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UniProtKB - P00156 (CYB_HUMAN)

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Protein

Cytochrome b

Gene

MT-CYB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.By similarity

Miscellaneous

Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm.By similarity

Cofactori

hemeBy similarityNote: Binds 2 heme groups non-covalently.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi83Iron 1 (heme b562 axial ligand)By similarity1
Metal bindingi97Iron 2 (heme b566 axial ligand)By similarity1
Metal bindingi182Iron 1 (heme b562 axial ligand)By similarity1
Metal bindingi196Iron 2 (heme b566 axial ligand)By similarity1
Binding sitei201UbiquinoneBy similarity1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein complex binding Source: Ensembl
  • ubiquinol-cytochrome-c reductase activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Biological processElectron transport, Respiratory chain, Transport
LigandHeme, Iron, Metal-binding, Ubiquinone

Enzyme and pathway databases

ReactomeiR-HSA-611105. Respiratory electron transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b
Alternative name(s):
Complex III subunit 3
Complex III subunit III
Cytochrome b-c1 complex subunit 3
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Gene namesi
Name:MT-CYB
Synonyms:COB, CYTB, MTCYB
Encoded oniMitochondrion
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Mitochondrion

Organism-specific databases

EuPathDBiHostDB:ENSG00000198727.2.
HGNCiHGNC:7427. MT-CYB.
MIMi516020. gene.
neXtProtiNX_P00156.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei33 – 53HelicalBy similarityAdd BLAST21
Transmembranei77 – 98HelicalBy similarityAdd BLAST22
Transmembranei113 – 133HelicalBy similarityAdd BLAST21
Transmembranei178 – 198HelicalBy similarityAdd BLAST21
Transmembranei226 – 246HelicalBy similarityAdd BLAST21
Transmembranei288 – 308HelicalBy similarityAdd BLAST21
Transmembranei320 – 340HelicalBy similarityAdd BLAST21
Transmembranei347 – 367HelicalBy similarityAdd BLAST21

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Defects in MT-CYB are a rare cause of mitochondrial dysfunction underlying different myopathies. They include mitochondrial encephalomyopathy, hypertrophic cardiomyopathy (HCM), and sporadic mitochondrial myopathy (MM). In mitochondrial myopathy, exercise intolerance is the predominant symptom. Additional features include lactic acidosis, muscle weakness and/or myoglobinuria. Defects in MTCYB are also found in cases of exercise intolerance accompanied by deafness, mental retardation, retinitis pigmentosa, cataract, growth retardation, epilepsy (multisystem disorder).2 Publications
Cardiomyopathy, infantile histiocytoid (CMIH)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA heart disease characterized by the presence of pale granular foamy histiocyte-like cells within the myocardium. It usually affects children younger than 2 years of age, with a clear predominance of females over males. Infants present with dysrhythmia or cardiac arrest. The clinical course is usually fulminant, sometimes simulating sudden infant death syndrome.
See also OMIM:500000
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013656251G → D in CMIH. 1 PublicationCorresponds to variant dbSNP:rs207460003Ensembl.1
Leber hereditary optic neuropathy (LHON)1 Publication
The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.
Disease descriptionA maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes.
See also OMIM:535000
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_002197171D → N in LHON; secondary mutation; does not seem to directly cause the disease. 1 PublicationCorresponds to variant dbSNP:rs41518645Ensembl.1
Natural variantiVAR_002199356V → M in LHON; secondary mutation; does not seem to directly cause the disease. 2 PublicationsCorresponds to variant dbSNP:rs200336777Ensembl.1

Keywords - Diseasei

Cardiomyopathy, Cataract, Deafness, Disease mutation, Leber hereditary optic neuropathy, Primary mitochondrial disease

Organism-specific databases

DisGeNETi4519.
GeneReviewsiMT-CYB.
MalaCardsiMT-CYB.
MIMi500000. phenotype.
535000. phenotype.
OpenTargetsiENSG00000198727.
Orphaneti137675. Histiocytoid cardiomyopathy.
1460. Isolated CoQ-cytochrome C reductase deficiency.
104. Leber hereditary optic neuropathy.
PharmGKBiPA31234.

Chemistry databases

DrugBankiDB08453. 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE.
DB07778. FAMOXADONE.
DB07401. METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE.
DB08330. METHYL (2Z)-3-METHOXY-2-{2-[(E)-2-PHENYLVINYL]PHENYL}ACRYLATE.
DB08690. UBIQUINONE-2.

Polymorphism and mutation databases

DMDMi408360043.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000610451 – 380Cytochrome bAdd BLAST380

Proteomic databases

EPDiP00156.
PaxDbiP00156.
PeptideAtlasiP00156.
PRIDEiP00156.
TopDownProteomicsiP00156.

PTM databases

iPTMnetiP00156.
PhosphoSitePlusiP00156.

Expressioni

Gene expression databases

BgeeiENSG00000198727.
ExpressionAtlasiP00156. baseline and differential.

Organism-specific databases

HPAiCAB032215.
HPA068400.

Interactioni

Subunit structurei

The cytochrome bc1 complex contains 11 subunits: 3 respiratory subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of UQCRFS1). This cytochrome bc1 complex then forms a dimer.By similarity

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi110619. 12 interactors.
IntActiP00156. 3 interactors.
MINTiP00156.
STRINGi9606.ENSP00000354554.

Chemistry databases

BindingDBiP00156.

Structurei

Secondary structure

1380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 7Combined sources4
Helixi9 – 17Combined sources9
Beta strandi22 – 24Combined sources3
Helixi29 – 31Combined sources3
Helixi32 – 52Combined sources21
Helixi61 – 70Combined sources10
Helixi76 – 103Combined sources28
Helixi106 – 108Combined sources3
Helixi110 – 131Combined sources22
Turni132 – 134Combined sources3
Helixi137 – 148Combined sources12
Helixi149 – 152Combined sources4
Turni154 – 156Combined sources3
Helixi157 – 165Combined sources9
Beta strandi167 – 170Combined sources4
Helixi172 – 200Combined sources29
Turni201 – 203Combined sources3
Helixi214 – 216Combined sources3
Beta strandi217 – 219Combined sources3
Helixi220 – 244Combined sources25
Beta strandi249 – 251Combined sources3
Beta strandi255 – 258Combined sources4
Helixi272 – 283Combined sources12
Beta strandi284 – 286Combined sources3
Helixi289 – 303Combined sources15
Helixi304 – 307Combined sources4
Helixi315 – 317Combined sources3
Helixi319 – 339Combined sources21
Helixi345 – 363Combined sources19
Helixi365 – 376Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5XTEelectron microscopy3.40J/V2-379[»]
5XTHelectron microscopy3.90AJ/AV2-379[»]
5XTIelectron microscopy17.40AJ/AV2-379[»]
ProteinModelPortaliP00156.
SMRiP00156.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome b family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4663. Eukaryota.
COG1290. LUCA.
GeneTreeiENSGT00390000017948.
HOVERGENiHBG017694.
InParanoidiP00156.
KOiK00412.
OMAiHETGSNN.
OrthoDBiEOG091G0DW4.
PhylomeDBiP00156.
TreeFamiTF353088.

Family and domain databases

CDDicd00290. cytochrome_b_C. 1 hit.
cd00284. Cytochrome_b_N. 1 hit.
Gene3Di1.20.810.10. 1 hit.
InterProiView protein in InterPro
IPR005798. Cyt_b/b6_C.
IPR036150. Cyt_b/b6_C_sf.
IPR005797. Cyt_b/b6_N.
IPR027387. Cytb/b6-like_sf.
IPR030689. Cytochrome_b.
IPR016174. Di-haem_cyt_TM.
PfamiView protein in Pfam
PF00032. Cytochrom_B_C. 1 hit.
PF00033. Cytochrome_B. 1 hit.
PIRSFiPIRSF038885. COB. 1 hit.
SUPFAMiSSF81342. SSF81342. 1 hit.
SSF81648. SSF81648. 1 hit.
PROSITEiView protein in PROSITE
PS51003. CYTB_CTER. 1 hit.
PS51002. CYTB_NTER. 1 hit.

Sequencei

Sequence statusi: Complete.

P00156-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPMRKTNPL MKLINHSFID LPTPSNISAW WNFGSLLGAC LILQITTGLF 
        60         70         80         90        100
LAMHYSPDAS TAFSSIAHIT RDVNYGWIIR YLHANGASMF FICLFLHIGR 
       110        120        130        140        150
GLYYGSFLYS ETWNIGIILL LATMATAFMG YVLPWGQMSF WGATVITNLL 
       160        170        180        190        200
SAIPYIGTDL VQWIWGGYSV DSPTLTRFFT FHFILPFIIA ALATLHLLFL 
       210        220        230        240        250
HETGSNNPLG ITSHSDKITF HPYYTIKDAL GLLLFLLSLM TLTLFSPDLL 
       260        270        280        290        300
GDPDNYTLAN PLNTPPHIKP EWYFLFAYTI LRSVPNKLGG VLALLLSILI 
       310        320        330        340        350
LAMIPILHMS KQQSMMFRPL SQSLYWLLAA DLLILTWIGG QPVSYPFTII 
       360        370        380
GQVASVLYFT TILILMPTIS LIENKMLKWA
Length:380
Mass (Da):42,718
Last modified:October 3, 2012 - v2
Checksum:i600E520C262E5498
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0085857T → ICombined sources7 PublicationsCorresponds to variant dbSNP:rs193302980Ensembl.1
Natural variantiVAR_0136438N → S3 PublicationsCorresponds to variant dbSNP:rs28357679Ensembl.1
Natural variantiVAR_01364418F → L3 PublicationsCorresponds to variant dbSNP:rs28357681Ensembl.1
Natural variantiVAR_01364534G → S in mitochondrial myopathy; sporadic. 1 PublicationCorresponds to variant dbSNP:rs207459998Ensembl.1
Natural variantiVAR_03305835S → P in exercice intolerance; with cardiomyopathy and septo-optic dysplasia. 1 PublicationCorresponds to variant dbSNP:rs207460004Ensembl.1
Natural variantiVAR_01557139A → T1 PublicationCorresponds to variant dbSNP:rs2853505Ensembl.1
Natural variantiVAR_01364639A → V1 Publication1
Natural variantiVAR_01364778I → T1 PublicationCorresponds to variant dbSNP:rs200786872Ensembl.1
Natural variantiVAR_01557278I → V1 PublicationCorresponds to variant dbSNP:rs199997767Ensembl.1
Natural variantiVAR_00838880R → H in colorectal cancer. 1 PublicationCorresponds to variant dbSNP:rs207459995Ensembl.1
Natural variantiVAR_00858687A → P1 Publication1
Natural variantiVAR_013648122A → T2 PublicationsCorresponds to variant dbSNP:rs28357685Ensembl.1
Natural variantiVAR_013649123T → A1 Publication1
Natural variantiVAR_013650151S → P in exercise intolerance. 1 PublicationCorresponds to variant dbSNP:rs207460001Ensembl.1
Natural variantiVAR_013651153I → T1 PublicationCorresponds to variant dbSNP:rs28357687Ensembl.1
Natural variantiVAR_013652164I → V1 PublicationCorresponds to variant dbSNP:rs201250154Ensembl.1
Natural variantiVAR_013653166G → E in hyperthrophic cardiomyopathy. 1 Publication1
Natural variantiVAR_002197171D → N in LHON; secondary mutation; does not seem to directly cause the disease. 1 PublicationCorresponds to variant dbSNP:rs41518645Ensembl.1
Natural variantiVAR_013654189 – 190IA → VT. 2
Natural variantiVAR_011339191A → T2 PublicationsCorresponds to variant dbSNP:rs2853507Ensembl.1
Natural variantiVAR_011340194T → A5 PublicationsCorresponds to variant dbSNP:rs2853508Ensembl.1
Natural variantiVAR_011341229A → T3 PublicationsCorresponds to variant dbSNP:rs193302993Ensembl.1
Natural variantiVAR_013655236L → I3 PublicationsCorresponds to variant dbSNP:rs193302994Ensembl.1
Natural variantiVAR_013657251 – 258Missing in mitochondrial myopathy; sporadic. 1 Publication8
Natural variantiVAR_013656251G → D in CMIH. 1 PublicationCorresponds to variant dbSNP:rs207460003Ensembl.1
Natural variantiVAR_033059251G → S Associated with susceptibility to obesity. 1 PublicationCorresponds to variant dbSNP:rs199951903Ensembl.1
Natural variantiVAR_013658255N → H in cardiomyopathy; fatal; post-partum. 1 Publication1
Natural variantiVAR_015573260N → D1 Publication1
Natural variantiVAR_008389276F → L in colorectal cancer. 1 PublicationCorresponds to variant dbSNP:rs207459996Ensembl.1
Natural variantiVAR_013659278Y → C in multisystem disorder. 1 PublicationCorresponds to variant dbSNP:rs207460002Ensembl.1
Natural variantiVAR_013660290G → D in exercise intolerance. 1 PublicationCorresponds to variant dbSNP:rs207459997Ensembl.1
Natural variantiVAR_013661306I → T1 PublicationCorresponds to variant dbSNP:rs369851331Ensembl.1
Natural variantiVAR_013662316M → T1 PublicationCorresponds to variant dbSNP:rs200975632Ensembl.1
Natural variantiVAR_013663329A → T1 Publication1
Natural variantiVAR_013664330A → T1 PublicationCorresponds to variant dbSNP:rs386829259Ensembl.1
Natural variantiVAR_013665334I → V1 PublicationCorresponds to variant dbSNP:rs386829260Ensembl.1
Natural variantiVAR_002198339G → E in mitochondrial myopathy. 1 Publication1
Natural variantiVAR_013666353V → M1 Publication1
Natural variantiVAR_002199356V → M in LHON; secondary mutation; does not seem to directly cause the disease. 2 PublicationsCorresponds to variant dbSNP:rs200336777Ensembl.1
Natural variantiVAR_013667360T → A1 PublicationCorresponds to variant dbSNP:rs28357376Ensembl.1
Natural variantiVAR_013668368T → I2 PublicationsCorresponds to variant dbSNP:rs202225494Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00662 Genomic DNA. Translation: CAA24038.1.
J01415 Genomic DNA. Translation: AAB58955.3.
U09500 Genomic DNA. Translation: AAA19775.1.
D38112 Genomic DNA. Translation: BAA77674.1.
AF346963 Genomic DNA. Translation: AAK17219.1.
AF346964 Genomic DNA. Translation: AAK17232.2.
AF346965 Genomic DNA. Translation: AAK17245.2.
AF346966 Genomic DNA. Translation: AAK17258.1.
AF346967 Genomic DNA. Translation: AAK17271.2.
AF346968 Genomic DNA. Translation: AAK17284.2.
AF346969 Genomic DNA. Translation: AAK17297.2.
AF346970 Genomic DNA. Translation: AAK17310.2.
AF346971 Genomic DNA. Translation: AAK17323.2.
AF346972 Genomic DNA. Translation: AAK17336.2.
AF346973 Genomic DNA. Translation: AAK17349.2.
AF346974 Genomic DNA. Translation: AAK17362.2.
AF346975 Genomic DNA. Translation: AAK17375.2.
AF346976 Genomic DNA. Translation: AAK17388.1.
AF346977 Genomic DNA. Translation: AAK17401.1.
AF346978 Genomic DNA. Translation: AAK17414.1.
AF346979 Genomic DNA. Translation: AAK17427.1.
AF346980 Genomic DNA. Translation: AAK17440.2.
AF346981 Genomic DNA. Translation: AAK17453.2.
AF346982 Genomic DNA. Translation: AAK17466.1.
AF346983 Genomic DNA. Translation: AAK17479.1.
AF346984 Genomic DNA. Translation: AAK17492.2.
AF346985 Genomic DNA. Translation: AAK17505.2.
AF346986 Genomic DNA. Translation: AAK17518.2.
AF346987 Genomic DNA. Translation: AAK17531.2.
AF346988 Genomic DNA. Translation: AAK17544.1.
AF346989 Genomic DNA. Translation: AAK17557.2.
AF346990 Genomic DNA. Translation: AAK17570.1.
AF346991 Genomic DNA. Translation: AAK17583.2.
AF346992 Genomic DNA. Translation: AAK17596.2.
AF346993 Genomic DNA. Translation: AAK17609.2.
AF346994 Genomic DNA. Translation: AAK17622.2.
AF346995 Genomic DNA. Translation: AAK17635.2.
AF346996 Genomic DNA. Translation: AAK17648.2.
AF346997 Genomic DNA. Translation: AAK17661.2.
AF346998 Genomic DNA. Translation: AAK17674.2.
AF346999 Genomic DNA. Translation: AAK17687.2.
AF347000 Genomic DNA. Translation: AAK17700.1.
AF347001 Genomic DNA. Translation: AAK17713.2.
AF347002 Genomic DNA. Translation: AAK17726.2.
AF347003 Genomic DNA. Translation: AAK17739.2.
AF347004 Genomic DNA. Translation: AAK17752.2.
AF347005 Genomic DNA. Translation: AAK17765.2.
AF347006 Genomic DNA. Translation: AAK17778.2.
AF347007 Genomic DNA. Translation: AAK17791.2.
AF347008 Genomic DNA. Translation: AAK17804.2.
AF347009 Genomic DNA. Translation: AAK17817.2.
AF347010 Genomic DNA. Translation: AAK17830.2.
AF347011 Genomic DNA. Translation: AAK17843.2.
AF347012 Genomic DNA. Translation: AAK17856.2.
AF347013 Genomic DNA. Translation: AAK17869.2.
AF347014 Genomic DNA. Translation: AAK17882.2.
AF347015 Genomic DNA. Translation: AAK17895.2.
AF381981 Genomic DNA. Translation: AAL54394.1.
AF381982 Genomic DNA. Translation: AAL54409.1.
AF381983 Genomic DNA. Translation: AAL54422.1.
AF381984 Genomic DNA. Translation: AAL54435.1.
AF381985 Genomic DNA. Translation: AAL54448.1.
AF381986 Genomic DNA. Translation: AAL54461.1.
AF381987 Genomic DNA. Translation: AAL54474.1.
AF381988 Genomic DNA. Translation: AAL54487.1.
AF381989 Genomic DNA. Translation: AAL54500.1.
AF381990 Genomic DNA. Translation: AAL54513.1.
AF381991 Genomic DNA. Translation: AAL54526.1.
AF381992 Genomic DNA. Translation: AAL54539.1.
AF381993 Genomic DNA. Translation: AAL54552.1.
AF381994 Genomic DNA. Translation: AAL54565.1.
AF381995 Genomic DNA. Translation: AAL54578.1.
AF381996 Genomic DNA. Translation: AAL54591.1.
AF381997 Genomic DNA. Translation: AAL54604.1.
AF381998 Genomic DNA. Translation: AAL54617.1.
AF381999 Genomic DNA. Translation: AAL54630.1.
AF382000 Genomic DNA. Translation: AAL54643.1.
AF382001 Genomic DNA. Translation: AAL54656.1.
AF382002 Genomic DNA. Translation: AAL54669.1.
AF382003 Genomic DNA. Translation: AAL54682.1.
AF382004 Genomic DNA. Translation: AAL54695.1.
AF382005 Genomic DNA. Translation: AAL54708.1.
AF382006 Genomic DNA. Translation: AAL54721.1.
AF382007 Genomic DNA. Translation: AAL54734.1.
AF382008 Genomic DNA. Translation: AAL54747.1.
AF382009 Genomic DNA. Translation: AAL54760.1.
AF382010 Genomic DNA. Translation: AAL54773.1.
AF382011 Genomic DNA. Translation: AAL54786.1.
AF382012 Genomic DNA. Translation: AAL54799.1.
AF382013 Genomic DNA. Translation: AAL54812.1.
AF465942 Genomic DNA. Translation: AAN14559.1.
AF465945 Genomic DNA. Translation: AAN14592.1.
AF465946 Genomic DNA. Translation: AAN14603.1.
AF465947 Genomic DNA. Translation: AAN14614.1.
AF465948 Genomic DNA. Translation: AAN14625.1.
AF465949 Genomic DNA. Translation: AAN14636.1.
AF465953 Genomic DNA. Translation: AAN14680.1.
AF465956 Genomic DNA. Translation: AAN14713.1.
AF465968 Genomic DNA. Translation: AAN14845.1.
AF465971 Genomic DNA. Translation: AAN14878.1.
AF465972 Genomic DNA. Translation: AAN14889.1.
AF465973 Genomic DNA. Translation: AAN14900.1.
AF465974 Genomic DNA. Translation: AAN14911.1.
AF465975 Genomic DNA. Translation: AAN14922.1.
AF465977 Genomic DNA. Translation: AAN14944.1.
M28016 mRNA. Translation: AAA31851.1.
PIRiA00151. CBHU.
RefSeqiYP_003024038.1. NC_012920.1.

Genome annotation databases

EnsembliENST00000361789; ENSP00000354554; ENSG00000198727.
GeneIDi4519.
KEGGihsa:4519.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCYB_HUMAN
AccessioniPrimary (citable) accession number: P00156
Secondary accession number(s): Q34786
, Q8HBR6, Q8HNQ0, Q8HNQ1, Q8HNQ9, Q8HNR4, Q8HNR7, Q8W7V8, Q8WCV9, Q8WCY2, Q8WCY7, Q8WCY8, Q9B1A6, Q9B1B6, Q9B1B8, Q9B1D4, Q9B1X6, Q9B2V0, Q9B2V8, Q9B2W0, Q9B2W3, Q9B2W8, Q9B2X1, Q9B2X7, Q9B2X9, Q9B2Y3, Q9B2Z0, Q9B2Z4, Q9T6H6, Q9T9Y0, Q9TEH4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 3, 2012
Last modified: February 28, 2018
This is version 198 of the entry and version 2 of the sequence. See 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

Caution

The full-length protein contains only eight transmembrane helices, not nine as predicted by bioinformatics tools.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome