Reviewed,
UniProtKB/Swiss-Prot P00387 (NB5R3_HUMAN)
Last modified
July 7, 2009.
Version 137.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
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Names and origin
| Protein names | Recommended name: NADH-cytochrome b5 reductase 3 Short name=Cytochrome b5 reductase Short name=B5R EC=1.6.2.2 Alternative name(s): Diaphorase-1 Cleaved into the following 2 chains: 1- Recommended name: NADH-cytochrome b5 reductase 3 membrane-bound form 2- Recommended name: NADH-cytochrome b5 reductase 3 soluble form | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 301 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 | Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. |
| Catalytic activity | NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5. |
| Cofactor | FAD. |
| Subunit structure | Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2 By similarity. |
| Subcellular location | Isoform 1: Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side. Mitochondrion outer membrane; Lipid-anchor; Cytoplasmic side. Isoform 2: Cytoplasm. Note: Produces the soluble form found in erythrocytes. |
| Tissue specificity | Isoform 2 (soluble form) is expressed at late stages of erythroid maturation. |
| Polymorphism | Ser-117 seems to only be found in persons of African origin. The allele frequency is 0.23 in African Americans. It was not found in Caucasians, Asians, Indo-Aryans, or Arabs. There seems to be no effect on the enzyme activity. |
| Involvement in disease | Defects in CYB5R3 are the cause of hereditary methemoglobinemia (HM) [MIM:250800]. There are three forms of this disease: type 1 (HM1) in which the enzyme is only deficient in erythrocytes with a mild cyanosis; type 2 (HM2), in which the enzyme is completely deficient; type 3 (HM3) where the deficiency is seen in all blood cells. Type 2 is a severe form accompanied with mental retardation and neurological impairment. Ref.4 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 |
| Sequence similarities | Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select] | ||||||
| Isoform 1 (identifier: P00387-1) Also known as: M; 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 2 (identifier: P00387-2) Also known as: S; The sequence of this isoform differs from the canonical sequence as follows: 1-23: Missing. | ||||||
| Note: Produces the soluble form found in erythrocytes. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 301 | 300 | NADH-cytochrome b5 reductase 3 membrane-bound form | PRO_0000019392 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Chain | 27 – 301 | 275 | NADH-cytochrome b5 reductase 3 soluble form | PRO_0000019394 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 40 – 152 | 113 | FAD-binding FR-type | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 132 – 147 | 16 | FAD By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 171 – 206 | 36 | FAD By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 42 | 1 | N6-acetyllysine By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 43 | 1 | Phosphotyrosine Ref.17 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 120 | 1 | N6-acetyllysine By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 130 | 1 | Phosphotyrosine By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Lipidation | 2 | 1 | N-myristoyl glycine | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 23 | 23 | Missing in isoform 2. | VSP_010200 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 58 | 1 | R → Q in HM; type 1; 62% of activity. Ref.4 Ref.21 Ref.29 | VAR_004619 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 66 | 1 | S → P: dbSNP rs1130706. Ref.4 Ref.1 Ref.10 | VAR_018419 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 73 | 1 | L → P in HM; type 1. Ref.4 Ref.26 | VAR_010750 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 106 | 1 | V → M in HM; type 1; 77% of activity. Ref.22 | VAR_004620 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 117 | 1 | T → S: dbSNP rs1800457. Ref.7 Ref.25 | VAR_010751 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 128 | 1 | S → P in HM; type 2; Hiroshima. Ref.20 | VAR_004621 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 149 | 1 | L → P in HM; type 3. Ref.21 | VAR_004622 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 179 | 1 | A → V in HM; type 1. Ref.27 | VAR_010752 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 204 | 1 | C → R in HM; type 2. Ref.4 Ref.24 Ref.28 | VAR_010753 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 204 | 1 | C → Y in HM; type 1. Ref.4 Ref.24 Ref.28 | VAR_010754 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 256 | 1 | Missing in HM; type 1; retains approximately 38% of residual diaphorase activity. Ref.30 Ref.31 | VAR_037315 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 273 | 1 | Missing in HM; type 2. Ref.24 | VAR_010755 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 292 | 1 | G → D in HM; type 1; retains approximately 58% of residual diaphorase activity. Ref.30 Ref.31 | VAR_037316 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 299 | 1 | Missing in HM; type2; almost complete loss of activity. Ref.23 | VAR_004623 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 28 – 32 | 5 | QRSTP → RWPRA in AAA52307. Ref.10 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 29 | 1 | R → G in AAA59900. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 31 | 1 | T → K in CAA09006. Ref.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 31 | 1 | T → K in CAA09007. Ref.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 31 | 1 | T → K in CAA09008. Ref.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 34 – 35 | 2 | IT → LA in AAA52307. Ref.10 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 187 – 188 | 2 | ML → IV in CAA09006. Ref.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 187 – 188 | 2 | ML → IV in CAA09007. Ref.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 191 – 192 | 2 | IR → MS in CAA09006. Ref.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 191 – 192 | 2 | IR → MS in CAA09007. Ref.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 192 | 1 | R → G in AAA52306. Ref.10 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 233 – 234 | 2 | FK → CN in CAA09006. Ref.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 233 – 234 | 2 | FK → CN in CAA09007. Ref.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 280 | 1 | I → N in AAL87744. Ref.3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 43 – 52 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 54 – 63 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 78 – 85 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 88 – 94 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 104 – 111 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 115 – 118 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 126 – 133 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 139 – 146 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 148 – 153 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 156 – 159 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 168 – 171 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 173 – 180 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 181 – 183 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 184 – 195 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 203 – 212 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 213 – 215 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 219 – 228 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 230 – 232 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 233 – 241 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 247 – 252 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 255 – 261 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 265 – 267 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 270 – 275 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 277 – 282 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 285 – 291 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 295 – 297 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 298 – 300 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The organization and the complete nucleotide sequence of the human NADH-cytochrome b5 reductase gene." Tomatsu S., Kobayashi Y., Fukumaki Y., Yubisui T., Orii T., Sakaki Y. Gene 80:353-361(1989) [PubMed: 2479590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-66. Tissue: Placenta. |
| [2] | Voice M.W. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [3] | Yoon B., Chung H., Ko E., Lee D. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [4] | Lan F. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-66, VARIANTS HM GLN-58; PRO-73 AND TYR-204. Tissue: Leukocyte. |
| [5] | "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [6] | "A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [7] | NIEHS SNPs program Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-117. |
| [8] | "The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. Wright H.Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [9] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta. |
| [10] | "Molecular cloning of cDNAs of human liver and placenta NADH-cytochrome b5 reductase." Yubisui T., Naitoh Y., Zenno S., Tamura M., Takeshita M., Sakaki Y. Proc. Natl. Acad. Sci. U.S.A. 84:3609-3613(1987) [PubMed: 3035541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-301, VARIANT PRO-66. Tissue: Liver. |
| [11] | "Upregulation of voltage-gated Na+ channel expression and metastatic potential in human breast cancer: correlative studies on cell lines and biopsy tissues." Diss J.K.J., Fraser S.P., Coombes R.C., Djamgoz M.B.A. Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-250. |
| [12] | "The NH2-terminal structures of human and rat liver microsomal NADH-cytochrome b5 reductases." Murakami K., Yubisui T., Takeshita M., Miyata T. J. Biochem. 105:312-317(1989) [PubMed: 2498303] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-25, MYRISTOYLATION AT GLY-2. |
| [13] | "Complete amino acid sequence of NADH-cytochrome b5 reductase purified from human erythrocytes." Yubisui T., Miyata T., Iwanaga S., Tamura M., Takeshita M. J. Biochem. 99:407-422(1986) [PubMed: 3700359] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-301. Tissue: Erythrocyte. |
| [14] | "Amino acid sequence of NADH-cytochrome b5 reductase of human erythrocytes." Yubisui T., Miyata T., Iwanaga S., Tamura M., Yoshida S., Takeshita M., Nakajima H. J. Biochem. 96:579-582(1984) [PubMed: 6389526] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-301. Tissue: Erythrocyte. |
| [15] | "An erythroid-specific transcript generates the soluble form of NADH-cytochrome b5 reductase in humans." Bulbarelli A., Valentini A., De Silvestris M., Cappellini M.D., Borgese N. Blood 92:310-319(1998) [PubMed: 9639531] [Abstract] Cited for: ALTERNATIVE PROMOTER USAGE. |
| [16] | "Role of cysteine residues in human NADH-cytochrome b5 reductase studied by site-directed mutagenesis. Cys-273 and Cys-283 are located close to the NADH-binding site but are not catalytically essential." Shirabe K., Yubisui T., Nishino T., Takeshita M. J. Biol. Chem. 266:7531-7536(1991) [PubMed: 2019583] [Abstract] Cited for: MUTAGENESIS OF CYSTEINE RESIDUES. |
| [17] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, MASS SPECTROMETRY. |
| [18] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [19] | "Structure of human erythrocyte NADH-cytochrome b5 reductase." Bando S., Takano T., Yubisui T., Shirabe K., Takeshita M., Nakagawa A. Acta Crystallogr. D 60:1929-1934(2004) [PubMed: 15502298] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 31-301. |
| [20] | "Structural role of serine 127 in the NADH-binding site of human NADH-cytochrome b5 reductase." Yubisui T., Shirabe K., Takeshita M., Kobayashi Y., Fukumaki Y., Sakaki Y., Takano T. J. Biol. Chem. 266:66-70(1991) [PubMed: 1898726] [Abstract] Cited for: VARIANT HM PRO-128. |
| [21] | "Exonic point mutations in NADH-cytochrome B5 reductase genes of homozygotes for hereditary methemoglobinemia, types I and III: putative mechanisms of tissue-dependent enzyme deficiency." Katsube T., Sakamoto N., Kobayashi Y., Seki R., Hirano M., Tanishima K., Tomoda A., Takazakura E., Yubisui T., Takeshita M., Sakaki Y., Fukumaki Y. Am. J. Hum. Genet. 48:799-808(1991) [PubMed: 1707593] [Abstract] Cited for: VARIANTS HM GLN-58 AND PRO-149. |
| [22] | "Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type)." Shirabe K., Yubisui T., Borgese N., Tang C.-Y., Hultquist D.E., Takeshita M. J. Biol. Chem. 267:20416-20421(1992) [PubMed: 1400360] [Abstract] Cited for: VARIANT HM MET-106. |
| [23] | "An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase gene results in hereditary methemoglobinemia type II (generalized type). A functional implication for the role of the COOH-terminal region of the enzyme." Shirabe K., Fujimoto Y., Yubisui T., Takeshita M. J. Biol. Chem. 269:5952-5957(1994) [PubMed: 8119939] [Abstract] Cited for: VARIANT HM PHE-299 DEL. |
| [24] | "Four new mutations in the NADH-cytochrome b5 reductase gene from patients with recessive congenital methemoglobinemia type II." Vieira L.M., Kaplan J.-C., Kahn A., Leroux A. Blood 85:2254-2262(1995) [PubMed: 7718898] [Abstract] Cited for: VARIANTS HM ARG-204 AND MET-273 DEL. |
| [25] | "A high-frequency polymorphism of NADH-cytochrome b5 reductase in African-Americans." Jenkins M.M., Prchal J.T. Hum. Genet. 99:248-250(1997) [PubMed: 9048929] [Abstract] Cited for: VARIANT SER-117. |
| [26] | "Identification of a novel point mutation (Leu72-to-Pro) in the NADH-cytochrome b5 reductase gene of a patient with hereditary methaemoglobinaemia type I." Wu Y.-S., Huang C.-H., Wan Y., Huang Q.-J., Zhu Z.-Y. Br. J. Haematol. 102:575-577(1998) [PubMed: 9695975] [Abstract] Cited for: VARIANT HM PRO-73. |
| [27] | "Molecular basis of hereditary methaemoglobinaemia, types I and II: two novel mutations in the NADH-cytochrome b5 reductase gene." Higasa K., Manabe J.I., Yubisui T., Sumimoto H., Pung-Amritt P., Tanphaichitr V.S., Fukumaki Y. Br. J. Haematol. 103:922-930(1998) [PubMed: 9886302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-83 AND 171-187, VARIANT HM VAL-179. |
| [28] | "A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia." Wang Y., Wu Y.-S., Zheng P.-Z., Yang W.-X., Fang G.-A., Tang Y.-C., Xie F., Lan F.-H., Zhu Z.-Y. Blood 95:3250-3255(2000) [PubMed: 10807796] [Abstract] Cited for: VARIANT HM TYR-204. |
| [29] | "Arginine-glutamine replacement at residue 57 of NADH-cytochrome b5 reductase in Chinese hereditary methemoglobinemia." Huang C.-H., Xie Y., Wang Y., Wu Y.-S. Zhonghua Xue Ye Xue Za Zhi 18:200-203(1997) [PubMed: 15622768] [Abstract] Cited for: VARIANT HM GLN-58. |
| [30] | "Familial idiopathic methemoglobinemia revisited: original cases reveal 2 novel mutations in NADH-cytochrome b5 reductase." Percy M.J., Gillespie M.J.S., Savage G., Hughes A.E., McMullin M.F., Lappin T.R.J. Blood 100:3447-3449(2002) [PubMed: 12393396] [Abstract] Cited for: VARIANTS HM GLU-256 DEL AND ASP-292. |
| [31] | "Recessive congenital methaemoglobinaemia: functional characterization of the novel D239G mutation in the NADH-binding lobe of cytochrome b5 reductase." Percy M.J., Crowley L.J., Davis C.A., McMullin M.F., Savage G., Hughes J., McMahon C., Quinn R.J.M., Smith O., Barber M.J., Lappin T.R.J. Br. J. Haematol. 129:847-853(2005) [PubMed: 15953014] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS HM GLU-256 DEL AND ASP-292. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
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M28713 M28711 Genomic DNA. Translation: AAA59900.1. Y09501 mRNA. Translation: CAA70696.1. AF361370 mRNA. Translation: AAL87744.1. AJ010116 mRNA. Translation: CAA09006.1. AJ010117 mRNA. Translation: CAA09007.1. AJ010118 mRNA. Translation: CAA09008.1. BT009821 mRNA. Translation: AAP88823.1. CR456435 mRNA. Translation: CAG30321.1. AY341030 Genomic DNA. Translation: AAP88936.1. AF061830 Genomic DNA. Translation: AAF06818.1. AF061831 Genomic DNA. Translation: AAF06819.1. BC004821 mRNA. Translation: AAH04821.1. Z93241 Genomic DNA. Translation: CAB42843.1. Z93241 Genomic DNA. Translation: CAQ08414.1. AJ310899 mRNA. Translation: CAC84523.1. AJ310900 mRNA. Translation: CAC84524.1. M16461 mRNA. Translation: AAA52306.1. M16462 mRNA. Translation: AAA52307.1. | |||||||||||||||||||
| IPI | IPI00328415. IPI00446235. | ||||||||||||||||||
| PIR | RDHUB5. JS0468. | ||||||||||||||||||
| RefSeq | NP_000389.1. NP_001123291.1. NP_015565.1. | ||||||||||||||||||
| UniGene | Hs.700572 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P00387. 1 interaction. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P00387. | ||||||||||||||||||
2-D gel databases | |||||||||||||||||||
| REPRODUCTION-2DPAGE | IPI00446235. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | P00387. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSG00000100243. Homo sapiens. [Contig view] | ||||||||||||||||||
| GeneID | 1727. | ||||||||||||||||||
| KEGG | hsa:1727. | ||||||||||||||||||
| UCSC | uc003bcw.2. human. uc003bcz.2. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| GeneCards | GC22M041340. | ||||||||||||||||||
| H-InvDB | HIX0016545. | ||||||||||||||||||
| HGNC | HGNC:2873. CYB5R3. | ||||||||||||||||||
| HPA | HPA001566. | ||||||||||||||||||
| MIM | 250800. gene+phenotype. | ||||||||||||||||||
| Orphanet | 621. Hereditary methemoglobinemia. 139373. Recessive hereditary methemoglobinemia type 1. 139380. Recessive hereditary methemoglobinemia type 2. | ||||||||||||||||||
| PharmGKB | PA27331. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | P00387. | ||||||||||||||||||
| OMA | P00387. ARFKFAL. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BRENDA | 1.6.2.2. 247. | ||||||||||||||||||
| Reactome | REACT_11193. Metabolism of vitamins and cofactors. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P00387. | ||||||||||||||||||
| Bgee | P00387. | ||||||||||||||||||
| CleanEx | HS_CYB5R3. | ||||||||||||||||||
| GermOnline | ENSG00000100243. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view] | ||||||||||||||||||
| Pfam | PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00406. CYTB5RDTASE. PR00371. FPNCR. | ||||||||||||||||||
| PROSITE | PS51384. FAD_FR. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| DrugBank | DB00157. NADH. | ||||||||||||||||||
| NextBio | 6983. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | NB5R3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P00387 Secondary accession number(s): B1AHF2 Q9UL56 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 22 Human chromosome 22: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


