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P30043

- BLVRB_HUMAN

UniProt

P30043 - BLVRB_HUMAN

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Protein

Flavin reductase (NADPH)

Gene

BLVRB

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

Functioni

Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe3+ iron to Fe2+ in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin.1 Publication

Catalytic activityi

Reduced riboflavin + NADP+ = riboflavin + NADPH.
Bilirubin + NAD(P)+ = biliverdin + NAD(P)H.

Enzyme regulationi

Mesobiliverdin acts as competitve inhibitor for flavin reduction, indicating that flavin and tetrapyrrole substrates compete for the same site.1 Publication

Kineticsi

  1. KM=36 µM for NADP2 Publications
  2. KM=5.6 mM for NADH2 Publications
  3. KM=0.3 µM for biliverdin IX-beta2 Publications
  4. KM=52 µM for FMN2 Publications
  5. KM=125 µM for FAD2 Publications
  6. KM=53 µM for riboflavin2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei35 – 351NADP
Binding sitei132 – 1321NADP
Binding sitei153 – 1531Substrate
Binding sitei154 – 1541NADP; via amide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156NADP
Nucleotide bindingi54 – 552NADP
Nucleotide bindingi75 – 784NADP

GO - Molecular functioni

  1. biliverdin reductase activity Source: UniProtKB
  2. riboflavin reductase (NADPH) activity Source: UniProtKB

GO - Biological processi

  1. heme catabolic process Source: UniProtKB
  2. porphyrin-containing compound metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_22297. Heme degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Flavin reductase (NADPH) (EC:1.5.1.30)
Short name:
FR
Alternative name(s):
Biliverdin reductase B (EC:1.3.1.24)
Short name:
BVR-B
Biliverdin-IX beta-reductase
Green heme-binding protein
Short name:
GHBP
NADPH-dependent diaphorase
NADPH-flavin reductase
Short name:
FLR
Gene namesi
Name:BLVRB
Synonyms:FLR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:1063. BLVRB.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: HPA
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi153 – 1531H → A: Reduced affinity for biliverdin. 1 Publication

Organism-specific databases

PharmGKBiPA25374.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 206205Flavin reductase (NADPH)PRO_0000064948Add
BLAST

Proteomic databases

MaxQBiP30043.
PaxDbiP30043.
PRIDEiP30043.

2D gel databases

DOSAC-COBS-2DPAGEP30043.
REPRODUCTION-2DPAGEIPI00783862.
SWISS-2DPAGEP30043.
UCD-2DPAGEP30043.

PTM databases

PhosphoSiteiP30043.

Expressioni

Tissue specificityi

Predominantly expressed in liver and erythrocytes. At lower levels in heart, lung, adrenal gland and cerebrum.1 Publication

Gene expression databases

BgeeiP30043.
CleanExiHS_BLVRB.
ExpressionAtlasiP30043. baseline and differential.
GenevestigatoriP30043.

Organism-specific databases

HPAiHPA041698.
HPA041937.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi107114. 10 interactions.
IntActiP30043. 5 interactions.
MINTiMINT-5001335.
STRINGi9606.ENSP00000263368.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106
Helixi14 – 2512
Beta strandi29 – 357
Helixi37 – 393
Beta strandi42 – 443
Beta strandi48 – 536
Helixi58 – 658
Beta strandi69 – 735
Helixi86 – 10116
Beta strandi105 – 1095
Helixi112 – 1143
Helixi118 – 1203
Helixi123 – 1253
Helixi126 – 14116
Beta strandi144 – 1496
Beta strandi152 – 1554
Beta strandi164 – 1696
Beta strandi174 – 1774
Helixi178 – 18710
Helixi188 – 1903
Turni193 – 1964
Beta strandi198 – 2025

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HDOX-ray1.15A2-205[»]
1HE2X-ray1.20A2-205[»]
1HE3X-ray1.40A2-205[»]
1HE4X-ray1.40A2-205[»]
1HE5X-ray1.50A2-205[»]
ProteinModelPortaliP30043.
SMRiP30043. Positions 1-205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30043.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG239698.
HOGENOMiHOG000262432.
HOVERGENiHBG050695.
InParanoidiP30043.
KOiK05901.
OMAiTDEYNGH.
PhylomeDBiP30043.
TreeFamiTF324063.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30043-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVKKIAIFG ATGQTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPRPAHV
60 70 80 90 100
VVGDVLQAAD VDKTVAGQDA VIVLLGTRND LSPTTVMSEG ARNIVAAMKA
110 120 130 140 150
HGVDKVVACT SAFLLWDPTK VPPRLQAVTD DHIRMHKVLR ESGLKYVAVM
160 170 180 190 200
PPHIGDQPLT GAYTVTLDGR GPSRVISKHD LGHFMLRCLT TDEYDGHSTY

PSHQYQ
Length:206
Mass (Da):22,119
Last modified:January 23, 2007 - v3
Checksum:i3057E6D69A9F9F9F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161G → C AA sequence (PubMed:7929092)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461R → Q.1 Publication
Corresponds to variant rs11547746 [ dbSNP | Ensembl ].
VAR_019168

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26308 mRNA. Translation: BAA05370.1.
D32143 mRNA. Translation: BAA06874.1.
AK312137 mRNA. Translation: BAG35073.1.
AY340485 Genomic DNA. Translation: AAP88933.1.
AC010271 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW56969.1.
BC109371 mRNA. Translation: AAI09372.1.
CCDSiCCDS33029.1.
PIRiJC2070.
RefSeqiNP_000704.1. NM_000713.2.
UniGeneiHs.515785.

Genome annotation databases

EnsembliENST00000263368; ENSP00000263368; ENSG00000090013.
GeneIDi645.
KEGGihsa:645.
UCSCiuc002onw.2. human.

Polymorphism databases

DMDMi1706870.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26308 mRNA. Translation: BAA05370.1 .
D32143 mRNA. Translation: BAA06874.1 .
AK312137 mRNA. Translation: BAG35073.1 .
AY340485 Genomic DNA. Translation: AAP88933.1 .
AC010271 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW56969.1 .
BC109371 mRNA. Translation: AAI09372.1 .
CCDSi CCDS33029.1.
PIRi JC2070.
RefSeqi NP_000704.1. NM_000713.2.
UniGenei Hs.515785.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HDO X-ray 1.15 A 2-205 [» ]
1HE2 X-ray 1.20 A 2-205 [» ]
1HE3 X-ray 1.40 A 2-205 [» ]
1HE4 X-ray 1.40 A 2-205 [» ]
1HE5 X-ray 1.50 A 2-205 [» ]
ProteinModelPortali P30043.
SMRi P30043. Positions 1-205.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107114. 10 interactions.
IntActi P30043. 5 interactions.
MINTi MINT-5001335.
STRINGi 9606.ENSP00000263368.

Chemistry

DrugBanki DB00140. Riboflavin.

PTM databases

PhosphoSitei P30043.

Polymorphism databases

DMDMi 1706870.

2D gel databases

DOSAC-COBS-2DPAGE P30043.
REPRODUCTION-2DPAGE IPI00783862.
SWISS-2DPAGE P30043.
UCD-2DPAGE P30043.

Proteomic databases

MaxQBi P30043.
PaxDbi P30043.
PRIDEi P30043.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263368 ; ENSP00000263368 ; ENSG00000090013 .
GeneIDi 645.
KEGGi hsa:645.
UCSCi uc002onw.2. human.

Organism-specific databases

CTDi 645.
GeneCardsi GC19M040953.
HGNCi HGNC:1063. BLVRB.
HPAi HPA041698.
HPA041937.
MIMi 600941. gene.
neXtProti NX_P30043.
PharmGKBi PA25374.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239698.
HOGENOMi HOG000262432.
HOVERGENi HBG050695.
InParanoidi P30043.
KOi K05901.
OMAi TDEYNGH.
PhylomeDBi P30043.
TreeFami TF324063.

Enzyme and pathway databases

Reactomei REACT_22297. Heme degradation.

Miscellaneous databases

EvolutionaryTracei P30043.
GenomeRNAii 645.
NextBioi 2618.
PROi P30043.
SOURCEi Search...

Gene expression databases

Bgeei P30043.
CleanExi HS_BLVRB.
ExpressionAtlasi P30043. baseline and differential.
Genevestigatori P30043.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR016040. NAD(P)-bd_dom.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-flavin reductase."
    Chikuba K., Yubisui T., Shirabe K., Takeshita M.
    Biochem. Biophys. Res. Commun. 198:1170-1176(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-34; 63-87 AND 98-206.
    Tissue: Erythrocyte and Reticulocyte.
  2. "Molecular cloning and expression of human liver biliverdin-IXbeta reductase."
    Komuro A., Tobe T., Hashimoto K., Nakano Y., Yamaguchi T., Nakajima H., Tomita M.
    Biol. Pharm. Bull. 19:796-804(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  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].
    Tissue: Cerebellum.
  4. NIEHS SNPs program
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-46.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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].
    Tissue: Pancreas.
  8. "Complete amino acid sequence of biliverdin-IX beta reductase from human liver."
    Yamaguchi T., Komuro A., Nakano Y., Tomita M., Nakajima H.
    Biochem. Biophys. Res. Commun. 197:1518-1523(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-205.
    Tissue: Liver.
  9. "Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization."
    Yamaguchi T., Komoda Y., Nakajima H.
    J. Biol. Chem. 269:24343-24348(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21, SUBUNIT, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Tissue: Liver.
  10. "Human liver protein map: a reference database established by microsequencing and gel comparison."
    Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
    Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Tissue: Liver.
  11. Cited for: PROTEIN SEQUENCE OF 2-11.
    Tissue: Erythrocyte.
  12. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 40-92; 64-78; 106-124 AND 146-170, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  13. "Evidence that biliverdin-IX beta reductase and flavin reductase are identical."
    Shalloe F., Elliott G., Ennis O., Mantle T.J.
    Biochem. J. 316:385-387(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTITY OF FR AND BVR-B.
  14. "Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXbeta reductase (BVR-B)."
    Cunningham O., Gore M.G., Mantle T.J.
    Biochem. J. 345:393-399(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  15. "Computational and experimental studies on the catalytic mechanism of biliverdin-IXbeta reductase."
    Smith L.J., Browne S., Mulholland A.J., Mantle T.J.
    Biochem. J. 411:475-484(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-153.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme."
    Pereira P.J., Macedo-Ribeiro S., Parraga A., Perez-Luque R., Cunningham O., Darcy K., Mantle T.J., Coll M.
    Nat. Struct. Biol. 8:215-220(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEXES WITH MESOBILIVERDIN; BILIVERDIN; FLAVIN MONONUCLEOTIDE; LUMICHROME AND NADP, SUBUNIT.

Entry informationi

Entry nameiBLVRB_HUMAN
AccessioniPrimary (citable) accession number: P30043
Secondary accession number(s): A6NKD8
, B2R5C6, P32078, P53005, Q32LZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 149 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

External Data

Dasty 3