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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

  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

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

  1. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleoplasm 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.

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

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. 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.

Polymorphism and mutation databases

BioMutaiBLVRB.

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

MaxQBiP30043.
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: April 29, 2015
This is version 155 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.