UGDH

UGDH
Strwythurau PDB Human UniProt search: PDBe RCSB Rhestr o ddynodwyr PDB 2Q3E, 2QG4, 3ITK, 3KHU, 3PRJ, 3PTZ, 3TDK, 3TF5, 4EDF, 4QEJ, 4RJT
Dynodwyr
Cyfenwau	UGDH, GDH, UDP-GlcDH, UDPGDH, UGD, UDP-glucose 6-dehydrogenase, EIEE84, DEE84
Dynodwyr allanol	OMIM: 603370 HomoloGene: 2520 GeneCards: UGDH
EC number	1.1.1.22
Patrwm RNA pattern Rhagor o gyfeiriadau
Ontoleg y genyn Gweithrediad moleciwlaidd • NAD binding • catalytic activity • oxidoreductase activity • electron transfer activity • GO:0050229 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor • UDP-glucose 6-dehydrogenase activity Cydrannau o'r gell • nucleoplasm • extracellular exosome • cnewyllyn cell • cytosol Prosesau biolegol • UDP-glucuronate biosynthetic process • gastrulation with mouth forming second • metabolaeth • UDP-glucose metabolic process • glycosaminoglycan biosynthetic process • electron transport chain • heparan sulfate proteoglycan biosynthetic process • chondroitin sulfate biosynthetic process • protein hexamerization • carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologau
Species	Bod dynol	Llygoden
Entrez	7358	n/a
Ensembl	ENSG00000109814	n/a
UniProt	O60701	n/a
RefSeq (mRNA)	NM_001184700 NM_001184701 NM_003359	n/a
RefSeq (protein)	NP_001171629 NP_001171630 NP_003350	n/a
Lleoliad (UCSC)	n/a	n/a
PubMed search	[1]	n/a
Wicidata
Gweld/Golygu Bod dynol

Protein sy'n cael ei godio yn y corff dynol gan y genyn UGDH yw UGDH a elwir hefyd yn UDP-glucose 6-dehydrogenase (Saesneg). Segment o DNA yw'r genyn, sy'n amgodio ffwythiant arbennig. Mae'r genyn yma wedi ei leoli ar yr edefyn ôl o gromosom dynol 4, band 4p14.^[2]

Yn aml mae gan enynnau lawer o gyfystyron. Mae hyn oherwydd eu bod yn aml yn cael eu darganfod gan nifer o bobl mewn cyd-destunau gwahanol heb wybod mai'r un genynnau oeddyn nhw. Hefyd mae gan wahanol gymunedau gwyddonol safonau gwahanol ar gyfer enwi genynnau. Dyma restr o gyfystyron ar gyfer y genyn UGDH.

• "UDP-glucose dehydrogenase activity and optimal downstream cellular function require dynamic reorganization at the dimer-dimer subunit interfaces. ". J Biol Chem. 2013. PMID 24145036.
• "Hysteresis and negative cooperativity in human UDP-glucose dehydrogenase. ". Biochemistry. 2013. PMID 23363239.
• "Allostery and Hysteresis Are Coupled in Human UDP-Glucose Dehydrogenase. ". Biochemistry. 2017. PMID 27966912.
• "Hysteresis in human UDP-glucose dehydrogenase is due to a restrained hexameric structure that favors feedback inhibition. ". Biochemistry. 2014. PMID 25478983.
• "UDP-glucose dehydrogenase modulates proteoglycan synthesis in articular chondrocytes: its possible involvement and regulation in osteoarthritis.". Arthritis Res Ther. 2014. PMID 25465897.