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Protein

Cytosolic Fe-S cluster assembly factor NUBP2

Gene

NUBP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure.UniRule annotationBy similarity

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NUBP1 and two labile, bridging clusters between subunits of the NUBP1-NUBP2 heterotetramer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi196 – 1961Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation
Metal bindingi199 – 1991Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 298ATPUniRule annotation

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • nucleotide binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-2564830. Cytosolic iron-sulfur cluster assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic Fe-S cluster assembly factor NUBP2UniRule annotation
Alternative name(s):
Nucleotide-binding protein 2UniRule annotation
Short name:
NBP 2UniRule annotation
Gene namesi
Name:NUBP2UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:8042. NUBP2.

Subcellular locationi

  • Nucleus UniRule annotation
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome UniRule annotation
  • Cytoplasm By similarity
  • Cytoplasmcytoskeletoncilium axoneme By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing center By similarity

  • Note: Enriched at the centrosomes during mitosis. Enriched in centrioles of microtubule asters during prophase, prometaphase and telophase stages of mitosis (By similarity). Localized at centrioles and in the nucleus at interphase (By similarity). Colocalizes with nubp-1 at prometaphase (By similarity).UniRule annotationBy similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31824.

Polymorphism and mutation databases

DMDMi13632176.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Cytosolic Fe-S cluster assembly factor NUBP2PRO_0000184945Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineUniRule annotationCombined sources1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9Y5Y2.
MaxQBiQ9Y5Y2.
PaxDbiQ9Y5Y2.
PeptideAtlasiQ9Y5Y2.
PRIDEiQ9Y5Y2.

PTM databases

iPTMnetiQ9Y5Y2.
PhosphoSiteiQ9Y5Y2.

Expressioni

Tissue specificityi

Widely expressed with highest expression in skeletal muscle.

Developmental stagei

Expressed in fetal brain, lung, liver and kidney.

Gene expression databases

BgeeiQ9Y5Y2.
CleanExiHS_NUBP2.
ExpressionAtlasiQ9Y5Y2. baseline and differential.

Organism-specific databases

HPAiHPA041704.

Interactioni

Subunit structurei

Heterotetramer of 2 NUBP1 and 2 NUBP2 chains (By similarity). Interacts with KIFC1 (By similarity). Interacts with NUBP1 (PubMed:18573874).UniRule annotationBy similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KRTAP10-7P604093EBI-1048886,EBI-10172290
NOTCH2NLQ7Z3S93EBI-1048886,EBI-945833
TNS2Q63HR23EBI-1048886,EBI-949753

Protein-protein interaction databases

BioGridi115408. 53 interactions.
IntActiQ9Y5Y2. 4 interactions.
STRINGi9606.ENSP00000262302.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5Y2.
SMRiQ9Y5Y2. Positions 10-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG410KCSJ. Eukaryota.
COG0489. LUCA.
GeneTreeiENSGT00550000075057.
HOGENOMiHOG000079916.
HOVERGENiHBG051027.
InParanoidiQ9Y5Y2.
OMAiQEFPRSP.
OrthoDBiEOG7D59NZ.
PhylomeDBiQ9Y5Y2.
TreeFamiTF354321.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_02040. Mrp_NBP35.
MF_03039. NUBP2.
InterProiIPR019591. Mrp/NBP35_ATP-bd.
IPR000808. Mrp_CS.
IPR028600. NUBP2/Cfd1_eukaryotes.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23264. PTHR23264. 1 hit.
PfamiPF10609. ParA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS01215. MRP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y5Y2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAAAEPGNL AGVRHIILVL SGKGGVGKST ISTELALALR HAGKKVGILD
60 70 80 90 100
VDLCGPSIPR MLGAQGRAVH QCDRGWAPVF LDREQSISLM SVGFLLEKPD
110 120 130 140 150
EAVVWRGPKK NALIKQFVSD VAWGELDYLV VDTPPGTSDE HMATIEALRP
160 170 180 190 200
YQPLGALVVT TPQAVSVGDV RRELTFCRKT GLRVMGIVEN MSGFTCPHCT
210 220 230 240 250
ECTSVFSRGG GEELAQLAGV PFLGSVPLDP ALMRTLEEGH DFIQEFPGSP
260 270
AFAALTSIAQ KILDATPACL P
Length:271
Mass (Da):28,825
Last modified:November 1, 1999 - v1
Checksum:i3B1AB82C4FE9C8EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421F → S in BAA91471 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti200 – 2001T → A.
Corresponds to variant rs57822546 [ dbSNP | Ensembl ].
VAR_061353
Natural varianti250 – 2501P → S.
Corresponds to variant rs35030308 [ dbSNP | Ensembl ].
VAR_050099
Natural varianti266 – 2661T → M.
Corresponds to variant rs34028164 [ dbSNP | Ensembl ].
VAR_050100

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF118394 mRNA. Translation: AAD45242.1.
AK001023 mRNA. Translation: BAA91471.1.
CH471112 Genomic DNA. Translation: EAW85613.1.
CH471112 Genomic DNA. Translation: EAW85617.1.
BC002768 mRNA. Translation: AAH02768.1.
BC008005 mRNA. Translation: AAH08005.1.
CCDSiCCDS10445.1.
RefSeqiNP_001271430.1. NM_001284501.1.
NP_036357.1. NM_012225.3.
UniGeneiHs.256549.

Genome annotation databases

EnsembliENST00000262302; ENSP00000262302; ENSG00000095906.
GeneIDi10101.
KEGGihsa:10101.
UCSCiuc002cmw.6. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF118394 mRNA. Translation: AAD45242.1.
AK001023 mRNA. Translation: BAA91471.1.
CH471112 Genomic DNA. Translation: EAW85613.1.
CH471112 Genomic DNA. Translation: EAW85617.1.
BC002768 mRNA. Translation: AAH02768.1.
BC008005 mRNA. Translation: AAH08005.1.
CCDSiCCDS10445.1.
RefSeqiNP_001271430.1. NM_001284501.1.
NP_036357.1. NM_012225.3.
UniGeneiHs.256549.

3D structure databases

ProteinModelPortaliQ9Y5Y2.
SMRiQ9Y5Y2. Positions 10-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115408. 53 interactions.
IntActiQ9Y5Y2. 4 interactions.
STRINGi9606.ENSP00000262302.

PTM databases

iPTMnetiQ9Y5Y2.
PhosphoSiteiQ9Y5Y2.

Polymorphism and mutation databases

DMDMi13632176.

Proteomic databases

EPDiQ9Y5Y2.
MaxQBiQ9Y5Y2.
PaxDbiQ9Y5Y2.
PeptideAtlasiQ9Y5Y2.
PRIDEiQ9Y5Y2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262302; ENSP00000262302; ENSG00000095906.
GeneIDi10101.
KEGGihsa:10101.
UCSCiuc002cmw.6. human.

Organism-specific databases

CTDi10101.
GeneCardsiNUBP2.
H-InvDBHIX0173260.
HGNCiHGNC:8042. NUBP2.
HPAiHPA041704.
MIMi610779. gene.
neXtProtiNX_Q9Y5Y2.
PharmGKBiPA31824.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410KCSJ. Eukaryota.
COG0489. LUCA.
GeneTreeiENSGT00550000075057.
HOGENOMiHOG000079916.
HOVERGENiHBG051027.
InParanoidiQ9Y5Y2.
OMAiQEFPRSP.
OrthoDBiEOG7D59NZ.
PhylomeDBiQ9Y5Y2.
TreeFamiTF354321.

Enzyme and pathway databases

ReactomeiR-HSA-2564830. Cytosolic iron-sulfur cluster assembly.

Miscellaneous databases

GeneWikiiNUBP2.
GenomeRNAii10101.
PROiQ9Y5Y2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5Y2.
CleanExiHS_NUBP2.
ExpressionAtlasiQ9Y5Y2. baseline and differential.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_02040. Mrp_NBP35.
MF_03039. NUBP2.
InterProiIPR019591. Mrp/NBP35_ATP-bd.
IPR000808. Mrp_CS.
IPR028600. NUBP2/Cfd1_eukaryotes.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23264. PTHR23264. 1 hit.
PfamiPF10609. ParA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS01215. MRP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two novel mouse genes -- Nubp2, mapped to the T-complex on chromosome 17, and Nubp1, mapped to chromosome 16 -- establish a new gene family of nucleotide-binding proteins in eukaryotes."
    Nakashima H., Grahovac M.J., Mazzarella R., Fujiwara H., Kitchen J.R., Threat T.A., Ko M.S.H.
    Genomics 60:152-160(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Teratocarcinoma.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Ovary.
  5. "Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis."
    Stehling O., Netz D.J.A., Niggemeyer B., Roesser R., Eisenstein R.S., Puccio H., Pierik A.J., Lill R.
    Mol. Cell. Biol. 28:5517-5528(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUBP1.
  6. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-14; 29-40; 45-60; 75-83 AND 209-261, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNUBP2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5Y2
Secondary accession number(s): D3DU80, Q9NWB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.