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Q7L1T6

- NB5R4_HUMAN

UniProt

Q7L1T6 - NB5R4_HUMAN

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Protein

Cytochrome b5 reductase 4

Gene

CYB5R4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS). Reduces a variety of substrates in vitro, such as cytochrome c, feericyanide and methemoglobin.

Catalytic activityi

NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.

Cofactori

FAD.1 Publication

Redox potential

E0 is -108 mV.

Kineticsi

  1. KM=25 mM for O2

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi89 – 891Iron (heme axial ligand)
Metal bindingi112 – 1121Iron (heme axial ligand)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi365 – 38016FADBy similarityAdd
BLAST
Nucleotide bindingi392 – 42433FADBy similarityAdd
BLAST

GO - Molecular functioni

  1. cytochrome-b5 reductase activity, acting on NAD(P)H Source: UniProtKB
  2. flavin adenine dinucleotide binding Source: Ensembl
  3. heme binding Source: Ensembl
  4. metal ion binding Source: UniProtKB-KW
  5. NAD(P)H oxidase activity Source: UniProtKB
  6. NADPH-hemoprotein reductase activity Source: Ensembl
  7. oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor Source: UniProtKB

GO - Biological processi

  1. cell development Source: UniProtKB
  2. detection of oxygen Source: UniProtKB
  3. generation of precursor metabolites and energy Source: UniProtKB
  4. glucose homeostasis Source: UniProtKB
  5. insulin secretion Source: UniProtKB
  6. NADP metabolic process Source: Ensembl
  7. oxidation-reduction process Source: UniProtKB
  8. response to antibiotic Source: UniProtKB
  9. superoxide metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b5 reductase 4 (EC:1.6.2.2)
Alternative name(s):
Flavohemoprotein b5/b5R
Short name:
b5+b5R
N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein
cb5/cb5R
Gene namesi
Name:CYB5R4
Synonyms:NCB5OR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:20147. CYB5R4.

Subcellular locationi

Endoplasmic reticulum 2 Publications
Note: Soluble protein.

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134904907.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Cytochrome b5 reductase 4PRO_0000287556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ7L1T6.
PaxDbiQ7L1T6.
PRIDEiQ7L1T6.

PTM databases

PhosphoSiteiQ7L1T6.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ7L1T6.
CleanExiHS_CYB5R4.
ExpressionAtlasiQ7L1T6. baseline and differential.
GenevestigatoriQ7L1T6.

Organism-specific databases

HPAiHPA018992.

Interactioni

Protein-protein interaction databases

BioGridi119347. 2 interactions.
IntActiQ7L1T6. 1 interaction.
MINTiMINT-4714403.
STRINGi9606.ENSP00000358695.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 575
Helixi59 – 646
Beta strandi70 – 756
Beta strandi78 – 814
Helixi83 – 853
Turni86 – 883
Helixi93 – 975
Turni98 – 1014
Helixi105 – 1128
Helixi117 – 1204
Helixi122 – 1243
Beta strandi125 – 1295
Helixi133 – 1364

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LF5X-ray1.25A/B51-137[»]
ProteinModelPortaliQ7L1T6.
SMRiQ7L1T6. Positions 51-137, 275-495.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7L1T6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 13077Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini165 – 25692CSPROSITE-ProRule annotationAdd
BLAST
Domaini273 – 385113FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CS domain.PROSITE-ProRule annotation
Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0543.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000230826.
HOVERGENiHBG108174.
InParanoidiQ7L1T6.
OMAiKDYHEEK.
OrthoDBiEOG718KBZ.
PhylomeDBiQ7L1T6.
TreeFamiTF313874.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
3.10.120.10. 1 hit.
InterProiIPR007052. CS_dom.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR008978. HSP20-like_chaperone.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF04969. CS. 1 hit.
PF00173. Cyt-b5. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
SUPFAMiSSF49764. SSF49764. 1 hit.
SSF55856. SSF55856. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51203. CS. 1 hit.
PS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7L1T6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLNVPSQSFP APRSQQRVAS GGRSKVPLKQ GRSLMDWIRL TKSGKDLTGL
60 70 80 90 100
KGRLIEVTEE ELKKHNKKDD CWICIRGFVY NVSPYMEYHP GGEDELMRAA
110 120 130 140 150
GSDGTELFDQ VHRWVNYESM LKECLVGRMA IKPAVLKDYR EEEKKVLNGM
160 170 180 190 200
LPKSQVTDTL AKEGPSYPSY DWFQTDSLVT IAIYTKQKDI NLDSIIVDHQ
210 220 230 240 250
NDSFRAETII KDCLYLIHIG LSHEVQEDFS VRVVESVGKI EIVLQKKENT
260 270 280 290 300
SWDFLGHPLK NHNSLIPRKD TGLYYRKCQL ISKEDVTHDT RLFCLMLPPS
310 320 330 340 350
THLQVPIGQH VYLKLPITGT EIVKPYTPVS GSLLSEFKEP VLPNNKYIYF
360 370 380 390 400
LIKIYPTGLF TPELDRLQIG DFVSVSSPEG NFKISKFQEL EDLFLLAAGT
410 420 430 440 450
GFTPMVKILN YALTDIPSLR KVKLMFFNKT EDDIIWRSQL EKLAFKDKRL
460 470 480 490 500
DVEFVLSAPI SEWNGKQGHI SPALLSEFLK RNLDKSKVLV CICGPVPFTE
510 520
QGVRLLHDLN FSKNEIHSFT A
Length:521
Mass (Da):59,474
Last modified:August 30, 2005 - v1
Checksum:i9D83BAB387E3B0F4
GO

Sequence cautioni

The sequence AAF04812.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAI19905.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI22326.1 differs from that shown. Reason: Erroneous gene model prediction.

Polymorphismi

Variants Arg-187 and Arg-223 do not influence the pathogenesis of non-autoimmune diabetes.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401R → H.1 Publication
Corresponds to variant rs61762820 [ dbSNP | Ensembl ].
VAR_047967
Natural varianti187 – 1871Q → R.1 Publication
VAR_032323
Natural varianti223 – 2231H → R.1 Publication
Corresponds to variant rs141290525 [ dbSNP | Ensembl ].
VAR_032324
Natural varianti267 – 2671P → A.1 Publication
Corresponds to variant rs61382555 [ dbSNP | Ensembl ].
VAR_047968
Natural varianti282 – 2821S → P.
Corresponds to variant rs10080628 [ dbSNP | Ensembl ].
VAR_032325
Natural varianti316 – 3161P → S.1 Publication
Corresponds to variant rs10080628 [ dbSNP | Ensembl ].
VAR_047969
Natural varianti371 – 3711D → Y in a breast cancer sample; somatic mutation. 1 Publication
VAR_036240
Natural varianti390 – 3901L → M in a breast cancer sample; somatic mutation. 1 Publication
VAR_036241

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EU448291 Genomic DNA. Translation: ACA06109.1.
AL139232, AL034347 Genomic DNA. Translation: CAI19904.2.
AL034347, AL139232 Genomic DNA. Translation: CAI22325.2.
AL034347, AL139232 Genomic DNA. Translation: CAI22326.1. Sequence problems.
AL139232, AL034347 Genomic DNA. Translation: CAI19905.1. Sequence problems.
BC025380 mRNA. Translation: AAH25380.2.
AF169803 mRNA. Translation: AAF04812.1. Different initiation.
CCDSiCCDS5000.2.
RefSeqiNP_057314.2. NM_016230.3.
UniGeneiHs.5741.

Genome annotation databases

EnsembliENST00000369681; ENSP00000358695; ENSG00000065615.
GeneIDi51167.
KEGGihsa:51167.
UCSCiuc003pkf.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EU448291 Genomic DNA. Translation: ACA06109.1 .
AL139232 , AL034347 Genomic DNA. Translation: CAI19904.2 .
AL034347 , AL139232 Genomic DNA. Translation: CAI22325.2 .
AL034347 , AL139232 Genomic DNA. Translation: CAI22326.1 . Sequence problems.
AL139232 , AL034347 Genomic DNA. Translation: CAI19905.1 . Sequence problems.
BC025380 mRNA. Translation: AAH25380.2 .
AF169803 mRNA. Translation: AAF04812.1 . Different initiation.
CCDSi CCDS5000.2.
RefSeqi NP_057314.2. NM_016230.3.
UniGenei Hs.5741.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LF5 X-ray 1.25 A/B 51-137 [» ]
ProteinModelPortali Q7L1T6.
SMRi Q7L1T6. Positions 51-137, 275-495.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119347. 2 interactions.
IntActi Q7L1T6. 1 interaction.
MINTi MINT-4714403.
STRINGi 9606.ENSP00000358695.

PTM databases

PhosphoSitei Q7L1T6.

Proteomic databases

MaxQBi Q7L1T6.
PaxDbi Q7L1T6.
PRIDEi Q7L1T6.

Protocols and materials databases

DNASUi 51167.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369681 ; ENSP00000358695 ; ENSG00000065615 .
GeneIDi 51167.
KEGGi hsa:51167.
UCSCi uc003pkf.3. human.

Organism-specific databases

CTDi 51167.
GeneCardsi GC06P084569.
HGNCi HGNC:20147. CYB5R4.
HPAi HPA018992.
MIMi 608343. gene.
neXtProti NX_Q7L1T6.
PharmGKBi PA134904907.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0543.
GeneTreei ENSGT00390000008881.
HOGENOMi HOG000230826.
HOVERGENi HBG108174.
InParanoidi Q7L1T6.
OMAi KDYHEEK.
OrthoDBi EOG718KBZ.
PhylomeDBi Q7L1T6.
TreeFami TF313874.

Miscellaneous databases

EvolutionaryTracei Q7L1T6.
GeneWikii CYB5R4.
GenomeRNAii 51167.
NextBioi 54103.
PROi Q7L1T6.
SOURCEi Search...

Gene expression databases

Bgeei Q7L1T6.
CleanExi HS_CYB5R4.
ExpressionAtlasi Q7L1T6. baseline and differential.
Genevestigatori Q7L1T6.

Family and domain databases

Gene3Di 2.60.40.790. 1 hit.
3.10.120.10. 1 hit.
InterProi IPR007052. CS_dom.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR008978. HSP20-like_chaperone.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF04969. CS. 1 hit.
PF00173. Cyt-b5. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PRINTSi PR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
SUPFAMi SSF49764. SSF49764. 1 hit.
SSF55856. SSF55856. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51203. CS. 1 hit.
PS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. SeattleSNPs variation discovery resource
    Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-140; ALA-267 AND SER-316.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Testis.
  4. "Identification of a cytochrome b-type NAD(P)H oxidoreductase ubiquitously expressed in human cells."
    Zhu H., Qiu H., Yoon H.-W., Huang S., Bunn H.F.
    Proc. Natl. Acad. Sci. U.S.A. 96:14742-14747(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-521, SUBCELLULAR LOCATION, HEME-BINDING, FAD-BINDING, TISSUE SPECIFICITY.
  5. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Study of the individual cytochrome b5 and cytochrome b5 reductase domains of Ncb5or reveals a unique heme pocket and a possible role of the CS domain."
    Deng B., Parthasarathy S., Wang W., Gibney B.R., Battaile K.P., Lovell S., Benson D.R., Zhu H.
    J. Biol. Chem. 285:30181-30191(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 51-137, HEME-BINDING SITES.
  7. "Variation in NCB5OR: studies of relationships to type 2 diabetes, maturity-onset diabetes of the young, and gestational diabetes mellitus."
    Andersen G., Wegner L., Rose C.S., Xie J., Zhu H., Larade K., Johansen A., Ek J., Lauenborg J., Drivsholm T., Borch-Johnsen K., Damm P., Hansen T., Bunn H.F., Pedersen O.
    Diabetes 53:2992-2997(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARG-187 AND ARG-223.
  8. Cited for: SUBCELLULAR LOCATION.
  9. Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-371 AND MET-390.

Entry informationi

Entry nameiNB5R4_HUMAN
AccessioniPrimary (citable) accession number: Q7L1T6
Secondary accession number(s): B1AEM2
, Q5TGI9, Q9NUE4, Q9UHI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: August 30, 2005
Last modified: October 29, 2014
This is version 94 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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