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Protein

Cytochrome c oxidase subunit 6A1, mitochondrial

Gene

COX6A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.

GO - Molecular functioni

  1. cytochrome-c oxidase activity Source: InterPro

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. generation of precursor metabolites and energy Source: ProtInc
  3. respiratory electron transport chain Source: Reactome
  4. small molecule metabolic process Source: Reactome
  5. transmembrane transport Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_22393. Respiratory electron transport.
REACT_268444. Orphan transporters.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 6A1, mitochondrial
Alternative name(s):
Cytochrome c oxidase polypeptide VIa-liver
Cytochrome c oxidase subunit VIA-liver
Short name:
COX VIa-L
Gene namesi
Name:COX6A1
Synonyms:COX6AL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:2277. COX6A1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Reactome
  2. mitochondrial respiratory chain complex IV Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease, recessive, intermediate type, D (CMTRID)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Recessive intermediate forms of Charcot-Marie-Tooth disease are characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec.

See also OMIM:616039

Keywords - Diseasei

Charcot-Marie-Tooth disease, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi616039. phenotype.
PharmGKBiPA26794.

Polymorphism and mutation databases

BioMutaiCOX6A1.
DMDMi6166030.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424Mitochondrion1 PublicationAdd
BLAST
Chaini25 – 10985Cytochrome c oxidase subunit 6A1, mitochondrialPRO_0000006119Add
BLAST

Proteomic databases

MaxQBiP12074.
PaxDbiP12074.
PRIDEiP12074.

2D gel databases

SWISS-2DPAGEP12074.

PTM databases

PhosphoSiteiP12074.

Expressioni

Gene expression databases

BgeeiP12074.
CleanExiHS_COX6A1.
ExpressionAtlasiP12074. baseline and differential.
GenevestigatoriP12074.

Organism-specific databases

HPAiHPA062394.

Interactioni

Protein-protein interaction databases

BioGridi107730. 3 interactions.
IntActiP12074. 2 interactions.
STRINGi9606.ENSP00000229379.

Structurei

3D structure databases

ProteinModelPortaliP12074.
SMRiP12074. Positions 25-107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG279259.
GeneTreeiENSGT00390000002756.
HOGENOMiHOG000193965.
HOVERGENiHBG060482.
InParanoidiP12074.
KOiK02266.
OMAiNAYLKHQ.
OrthoDBiEOG757D0Z.
PhylomeDBiP12074.
TreeFamiTF105064.

Family and domain databases

Gene3Di4.10.95.10. 1 hit.
InterProiIPR001349. Cyt_c_oxidase_su6a.
IPR018507. Cyt_c_oxidase_su6a_CS.
[Graphical view]
PANTHERiPTHR11504. PTHR11504. 1 hit.
PfamiPF02046. COX6A. 1 hit.
[Graphical view]
PIRSFiPIRSF000277. COX6A1. 1 hit.
ProDomiPD006036. Cyt_c_oxidase_su6a. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF81411. SSF81411. 1 hit.
PROSITEiPS01329. COX6A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12074-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVVGVSSVS RLLGRSRPQL GRPMSSGAHG EEGSARMWKT LTFFVALPGV
60 70 80 90 100
AVSMLNVYLK SHHGEHERPE FIAYPHLRIR TKPFPWGDGN HTLFHNPHVN

PLPTGYEDE
Length:109
Mass (Da):12,155
Last modified:July 15, 1999 - v4
Checksum:i0040F47CECE767B1
GO

Sequence cautioni

The sequence CAA33392.1 differs from that shown. Reason: Frameshift at position 17. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK312009 mRNA. Translation: BAG34947.1.
AL021546 Genomic DNA. Translation: CAA16494.1.
BC007723 mRNA. Translation: AAH07723.1.
BC070186 mRNA. Translation: AAH70186.1.
BC107861 mRNA. Translation: AAI07862.1.
X15341 mRNA. Translation: CAA33392.1. Frameshift.
CCDSiCCDS9197.1.
RefSeqiNP_004364.2. NM_004373.3.
UniGeneiHs.369624.

Genome annotation databases

EnsembliENST00000229379; ENSP00000229379; ENSG00000111775.
GeneIDi1337.
KEGGihsa:1337.
UCSCiuc001tyf.2. human.

Polymorphism and mutation databases

BioMutaiCOX6A1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK312009 mRNA. Translation: BAG34947.1.
AL021546 Genomic DNA. Translation: CAA16494.1.
BC007723 mRNA. Translation: AAH07723.1.
BC070186 mRNA. Translation: AAH70186.1.
BC107861 mRNA. Translation: AAI07862.1.
X15341 mRNA. Translation: CAA33392.1. Frameshift.
CCDSiCCDS9197.1.
RefSeqiNP_004364.2. NM_004373.3.
UniGeneiHs.369624.

3D structure databases

ProteinModelPortaliP12074.
SMRiP12074. Positions 25-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107730. 3 interactions.
IntActiP12074. 2 interactions.
STRINGi9606.ENSP00000229379.

PTM databases

PhosphoSiteiP12074.

Polymorphism and mutation databases

BioMutaiCOX6A1.
DMDMi6166030.

2D gel databases

SWISS-2DPAGEP12074.

Proteomic databases

MaxQBiP12074.
PaxDbiP12074.
PRIDEiP12074.

Protocols and materials databases

DNASUi1337.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229379; ENSP00000229379; ENSG00000111775.
GeneIDi1337.
KEGGihsa:1337.
UCSCiuc001tyf.2. human.

Organism-specific databases

CTDi1337.
GeneCardsiGC12P120875.
HGNCiHGNC:2277. COX6A1.
HPAiHPA062394.
MIMi602072. gene.
616039. phenotype.
neXtProtiNX_P12074.
PharmGKBiPA26794.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG279259.
GeneTreeiENSGT00390000002756.
HOGENOMiHOG000193965.
HOVERGENiHBG060482.
InParanoidiP12074.
KOiK02266.
OMAiNAYLKHQ.
OrthoDBiEOG757D0Z.
PhylomeDBiP12074.
TreeFamiTF105064.

Enzyme and pathway databases

ReactomeiREACT_22393. Respiratory electron transport.
REACT_268444. Orphan transporters.

Miscellaneous databases

ChiTaRSiCOX6A1. human.
GeneWikiiCOX6A1.
GenomeRNAii1337.
NextBioi5431.
PROiP12074.
SOURCEiSearch...

Gene expression databases

BgeeiP12074.
CleanExiHS_COX6A1.
ExpressionAtlasiP12074. baseline and differential.
GenevestigatoriP12074.

Family and domain databases

Gene3Di4.10.95.10. 1 hit.
InterProiIPR001349. Cyt_c_oxidase_su6a.
IPR018507. Cyt_c_oxidase_su6a_CS.
[Graphical view]
PANTHERiPTHR11504. PTHR11504. 1 hit.
PfamiPF02046. COX6A. 1 hit.
[Graphical view]
PIRSFiPIRSF000277. COX6A1. 1 hit.
ProDomiPD006036. Cyt_c_oxidase_su6a. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF81411. SSF81411. 1 hit.
PROSITEiPS01329. COX6A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Brain.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Brain, Testis and Uterus.
  4. "Sequence of a cDNA specifying subunit VIa of human cytochrome c oxidase."
    Fabrizi G.M., Rizzuto R., Nakase H., Mita S., Kadenbach B., Schon E.A.
    Nucleic Acids Res. 17:6409-6409(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-109.
    Tissue: Liver.
  5. "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 25-36.
    Tissue: Liver.
  6. Cited for: INVOLVEMENT IN CMTRID.

Entry informationi

Entry nameiCX6A1_HUMAN
AccessioniPrimary (citable) accession number: P12074
Secondary accession number(s): B2R500, O43714, Q32Q37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 15, 1999
Last modified: April 29, 2015
This is version 149 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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.