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NUBP2

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NUBP2
Identifikatori
AliasiNUBP2
Vanjski ID-jeviOMIM: 610779 MGI: 1347072 HomoloGene: 8057 GeneCards: NUBP2
Lokacija gena (čovjek)
Hromosom 16 (čovjek)
Hrom.Hromosom 16 (čovjek)[1]
Hromosom 16 (čovjek)
Genomska lokacija za NUBP2
Genomska lokacija za NUBP2
Bend16p13.3Početak1,782,932 bp[1]
Kraj1,789,186 bp[1]
Lokacija gena (miš)
Hromosom 17 (miš)
Hrom.Hromosom 17 (miš)[2]
Hromosom 17 (miš)
Genomska lokacija za NUBP2
Genomska lokacija za NUBP2
Bend17 A3.3|17 12.53 cMPočetak24,882,611 bp[2]
Kraj24,886,349 bp[2]
Ontologija gena
Molekularna funkcija• 4 iron, 4 sulfur cluster binding
• iron-sulfur cluster binding
• GO:0001948, GO:0016582 vezivanje za proteine
• ATP binding
• vezivanje iona metala
• nucleotide binding
Ćelijska komponenta• citoplazma
• Centriole
• projekcija ćelije
• spindle pole centrosome
• Treplja
• citoskelet
• jedro
• centar organizacije mikrotubula
• citosol
Biološki proces• cell projection organization
• iron-sulfur cluster assembly
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez

10101

26426

Ensembl

ENSG00000095906

ENSMUSG00000039183

UniProt

Q9Y5Y2

Q9R061

RefSeq (mRNK)

NM_001284501
NM_001284502
NM_012225

NM_011956
NM_001355396

RefSeq (bjelančevina)

NP_001271430
NP_001271431
NP_036357

NP_036086
NP_001342325

Lokacija (UCSC)Chr 16: 1.78 – 1.79 MbChr 17: 24.88 – 24.89 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš
ATPazoiki ParA/MinD
Identifikatori
SimbolParA

Nukleotid-vezujući protein 2 (NBP 2), znan i kao citosolni Fe-S klasterski sklopni faktor NUBP2 je protein koji je kod ljudi kodoran genom NUBP2.[5]

NUBP2 je član potporodice gena NUBP/MRP proteina koji vežu ATP[6] U eukariota postoje dva tipa: NUBP1 i NUBP2, i jedan novi ljudski gen koji kodirira proteine koji vežu NBP nukleotide (NUBP/MRP-pridruženi protein otpornosti na više lijekova)[5] u ćelijama sisara zahtijeva sazrijevanje citosolnog [7] gvožđe-sumpornih (Fe/S)[8] proteina jer je Nubp1 uključen u stvaranje vanmitohondrijskih Fe/S proteina.[6] Inhibitor ćelijdske diobe MinD je homologan [9] i iključuje dvije proteinske komponente (FeS) proteinskog sklopnog mehanizma sličnog citosolnoj[6] rastvorljivoj[8] P-petlji[9] NTPaze gdje Nar1[10][11] potreban je za sklapanje,[12] identificiranog Cfd1p[13][14] u biogenezi citosolnnog i jedarnog proteina Fe/S[8] kod kvasca.[15] Nubp proteini NTPaza Nbp35p.[11][12] MinD je homolog članova MinD-u E. coli, asrodnika porodice ParA.[9][16][17]

Aminokiselinska sekvenca

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Dužina polipeptidnog lanca je 271 aminokiselina, a molekulska težina 28.825 Da.[18].

1020304050
MEAAAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHAGKKVGILD
VDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDREQSISLMSVGFLLEKPD
EAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALRP
YQPLGALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCT
ECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPGSP
AFAALTSIAQKILDATPACLP
Simboli

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

Morfologija

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NBP35 bakterijski plazmidi F (klasični spollni faktor Escherichia coli) [9] nalaze se u svim jedarnim genima u vegetativnim i gametskim bičevima jednoćelijskih zelenih algi C. reinhardtii i jedarnoj biogenezi Fe/S proteina potrebnoj za citosolni sklop proteina gvožđe-sumpor; MNP =MRP-liki; MRP, sličnom MRP/NBP35-likoj P-l NTPazi, a funkcionira kao minD-luk ATPaza MinD ćelijske diobe archaea i homolozi NUBP1. Gen NBP35 konzerviran je u arhejama [19] Bacteria, Metazoa, Fungi i ostalim eukariotima i uz znatna odstupanja od kvaščevih Cfd1-Nbp35 i Fe-S čovjeka. U kompleksu skela [20] proteina koji stvara velike molekulske sklopove u kojima se čuvaju Fe (III) i 4Fe-4S koji se smatraju sekundarnim u odnosu na defektno inaktivirane da bi izvršili svoje funkcije kao fiziološki relevantni oblik Fe / S proteina. Regulator gvožđe-proteina 1 (IRP 1) regulira se putem [14] sprečavanja nedostataka i povećane stope mutacija[17] koj karakteriziraju biljne P-petlje NTPaza sa sličnošću sekvence sa Nbp35 homolozima of NUBP1.[21]

Interakcije

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Pokazano je da NUBP2 komuniciraju sa

  • ACO1 proteinom koji veže element na gvožđe 1 (IRE-BP 1) (protein koji reguliše željezo 1) (IRP1) [14][22]
  • MAPK8IP3 C-jun-amino-terminalni kinazni interakcijski protein 3 (JNK-interakcijski protein 3) (JIP-3)[23]
  • IGFALS prekursor lanca labilnog lanca proteina koji veže protein sličan insulinu (ALS)[23][24]
  • KIF11 Kinezinoliki protein KIF11 (kinezinu-srodni motorni protein Eg5)[25]
  • SEPP1 Selenoprotein P precursor (SeP)[17]
  • CA1 ugljik-anhidraza 1 (EC 4.2.1.1) (ugljik- anhidraza I) (karbonat-dehidrataza I) (CA-I)[16][17][21]

Reference

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  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000095906 - Ensembl, maj 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000039183 - Ensembl, maj 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 Nakashima H, Grahovac MJ, Mazzarella R, et al. (1999). "Two novel mouse genes--Nubp2, mapped to the t-complex on chromosome 17, and Nubp1, mapped to chromosome 16--establish a new gene family of nucleotide-binding proteins in eukaryotes". Genomics. 60 (2): 152–60. doi:10.1006/geno.1999.5898. PMID 10486206.
  6. 1 2 3 Stehling O, Netz DJ, Niggemeyer B, et al. (2008). "Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis". Mol. Cell. Biol. 28 (17): 5517–28. doi:10.1128/MCB.00545-08. PMC 2519719. PMID 18573874.
  7. ↑ Netz DJ, Pierik AJ, Stümpfig M, Mühlenhoff U, Lill R (2007). "The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol". Nat Chem Biol. 3 (5): 278–86. doi:10.1038/nchembio872. PMID 17401378.
  8. 1 2 3 Hausmann A, Aguilar Netz DJ, Balk J, Pierik AJ, Mühlenhoff U, Lill R (2005). "The eukaryotic P-loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery". Proc Natl Acad Sci U S A. 102 (9): 3266–71. Bibcode:2005PNAS..102.3266H. doi:10.1073/pnas.0406447102. PMC 552912. PMID 15728363.
  9. 1 2 3 4 Motallebi-Veshareh M, Rouch DA, Thomas CM (1990). "A family of ATPases involved in active partitioning of diverse bacterial plasmids". Mol. Microbiol. 4 (9): 1455–63. doi:10.1111/j.1365-2958.1990.tb02056.x. PMID 2149583. S2CID 40829252.
  10. ↑ Balk J, Aguilar Netz DJ, Tepper K, Pierik AJ, Lill R (2005). "The essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly". Mol Cell Biol. 25 (24): 10833–41. doi:10.1128/MCB.25.24.10833-10841.2005. PMC 1316972. PMID 16314508.
  11. 1 2 Rutherford JC, Ojeda L, Balk J, Mühlenhoff U, Lill R, Winge DR (2005). "Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis". J Biol Chem. 280 (11): 10135–40. doi:10.1074/jbc.M413731200. PMID 15649888. Arhivirano s originala, 12. 3. 2012. Pristupljeno 8. 7. 2021.
  12. 1 2 Balk J, Pierik AJ, Aguilar Netz DJ, Mühlenhoff U, Lill R (2005). "Nar1p, a conserved eukaryotic protein with similarity to Fe-only hydrogenases, functions in cytosolic iron-sulphur protein biogenesis". Biochem Soc Trans. 33 (Pt.1): 86–9. doi:10.1042/BST0330086. PMID 15667273. Arhivirano s originala, 12. 3. 2012. Pristupljeno 8. 7. 2021.
  13. ↑ Yarunin A, Panse VG, Petfalski E, Dez C, Tollervey D, Hurt EC (2005). "Functional link between ribosome formation and biogenesis of iron-sulfur proteins". EMBO J. 24 (3): 580–8. doi:10.1038/sj.emboj.7600540. PMC 548649. PMID 15660135.
  14. 1 2 3 Roy A, Solodovnikova N, Nicholson T, et al. (2003). "A novel eukaryotic factor for cytosolic Fe-S cluster assembly". EMBO J. 22 (18): 4826–35. doi:10.1093/emboj/cdg455. PMC 212722. PMID 12970194.
  15. ↑ Okuno T, Yamabayashi H, Kogure K (2010). "Comparison of intracellular localization of Nubp1 and Nubp2 using GFP fusion proteins". Mol Biol Rep. 37 (3): 1165–8. doi:10.1007/s11033-009-9477-7. PMID 19263241. S2CID 998955.
  16. 1 2 Bignell C, Thomas CM (2001). "The bacterial ParA-ParB partitioning proteins". J Biotechnol. 91 (2): 1–34. doi:10.1016/S0168-1656(01)00293-0. ISSN 0168-1656. PMID 11522360.
  17. 1 2 3 4 Fukushima K, Ogawa H, Takahashi K, Naito H, Funayama Y, Kitayama T, Yonezawa H, Sasaki I (2003). "Non-pathogenic bacteria modulate colonic epithelial gene expression in germ-free mice". Scand J Gastroenterol. 38 (6): 626–34. doi:10.1080/00365510310000376. ISSN 0036-5521. PMID 12825871. S2CID 25927173.
  18. ↑ "UniProt, Q9Y5Y2". Pristupljeno 8. 7. 2021.
  19. ↑ Kohbushi H, Nakai Y, Kikuchi S, Yabe T, Hori H, Nakai M (2009). "Arabidopsis cytosolic Nbp35 homodimer can assemble both [2Fe-2S] and [4Fe-4S] clusters in two distinct domains". Biochem Biophys Res Commun. 378 (4): 810–5. doi:10.1016/j.bbrc.2008.11.138. PMID 19084504.
  20. ↑ Bych K, Netz DJ, Vigani G, Bill E, Lill R, Pierik AJ, Balk J (2008). "The essential cytosolic iron-sulfur protein Nbp35 acts without Cfd1 partner in the green lineage". J Biol Chem. 283 (51): 35797–804. doi:10.1074/jbc.M807303200. PMID 18957412.
  21. 1 2 "Entrez Gene: UniGene Hs.256549 Nucleotide binding protein 2 (MinD homolog, E. coli) (NUBP2)".
  22. ↑ "Entrez Gene: NUCLEOTIDE-BINDING PROTEIN 2; NUBP2 CYTOSOLIC FE-S CLUSTER DEFICIENT 1, S. CEREVISIAE, HOMOLOG OF; CFD1 Gene map locus: 16p13.3".
  23. 1 2 Kargul GJ, Nagaraja R, Shimada T, Grahovac MJ, Lim MK, Nakashima H, Waeltz P, Ma P, Chen E, Schlessinger D, Ko MS (2000). "Eleven densely clustered genes, six of them novel, in 176 kb of mouse t-complex DNA". Genome Res. 10 (7): 916–23. doi:10.1101/gr.10.7.916. PMC 310918. PMID 10899141.
  24. ↑ Sano Y, Shimada T, Nakashima H, Nicholson RH, Eliason JF, Kocarek TA, Ko MS (2001). "Random monoallelic expression of three genes clustered within 60 kb of mouse t complex genomic DNA". Genome Res. 11 (11): 1833–41. doi:10.1101/gr.194301. PMC 311134. PMID 11691847.
  25. ↑ Christodoulou A, Lederer CW, Surrey T, Vernos I, Santama N (2006). "Motor protein KIFC5A interacts with Nubp1 and Nubp2, and is implicated in the regulation of centrosome duplication". J Cell Sci. 119 (Pt 10): 2035–47. doi:10.1242/jcs.02922. PMID 16638812.

Dopunska literatura

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