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Protein

Cytochrome c oxidase subunit 5B, mitochondrial

Gene

COX5B

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Zinc
Metal bindingi93 – 931Zinc
Metal bindingi113 – 1131Zinc
Metal bindingi116 – 1161Zinc

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi1.9.3.1. 908.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 5B, mitochondrial
Alternative name(s):
Cytochrome c oxidase polypeptide VIa
Cytochrome c oxidase polypeptide Vb
Gene namesi
Name:COX5B
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 11

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • respiratory chain complex IV Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3131Mitochondrion2 PublicationsAdd
BLAST
Chaini32 – 12998Cytochrome c oxidase subunit 5B, mitochondrialPRO_0000197028Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-acetyllysineBy similarity
Modified residuei86 – 861N6-acetyllysineBy similarity
Modified residuei121 – 1211N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00428.
PRIDEiP00428.

PTM databases

iPTMnetiP00428.

Interactioni

Protein-protein interaction databases

DIPiDIP-38985N.
IntActiP00428. 2 interactions.
STRINGi9913.ENSBTAP00000024678.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 434Combined sources
Helixi46 – 5611Combined sources
Beta strandi74 – 763Combined sources
Beta strandi78 – 814Combined sources
Beta strandi83 – 919Combined sources
Beta strandi94 – 963Combined sources
Beta strandi101 – 1099Combined sources
Beta strandi111 – 1133Combined sources
Turni114 – 1163Combined sources
Beta strandi119 – 1235Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCCX-ray2.80F/S32-129[»]
1OCOX-ray2.80F/S32-129[»]
1OCRX-ray2.35F/S32-129[»]
1OCZX-ray2.90F/S32-129[»]
1V54X-ray1.80F/S32-129[»]
1V55X-ray1.90F/S32-129[»]
2DYRX-ray1.80F/S32-129[»]
2DYSX-ray2.20F/S32-129[»]
2EIJX-ray1.90F/S32-129[»]
2EIKX-ray2.10F/S32-129[»]
2EILX-ray2.10F/S32-129[»]
2EIMX-ray2.60F/S32-129[»]
2EINX-ray2.70F/S32-129[»]
2OCCX-ray2.30F/S32-129[»]
2Y69X-ray1.95F/S1-129[»]
2YBBelectron microscopy19.00Q32-129[»]
2ZXWX-ray2.50F/S32-129[»]
3ABKX-ray2.00F/S32-129[»]
3ABLX-ray2.10F/S32-129[»]
3ABMX-ray1.95F/S32-129[»]
3AG1X-ray2.20F/S32-129[»]
3AG2X-ray1.80F/S32-129[»]
3AG3X-ray1.80F/S32-129[»]
3AG4X-ray2.05F/S32-129[»]
3ASNX-ray3.00F/S32-129[»]
3ASOX-ray2.30F/S32-129[»]
3WG7X-ray1.90F/S32-129[»]
3X2QX-ray2.00F/S32-129[»]
ProteinModelPortaliP00428.
SMRiP00428. Positions 32-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00428.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3352. Eukaryota.
ENOG4111XEM. LUCA.
GeneTreeiENSGT00390000011010.
HOGENOMiHOG000184129.
HOVERGENiHBG051089.
InParanoidiP00428.
KOiK02265.
OMAiPYNMLPP.
OrthoDBiEOG7D85ZC.
TreeFamiTF105063.

Family and domain databases

Gene3Di2.60.11.10. 1 hit.
InterProiIPR002124. Cyt_c_oxidase_su5b.
IPR020893. Cyt_c_oxidase_su5b_Zn_BS.
[Graphical view]
PANTHERiPTHR10122. PTHR10122. 1 hit.
PfamiPF01215. COX5B. 1 hit.
[Graphical view]
ProDomiPD007270. Cyt_c_oxidase_su5b. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS00848. COX5B_1. 1 hit.
PS51359. COX5B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00428-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRLLRGVG ALASQALRAR GPNGVSVVRS MASGGGVPTD EEQATGLERE
60 70 80 90 100
VMLAARKGQD PYNILAPKAT SGTKEDPNLV PSITNKRIVG CICEEDNSTV
110 120
IWFWLHKGEA QRCPSCGTHY KLVPHQLAH
Length:129
Mass (Da):13,834
Last modified:June 27, 2006 - v2
Checksum:iC78CE7552CE6C313
GO

Sequence cautioni

The sequence AAA30465.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102579 mRNA. Translation: AAI02580.1.
BC147855 mRNA. Translation: AAI47856.1.
M19962 mRNA. Translation: AAA30465.1. Different initiation.
PIRiA00495. OGBO6A.
RefSeqiNP_001029218.1. NM_001034046.2.
UniGeneiBt.87845.

Genome annotation databases

EnsembliENSBTAT00000024678; ENSBTAP00000024678; ENSBTAG00000018542.
GeneIDi287012.
KEGGibta:287012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102579 mRNA. Translation: AAI02580.1.
BC147855 mRNA. Translation: AAI47856.1.
M19962 mRNA. Translation: AAA30465.1. Different initiation.
PIRiA00495. OGBO6A.
RefSeqiNP_001029218.1. NM_001034046.2.
UniGeneiBt.87845.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCCX-ray2.80F/S32-129[»]
1OCOX-ray2.80F/S32-129[»]
1OCRX-ray2.35F/S32-129[»]
1OCZX-ray2.90F/S32-129[»]
1V54X-ray1.80F/S32-129[»]
1V55X-ray1.90F/S32-129[»]
2DYRX-ray1.80F/S32-129[»]
2DYSX-ray2.20F/S32-129[»]
2EIJX-ray1.90F/S32-129[»]
2EIKX-ray2.10F/S32-129[»]
2EILX-ray2.10F/S32-129[»]
2EIMX-ray2.60F/S32-129[»]
2EINX-ray2.70F/S32-129[»]
2OCCX-ray2.30F/S32-129[»]
2Y69X-ray1.95F/S1-129[»]
2YBBelectron microscopy19.00Q32-129[»]
2ZXWX-ray2.50F/S32-129[»]
3ABKX-ray2.00F/S32-129[»]
3ABLX-ray2.10F/S32-129[»]
3ABMX-ray1.95F/S32-129[»]
3AG1X-ray2.20F/S32-129[»]
3AG2X-ray1.80F/S32-129[»]
3AG3X-ray1.80F/S32-129[»]
3AG4X-ray2.05F/S32-129[»]
3ASNX-ray3.00F/S32-129[»]
3ASOX-ray2.30F/S32-129[»]
3WG7X-ray1.90F/S32-129[»]
3X2QX-ray2.00F/S32-129[»]
ProteinModelPortaliP00428.
SMRiP00428. Positions 32-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-38985N.
IntActiP00428. 2 interactions.
STRINGi9913.ENSBTAP00000024678.

PTM databases

iPTMnetiP00428.

Proteomic databases

PaxDbiP00428.
PRIDEiP00428.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000024678; ENSBTAP00000024678; ENSBTAG00000018542.
GeneIDi287012.
KEGGibta:287012.

Organism-specific databases

CTDi1329.

Phylogenomic databases

eggNOGiKOG3352. Eukaryota.
ENOG4111XEM. LUCA.
GeneTreeiENSGT00390000011010.
HOGENOMiHOG000184129.
HOVERGENiHBG051089.
InParanoidiP00428.
KOiK02265.
OMAiPYNMLPP.
OrthoDBiEOG7D85ZC.
TreeFamiTF105063.

Enzyme and pathway databases

BRENDAi1.9.3.1. 908.

Miscellaneous databases

EvolutionaryTraceiP00428.

Family and domain databases

Gene3Di2.60.11.10. 1 hit.
InterProiIPR002124. Cyt_c_oxidase_su5b.
IPR020893. Cyt_c_oxidase_su5b_Zn_BS.
[Graphical view]
PANTHERiPTHR10122. PTHR10122. 1 hit.
PfamiPF01215. COX5B. 1 hit.
[Graphical view]
ProDomiPD007270. Cyt_c_oxidase_su5b. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS00848. COX5B_1. 1 hit.
PS51359. COX5B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus and Hereford.
    Tissue: Heart ventricle and Ileum.
  2. "Studies on cytochrome c oxidase, IX. The primary structure of polypeptide VIa."
    Biewald R., Buse G.
    Hoppe-Seyler's Z. Physiol. Chem. 363:1141-1153(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-129.
  3. "Tissue-specific differences between heart and liver cytochrome c oxidase."
    Yanamura W., Zhang Y.-Z., Takamiya S., Capaldi R.A.
    Biochemistry 27:4909-4914(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-57.
    Tissue: Liver.
  4. "Sequence of cDNAs encoding subunit Vb of human and bovine cytochrome c oxidase."
    Zeviani M., Sakoda S., Sherbany A., Nakase H., Rizzuto R., Samitt C.E., Dimauro S., Schon E.A.
    Gene 65:1-11(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-129.
  5. "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A."
    Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.
    Science 272:1136-1144(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-129.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-129.
    Tissue: Heart.
  7. "X-ray structure of azide-bound fully oxidized cytochrome c oxidase from bovine heart at 2.9 A resolution."
    Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T., Shinzawa-Itoh K., Nakashima R., Yoshikawa S.
    Acta Crystallogr. D 56:529-535(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 32-129.
    Tissue: Heart.

Entry informationi

Entry nameiCOX5B_BOVIN
AccessioniPrimary (citable) accession number: P00428
Secondary accession number(s): A6QL66, P11949, Q3T041
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 27, 2006
Last modified: June 8, 2016
This is version 143 of the entry and version 2 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.