*Sniffles* I wanna know my apartment too... No idea where I have to look, even. My screen reader says nada that could be that... Unless it's not showing up on the frontpage...
...I'm about as lost as Hope... Though she at least can see shapes. Hehe.
..........
Okay, NVM, it shows up in my profile's URL,...
2874
Last edited by Storm; Nov 6th, 2013 at 01:36 AM.
Witch_Doctor liked this post
Great! My Apartment/Gene ID works on tumors and balls.
I guess I'm responsible for the dead behemoths.
This gene belongs to a family of genes that are expressed in a variety of tumors but not in normal tissues, except for the testis. The sequences of the family members are highly related but differ by scattered nucleotide substitutions. The antigenic peptide YRPRPRRY, which is also encoded by several other family members, is recognized by autologous cytolytic T lymphocytes. [provided by RefSeq, Jul 2008]
Call Sign: Jive Turkey
Ladies and Gentlemen, straight from Mysterical Island, it's the Shaman of Schiznick, the Mofo with the Mojo, the Mad Scientist of the Jungle, the Doctor is in!
Doctor? Doctor who?
NO! Witch Doctor, fool!
1362 here.. I got a Balcony but I removed all the flower pots.
Looked it up under the gene thingy.. Then found this on a wiki.. I am lost.. But looks like its bad..
carboxypeptidase D
Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active site serine residue) includes (EC 3.4.16.6, cereal serine carboxypeptidase II, Saccharomyces cerevisiae KEX1 gene product, carboxypeptidase Kex1, gene KEX1 serine carboxypeptidase, KEX1 carboxypeptidase, KEX1 proteinase, KEX1DELTAp, CPDW-II, serine carboxypeptidase, Phaseolus proteinase) is an enzyme.[1][2][3][4] This enzyme has an optimal pH of 4.5-6.0, is inhibited by diisopropyl fluorophosphate, and catalyses the following chemical reaction
Preferential release of a C-terminal arginine or lysine residue
A completely distinct enzyme has also been named carboxypeptidase D (EC number 3.4.17.22). This second enzyme is a metallocarboxypeptidase (i.e. uses a zinc ion in the active site instead of a serine residue) and is broadly expressed in mammalian tissues.[5] Like the serine carboxypeptidase, the metallocarboxypeptidase D also removes C-terminal arginine or lysine residues from peptides, with an optimal pH range of 5 to 7. Metallocarboxypeptidase D is located in the trans Golgi network where it contributes to the biosynthesis of neuropeptides and peptide hormones (such as insulin) along with carboxypeptidase E. In addition to this role, metallocarboxypeptidase D contributes to the processing of proteins, following the action of furin (an endoprotease located in the trans Golgi network). The duck ortholog of metallocarboxypeptidase D was named gp180 and is a receptor for uptake of duck hepatitis B virus.[6] In fruit fly (Drosophila melanogaster), carboxypeptidase D is known as the silver mutation, with defects causing altered wing shape.[7] Metallocarboxypeptidase D is generally a membrane-bound protein, although in some organisms a soluble form is generated by either differential RNA splicing or by proteolytic activity.[8][9] In the scientific literature, most of the published articles using the name "Carboxypeptidase D" in the title refer to metallocarboxypeptidase D and not the serine carboxypeptidase.
Last edited by Merlin1274; Nov 6th, 2013 at 06:31 AM.
Call Sign: Jive TurkeyMerlin1274 liked this post
Ladies and Gentlemen, straight from Mysterical Island, it's the Shaman of Schiznick, the Mofo with the Mojo, the Mad Scientist of the Jungle, the Doctor is in!
Doctor? Doctor who?
NO! Witch Doctor, fool!
Well, my days of not taking you seriously are certainly coming to a middle.Merlin1274, Witch_Doctor liked this post
Call Sign: Jive Turkeyscbubba liked this post
Ladies and Gentlemen, straight from Mysterical Island, it's the Shaman of Schiznick, the Mofo with the Mojo, the Mad Scientist of the Jungle, the Doctor is in!
Doctor? Doctor who?
NO! Witch Doctor, fool!
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