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Protein Page:
NDUFB6 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
NDUFB6 Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Belongs to the complex I NDUFB6 subunit family. Note: This description may include information from UniProtKB.
Protein type: Mitochondrial; Energy Metabolism - oxidative phosphorylation; Oxidoreductase; EC 1.6.99.3; EC 1.6.5.3; Membrane protein, integral
Cellular Component: mitochondrial membrane; mitochondrial inner membrane; integral to membrane; mitochondrial respiratory chain complex I
Molecular Function: NADH dehydrogenase (ubiquinone) activity
Biological Process: cellular metabolic process; mitochondrial electron transport, NADH to ubiquinone
Reference #:  O95139 (UniProtKB)
Alt. Names/Synonyms: B17; CI; CI-B17; complex I, mitochondrial respiratory chain, B17 subunit; Complex I-B17; MGC13675; NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 6, 17kDa; NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6; NADH-ubiquinone oxidoreductase B17 subunit; NADH-ubiquinone oxidoreductase beta subunit, 6; NDUB6; NDUFB6
Gene Symbols: NDUFB6
Molecular weight: 15,489 Da
Basal Isoelectric point: 9.63  Predict pI for various phosphorylation states
Select Structure to View Below

NDUFB6

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 T2-p ______MtGYtPDEK
1 0 T5-p ___MtGYtPDEKLRL
0 1 K9 tGYtPDEKLRLQQLR
0 2 K24 ELRRRWLKDQELsPR
0 1 K24-ub ELRRRWLkDQELsPR
0 1 K24 ELRRRWLKDQELsPR
1 3 S29-p WLkDQELsPREPVLP
0 1 K49-ub PMEKFWNkFLENksP
0 1 K54-ub WNkFLENksPWRKMV
1 0 S55-p NkFLENksPWRKMVH
0 1 G63 PWRKMVHGVYkkSIF
0 1 G63 PWRKMVHGVYkkSIF
0 41 K66-ac KMVHGVYkkSIFVFT
0 1 K66-sc KMVHGVYkkSIFVFT
0 2 K67-ac MVHGVYkkSIFVFTH
0 1 Y88 IIHYYMKYHVSEkPy
0 1 K93-ub MKYHVSEkPyGIVEK
0 1 Y95-p YHVSEkPyGIVEKKS
0 1 T109 SRIFPGDTILEtGEV
0 1 T113-p PGDTILEtGEVIPPM
  NDUFB6 iso2  
T2 ______MTGYTPDEK
T5 ___MTGYTPDEKLRL
K9 TGYTPDEKLRLQQLR
K24 ELRRRWLKDQELSPR
K24 ELRRRWLKDQELSPR
K24 ELRRRWLKDQELSPR
S29 WLKDQELSPREPVLP
K49 PMEKFWNKFLENKSP
K54 WNKFLENKSPWRKMV
S55 NKFLENKSPWRKMVH
G63 PWRKMVHGVYKKSIF
G63 PWRKMVHGVYKKSIF
K66 KMVHGVYKKSIFVFT
K66 KMVHGVYKKSIFVFT
K67 MVHGVYKKSIFVFTH
Y88-p IIHYYMKyHVSGDtI
- gap
- under review  
T94-p KyHVSGDtILETGEV
- gap
  mouse

 
S2 ______MSGYTPDEk
T5 ___MSGYTPDEkLRL
K9-ac SGYTPDEkLRLQQLR
K24-ac ELRRRWLkDQELSPR
K24 ELRRRWLKDQELSPR
K24-sc ELRRRWLkDQELSPR
S29 WLkDQELSPREPVLP
N49 PLERFWDNFLRDGAV
G54 WDNFLRDGAVWKNMV
A55 DNFLRDGAVWKNMVF
K63-ac VWKNMVFkAYRSSLF
K63-sc VWKNMVFkAYRSSLF
R66 NMVFkAYRSSLFAVS
R66 NMVFkAYRSSLFAVS
S67 MVFkAYRSSLFAVSH
Y88 FVHYYVKYHMATKPY
K93 VKYHMATKPYTIVSS
Y95 YHMATKPYTIVSSKP
T109 PRIFPGDTILETGEV
T113 PGDTILETGEVIPPM
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