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P53004

- BIEA_HUMAN

UniProt

P53004 - BIEA_HUMAN

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Protein
Biliverdin reductase A
Gene
BLVRA, BLVR, BVR
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 zinc ion per subunit.

Pathwayi

Sites

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
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 – 22
PRO_0000010852
Chaini3 – 296294Biliverdin reductase A1 Publication
PRO_0000010853Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei174 – 1741Phosphothreonine
Modified residuei178 – 1781Phosphoserine
Modified residuei230 – 2301Phosphoserine
Modified residuei248 – 2481N6-acetyllysine
Modified residuei253 – 2531N6-acetyllysine

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.

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211L → S in AAH05902. 1 Publication
Sequence conflicti154 – 1552AG → SD in CAA63635. 1 Publication
Sequence conflicti160 – 1601E → D in CAA63635. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 139 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

Dasty 3

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