NUBP2_MOUSE
ID NUBP2_MOUSE Reviewed; 275 AA.
AC Q9R061;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP2 {ECO:0000255|HAMAP-Rule:MF_03039};
DE AltName: Full=Nucleotide-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_03039};
DE Short=NBP 2 {ECO:0000255|HAMAP-Rule:MF_03039};
GN Name=Nubp2;
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=C57BL/6J; TISSUE=Ectoplacental cone;
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; TISSUE=Embryo;
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=C57BL/6J; 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 INTERACTION WITH KIFC1 AND NUBP2, AND SUBCELLULAR LOCATION.
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=Brain, Heart, Kidney, Liver, Lung, 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 NUBP1, AND SUBCELLULAR LOCATION.
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. Negatively regulates cilium formation
CC and structure (PubMed:23807208). {ECO:0000255|HAMAP-Rule:MF_03039,
CC ECO:0000269|PubMed:23807208}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03039};
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_03039};
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains (By similarity).
CC Interacts with KIFC1 (PubMed:16638812). Interacts with NUBP1
CC (PubMed:16638812, PubMed:23807208). {ECO:0000255|HAMAP-Rule:MF_03039,
CC ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:23807208}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03039,
CC ECO:0000269|PubMed:16638812}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03039,
CC ECO:0000269|PubMed:16638812}. Cytoplasm {ECO:0000269|PubMed:23807208}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:23807208}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton,
CC microtubule organizing center {ECO:0000269|PubMed:23807208}.
CC Note=Enriched at the centrosomes during mitosis (By similarity).
CC Enriched in centrioles of microtubule asters during prophase,
CC prometaphase and telophase stages of mitosis (PubMed:23807208).
CC Localized at centrioles and in the nucleus at interphase
CC (PubMed:23807208). Colocalizes with nubp-1 at prometaphase
CC (PubMed:23807208). {ECO:0000255|HAMAP-Rule:MF_03039,
CC ECO:0000269|PubMed:23807208}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DEVELOPMENTAL STAGE: Expressed at 7, 11, 15 and 17 dpc.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP2/CFD1 subfamily. {ECO:0000255|HAMAP-Rule:MF_03039}.
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DR EMBL; AF114169; AAF01785.1; -; mRNA.
DR EMBL; AK003816; BAB23013.1; -; mRNA.
DR EMBL; BC012635; AAH12635.1; -; mRNA.
DR CCDS; CCDS28500.1; -.
DR RefSeq; NP_036086.1; NM_011956.3.
DR AlphaFoldDB; Q9R061; -.
DR SMR; Q9R061; -.
DR BioGRID; 204978; 2.
DR STRING; 10090.ENSMUSP00000049319; -.
DR PhosphoSitePlus; Q9R061; -.
DR EPD; Q9R061; -.
DR MaxQB; Q9R061; -.
DR PaxDb; Q9R061; -.
DR PeptideAtlas; Q9R061; -.
DR PRIDE; Q9R061; -.
DR ProteomicsDB; 293804; -.
DR Antibodypedia; 23260; 89 antibodies from 18 providers.
DR Ensembl; ENSMUST00000044252; ENSMUSP00000049319; ENSMUSG00000039183.
DR GeneID; 26426; -.
DR KEGG; mmu:26426; -.
DR UCSC; uc008ayo.2; mouse.
DR CTD; 10101; -.
DR MGI; MGI:1347072; Nubp2.
DR VEuPathDB; HostDB:ENSMUSG00000039183; -.
DR eggNOG; KOG3022; Eukaryota.
DR GeneTree; ENSGT00950000183193; -.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; Q9R061; -.
DR OMA; QGWVPVY; -.
DR OrthoDB; 1166096at2759; -.
DR PhylomeDB; Q9R061; -.
DR TreeFam; TF354321; -.
DR BioGRID-ORCS; 26426; 27 hits in 72 CRISPR screens.
DR PRO; PR:Q9R061; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9R061; protein.
DR Bgee; ENSMUSG00000039183; Expressed in spermatocyte and 248 other tissues.
DR ExpressionAtlas; Q9R061; baseline and differential.
DR Genevisible; Q9R061; 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; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031616; C:spindle pole centrosome; IDA: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; IBA:GO_Central.
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:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR HAMAP; MF_03039; NUBP2; 1.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028600; NUBP2/Cfd1_eukaryotes.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR23264; PTHR23264; 1.
DR Pfam; PF10609; ParA; 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; Reference proteome.
FT CHAIN 1..275
FT /note="Cytosolic Fe-S cluster assembly factor NUBP2"
FT /id="PRO_0000184946"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT BINDING 200
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT BINDING 203
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Y2, ECO:0000255|HAMAP-
FT Rule:MF_03039"
SQ SEQUENCE 275 AA; 29518 MW; FE0C23BE4691B4CD CRC64;
MEAAAGERAE PGNLAGVRHI ILVLSGKGGV GKSTISTELA LALRHQGKKV GILDVDLCGP
SIPHMLRAQG KAVHQCDNGW VPVFVDQEQS ISLMSVGFLL ENPDEAVVWR GPKKHALIKQ
FVSDVAWGQL DYLVVDTPPG TSDEHMATME ALRPYRPLGA LVVTTPQAVS IGDVRRELTF
CKKTGLQVIG VIENMSGFTC PHCAECTNVF SSGSGEELAR LAGVPFLGSV PLDSQLTRSL
EEGRDFIQEF PKSTAYSALT SIAQRVVHRM SALCS
