Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13  

UniProtKB / Swiss-Prot ID :  NDUAD_HUMAN

Gene Name (Synonyms) : 
NDUFA13, GRIM19 CDA016, CGI-39  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Mitochondrion inner membrane; Single-pass membrane protein; Matrix side. Nucleus. Note=May be translocated into the nucleus upon IFN/RA treatment. 

Protein Function :  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. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes. 

Transmembrane Topology (topPTM) : NDUAD_HUMAN 

Protein Sequence MAASKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMLAIGIGTLIYGHWSIMKWNRERRRLQIEDFEARIA...
Predicted Secondary Structure CCCCCCHHCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
5K -> N (in a Hurthle cell variant ofpapillary carcinoma sample).
115R -> P (in a Hurthle cell variant ofpapillary carcinoma sample).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ASKVKQDMP
CCCCHHCCC
44.30Phosphositeplus
Link-
22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PIDYKRNLP
CCCCCCCCC
30.94Phosphositeplus
Link-
79PhosphothreonineLQAETDRRT
HHHHHHHHH
37.51Phosphositeplus
Link-
99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AIIMKDVPD
HHHHHCCCC
45.20Phosphositeplus
Link-
105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VPDWKVGES
CCCCCCHHH
47.98Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
HTRA2_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
EBI-1374040
EBI-1375002
EBI-1
intact17297443
17297443
17297443
17297443
17297443
17297443
STAT3_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:09452HPRD12628925
ACPM_HUMANENSP00000252576STRING
NDUB4_HUMANENSP00000252576STRING
NDUB7_HUMANENSP00000252576STRING
NDUB3_HUMANENSP00000252576STRING
NDUA2_HUMANENSP00000252576STRING
NDUB5_HUMANENSP00000252576STRING
NDUC1_HUMANENSP00000252576STRING
NDUBA_HUMANENSP00000252576STRING
NDUB9_HUMANENSP00000252576STRING
NDUC2_HUMANENSP00000252576STRING
NDUB8_HUMANENSP00000252576STRING
NDUA7_HUMANENSP00000252576STRING
NDUA3_HUMANENSP00000252576STRING
NDUAB_HUMANENSP00000252576STRING
NDUAC_HUMANENSP00000252576STRING
NDUB1_HUMANENSP00000252576STRING
NDUA6_HUMANENSP00000252576STRING
NDUA4_HUMANENSP00000252576STRING
NU6M_HUMANENSP00000252576STRING
NU1M_HUMANENSP00000252576STRING
NU4LM_HUMANENSP00000252576STRING
NU5M_HUMANENSP00000252576STRING
NU4M_HUMANENSP00000252576STRING
NU2M_HUMANENSP00000252576STRING
NU3M_HUMANENSP00000252576STRING
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Disease Reference
Kegg disease
OMIM disease
607464Hurthle cell thyroid carcinoma (HCTC)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures