXNRD1. human.
NextBio	35480617.

Entry information

Entry name

B7Z904_HUMAN

Accession

Primary (citable) accession number: B7Z904

Entry history

Integrated into UniProtKB/TrEMBL:	March 3, 2009
Last sequence update:	March 3, 2009
Last modified:	May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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.