NUBP1_HUMAN
ID NUBP1_HUMAN Reviewed; 320 AA.
AC P53384; Q32M30; Q498A9; Q53FS7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 173.
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 {ECO:0000255|HAMAP-Rule:MF_03038}; Synonyms=NBP, NBP1;
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] (ISOFORM 1).
RX PubMed=7926816; DOI=10.1016/0378-1119(94)90082-5;
RA Shahrestanifar M., Saha D.P., Scala L.A., Basu A., Howells R.D.;
RT "Cloning of a human cDNA encoding a putative nucleotide-binding protein
RT related to Escherichia coli MinD.";
RL Gene 147:281-285(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-39.
RC TISSUE=Spleen;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-39.
RC TISSUE=Eye;
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, INTERACTION WITH NUBP2, SUBCELLULAR LOCATION, AND EPR
RP SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 (PubMed:18573874). Required for maturation of
CC extramitochondrial Fe-S proteins (PubMed:18573874). The NUBP1-NUBP2
CC heterotetramer forms a Fe-S scaffold complex, mediating the de novo
CC assembly of an Fe-S cluster and its transfer to target apoproteins
CC (PubMed:18573874). Implicated in the regulation of centrosome
CC duplication (By similarity). Negatively regulates cilium formation and
CC structure (By similarity). {ECO:0000250|UniProtKB:Q9R060,
CC ECO:0000269|PubMed:18573874}.
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 (By similarity).
CC Interacts with KIFC1 (By similarity). Interacts with NUBP2
CC (PubMed:18573874). Interacts with the BBS/CCT complex subunit CCT1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9R060, ECO:0000255|HAMAP-
CC Rule:MF_03038, ECO:0000269|PubMed:18573874}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038,
CC ECO:0000269|PubMed:18573874, ECO:0000269|PubMed:29848660}. Nucleus
CC {ECO:0000250|UniProtKB:Q9R060}. Cell projection
CC {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton,
CC microtubule organizing center {ECO:0000250|UniProtKB:Q9R060}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Note=Enriched in centrioles
CC of microtubule asters during prophase, prometaphase and telophase
CC stages of mitosis. Localized at centrioles and in the nucleus at
CC interphase. Colocalizes with nubp-2 at prometaphase. Specifically
CC localizes to the axenome of motile cilia as opposed to primary non-
CC motile cilia. Localization is independent of NUBP2 and KIFC1.
CC {ECO:0000250|UniProtKB:Q9R060}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P53384-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53384-2; Sequence=VSP_029043;
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; U01833; AAA61932.1; -; mRNA.
DR EMBL; AK223204; BAD96924.1; -; mRNA.
DR EMBL; BC100290; AAI00291.1; -; mRNA.
DR EMBL; BC109322; AAI09323.1; -; mRNA.
DR EMBL; BC109323; AAI09324.1; -; mRNA.
DR CCDS; CCDS10543.1; -. [P53384-1]
DR CCDS; CCDS61839.1; -. [P53384-2]
DR PIR; JC4010; JC4010.
DR RefSeq; NP_001265435.1; NM_001278506.1. [P53384-2]
DR RefSeq; NP_002475.2; NM_002484.3. [P53384-1]
DR AlphaFoldDB; P53384; -.
DR SMR; P53384; -.
DR BioGRID; 110762; 85.
DR IntAct; P53384; 3.
DR MINT; P53384; -.
DR STRING; 9606.ENSP00000283027; -.
DR GlyGen; P53384; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P53384; -.
DR PhosphoSitePlus; P53384; -.
DR BioMuta; NUBP1; -.
DR DMDM; 257050984; -.
DR EPD; P53384; -.
DR jPOST; P53384; -.
DR MassIVE; P53384; -.
DR MaxQB; P53384; -.
DR PaxDb; P53384; -.
DR PeptideAtlas; P53384; -.
DR PRIDE; P53384; -.
DR ProteomicsDB; 56579; -. [P53384-1]
DR ProteomicsDB; 56580; -. [P53384-2]
DR Antibodypedia; 24622; 145 antibodies from 20 providers.
DR DNASU; 4682; -.
DR Ensembl; ENST00000283027.10; ENSP00000283027.5; ENSG00000103274.11. [P53384-1]
DR Ensembl; ENST00000433392.6; ENSP00000409654.2; ENSG00000103274.11. [P53384-2]
DR GeneID; 4682; -.
DR KEGG; hsa:4682; -.
DR MANE-Select; ENST00000283027.10; ENSP00000283027.5; NM_002484.4; NP_002475.2.
DR UCSC; uc002daa.3; human. [P53384-1]
DR CTD; 4682; -.
DR DisGeNET; 4682; -.
DR GeneCards; NUBP1; -.
DR HGNC; HGNC:8041; NUBP1.
DR HPA; ENSG00000103274; Low tissue specificity.
DR MIM; 600280; gene.
DR neXtProt; NX_P53384; -.
DR OpenTargets; ENSG00000103274; -.
DR PharmGKB; PA31823; -.
DR VEuPathDB; HostDB:ENSG00000103274; -.
DR eggNOG; KOG3022; Eukaryota.
DR GeneTree; ENSGT00950000183193; -.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; P53384; -.
DR OMA; QHITFKD; -.
DR OrthoDB; 1166096at2759; -.
DR PhylomeDB; P53384; -.
DR TreeFam; TF300755; -.
DR PathwayCommons; P53384; -.
DR Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
DR SignaLink; P53384; -.
DR BioGRID-ORCS; 4682; 745 hits in 1093 CRISPR screens.
DR ChiTaRS; NUBP1; human.
DR GenomeRNAi; 4682; -.
DR Pharos; P53384; Tbio.
DR PRO; PR:P53384; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P53384; protein.
DR Bgee; ENSG00000103274; Expressed in monocyte and 178 other tissues.
DR ExpressionAtlas; P53384; baseline and differential.
DR Genevisible; P53384; HS.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IDA:UniProtKB.
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:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0051642; P:centrosome localization; IEA:Ensembl.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IEA:Ensembl.
DR GO; GO:0072697; P:protein localization to cell cortex; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
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; Alternative splicing; ATP-binding; Cell projection;
KW Cilium; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Iron;
KW Iron-sulfur; 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_0000184943"
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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5I0L4"
FT VAR_SEQ 110..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029043"
FT VARIANT 39
FT /note="P -> A (in dbSNP:rs2233531)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_020359"
FT CONFLICT 204
FT /note="V -> L (in Ref. 1; AAA61932)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="G -> P (in Ref. 1; AAA61932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 34534 MW; 346E1C694224E437 CRC64;
MEEVPHDCPG ADSAQAGRGA SCQGCPNQRL CASGAGATPD TAIEEIKEKM KTVKHKILVL
SGKGGVGKST FSAHLAHGLA EDENTQIALL DIDICGPSIP KIMGLEGEQV HQSGSGWSPV
YVEDNLGVMS VGFLLSSPDD AVIWRGPKKN GMIKQFLRDV DWGEVDYLIV DTPPGTSDEH
LSVVRYLATA HIDGAVIITT PQEVSLQDVR KEINFCRKVK LPIIGVVENM SGFICPKCKK
ESQIFPPTTG GAELMCQDLE VPLLGRVPLD PLIGKNCDKG QSFFIDAPDS PATLAYRSII
QRIQEFCNLH QSKEENLISS
