ID NUBP2_HUMAN Reviewed; 271 AA.
AC Q9Y5Y2; D3DU80; Q9NWB2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 189.
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 {ECO:0000255|HAMAP-Rule:MF_03039};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Teratocarcinoma;
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 TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Ovary;
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 [5]
RP INTERACTION WITH NUBP1.
RX PubMed=18573874; DOI=10.1128/mcb.00545-08;
RA Stehling O., Netz D.J.A., Niggemeyer B., Roesser R., Eisenstein R.S.,
RA Puccio H., Pierik A.J., Lill R.;
RT "Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly
RT and iron homeostasis.";
RL Mol. Cell. Biol. 28:5517-5528(2008).
RN [6]
RP PROTEIN SEQUENCE OF 1-14; 29-40; 45-60; 75-83 AND 209-261, ACETYLATION AT
RP MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=29848660; DOI=10.1242/jcs.211433;
RA Ben-Shimon L., Paul V.D., David-Kadoch G., Volpe M., Stuempfig M., Bill E.,
RA Muehlenhoff U., Lill R., Ben-Aroya S.;
RT "Fe-S cluster coordination of the chromokinesin KIF4A alters its
RT subcellular localization during mitosis.";
RL J. Cell Sci. 131:0-0(2018).
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. {ECO:0000250|UniProtKB:Q9R061, ECO:0000255|HAMAP-
CC Rule:MF_03039}.
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 (By similarity). Interacts with NUBP1
CC (PubMed:18573874). {ECO:0000250|UniProtKB:Q9R061, ECO:0000255|HAMAP-
CC Rule:MF_03039, ECO:0000269|PubMed:18573874}.
CC -!- INTERACTION:
CC Q9Y5Y2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1048886, EBI-3867333;
CC Q9Y5Y2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1048886, EBI-6509505;
CC Q9Y5Y2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1048886, EBI-11959885;
CC Q9Y5Y2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-1048886, EBI-10172290;
CC Q9Y5Y2; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-1048886, EBI-11958364;
CC Q9Y5Y2; Q99750: MDFI; NbExp=3; IntAct=EBI-1048886, EBI-724076;
CC Q9Y5Y2; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-1048886, EBI-945833;
CC Q9Y5Y2; Q8TB37: NUBPL; NbExp=6; IntAct=EBI-1048886, EBI-12852610;
CC Q9Y5Y2; P22735: TGM1; NbExp=3; IntAct=EBI-1048886, EBI-2562368;
CC Q9Y5Y2; Q63HR2: TNS2; NbExp=3; IntAct=EBI-1048886, EBI-949753;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03039}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000255|HAMAP-Rule:MF_03039}. Cytoplasm
CC {ECO:0000269|PubMed:29848660}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q9R061}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q9R061}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000250|UniProtKB:Q9R061}. Note=Enriched at the
CC centrosomes during mitosis. Enriched in centrioles of microtubule
CC asters during prophase, prometaphase and telophase stages of mitosis
CC (By similarity). Localized at centrioles and in the nucleus at
CC interphase (By similarity). Colocalizes with nubp-1 at prometaphase (By
CC similarity). {ECO:0000250|UniProtKB:Q9R061, ECO:0000255|HAMAP-
CC Rule:MF_03039}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in
CC skeletal muscle.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, lung, liver and kidney.
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; AF118394; AAD45242.1; -; mRNA.
DR EMBL; AK001023; BAA91471.1; -; mRNA.
DR EMBL; CH471112; EAW85613.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85617.1; -; Genomic_DNA.
DR EMBL; BC002768; AAH02768.1; -; mRNA.
DR EMBL; BC008005; AAH08005.1; -; mRNA.
DR CCDS; CCDS10445.1; -.
DR RefSeq; NP_001271430.1; NM_001284501.1.
DR RefSeq; NP_036357.1; NM_012225.3.
DR AlphaFoldDB; Q9Y5Y2; -.
DR SMR; Q9Y5Y2; -.
DR BioGRID; 115408; 187.
DR ComplexPortal; CPX-2823; NUBP1-NUBP2 iron-sulfur cluster assembly scaffold complex.
DR IntAct; Q9Y5Y2; 27.
DR MINT; Q9Y5Y2; -.
DR STRING; 9606.ENSP00000262302; -.
DR GlyCosmos; Q9Y5Y2; 2 sites, 1 glycan.
DR GlyGen; Q9Y5Y2; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9Y5Y2; -.
DR PhosphoSitePlus; Q9Y5Y2; -.
DR BioMuta; NUBP2; -.
DR DMDM; 13632176; -.
DR EPD; Q9Y5Y2; -.
DR jPOST; Q9Y5Y2; -.
DR MassIVE; Q9Y5Y2; -.
DR MaxQB; Q9Y5Y2; -.
DR PaxDb; 9606-ENSP00000262302; -.
DR PeptideAtlas; Q9Y5Y2; -.
DR ProteomicsDB; 86538; -.
DR Pumba; Q9Y5Y2; -.
DR Antibodypedia; 23260; 100 antibodies from 19 providers.
DR DNASU; 10101; -.
DR Ensembl; ENST00000262302.14; ENSP00000262302.9; ENSG00000095906.17.
DR GeneID; 10101; -.
DR KEGG; hsa:10101; -.
DR MANE-Select; ENST00000262302.14; ENSP00000262302.9; NM_012225.4; NP_036357.1.
DR UCSC; uc002cmw.6; human.
DR AGR; HGNC:8042; -.
DR CTD; 10101; -.
DR DisGeNET; 10101; -.
DR GeneCards; NUBP2; -.
DR HGNC; HGNC:8042; NUBP2.
DR HPA; ENSG00000095906; Low tissue specificity.
DR MIM; 610779; gene.
DR neXtProt; NX_Q9Y5Y2; -.
DR OpenTargets; ENSG00000095906; -.
DR PharmGKB; PA31824; -.
DR VEuPathDB; HostDB:ENSG00000095906; -.
DR eggNOG; KOG3022; Eukaryota.
DR GeneTree; ENSGT00950000183193; -.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; Q9Y5Y2; -.
DR OMA; KTMMIKQ; -.
DR OrthoDB; 228512at2759; -.
DR PhylomeDB; Q9Y5Y2; -.
DR TreeFam; TF354321; -.
DR PathwayCommons; Q9Y5Y2; -.
DR Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
DR SignaLink; Q9Y5Y2; -.
DR BioGRID-ORCS; 10101; 601 hits in 1180 CRISPR screens.
DR ChiTaRS; NUBP2; human.
DR GeneWiki; NUBP2; -.
DR GenomeRNAi; 10101; -.
DR Pharos; Q9Y5Y2; Tbio.
DR PRO; PR:Q9Y5Y2; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9Y5Y2; Protein.
DR Bgee; ENSG00000095906; Expressed in thymus and 103 other cell types or tissues.
DR ExpressionAtlas; Q9Y5Y2; baseline and differential.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0031616; C:spindle pole centrosome; IEA:Ensembl.
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:0000166; F:nucleotide binding; TAS:ProtInc.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR CDD; cd02037; Mrp_NBP35; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR HAMAP; MF_03039; NUBP2; 1.
DR InterPro; IPR000808; Mrp-like_CS.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR028600; NUBP2/Cfd1_eukaryotes.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR23264:SF38; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR NUBP2; 1.
DR PANTHER; PTHR23264; NUCLEOTIDE-BINDING PROTEIN NBP35 YEAST -RELATED; 1.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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;
KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..271
FT /note="Cytosolic Fe-S cluster assembly factor NUBP2"
FT /id="PRO_0000184945"
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03039"
FT BINDING 196
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 199
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:0000255|HAMAP-Rule:MF_03039,
FT ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT VARIANT 200
FT /note="T -> A (in dbSNP:rs57822546)"
FT /id="VAR_061353"
FT VARIANT 250
FT /note="P -> S (in dbSNP:rs35030308)"
FT /id="VAR_050099"
FT VARIANT 266
FT /note="T -> M (in dbSNP:rs34028164)"
FT /id="VAR_050100"
FT CONFLICT 242
FT /note="F -> S (in Ref. 2; BAA91471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 28825 MW; 3B1AB82C4FE9C8EE CRC64;
MEAAAEPGNL AGVRHIILVL SGKGGVGKST ISTELALALR HAGKKVGILD VDLCGPSIPR
MLGAQGRAVH QCDRGWAPVF LDREQSISLM SVGFLLEKPD EAVVWRGPKK NALIKQFVSD
VAWGELDYLV VDTPPGTSDE HMATIEALRP YQPLGALVVT TPQAVSVGDV RRELTFCRKT
GLRVMGIVEN MSGFTCPHCT ECTSVFSRGG GEELAQLAGV PFLGSVPLDP ALMRTLEEGH
DFIQEFPGSP AFAALTSIAQ KILDATPACL P
//
