rdf:type |
|
lifeskim:mentions |
umls-concept:C0001128,
umls-concept:C0033684,
umls-concept:C0034793,
umls-concept:C0036025,
umls-concept:C0086418,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C1412933,
umls-concept:C1510421,
umls-concept:C1552599,
umls-concept:C1704787
|
pubmed:issue |
4
|
pubmed:dateCreated |
1998-6-18
|
pubmed:databankReference |
|
pubmed:abstractText |
Mam33p (mitochondrial acidic matrix protein) is a soluble protein, located in mitochondria of Saccharomyces cerevisiae. It is synthesized as a precursor with an N-terminal mitochondrial targeting sequence that is processed on import. Mam33p assembles to a homo-oligomeric complex in the mitochondrial matrix. It can bind to the sorting signal of cytochrome b2 that directs this protein into the intermembrane space. Mam33p is encoded by an 801 bp open reading frame. Gene disruption did not result in a significant growth defect. Mam33p exhibits sequence similarity to gC1q-R, a human protein that has been implicated in the binding of complement factor C1q and kininogen.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD44,
http://linkedlifedata.com/resource/pubmed/chemical/C1QBP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase (Cytochrome),
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/complement 1q receptor
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0749-503X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
14
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
303-10
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9559539-Amino Acid Sequence,
pubmed-meshheading:9559539-Antigens, CD44,
pubmed-meshheading:9559539-Base Sequence,
pubmed-meshheading:9559539-Carrier Proteins,
pubmed-meshheading:9559539-Fungal Proteins,
pubmed-meshheading:9559539-Humans,
pubmed-meshheading:9559539-L-Lactate Dehydrogenase,
pubmed-meshheading:9559539-L-Lactate Dehydrogenase (Cytochrome),
pubmed-meshheading:9559539-Membrane Glycoproteins,
pubmed-meshheading:9559539-Mitochondria,
pubmed-meshheading:9559539-Mitochondrial Proteins,
pubmed-meshheading:9559539-Molecular Sequence Data,
pubmed-meshheading:9559539-Phenotype,
pubmed-meshheading:9559539-Receptors, Complement,
pubmed-meshheading:9559539-Saccharomyces cerevisiae,
pubmed-meshheading:9559539-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9559539-Sequence Alignment
|
pubmed:year |
1998
|
pubmed:articleTitle |
Mam33p, an oligomeric, acidic protein in the mitochondrial matrix of Saccharomyces cerevisiae is related to the human complement receptor gC1q-R.
|
pubmed:affiliation |
Institut für Physiologische Chemie, München, Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|