Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Flavin reductase (NADPH)

Gene

BLVRB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

    • biliverdin reductase activity Source: UniProtKB
    • riboflavin reductase (NADPH) activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BRENDAi1.3.1.24. 2681.
    1.5.1.30. 2681.
    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 Componenti: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:1063. BLVRB.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    • nucleoplasm Source: HPA
    • 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.

    Chemistry

    DrugBankiDB00140. Riboflavin.

    Polymorphism and mutation databases

    BioMutaiBLVRB.
    DMDMi1706870.

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    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. 12 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 – 106Combined sources
    Helixi14 – 2512Combined sources
    Beta strandi29 – 357Combined sources
    Helixi37 – 393Combined sources
    Beta strandi42 – 443Combined sources
    Beta strandi48 – 536Combined sources
    Helixi58 – 658Combined sources
    Beta strandi69 – 735Combined sources
    Helixi86 – 10116Combined sources
    Beta strandi105 – 1095Combined sources
    Helixi112 – 1143Combined sources
    Helixi118 – 1203Combined sources
    Helixi123 – 1253Combined sources
    Helixi126 – 14116Combined sources
    Beta strandi144 – 1496Combined sources
    Beta strandi152 – 1554Combined sources
    Beta strandi164 – 1696Combined sources
    Beta strandi174 – 1774Combined sources
    Helixi178 – 18710Combined sources
    Helixi188 – 1903Combined sources
    Turni193 – 1964Combined sources
    Beta strandi198 – 2025Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Protein-protein interaction databases

    BioGridi107114. 12 interactions.
    IntActiP30043. 5 interactions.
    MINTiMINT-5001335.
    STRINGi9606.ENSP00000263368.

    Chemistry

    DrugBankiDB00140. Riboflavin.

    PTM databases

    PhosphoSiteiP30043.

    Polymorphism and mutation databases

    BioMutaiBLVRB.
    DMDMi1706870.

    2D gel databases

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

    Proteomic databases

    PaxDbiP30043.
    PRIDEiP30043.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi645.
    GeneCardsiGC19M040953.
    HGNCiHGNC:1063. BLVRB.
    HPAiHPA041698.
    HPA041937.
    MIMi600941. gene.
    neXtProtiNX_P30043.
    PharmGKBiPA25374.
    GenAtlasiSearch...

    Phylogenomic databases

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

    Enzyme and pathway databases

    BRENDAi1.3.1.24. 2681.
    1.5.1.30. 2681.
    ReactomeiREACT_22297. Heme degradation.

    Miscellaneous databases

    EvolutionaryTraceiP30043.
    GenomeRNAii645.
    NextBioi2618.
    PROiP30043.
    SOURCEiSearch...

    Gene expression databases

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

    Family and domain databases

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

    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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "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: May 27, 2015
    This is version 156 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

    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 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.