A new protein sequence data bank

Claverie, Jean‐Michel; Sauvaget, Isabelle

doi:10.1038/318019a0

Cited by 18 publications

(9 citation statements)

References 4 publications

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“…relationships with proteins from phylogenetically distant organisms. The observed proportion of cross-phylum hits among all ORFs (54 % of the total) was remarkably close to recent theoretical estimates of 50-60% for a representative gene collection (Claverie, 1993;Green et al, 1993). About 40% of the cross-phylum hits included similarities to prokaryotic proteins, typical of members of ancestral protein families.…”

Section: Members Of Ancient Protein Familiessupporting

confidence: 88%

“…About 40% of the cross-phylum hits included similarities to prokaryotic proteins, typical of members of ancestral protein families. Most of the chromosome H/EST similarities fit into well known, evolutionarily conserved families, an observation compatible with the concept of a limited set of 'ancient conserved regions' in protein sequences, a significant fraction of which is already known (Claverie, 1993;Green et al, 1993).…”

Section: Members Of Ancient Protein Familiesmentioning

confidence: 62%

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Yeast chromosome III: new gene functions.

1994

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One year after the release of the sequence of yeast chromosome III, we have re‐examined its open reading frames (ORFs) by computer methods. More than 61% of the 171 probable gene products have significant sequence similarities in the current databases; as many as 54% have already known functions or are related to functionally characterized proteins, allowing partial prediction of protein function, 11 percentage points more than reported a year ago; 19% are similar to proteins of known three‐dimensional structure, allowing model building by homology. The most interesting new identifications include a sugar kinase distantly related to ribokinases, a phosphatidyl serine synthetase, a putative transcription regulator, a flavodoxin‐like protein, and a zinc finger protein belonging to a distinct subfamily. Several ORFs have similarities to uncharacterized proteins, resulting in new families in search of a function’. About 54% of ORFs match sequences from other phyla, including numerous fragments in the database of expressed sequence tags (ESTs). Most significant similarities to ESTs are with proteins in conserved families widely represented in the databases. About 30% of ORFs contain one or more predicted transmembrane segments. The increase in the power of functional and structural prediction comes from improvements in sequence analysis and from richer databases and is expected to facilitate substantially the experimental effort in characterizing the function of new gene products.

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Section: Members Of Ancient Protein Familiessupporting

confidence: 88%

Section: Members Of Ancient Protein Familiesmentioning

confidence: 62%

Yeast chromosome III: new gene functions.

1994

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“…The gel readings were recorded, edited and compared using the Staden programs (Staden, 1982). Computer analysis Protein sequence homology was studied with the protein sequence database (release 5.0) of the Protein Identification Resource (PIR) of the National Biomedical Research Foundation and with PGtrans protein data base (release 35.0) (Claverie and Sauvaget, 1985) of the Pasteur Institute, Paris. DNA sequence analysis was performed with EMBL nucleotide sequence data base (release 7).…”

Section: Dna Probes and Hybridizationmentioning

confidence: 99%

Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and genetic sequences encoding a receptor-like protein.

Roebroek¹,

Schalken²,

Leunissen³

et al. 1986

The EMBO Journal

206

109

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Recently we described that genetic sequences in the immediately upstream region of the c‐fes/fps proto‐oncogene, designated fur, constituted a transcription unit for a 4.5‐kb mRNA. Here we present characteristics of the genetic organization of fur and some features of its putative translation product which we call furin. The nucleotide sequence of a 3.1‐kbp fur‐specific cDNA isolated from a human cDNA library revealed an open reading frame of 1,498 bp from which the 499 carboxy‐terminal amino acids of the primary fur translational product could be deduced. Computer analysis indicated that furin contained a possible transmembrane domain which resembled that of class II MHC antigens. Furthermore, a cysteine‐rich region was present. Significant homology, especially with respect to the topography of cysteine residues, was found between the cysteine‐rich regions of the human insulin receptor, the human epidermal growth factor receptor and furin. From the data presented here we deduce that fur may encode a membrane‐associated protein with a recognition function.

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“…The N-terminal amino acid sequence found is not identical to any of the sequences collected by the protein sequence data banks available to us (see Materials and Methods), nor to any open reading frame of a Genebank, translated as PGtrans (Claverie and Sauvaget, 1985). However, a few sequences have been found that exhibit significant degrees of homology (Table 3).…”

Section: Sequence Data Analysismentioning

confidence: 91%

N‐Terminal Sequence of Pig Brain Choline Acetyltransferase Purified by a Rapid Procedure

Braun

Barde

Lottspeich

et al. 1987

Journal of Neurochemistry

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A procedure is reported that allows the purification and amino terminal sequencing of pig brain choline acetyltransferase. The enzyme (present in extremely low amounts in this tissue) is eluted together with its antibody from an affinity column by a mild pH shift and the resulting enzyme-antibody complex separated by gel electrophoresis. The band corresponding to the enzyme is electroeluted from the gel using volatile solutions allowing the direct determination of the amino acid composition and partial sequence. The first 11 residues are: Pro-Ile-Leu-Glu-Lys-Thr-Pro-Pro-Lys-Met-Ala.

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A new protein sequence data bank

Cited by 18 publications

References 4 publications

Yeast chromosome III: new gene functions.

Yeast chromosome III: new gene functions.

Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and genetic sequences encoding a receptor-like protein.

N‐Terminal Sequence of Pig Brain Choline Acetyltransferase Purified by a Rapid Procedure

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