DHX32

Putativna faktorska preradna pre-iRNK ATP-ovisna RNK helikaza DHX32 je enzim koji je kod ljudi kodiran genom DHX32.

DHX32
Identifikatori
Aliasi	DHX32
Vanjski ID-jevi	OMIM: 607960 MGI: 2141813 HomoloGene: 56798 GeneCards: DHX32
Lokacija gena (čovjek) Hrom. Hromosom 10 (čovjek) Bend 10q26.2 Početak 125,836,337 bp Kraj 125,896,436 bp
Lokacija gena (miš) Hrom. Hromosom 7 (miš) Bend 7|7 F3 Početak 133,322,671 bp Kraj 133,384,455 bp
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • nucleotide binding • GO:0001948, GO:0016582 vezivanje za proteine • ATP binding • hydrolase activity • GO:0008026 helicase activity • vezivanje sa RNK • GO:0034459 3'-5' RNA helicase activity Ćelijska komponenta • spliceosomal complex • mitohondrija • jedro • citoplazma Biološki proces • mRNA splicing, via spliceosome Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	55760	101437
Ensembl	ENSG00000089876	ENSMUSG00000030986
UniProt	Q7L7V1	Q8BZS9
RefSeq (mRNK)	NM_018180	NM_001286030 NM_001286031 NM_001286032 NM_133941 NM_001357685
RefSeq (bjelančevina)	NP_060650	NP_001272959 NP_001272960 NP_001272961 NP_598702 NP_001344614 NP_001390352 NP_001390353 NP_001390354
Lokacija (UCSC)	Chr 10: 125.84 – 125.9 Mb	Chr 7: 133.32 – 133.38 Mb
PubMed pretraga
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 743 aminokiseline, а molekulska težina 84.419

• C: Cistein
• D: Asparaginska kiselina
• E: Glutaminska kiselina
• F: Fenilalanin
• G: Glicin
• H: Histidin
• I: Izoleucin
• K: Lizin
• L: Leucin
• M: Metionin
• N: Asparagin
• P: Prolin
• Q: Glutamin
• R: Arginin
• S: Serin
• T: Treonin
• V: Valin
• W: Triptofan
• Y: Tirozin

10		20		30		40		50
MEEEGLECPN		SSSEKRYFPE		SLDSSDGDEE		EVLACEDLEL		NPFDGLPYSS
RYYKLLKERE		DLPIWKEKYS		FMENLLQNQI		VIVSGDAKCG		KSAQVPQWCA
EYCLSIHYQH		GGVICTQVHK		QTVVQLALRV		ADEMDVNIGH		EVGYVIPFEN
CCTNETILRY		CTDDMLQREM		MSNPFLGSYG		VIILDDIHER		SIATDVLLGL
LKDVLLARPE		LKLIINSSPH		LISKLNSYYG		NVPVIEVKNK		HPVEVVYLSE
AQKDSFESIL		RLIFEIHHSG		EKGDIVVFLA		CEQDIEKVCE		TVYQGSNLNP
DLGELVVVPL		YPKEKCSLFK		PLDETEKRCQ		VYQRRVVLTT		SSGEFLIWSN
SVRFVIDVGV		ERRKVYNPRI		RANSLVMQPI		SQSQAEIRKQ		ILGSSSSGKF
FCLYTEEFAS		KDMTPLKPAE		MQEANLTSMV		LFMKRIDIAG		LGHCDFMNRP
APESLMQALE		DLDYLAALDN		DGNLSEFGII		MSEFPLDPQL		SKSILASCEF
DCVDEVLTIA		AMVTAPNCFS		HVPHGAEEAA		LTCWKTFLHP		EGDHFTLISI
YKAYQDTTLN		SSSEYCVEKW		CRDYFLNCSA		LRMADVIRAE		LLEIIKRIEL
PYAEPAFGSK		ENTLNIKKAL		LSGYFMQIAR		DVDGSGNYLM		LTHKQVAQLH
PLSGYSITKK		MPEWVLFHKF		SISENNYIRI		TSEISPELFM		QLVPQYYFSN
LPPSESKDIL		QQVVDHLSPV		STMNKEQQMC		ETCPETEQRC		TLQ

Funkcija

Proteini iz kutije DEAD, karakterizirani konzerviranim motivom Asp-Glu-Ala-Asp (DEAD), su pretpostavljene RNK-helikaze. Uključeni su u brojne ćelijske procese koji obuhvataju promjenu sekundarne strukture RNK, poput translacijske inicijacije, jedarne i mitohondrijske prerade i sklapanje ribosoma i splajsosoma. Na osnovu njihovih obrazaca distribucije, vjeruje se da su neki članovi ove porodice proteina DEAD-kutije uključeni u embriogenezu, spermatogenezu, te ćelijski rast i diobu. Ovaj gen kodira člana ove porodice čija funkija nije utvrđena. Alternativna prerada ovog gena generira dvije varijante transkripta, ali priroda cijele dužine jedne od varijanti nije definirana.

Dopunska literatura

• Alli Z, Chen Y, Abdul Wajid S, et al. (2007). "A role for DHX32 in regulating T-cell apoptosis". Anticancer Res. 27 (1A): 373–7. PMID 17352256.
• Chen Y, Alli Z, Ackerley C, et al. (2007). "Altered distribution of heat shock protein 60 (Hsp60) with dysregulated expression of DHX32". Exp. Mol. Pathol. 82 (3): 256–61. doi:10.1016/j.yexmp.2006.11.002. PMID 17174952.
• Alli Z, Ackerley C, Chen Y, et al. (2007). "Nuclear and mitochondrial localization of the putative RNA helicase DHX32". Exp. Mol. Pathol. 81 (3): 245–8. doi:10.1016/j.yexmp.2006.07.005. PMID 16959245.
• Alli Z, Nam EH, Beimnet K, Abdelhaleem M (2006). "The activation-induced expression of DHX32 in Jurkat T cells is specific and involves calcium and nuclear factor of activated T cells". Cell. Immunol. 237 (2): 141–6. doi:10.1016/j.cellimm.2005.12.003. PMID 16414036.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Abdelhaleem M (2002). "The novel helicase homologue DDX32 is down-regulated in acute lymphoblastic leukemia". Leuk. Res. 26 (10): 945–54. doi:10.1016/S0145-2126(02)00040-1. PMID 12163057.
• Liu J, Yuan Y, Huan J, Shen Z (2001). "Inhibition of breast and brain cancer cell growth by BCCIPalpha, an evolutionarily conserved nuclear protein that interacts with BRCA2". Oncogene. 20 (3): 336–45. doi:10.1038/sj.onc.1204098. PMID 11313963.