Full text data of NUBP2
NUBP2
[Confidence: low (only semi-automatic identification from reviews)]
Cytosolic Fe-S cluster assembly factor NUBP2 (Nucleotide-binding protein 2; NBP 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cytosolic Fe-S cluster assembly factor NUBP2 (Nucleotide-binding protein 2; NBP 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y5Y2
ID NUBP2_HUMAN Reviewed; 271 AA.
AC Q9Y5Y2; D3DU80; Q9NWB2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP2;
DE AltName: Full=Nucleotide-binding protein 2;
DE Short=NBP 2;
GN Name=NUBP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 17, and Nubp1, mapped to chromosome 16 -- establish a new gene family
RT of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT assembly 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
RP AT MET-1, AND 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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC assembly (CIA) machinery. Required for maturation of
CC extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer
CC forms a Fe-S scaffold complex, mediating the de novo assembly of
CC an Fe-S cluster and its transfer to target apoproteins (By
CC similarity).
CC -!- COFACTOR: Binds 4 4Fe-4S clusters per heterotetramer. Contains two
CC stable clusters in the N-termini of NUBP1 and two labile, bridging
CC clusters between subunits of the NUBP1-NUBP2 heterotetramer (By
CC similarity).
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. Interacts
CC with KIFC1 (By similarity). Interacts with NUBP1.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome (By
CC similarity). Note=Enriched at the centrosomes during mitosis (By
CC similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in
CC skeletal muscle.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, lung, liver and
CC kidney.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP2/CFD1 subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001271430.1; NM_001284501.1.
DR RefSeq; NP_036357.1; NM_012225.3.
DR UniGene; Hs.256549; -.
DR ProteinModelPortal; Q9Y5Y2; -.
DR SMR; Q9Y5Y2; 10-246.
DR STRING; 9606.ENSP00000262302; -.
DR PhosphoSite; Q9Y5Y2; -.
DR DMDM; 13632176; -.
DR PaxDb; Q9Y5Y2; -.
DR PeptideAtlas; Q9Y5Y2; -.
DR PRIDE; Q9Y5Y2; -.
DR Ensembl; ENST00000262302; ENSP00000262302; ENSG00000095906.
DR GeneID; 10101; -.
DR KEGG; hsa:10101; -.
DR UCSC; uc002cmw.4; human.
DR CTD; 10101; -.
DR GeneCards; GC16P001832; -.
DR H-InvDB; HIX0173260; -.
DR HGNC; HGNC:8042; NUBP2.
DR HPA; HPA041704; -.
DR MIM; 610779; gene.
DR neXtProt; NX_Q9Y5Y2; -.
DR PharmGKB; PA31824; -.
DR eggNOG; COG0489; -.
DR HOGENOM; HOG000079916; -.
DR HOVERGEN; HBG051027; -.
DR InParanoid; Q9Y5Y2; -.
DR OMA; HMATVEA; -.
DR OrthoDB; EOG7D59NZ; -.
DR PhylomeDB; Q9Y5Y2; -.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; NUBP2; -.
DR GenomeRNAi; 10101; -.
DR NextBio; 38209; -.
DR PRO; PR:Q9Y5Y2; -.
DR ArrayExpress; Q9Y5Y2; -.
DR Bgee; Q9Y5Y2; -.
DR CleanEx; HS_NUBP2; -.
DR Genevestigator; Q9Y5Y2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; TAS:ProtInc.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR HAMAP; MF_03039; NUBP2; 1; -.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR019591; ATPase-like_ParA/MinD.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028600; NUBP2/Cfd1_eukaryotes.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13614; AAA_31; 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; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 271 Cytosolic Fe-S cluster assembly factor
FT NUBP2.
FT /FTId=PRO_0000184945.
FT NP_BIND 22 29 ATP (Potential).
FT METAL 196 196 Iron-sulfur (4Fe-4S); shared with dimeric
FT partner (By similarity).
FT METAL 199 199 Iron-sulfur (4Fe-4S); shared with dimeric
FT partner (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 200 200 T -> A (in dbSNP:rs57822546).
FT /FTId=VAR_061353.
FT VARIANT 250 250 P -> S (in dbSNP:rs35030308).
FT /FTId=VAR_050099.
FT VARIANT 266 266 T -> M (in dbSNP:rs34028164).
FT /FTId=VAR_050100.
FT CONFLICT 242 242 F -> S (in Ref. 2; BAA91471).
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
//
ID NUBP2_HUMAN Reviewed; 271 AA.
AC Q9Y5Y2; D3DU80; Q9NWB2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP2;
DE AltName: Full=Nucleotide-binding protein 2;
DE Short=NBP 2;
GN Name=NUBP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 17, and Nubp1, mapped to chromosome 16 -- establish a new gene family
RT of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT assembly 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
RP AT MET-1, AND 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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC assembly (CIA) machinery. Required for maturation of
CC extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer
CC forms a Fe-S scaffold complex, mediating the de novo assembly of
CC an Fe-S cluster and its transfer to target apoproteins (By
CC similarity).
CC -!- COFACTOR: Binds 4 4Fe-4S clusters per heterotetramer. Contains two
CC stable clusters in the N-termini of NUBP1 and two labile, bridging
CC clusters between subunits of the NUBP1-NUBP2 heterotetramer (By
CC similarity).
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. Interacts
CC with KIFC1 (By similarity). Interacts with NUBP1.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome (By
CC similarity). Note=Enriched at the centrosomes during mitosis (By
CC similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in
CC skeletal muscle.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, lung, liver and
CC kidney.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP2/CFD1 subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001271430.1; NM_001284501.1.
DR RefSeq; NP_036357.1; NM_012225.3.
DR UniGene; Hs.256549; -.
DR ProteinModelPortal; Q9Y5Y2; -.
DR SMR; Q9Y5Y2; 10-246.
DR STRING; 9606.ENSP00000262302; -.
DR PhosphoSite; Q9Y5Y2; -.
DR DMDM; 13632176; -.
DR PaxDb; Q9Y5Y2; -.
DR PeptideAtlas; Q9Y5Y2; -.
DR PRIDE; Q9Y5Y2; -.
DR Ensembl; ENST00000262302; ENSP00000262302; ENSG00000095906.
DR GeneID; 10101; -.
DR KEGG; hsa:10101; -.
DR UCSC; uc002cmw.4; human.
DR CTD; 10101; -.
DR GeneCards; GC16P001832; -.
DR H-InvDB; HIX0173260; -.
DR HGNC; HGNC:8042; NUBP2.
DR HPA; HPA041704; -.
DR MIM; 610779; gene.
DR neXtProt; NX_Q9Y5Y2; -.
DR PharmGKB; PA31824; -.
DR eggNOG; COG0489; -.
DR HOGENOM; HOG000079916; -.
DR HOVERGEN; HBG051027; -.
DR InParanoid; Q9Y5Y2; -.
DR OMA; HMATVEA; -.
DR OrthoDB; EOG7D59NZ; -.
DR PhylomeDB; Q9Y5Y2; -.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; NUBP2; -.
DR GenomeRNAi; 10101; -.
DR NextBio; 38209; -.
DR PRO; PR:Q9Y5Y2; -.
DR ArrayExpress; Q9Y5Y2; -.
DR Bgee; Q9Y5Y2; -.
DR CleanEx; HS_NUBP2; -.
DR Genevestigator; Q9Y5Y2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; TAS:ProtInc.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR HAMAP; MF_03039; NUBP2; 1; -.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR019591; ATPase-like_ParA/MinD.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028600; NUBP2/Cfd1_eukaryotes.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13614; AAA_31; 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; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 271 Cytosolic Fe-S cluster assembly factor
FT NUBP2.
FT /FTId=PRO_0000184945.
FT NP_BIND 22 29 ATP (Potential).
FT METAL 196 196 Iron-sulfur (4Fe-4S); shared with dimeric
FT partner (By similarity).
FT METAL 199 199 Iron-sulfur (4Fe-4S); shared with dimeric
FT partner (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 200 200 T -> A (in dbSNP:rs57822546).
FT /FTId=VAR_061353.
FT VARIANT 250 250 P -> S (in dbSNP:rs35030308).
FT /FTId=VAR_050099.
FT VARIANT 266 266 T -> M (in dbSNP:rs34028164).
FT /FTId=VAR_050100.
FT CONFLICT 242 242 F -> S (in Ref. 2; BAA91471).
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
//
MIM
610779
*RECORD*
*FIELD* NO
610779
*FIELD* TI
*610779 NUCLEOTIDE-BINDING PROTEIN 2; NUBP2
;;CYTOSOLIC Fe-S CLUSTER DEFICIENT 1, S. CEREVISIAE, HOMOLOG OF; CFD1
read more*FIELD* TX
DESCRIPTION
NUBP2 is a member of the NUBP/MRP gene subfamily of ATP-binding proteins
(see NUBP1; 600280) (Nakashima et al., 1999).
CLONING
Nakashima et al. (1999) cloned mouse Nubp2 and used the murine sequence
as a probe in EST database analysis, followed by screening a human
teratoma cDNA library to clone full-length human NUBP2. The 271-amino
acid human NUBP2 protein shares 72.6% amino acid similarity with mouse
Nubp2. Northern blot analysis detected a 1.4-kb NUBP2 transcript with
ubiquitous expression in all human adult and fetal tissues tested, with
highest expression in adult skeletal muscle. NUBP2 contains conserved an
ATP/GTP binding motif A (P-loop), an ATP/GTP binding motif A-prime, and
NUBP/MRP alpha and beta motifs. NUBP2 lacks an additional N-terminal
sequence with 4 cysteine residues that is present in NUBP1.
GENE FUNCTION
Roy et al. (2003) showed that yeast Cfd1 was required for cytosolic Fe-S
cluster biogenesis and conversion of mammalian IRP1 (ACO1; 100880) to
cytosolic aconitase in yeast.
Stehling et al. (2008) found that NBP35 (NUBP1) interacted with
coexpressed CFD1 in transfected HeLa cells, suggesting that, like NBP35,
CFD1 may function in the regulation of cellular iron homeostasis and
cytosolic Fe-S protein assembly.
MAPPING
Hartz (2012) mapped the NUBP2 gene to chromosome 16p13.3 based on an
alignment of the NUBP2 sequence (GenBank GENBANK AF118394) with the
genomic sequence (GRCh37).
Nakashima et al. (1999) mapped the mouse Nubp2 gene to the t-complex
region of chromosome 17, which shows homology of synteny to human
chromosome 16p13.3.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 9/11/2012.
2. Nakashima, H.; Grahovac, M. J.; Mazzarella, R.; Fujiwara, H.; Kitchen,
J. R.; Threat, T. A.; Ko, M. S. H.: Two novel mouse genes--Nubp2,
mapped to the t-complex on chromosome 17, and Nubp1, mapped to the
chromosome 16--establish a new gene family of nucleotide-binding proteins
in eukaryotes. Genomics 60: 152-160, 1999.
3. Roy, A.; Solodovnikova, N.; Nicholson, T.; Antholine, W.; Walden,
W. E.: A novel eukaryotic factor for cytosolic Fe-S cluster assembly. EMBO
J. 22: 4826-4835, 2003.
4. Stehling, O.; Netz, D. J. A.; Niggemeyer, B.; Rosser, R.; Eisenstein,
R. S.; Puccio, H.; Pierik, A. J.; Lill, R.: Human Nbp35 is essential
for both cytosolic iron-sulfur protein assembly and iron homeostasis. Molec.
Cell. Biol. 28: 5517-5528, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 09/17/2012
*FIELD* CD
Dorothy S. Reilly: 2/20/2007
*FIELD* ED
mgross: 09/17/2012
carol: 10/21/2011
wwang: 2/21/2007
*RECORD*
*FIELD* NO
610779
*FIELD* TI
*610779 NUCLEOTIDE-BINDING PROTEIN 2; NUBP2
;;CYTOSOLIC Fe-S CLUSTER DEFICIENT 1, S. CEREVISIAE, HOMOLOG OF; CFD1
read more*FIELD* TX
DESCRIPTION
NUBP2 is a member of the NUBP/MRP gene subfamily of ATP-binding proteins
(see NUBP1; 600280) (Nakashima et al., 1999).
CLONING
Nakashima et al. (1999) cloned mouse Nubp2 and used the murine sequence
as a probe in EST database analysis, followed by screening a human
teratoma cDNA library to clone full-length human NUBP2. The 271-amino
acid human NUBP2 protein shares 72.6% amino acid similarity with mouse
Nubp2. Northern blot analysis detected a 1.4-kb NUBP2 transcript with
ubiquitous expression in all human adult and fetal tissues tested, with
highest expression in adult skeletal muscle. NUBP2 contains conserved an
ATP/GTP binding motif A (P-loop), an ATP/GTP binding motif A-prime, and
NUBP/MRP alpha and beta motifs. NUBP2 lacks an additional N-terminal
sequence with 4 cysteine residues that is present in NUBP1.
GENE FUNCTION
Roy et al. (2003) showed that yeast Cfd1 was required for cytosolic Fe-S
cluster biogenesis and conversion of mammalian IRP1 (ACO1; 100880) to
cytosolic aconitase in yeast.
Stehling et al. (2008) found that NBP35 (NUBP1) interacted with
coexpressed CFD1 in transfected HeLa cells, suggesting that, like NBP35,
CFD1 may function in the regulation of cellular iron homeostasis and
cytosolic Fe-S protein assembly.
MAPPING
Hartz (2012) mapped the NUBP2 gene to chromosome 16p13.3 based on an
alignment of the NUBP2 sequence (GenBank GENBANK AF118394) with the
genomic sequence (GRCh37).
Nakashima et al. (1999) mapped the mouse Nubp2 gene to the t-complex
region of chromosome 17, which shows homology of synteny to human
chromosome 16p13.3.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 9/11/2012.
2. Nakashima, H.; Grahovac, M. J.; Mazzarella, R.; Fujiwara, H.; Kitchen,
J. R.; Threat, T. A.; Ko, M. S. H.: Two novel mouse genes--Nubp2,
mapped to the t-complex on chromosome 17, and Nubp1, mapped to the
chromosome 16--establish a new gene family of nucleotide-binding proteins
in eukaryotes. Genomics 60: 152-160, 1999.
3. Roy, A.; Solodovnikova, N.; Nicholson, T.; Antholine, W.; Walden,
W. E.: A novel eukaryotic factor for cytosolic Fe-S cluster assembly. EMBO
J. 22: 4826-4835, 2003.
4. Stehling, O.; Netz, D. J. A.; Niggemeyer, B.; Rosser, R.; Eisenstein,
R. S.; Puccio, H.; Pierik, A. J.; Lill, R.: Human Nbp35 is essential
for both cytosolic iron-sulfur protein assembly and iron homeostasis. Molec.
Cell. Biol. 28: 5517-5528, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 09/17/2012
*FIELD* CD
Dorothy S. Reilly: 2/20/2007
*FIELD* ED
mgross: 09/17/2012
carol: 10/21/2011
wwang: 2/21/2007