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P53004

- BIEA_HUMAN

UniProt

P53004 - BIEA_HUMAN

Protein

Biliverdin reductase A

Gene

BLVRA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (10 Oct 2002)
      Previous versions | rss
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    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

    Binds 1 zinc ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei98 – 981NAD or NADP; via carbonyl oxygen
    Metal bindingi280 – 2801ZincSequence Analysis
    Metal bindingi281 – 2811ZincSequence Analysis
    Metal bindingi292 – 2921ZincSequence Analysis
    Metal bindingi293 – 2931ZincSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 206NAD or NADP
    Nucleotide bindingi44 – 463NAD or NADP
    Nucleotide bindingi77 – 804NAD or NADP

    GO - Molecular functioni

    1. biliverdin reductase activity Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. heme catabolic process Source: UniProtKB
    2. oxidation-reduction process Source: UniProtKB
    3. porphyrin-containing compound metabolic process Source: Reactome
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, NADP, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02928-MONOMER.
    ReactomeiREACT_22297. Heme degradation.
    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
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:1062. BLVRA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Hyperbiliverdinemia (HBLVD) [MIM:614156]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi614156. phenotype.
    Orphaneti276405. Hyperbiliverdinemia.
    PharmGKBiPA25373.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 222 PublicationsPRO_0000010852
    Chaini3 – 296294Biliverdin reductase A1 PublicationPRO_0000010853Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei174 – 1741Phosphothreonine1 Publication
    Modified residuei178 – 1781Phosphoserine1 Publication
    Modified residuei230 – 2301Phosphoserine1 Publication
    Modified residuei248 – 2481N6-acetyllysine1 Publication
    Modified residuei253 – 2531N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP53004.
    PaxDbiP53004.
    PeptideAtlasiP53004.
    PRIDEiP53004.

    2D gel databases

    OGPiP53004.
    REPRODUCTION-2DPAGEIPI00294158.

    PTM databases

    PhosphoSiteiP53004.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    ArrayExpressiP53004.
    BgeeiP53004.
    CleanExiHS_BLVRA.
    GenevestigatoriP53004.

    Organism-specific databases

    HPAiHPA042865.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi107113. 3 interactions.
    DIPiDIP-42180N.
    MINTiMINT-1212210.
    STRINGi9606.ENSP00000265523.

    Structurei

    Secondary structure

    1
    296
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 146
    Helixi18 – 2811
    Helixi33 – 364
    Beta strandi37 – 437
    Beta strandi50 – 534
    Helixi59 – 646
    Beta strandi70 – 734
    Helixi77 – 8913
    Beta strandi93 – 986
    Helixi104 – 11714
    Beta strandi121 – 1244
    Helixi126 – 1294
    Helixi131 – 14010
    Beta strandi145 – 15410
    Helixi159 – 1624
    Helixi165 – 1684
    Helixi170 – 18011
    Beta strandi182 – 19312
    Beta strandi198 – 20710
    Beta strandi212 – 2198
    Beta strandi226 – 23510
    Helixi250 – 26213
    Helixi268 – 29023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H63X-ray2.70A/B/C/D7-296[»]
    ProteinModelPortaliP53004.
    SMRiP53004. Positions 7-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53004.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 166Poly-Val

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG114525.
    HOGENOMiHOG000231884.
    HOVERGENiHBG003218.
    InParanoidiP53004.
    KOiK00214.
    OMAiKRILHCL.
    OrthoDBiEOG78WKS5.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P53004-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAEPERKFG VVVVGVGRAG SVRMRDLRNP HPSSAFLNLI GFVSRRELGS    50
    IDGVQQISLE DALSSQEVEV AYICSESSSH EDYIRQFLNA GKHVLVEYPM 100
    TLSLAAAQEL WELAEQKGKV LHEEHVELLM EEFAFLKKEV VGKDLLKGSL 150
    LFTAGPLEEE RFGFPAFSGI SRLTWLVSLF GELSLVSATL EERKEDQYMK 200
    MTVCLETEKK SPLSWIEEKG PGLKRNRYLS FHFKSGSLEN VPNVGVNKNI 250
    FLKDQNIFVQ KLLGQFSEKE LAAEKKRILH CLGLAEEIQK YCCSRK 296
    Length:296
    Mass (Da):33,428
    Last modified:October 10, 2002 - v2
    Checksum:i2CF2AA7F1CDDB707
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211L → S in AAH05902. (PubMed:15489334)Curated
    Sequence conflicti154 – 1552AG → SD in CAA63635. (PubMed:8631357)Curated
    Sequence conflicti160 – 1601E → D in CAA63635. (PubMed:8631357)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31A → T.3 Publications
    Corresponds to variant rs699512 [ dbSNP | Ensembl ].
    VAR_019230
    Natural varianti37 – 371L → V.1 Publication
    Corresponds to variant rs17245918 [ dbSNP | Ensembl ].
    VAR_019231
    Natural varianti56 – 561Q → R.1 Publication
    Corresponds to variant rs1050916 [ dbSNP | Ensembl ].
    VAR_014851

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UniGeneiHs.488143.

    Genome annotation databases

    EnsembliENST00000265523; ENSP00000265523; ENSG00000106605.
    ENST00000402924; ENSP00000385757; ENSG00000106605.
    GeneIDi644.
    KEGGihsa:644.
    UCSCiuc003tir.3. human.

    Polymorphism databases

    DMDMi23830892.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS5472.1.
    PIRi G02066.
    S62624.
    RefSeqi NP_000703.2. NM_000712.3.
    NP_001240752.1. NM_001253823.1.
    UniGenei Hs.488143.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H63 X-ray 2.70 A/B/C/D 7-296 [» ]
    ProteinModelPortali P53004.
    SMRi P53004. Positions 7-291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107113. 3 interactions.
    DIPi DIP-42180N.
    MINTi MINT-1212210.
    STRINGi 9606.ENSP00000265523.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P53004.

    Polymorphism databases

    DMDMi 23830892.

    2D gel databases

    OGPi P53004.
    REPRODUCTION-2DPAGE IPI00294158.

    Proteomic databases

    MaxQBi P53004.
    PaxDbi P53004.
    PeptideAtlasi P53004.
    PRIDEi P53004.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265523 ; ENSP00000265523 ; ENSG00000106605 .
    ENST00000402924 ; ENSP00000385757 ; ENSG00000106605 .
    GeneIDi 644.
    KEGGi hsa:644.
    UCSCi uc003tir.3. human.

    Organism-specific databases

    CTDi 644.
    GeneCardsi GC07P043798.
    HGNCi HGNC:1062. BLVRA.
    HPAi HPA042865.
    MIMi 109750. gene.
    614156. phenotype.
    neXtProti NX_P53004.
    Orphaneti 276405. Hyperbiliverdinemia.
    PharmGKBi PA25373.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG114525.
    HOGENOMi HOG000231884.
    HOVERGENi HBG003218.
    InParanoidi P53004.
    KOi K00214.
    OMAi KRILHCL.
    OrthoDBi EOG78WKS5.
    PhylomeDBi P53004.
    TreeFami TF342889.

    Enzyme and pathway databases

    UniPathwayi UPA00684 .
    BioCyci MetaCyc:HS02928-MONOMER.
    Reactomei REACT_22297. Heme degradation.

    Miscellaneous databases

    EvolutionaryTracei P53004.
    GenomeRNAii 644.
    NextBioi 2614.
    PROi P53004.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53004.
    Bgeei P53004.
    CleanExi HS_BLVRA.
    Genevestigatori P53004.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR017094. Biliverdin_Rdtase_A.
    IPR015249. Biliverdin_Rdtase_cat.
    IPR016040. NAD(P)-bd_dom.
    IPR000683. Oxidoreductase_N.
    [Graphical view ]
    Pfami PF09166. Biliv-reduc_cat. 1 hit.
    PF01408. GFO_IDH_MocA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037032. Biliverdin_reductase_A. 1 hit.
    ProDomi PD040165. Biliverdin_Rdtase_cat. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the cDNA encoding human biliverdin-IX alpha reductase."
      Komuro A., Tobe T., Nakano Y., Yamaguchi T., Tomita M.
      Biochim. Biophys. Acta 1309:89-99(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-3.
    2. "Human biliverdin IXalpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes."
      Maines M.D., Polevoda B.V., Huang T.-J., McCoubrey W.K. Jr.
      Eur. J. Biochem. 235:372-381(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    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: Skeletal muscle.
    4. NIEHS SNPs program
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-3; VAL-37 AND ARG-56.
    5. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANT THR-3.
      Tissue: Brain and Prostate.
    7. "Purification and characterization of human biliverdin reductase."
      Maines M.D., Trakshel G.M.
      Arch. Biochem. Biophys. 300:320-326(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 3-36; 48-74 AND 228-248.
      Tissue: Liver.
    8. "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 3-22.
      Tissue: Liver.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "A novel mutation in the biliverdin reductase-A gene combined with liver cirrhosis results in hyperbiliverdinaemia (green jaundice)."
      Gafvels M., Holmstrom P., Somell A., Sjovall F., Svensson J.O., Stahle L., Broome U., Stal P.
      Liver Int. 29:1116-1124(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HBLVD.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174 AND SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-248 AND LYS-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Crystal structure of human biliverdin reductase A."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-296 IN COMPLEX WITH NADP.

    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: October 1, 2014
    This is version 140 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

    External Data

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