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Protein

Biliverdin reductase A

Gene

BLVRA

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

Functioni

Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.

Catalytic activityi

Bilirubin + NAD(P)+ = biliverdin + NAD(P)H.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Pathwayi: protoheme degradation

This protein is involved in the pathway protoheme degradation, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway protoheme degradation and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei98NAD or NADP; via carbonyl oxygen1
Metal bindingi280ZincSequence analysis1
Metal bindingi281ZincSequence analysis1
Metal bindingi292ZincSequence analysis1
Metal bindingi293ZincSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 20NAD or NADP6
Nucleotide bindingi44 – 46NAD or NADP3
Nucleotide bindingi77 – 80NAD or NADP4

GO - Molecular functioni

  • biliverdin reductase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • heme catabolic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS02928-MONOMER.
ZFISH:HS02928-MONOMER.
BRENDAi1.3.1.24. 2681.
ReactomeiR-HSA-189483. Heme degradation.
SIGNORiP53004.
UniPathwayiUPA00684.

Names & Taxonomyi

Protein namesi
Recommended name:
Biliverdin reductase A (EC:1.3.1.24)
Short name:
BVR A
Alternative name(s):
Biliverdin-IX alpha-reductase
Gene namesi
Name:BLVRA
Synonyms:BLVR, BVR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:1062. BLVRA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Hyperbiliverdinemia (HBLVD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition characterized by a green discoloration of the skin, urine, serum, and other bodily fluids. It is due to increased biliverdin resulting from inefficient conversion to bilirubin. Affected individuals appear to have symptoms only in the context of obstructive cholestasis and/or liver failure. In some cases, green jaundice can resolve after resolution of obstructive cholestasis.
See also OMIM:614156

Organism-specific databases

DisGeNETi644.
MalaCardsiBLVRA.
MIMi614156. phenotype.
OpenTargetsiENSG00000106605.
Orphaneti276405. Hyperbiliverdinemia.
PharmGKBiPA25373.

Polymorphism and mutation databases

BioMutaiBLVRA.
DMDMi23830892.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000108521 – 22 Publications2
ChainiPRO_00000108533 – 296Biliverdin reductase A1 PublicationAdd BLAST294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei174PhosphothreonineCombined sources1
Modified residuei178PhosphoserineCombined sources1
Modified residuei230PhosphoserineCombined sources1
Modified residuei248N6-acetyllysineCombined sources1
Modified residuei253N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP53004.
MaxQBiP53004.
PaxDbiP53004.
PeptideAtlasiP53004.
PRIDEiP53004.

2D gel databases

OGPiP53004.
REPRODUCTION-2DPAGEIPI00294158.

PTM databases

iPTMnetiP53004.
PhosphoSitePlusiP53004.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSG00000106605.
CleanExiHS_BLVRA.
ExpressionAtlasiP53004. baseline and differential.
GenevisibleiP53004. HS.

Organism-specific databases

HPAiHPA042865.
HPA054322.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
LNX1Q8TBB13EBI-7410441,EBI-739832

Protein-protein interaction databases

BioGridi107113. 16 interactors.
DIPiDIP-42180N.
IntActiP53004. 2 interactors.
MINTiMINT-1212210.
STRINGi9606.ENSP00000265523.

Structurei

Secondary structure

1296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 14Combined sources6
Helixi18 – 28Combined sources11
Helixi33 – 36Combined sources4
Beta strandi37 – 43Combined sources7
Beta strandi50 – 53Combined sources4
Helixi59 – 64Combined sources6
Beta strandi70 – 73Combined sources4
Helixi77 – 89Combined sources13
Beta strandi93 – 98Combined sources6
Helixi104 – 117Combined sources14
Beta strandi121 – 124Combined sources4
Helixi126 – 129Combined sources4
Helixi131 – 140Combined sources10
Beta strandi145 – 154Combined sources10
Helixi159 – 162Combined sources4
Helixi165 – 168Combined sources4
Helixi170 – 180Combined sources11
Beta strandi182 – 193Combined sources12
Beta strandi198 – 207Combined sources10
Beta strandi212 – 219Combined sources8
Beta strandi226 – 235Combined sources10
Helixi250 – 262Combined sources13
Helixi268 – 290Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H63X-ray2.70A/B/C/D7-296[»]
ProteinModelPortaliP53004.
SMRiP53004.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53004.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi11 – 16Poly-Val6

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IH7U. Eukaryota.
ENOG4111FZX. LUCA.
GeneTreeiENSGT00390000011072.
HOGENOMiHOG000231884.
HOVERGENiHBG003218.
InParanoidiP53004.
KOiK00214.
OMAiNMPNVGV.
OrthoDBiEOG091G0E2N.
PhylomeDBiP53004.
TreeFamiTF342889.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR017094. Biliverdin_Rdtase_A.
IPR015249. Biliverdin_Rdtase_cat.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF09166. Biliv-reduc_cat. 1 hit.
PF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
PIRSFiPIRSF037032. Biliverdin_reductase_A. 1 hit.
ProDomiPD040165. Biliverdin_Rdtase_cat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P53004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAEPERKFG VVVVGVGRAG SVRMRDLRNP HPSSAFLNLI GFVSRRELGS
60 70 80 90 100
IDGVQQISLE DALSSQEVEV AYICSESSSH EDYIRQFLNA GKHVLVEYPM
110 120 130 140 150
TLSLAAAQEL WELAEQKGKV LHEEHVELLM EEFAFLKKEV VGKDLLKGSL
160 170 180 190 200
LFTAGPLEEE RFGFPAFSGI SRLTWLVSLF GELSLVSATL EERKEDQYMK
210 220 230 240 250
MTVCLETEKK SPLSWIEEKG PGLKRNRYLS FHFKSGSLEN VPNVGVNKNI
260 270 280 290
FLKDQNIFVQ KLLGQFSEKE LAAEKKRILH CLGLAEEIQK YCCSRK
Length:296
Mass (Da):33,428
Last modified:October 10, 2002 - v2
Checksum:i2CF2AA7F1CDDB707
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti121L → S in AAH05902 (PubMed:15489334).Curated1
Sequence conflicti154 – 155AG → SD in CAA63635 (PubMed:8631357).Curated2
Sequence conflicti160E → D in CAA63635 (PubMed:8631357).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0192303A → T.3 PublicationsCorresponds to variant rs699512dbSNPEnsembl.1
Natural variantiVAR_01923137L → V.1 PublicationCorresponds to variant rs17245918dbSNPEnsembl.1
Natural variantiVAR_01485156Q → R.1 PublicationCorresponds to variant rs1050916dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34877 mRNA. Translation: AAC35588.1.
X93086 mRNA. Translation: CAA63635.1.
AK291862 mRNA. Translation: BAF84551.1.
AY616754 Genomic DNA. Translation: AAT11126.1.
AC005189 Genomic DNA. No translation available.
AC004939 Genomic DNA. Translation: AAD05025.1.
AC004985 Genomic DNA. Translation: AAP21879.1.
BC005902 mRNA. Translation: AAH05902.1.
BC008456 mRNA. Translation: AAH08456.1.
CCDSiCCDS5472.1.
PIRiG02066.
S62624.
RefSeqiNP_000703.2. NM_000712.3.
NP_001240752.1. NM_001253823.1.
XP_011513776.1. XM_011515474.2.
XP_016868009.1. XM_017012520.1.
UniGeneiHs.488143.

Genome annotation databases

EnsembliENST00000265523; ENSP00000265523; ENSG00000106605.
ENST00000402924; ENSP00000385757; ENSG00000106605.
GeneIDi644.
KEGGihsa:644.
UCSCiuc003tir.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34877 mRNA. Translation: AAC35588.1.
X93086 mRNA. Translation: CAA63635.1.
AK291862 mRNA. Translation: BAF84551.1.
AY616754 Genomic DNA. Translation: AAT11126.1.
AC005189 Genomic DNA. No translation available.
AC004939 Genomic DNA. Translation: AAD05025.1.
AC004985 Genomic DNA. Translation: AAP21879.1.
BC005902 mRNA. Translation: AAH05902.1.
BC008456 mRNA. Translation: AAH08456.1.
CCDSiCCDS5472.1.
PIRiG02066.
S62624.
RefSeqiNP_000703.2. NM_000712.3.
NP_001240752.1. NM_001253823.1.
XP_011513776.1. XM_011515474.2.
XP_016868009.1. XM_017012520.1.
UniGeneiHs.488143.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H63X-ray2.70A/B/C/D7-296[»]
ProteinModelPortaliP53004.
SMRiP53004.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107113. 16 interactors.
DIPiDIP-42180N.
IntActiP53004. 2 interactors.
MINTiMINT-1212210.
STRINGi9606.ENSP00000265523.

PTM databases

iPTMnetiP53004.
PhosphoSitePlusiP53004.

Polymorphism and mutation databases

BioMutaiBLVRA.
DMDMi23830892.

2D gel databases

OGPiP53004.
REPRODUCTION-2DPAGEIPI00294158.

Proteomic databases

EPDiP53004.
MaxQBiP53004.
PaxDbiP53004.
PeptideAtlasiP53004.
PRIDEiP53004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265523; ENSP00000265523; ENSG00000106605.
ENST00000402924; ENSP00000385757; ENSG00000106605.
GeneIDi644.
KEGGihsa:644.
UCSCiuc003tir.4. human.

Organism-specific databases

CTDi644.
DisGeNETi644.
GeneCardsiBLVRA.
HGNCiHGNC:1062. BLVRA.
HPAiHPA042865.
HPA054322.
MalaCardsiBLVRA.
MIMi109750. gene.
614156. phenotype.
neXtProtiNX_P53004.
OpenTargetsiENSG00000106605.
Orphaneti276405. Hyperbiliverdinemia.
PharmGKBiPA25373.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IH7U. Eukaryota.
ENOG4111FZX. LUCA.
GeneTreeiENSGT00390000011072.
HOGENOMiHOG000231884.
HOVERGENiHBG003218.
InParanoidiP53004.
KOiK00214.
OMAiNMPNVGV.
OrthoDBiEOG091G0E2N.
PhylomeDBiP53004.
TreeFamiTF342889.

Enzyme and pathway databases

UniPathwayiUPA00684.
BioCyciMetaCyc:HS02928-MONOMER.
ZFISH:HS02928-MONOMER.
BRENDAi1.3.1.24. 2681.
ReactomeiR-HSA-189483. Heme degradation.
SIGNORiP53004.

Miscellaneous databases

ChiTaRSiBLVRA. human.
EvolutionaryTraceiP53004.
GenomeRNAii644.
PROiP53004.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106605.
CleanExiHS_BLVRA.
ExpressionAtlasiP53004. baseline and differential.
GenevisibleiP53004. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR017094. Biliverdin_Rdtase_A.
IPR015249. Biliverdin_Rdtase_cat.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF09166. Biliv-reduc_cat. 1 hit.
PF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
PIRSFiPIRSF037032. Biliverdin_reductase_A. 1 hit.
ProDomiPD040165. Biliverdin_Rdtase_cat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBIEA_HUMAN
AccessioniPrimary (citable) accession number: P53004
Secondary accession number(s): A8K747
, O95019, Q86UX0, Q96QL4, Q9BRW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 10, 2002
Last modified: November 30, 2016
This is version 164 of the entry and version 2 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

Miscellaneous

Uses the reactants NADH or NADPH depending on the pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7). NADPH, however, is the probable reactant in biological systems.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.