NUBP1_MOUSE
ID NUBP1_MOUSE Reviewed; 320 AA.
AC Q9R060; Q3U053; Q7TMI1; Q9CRM5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1 {ECO:0000255|HAMAP-Rule:MF_03038};
DE AltName: Full=Nucleotide-binding protein 1 {ECO:0000255|HAMAP-Rule:MF_03038};
DE Short=NBP 1 {ECO:0000255|HAMAP-Rule:MF_03038};
GN Name=Nubp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=10486206; DOI=10.1006/geno.1999.5898;
RA Nakashima H., Grahovac M.J., Mazzarella R., Fujiwara H., Kitchen J.R.,
RA Threat T.A., Ko M.S.H.;
RT "Two novel mouse genes -- Nubp2, mapped to the T-complex on chromosome 17,
RT and Nubp1, mapped to chromosome 16 -- establish a new gene family of
RT nucleotide-binding proteins in eukaryotes.";
RL Genomics 60:152-160(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Retina, Spleen, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH KIFC1 AND NUBP2.
RX PubMed=16638812; DOI=10.1242/jcs.02922;
RA Christodoulou A., Lederer C.W., Surrey T., Vernos I., Santama N.;
RT "Motor protein KIFC5A interacts with Nubp1 and Nubp2, and is implicated in
RT the regulation of centrosome duplication.";
RL J. Cell Sci. 119:2035-2047(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, INTERACTION WITH CCT1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23807208; DOI=10.1007/s00018-013-1401-6;
RA Kypri E., Christodoulou A., Maimaris G., Lethan M., Markaki M.,
RA Lysandrou C., Lederer C.W., Tavernarakis N., Geimer S., Pedersen L.B.,
RA Santama N.;
RT "The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of
RT ciliogenesis.";
RL Cell. Mol. Life Sci. 71:517-538(2014).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC assembly (CIA) machinery. Required for maturation of extramitochondrial
CC Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold
CC complex, mediating the de novo assembly of an Fe-S cluster and its
CC transfer to target apoproteins (By similarity). Implicated in the
CC regulation of centrosome duplication (PubMed:16638812,
CC PubMed:23807208). Negatively regulates cilium formation and structure
CC (PubMed:23807208). {ECO:0000255|HAMAP-Rule:MF_03038,
CC ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:23807208}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03038};
CC Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable
CC clusters in the N-termini of NUBP1 and two labile, bridging clusters
CC between subunits of the NUBP1-NUBP2 heterotetramer. {ECO:0000255|HAMAP-
CC Rule:MF_03038};
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains
CC (PubMed:16638812). Interacts with KIFC1 (PubMed:16638812). Interacts
CC with NUBP2 (PubMed:16638812). Interacts with the BBS/CCT complex
CC subunit CCT1 (PubMed:23807208). {ECO:0000255|HAMAP-Rule:MF_03038,
CC ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:23807208}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038,
CC ECO:0000269|PubMed:23807208}. Nucleus {ECO:0000269|PubMed:23807208}.
CC Cell projection {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton,
CC cilium axoneme {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton,
CC cilium basal body {ECO:0000269|PubMed:23807208}. Cytoplasm,
CC cytoskeleton, microtubule organizing center
CC {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:23807208}.
CC Note=Enriched in centrioles of microtubule asters during prophase,
CC prometaphase and telophase stages of mitosis. Localized at centrioles
CC and in the nucleus at interphase. Colocalizes with NUBP2 at
CC prometaphase. Specifically localizes to the axenome of motile cilia as
CC opposed to primary non-motile cilia. Localization is independent of
CC NUBP2 and KIFC1. {ECO:0000269|PubMed:23807208}.
CC -!- TISSUE SPECIFICITY: Expressed in trachea epithelial cells, and kidney
CC inner medullary collecting duct cells. {ECO:0000269|PubMed:23807208}.
CC -!- INDUCTION: High and constant expression in cycling cells. Down-
CC regulated upon cell cycle exit and quiescence.
CC {ECO:0000269|PubMed:23807208}.
CC -!- MISCELLANEOUS: NIH3T3 cells expressing reduced levels of Nubp1 show an
CC increase in number of centrosomes per cell and an increase in the
CC fraction of multinucleated cells.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP1/NBP35 subfamily. {ECO:0000255|HAMAP-Rule:MF_03038}.
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DR EMBL; AF114170; AAF01786.1; -; mRNA.
DR EMBL; AK020141; BAB32007.1; -; mRNA.
DR EMBL; AK157212; BAE34002.1; -; mRNA.
DR EMBL; BC055436; AAH55436.1; -; mRNA.
DR CCDS; CCDS27948.1; -.
DR RefSeq; NP_036085.1; NM_011955.2.
DR AlphaFoldDB; Q9R060; -.
DR SMR; Q9R060; -.
DR BioGRID; 204977; 6.
DR STRING; 10090.ENSMUSP00000023146; -.
DR PhosphoSitePlus; Q9R060; -.
DR EPD; Q9R060; -.
DR MaxQB; Q9R060; -.
DR PaxDb; Q9R060; -.
DR PeptideAtlas; Q9R060; -.
DR PRIDE; Q9R060; -.
DR ProteomicsDB; 289948; -.
DR Antibodypedia; 24622; 145 antibodies from 20 providers.
DR DNASU; 26425; -.
DR Ensembl; ENSMUST00000023146; ENSMUSP00000023146; ENSMUSG00000022503.
DR GeneID; 26425; -.
DR KEGG; mmu:26425; -.
DR UCSC; uc007ydo.2; mouse.
DR CTD; 4682; -.
DR MGI; MGI:1347073; Nubp1.
DR VEuPathDB; HostDB:ENSMUSG00000022503; -.
DR eggNOG; KOG3022; Eukaryota.
DR GeneTree; ENSGT00950000183193; -.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; Q9R060; -.
DR OMA; QHITFKD; -.
DR OrthoDB; 1166096at2759; -.
DR PhylomeDB; Q9R060; -.
DR TreeFam; TF300755; -.
DR BioGRID-ORCS; 26425; 26 hits in 70 CRISPR screens.
DR ChiTaRS; Nubp1; mouse.
DR PRO; PR:Q9R060; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9R060; protein.
DR Bgee; ENSMUSG00000022503; Expressed in ear vesicle and 256 other tissues.
DR ExpressionAtlas; Q9R060; baseline and differential.
DR Genevisible; Q9R060; MM.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISO:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:MGI.
DR GO; GO:0072697; P:protein localization to cell cortex; IMP:MGI.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR HAMAP; MF_03038; NUBP1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028601; NUBP1/Nbp35.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR23264; PTHR23264; 1.
DR Pfam; PF10609; ParA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Acetylation; ATP-binding; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..320
FT /note="Cytosolic Fe-S cluster assembly factor NUBP1"
FT /id="PRO_0000184944"
FT BINDING 8
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 31
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 235
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 238
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P53384"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5I0L4"
FT CONFLICT 170
FT /note="V -> I (in Ref. 3; AAH55436)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="C -> S (in Ref. 2; BAB32007)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="R -> K (in Ref. 3; AAH55436)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="H -> R (in Ref. 3; AAH55436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 34085 MW; AB56BDF7D730F311 CRC64;
MEEAPHGCPG ADSAQAGRGA SCQGCPNQRL CASGAGAAPD PAVEEIREKM KTVRHKLLVL
SGKGGVGKST FSAHLAHGLA EDGDTQVALL DIDICGPSIP KIMGLEGEQV HQSGSGWSPV
YVDDNLGVMS VGFLLSSPDD AVIWRGPKKN GMIKQFLRDV DWGDVDYLIV DTPPGTSDEH
LSVVQYLAAA HIDGAVILTT PQEVALQDVR KEISFCHKVK LPIIGVVENM SGFICPKCKK
ESQIFPPTTG GAEAMCQDLR IPLLGKVPLD PHIGKSCDKG QSFFVEAPDS PATAAYRSII
QRIRDFCNSH QSHAETLISP
