Protein accession number

Platyhelminth protein Accession number Human homologue Accession number % Identity % Similarity... 

There are many tissue-specific or cell-specific forms of FABP the MFGM form is most likely to be heart FABP, the sequence of which has been determined (Swiss Protein accession number P10790). However, it is possible that other forms of FABP also are associated with the MFGM (Mather, 2000). As yet, no functional role has been found for FABP of MFGM. 

Spot number Identified proteins Accession number Mowse score No. of peptides identified Sequence coverage <%)... 

Protein accession numbers claimed to be in supplementary material but none available. 

Fig. 19. Conserved domain search results. The query protein in the Genome BLAST Problem 1, NP 032294, contains a homeodomain between amino acid 195..253, highlighted by ovals. Perform this search for the protein accession number NP 032294 from the Genomes Problem 1 to reach the view shown in this figure. The query protein contains a homeodomain between amino acids 195..253.

Manual CDD search. A protein query can be also manually searched against the conserved domain database. The option is provided under the Protein panel at the Search the conserved domain database (rpsblast) link. Perform this searchfor the protein accession number NP 032294 from the Genomes problem 1 (Fig. 19). 

Clicking on a protein accession number from the list brings up further information (see Fig. 5), including the matched peptides, listed and mapped onto the protein sequence, as well as the percentage of sequence coverage and any unmatched masses. There will almost inevitably be some unmatched masses they can... 

FIGURE 1.1 A 2D-gel electrophoresis map of colorectal epithelia cells proteins from the SWISS- 2DPage database (entry CATD HUMAN, primary access number P07339) accessible from http //www.expasy.org/swiss-2dpage. 

In addition to bcl-2, another hitherto completely unexpected target for the actions of chronic lithium and VPA has been identified from the mRNA RT-PCR DD study described above. Another clone, also derived from a transcript whose levels were increased by both lithium and VPA, shows very strong homology to a human mRNA-binding protein, the AUH protein ([54, 55] Genbank accession number X79888). BESTFIT analysis revealed 83.2% sequence homology between this rodent clone and the human AUH protein [54—56]. 

Nuclear pore complex protein nu Accession number swissprot P52948... 

DR EMBL ACCESSION NUMBER PROTEIN ID STATUS IDENTIFIER. 

The SWISS-PROT and TrEMBL ID lines differ in the first two parts of the ID line. The first part is the entry name "ANP NOTCO" in the case of the SWISS-PROT example and "Q12757" in the TrEMBL example. The entry name used in all SP-TrEMBL entries is always the same as the accession number of the entry. The entry name used in REM-TrEMBL is the Protein ID tagged to the corresponding CDS in the EMBL Nucleotide Sequence Database. To the right of the entry name you will find either "preliminary" (in the TrEMBL entry) or STANDARD (in the SWISS-PROT entry). The data class used in TrEMBL is always PRELIMINARY. That means that the data are thoroughly checked by a computer,... 

The NCI domain of type VIII collagen is important for trimerization. ACRP30/adiponectin, a member of the complement Clq family of proteins,and the type X collagen NCI domain have similar structures as the NCI domain of type VIII collagen however, the type Vlll collagen NCI trimer lacks the buried calcium cluster found in the type X collagen NCI trimer. The crystal structure of this domain has similarity to the TNF (tumor necrosis factor) family of proteins (PDB accession number 1091). ... 

The crystal structure of the peptide substrate-binding domain (140—245 of 517 residues of human al subunit) of the human type I enzyme forms 2.5 tetratricopeptide (TPR) repeat domains with five a helices (PDB accession number ITJC). The organization of tyrosine residues is suggested to be key to its interaction with the substrate peptide in a polyproline II helix. The TPR motif is composed of a 34 amino acid repeated a helical motif, and is typically involved in protein-protein interactions. The tandem repeats of TPR motifs are found in many proteins related to chaperone, cell cycle, transcription, and protein transport... 

KcsA crystals suitable for X-ray crystallographic analysis using synchrotron radiation were obtained and the data collected and analyzed for multiple crystals and six different data sets as described in the 1998 Science publication (reference 15). The final KcsA pore structure, including amino acid residues 23 to 119 of the K+ channel, refined to 3.2 A. The X-ray data were deposited in the Protein Data Bank with the accession number 1BL8. 

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