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Protein

Cytochrome b5

Gene

CYB5A

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441Iron (heme axial ligand)PROSITE-ProRule annotation1 Publication
Metal bindingi68 – 681Iron (heme axial ligand)PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-196836. Vitamin C (ascorbate) metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b5
Gene namesi
Name:CYB5A
Synonyms:CYB5
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 24

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei109 – 13123HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 134133Cytochrome b5PRO_0000166008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei7 – 71N6-acetyllysineBy similarity
Modified residuei10 – 101N6-acetyllysineBy similarity
Modified residuei19 – 191N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00171.
PRIDEiP00171.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015944.

Structurei

Secondary structure

1
134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124Combined sources
Helixi14 – 174Combined sources
Beta strandi21 – 244Combined sources
Beta strandi25 – 306Combined sources
Beta strandi33 – 364Combined sources
Turni38 – 436Combined sources
Helixi49 – 546Combined sources
Beta strandi56 – 583Combined sources
Helixi60 – 656Combined sources
Helixi70 – 767Combined sources
Turni77 – 793Combined sources
Beta strandi80 – 845Combined sources
Helixi86 – 916Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CYOX-ray1.50A6-98[»]
1EHBX-ray1.90A8-89[»]
1ES1X-ray2.10A8-89[»]
1F03NMR-A8-89[»]
1F04NMR-A8-89[»]
1HKONMR-A2-105[»]
1I5UNMR-A8-89[»]
1J0QNMR-A8-89[»]
1LQXX-ray1.80A8-89[»]
1LR6X-ray1.90A8-89[»]
1M20X-ray1.80A8-89[»]
1M2IX-ray1.80A8-89[»]
1M2MX-ray1.80A8-89[»]
1M59X-ray1.90A8-89[»]
1NX7NMR-A8-89[»]
1SH4NMR-A8-89[»]
1U9MX-ray2.00A/B/C/D/E/F8-89[»]
1U9UX-ray1.86A8-89[»]
3OZZX-ray1.70B8-89[»]
4HINX-ray2.40A/B/C/D8-89[»]
ProteinModelPortaliP00171.
SMRiP00171. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00171.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 8577Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cytochrome b5 family.Curated
Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0537. Eukaryota.
COG5274. LUCA.
GeneTreeiENSGT00510000046507.
HOGENOMiHOG000039853.
HOVERGENiHBG002653.
InParanoidiP00171.
OMAiWTNWLIP.
OrthoDBiEOG78H3W2.
TreeFamiTF314537.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
[Graphical view]
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEESSKAVK YYTLEEIQKH NNSKSTWLIL HYKVYDLTKF LEEHPGGEEV
60 70 80 90 100
LREQAGGDAT ENFEDVGHST DARELSKTFI IGELHPDDRS KITKPSESII
110 120 130
TTIDSNPSWW TNWLIPAISA LFVALIYHLY TSEN
Length:134
Mass (Da):15,329
Last modified:January 23, 2007 - v3
Checksum:i7B7B605158D97525
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 54AEES → ZSZZBA AA sequence (PubMed:4810060).Curated
Sequence conflicti16 – 183EIQ → QIE AA sequence (PubMed:5391285).Curated
Sequence conflicti18 – 181Q → E AA sequence (PubMed:5272324).Curated
Sequence conflicti62 – 621N → D AA sequence (PubMed:5391285).Curated
Sequence conflicti62 – 621N → D AA sequence (PubMed:5272324).Curated
Sequence conflicti134 – 1341N → D AA sequence (PubMed:4810060).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13617 mRNA. Translation: CAA31949.1.
M63328, M63326, M63327 Genomic DNA. Translation: AAC14455.1. Sequence problems.
L22966 Genomic DNA. No translation available.
BC108113 mRNA. Translation: AAI08114.1.
PIRiA47215. CBBO5.
RefSeqiNP_776458.1. NM_174033.3.
UniGeneiBt.65097.

Genome annotation databases

EnsembliENSBTAT00000015944; ENSBTAP00000015944; ENSBTAG00000012012.
GeneIDi281110.
KEGGibta:281110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13617 mRNA. Translation: CAA31949.1.
M63328, M63326, M63327 Genomic DNA. Translation: AAC14455.1. Sequence problems.
L22966 Genomic DNA. No translation available.
BC108113 mRNA. Translation: AAI08114.1.
PIRiA47215. CBBO5.
RefSeqiNP_776458.1. NM_174033.3.
UniGeneiBt.65097.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CYOX-ray1.50A6-98[»]
1EHBX-ray1.90A8-89[»]
1ES1X-ray2.10A8-89[»]
1F03NMR-A8-89[»]
1F04NMR-A8-89[»]
1HKONMR-A2-105[»]
1I5UNMR-A8-89[»]
1J0QNMR-A8-89[»]
1LQXX-ray1.80A8-89[»]
1LR6X-ray1.90A8-89[»]
1M20X-ray1.80A8-89[»]
1M2IX-ray1.80A8-89[»]
1M2MX-ray1.80A8-89[»]
1M59X-ray1.90A8-89[»]
1NX7NMR-A8-89[»]
1SH4NMR-A8-89[»]
1U9MX-ray2.00A/B/C/D/E/F8-89[»]
1U9UX-ray1.86A8-89[»]
3OZZX-ray1.70B8-89[»]
4HINX-ray2.40A/B/C/D8-89[»]
ProteinModelPortaliP00171.
SMRiP00171. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015944.

Proteomic databases

PaxDbiP00171.
PRIDEiP00171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000015944; ENSBTAP00000015944; ENSBTAG00000012012.
GeneIDi281110.
KEGGibta:281110.

Organism-specific databases

CTDi1528.

Phylogenomic databases

eggNOGiKOG0537. Eukaryota.
COG5274. LUCA.
GeneTreeiENSGT00510000046507.
HOGENOMiHOG000039853.
HOVERGENiHBG002653.
InParanoidiP00171.
OMAiWTNWLIP.
OrthoDBiEOG78H3W2.
TreeFamiTF314537.

Enzyme and pathway databases

ReactomeiR-BTA-196836. Vitamin C (ascorbate) metabolism.

Miscellaneous databases

EvolutionaryTraceiP00171.
NextBioi20805181.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
[Graphical view]
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete nucleotide sequence of bovine liver cytochrome b5 mRNA."
    Cristiano R.J., Steggles A.W.
    Nucleic Acids Res. 17:799-799(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The isolation and characterization of the bovine cytochrome b5 gene, and a transcribed pseudogene."
    Cristiano R.J., Giordano S.J., Steggles A.W.
    Genomics 17:348-354(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal liver.
  4. "Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5."
    Abe K., Kimura S., Kizawa R., Anan F.K., Sugita Y.
    J. Biochem. 97:1659-1668(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-98, ACETYLATION AT ALA-2.
    Tissue: Erythrocyte.
  5. "Cytochrome b5 from microsomal membranes of equine, bovine, and porcine livers. Isolation and properties of preparations containing the membranous segment."
    Ozols J.
    Biochemistry 13:426-434(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11 AND 131-134.
  6. "Structure of cytochrome b5 and its topology in the microsomal membrane."
    Ozols J.
    Biochim. Biophys. Acta 997:121-130(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-6 AND 15-18, ACETYLATION AT ALA-2.
  7. "Correction of the amino acid sequence of calf liver microsomal cytochrome b5."
    Ozols J., Strittmatter P.
    J. Biol. Chem. 244:6617-6618(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 6-98.
  8. "Comparative study of the primary structures of cytochrome b5 from four species."
    Tsugita A., Kobayashi M., Tani S., Kyo S., Rashid M.A., Yoshida Y., Kajihara T., Hagihara B.
    Proc. Natl. Acad. Sci. U.S.A. 67:442-447(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 6-96.
  9. "The primary structure of the nonpolar segment of bovine cytochrome b5."
    Fleming P.J., Dailey H.A., Corcoran D., Strittmatter P.
    J. Biol. Chem. 253:5369-5372(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 92-134.
  10. "The structure of cytochrome b-5 at 2.0-A resolution."
    Mathews F.S., Argos P., Levine M.
    Cold Spring Harb. Symp. Quant. Biol. 37:387-395(1971)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OXIDIZED FORM.
  11. "The structure of ferrocytochrome b5 at 2.8-A resolution."
    Argos P., Mathews F.S.
    J. Biol. Chem. 250:747-751(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF REDUCED FORM.
  12. "Refinement and structural analysis of bovine cytochrome b5 at 1.5-A resolution."
    Durley R.C.E., Mathews F.S.
    Acta Crystallogr. D 52:65-76(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  13. "Crystal structure of recombinant trypsin-solubilized fragment of cytochrome b5 and the structural comparison with Val61His mutant."
    Wu J., Gan J.-H., Xia Z.-X., Wang Y.-H., Wang W.-H., Xue L.-L., Xie Y., Huang Z.-X.
    Proteins 40:249-257(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 8-89, MUTAGENESIS.
  14. "Structures of V45E and V45Y mutants and structure comparison of a variety of cytochrome b5 mutants."
    Gan J.-H., Wu J., Wang Z.-Q., Wang Y.-H., Huang Z.-X., Xia Z.-X.
    Acta Crystallogr. D 58:1298-1306(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 8-89, MUTAGENESIS.
  15. "X-ray crystallography, CD and kinetic studies revealed the essence of the abnormal behaviors of the cytochrome b5 Phe35->Tyr mutant."
    Yao P., Wu J., Wang Y.-H., Sun B.-Y., Xia Z.-X., Huang Z.-X.
    Eur. J. Biochem. 269:4287-4296(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 8-89, CIRCULAR DICHROISM ANALYSIS, MUTAGENESIS.
  16. "The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods."
    Muskett F.W., Kelly G.P., Whitford D.
    J. Mol. Biol. 258:172-189(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  17. "Solution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with cytochrome c."
    Wu Y., Wang Y., Qian C., Lu J., Li E., Wang W., Lu J., Xie Y., Wang J., Zhu D., Huang Z., Tang W.
    Eur. J. Biochem. 268:1620-1630(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 8-89, MUTAGENESIS.
  18. "Effects of charged amino-acid mutation on the solution structure of cytochrome b5 and binding between cytochrome b5 and cytochrome c."
    Qian C., Yao Y., Ye K., Wang J., Tang W., Wang Y., Wang W., Lu J., Xie Y., Huang Z.
    Protein Sci. 10:2451-2459(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 8-89, MUTAGENESIS.
  19. "The solution structure of the oxidized bovine microsomal cytochrome b5 mutant V61H."
    Cao C., Zhang Q., Xue L.-L., Ma J., Wang Y.-H., Wu H., Huang Z.-X.
    Biochem. Biophys. Res. Commun. 307:600-609(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 8-89, MUTAGENESIS.

Entry informationi

Entry nameiCYB5_BOVIN
AccessioniPrimary (citable) accession number: P00171
Secondary accession number(s): Q27947, Q28837, Q32PH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.