NUBP2 information

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

ParA/MinD ATPase like
ParA/MinD ATPase like
Identifiers
Symbol	ParA
Pfam	PF10609
InterPro	IPR019591
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

NUBP2
Identifiers
Aliases	NUBP2, CFD1, NBP 2, NUBP1, nucleotide binding protein 2, CIAO6, NUBP iron-sulfur cluster assembly factor 2, cytosolic
External IDs	OMIM: 610779; MGI: 1347072; HomoloGene: 8057; GeneCards: NUBP2; OMA:NUBP2 - orthologs
Gene location (Human)
Chr.	Chromosome 16 (human)
End	1,789,186 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	24,886,349 bp
RNA expression pattern
	Top expressed in
	thymus; ; right lobe of liver; ; right hemisphere of cerebellum; ; apex of heart; ; muscle of thigh; ; fundus; ; body of pancreas; ; right adrenal gland; ; gastrocnemius muscle; ; left adrenal cortex;
	Top expressed in
	spermatocyte; ; seminiferous tubule; ; spermatid; ; right kidney; ; morula; ; fetal liver hematopoietic progenitor cell; ; yolk sac; ; blastocyst; ; embryo; ; proximal tubule;
	More reference expression data
	n/a
Gene ontology
Molecular function	4 iron, 4 sulfur cluster binding; iron-sulfur cluster binding; protein binding; ATP binding; metal ion binding; nucleotide binding;
Cellular component	cytoplasm; centriole; cell projection; spindle pole centrosome; cilium; cytoskeleton; nucleus; microtubule organizing center; cytosol;
Biological process	cell projection organization; iron-sulfur cluster assembly;
	Sources:Amigo / QuickGO
Orthologs
	10101
	26426
	ENSG00000095906
	ENSMUSG00000039183
	Q9Y5Y2
	Q9R061
	NM_001284501; NM_001284502; NM_012225
	NM_011956; NM_001355396
	NP_001271430; NP_001271431; NP_036357
	NP_036086; NP_001342325
	Wikidata
View/Edit Human	View/Edit Mouse

Nucleotide-binding protein 2 (NBP 2) also known as cytosolic Fe-S cluster assembly factor NUBP2 is a protein that in humans is encoded by the NUBP2 gene.^[5]

NUBP2 is a member of the NUBP/MRP gene subfamily of ATP-binding proteins.^[6] There are two types in eukaryotes NUBP1 and NUBP2, and one novel human gene that define NBP nucleotide-binding proteins (NUBP/MRP-multidrug resistance-associated protein)^[5] in mammalian cells requires the maturation of cytosolic^[7] iron-sulfur (Fe/S)^[8] proteins as Nubp1 is involved in the formation of extramitochondrial Fe/S proteins^[6] the cell division inhibitor MinD is homologous^[9] and involve two proteins components of the (FeS) protein assembly machinery closely similar cytosolic^[6] soluble^[8] P loop^[9] NTPase where Nar1^[10]^[11] is required for assembly,^[12] identified Cfd1p^[13]^[14] in cytosolic and nuclear Fe/S protein biogenesis^[8] in yeast.^[15] Nubp proteins NTPase Nbp35p.^[11]^[12] MinD is homologous to members in MinD of E. coli, a relative of the ParA family.^[9]^[16]^[17]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000095906 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000039183 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b 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.
^ ^a ^b ^c 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.
^ 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.
^ ^a ^b ^c 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.
^ ^a ^b ^c 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.
^ 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.
^ ^a ^b 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.
^ ^a ^b 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. Archived from the original on 2012-03-12. Retrieved 2010-12-23.
^ 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.
^ 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.
^ 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.
^ 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.
^ 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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000095906 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000039183 – Ensembl, May 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.

[pmid10486206-5] 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.

[pmid18573874-6] 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.

[pmid17401378-7] 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.

[pmid15728363-8] 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.

[pmid2149583-9] 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.

[pmid16314508-10] 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.

[pmid15649888-11] 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.

[pmid15667273-12] 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. Archived from the original on 2012-03-12. Retrieved 2010-12-23.

[pmid15660135-13] 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.

[pmid12970194-14] 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.

[pmid19263241-15] 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.

[pmid11522360-16] 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.

[pmid12825871-17] 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.