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P53384 (NUBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosolic Fe-S cluster assembly factor NUBP1
Alternative name(s):
Nucleotide-binding protein 1
Short name=NBP 1
Gene names
Name:NUBP1
Synonyms:NBP, NBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Implicated in the regulation of centrosome duplication By similarity. 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. Ref.4

Cofactor

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 By similarity.

Subunit structure

Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. Interacts with KIFC1 By similarity. Interacts with NUBP2. Ref.4

Subcellular location

Cytoplasm Ref.4.

Sequence similarities

Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   Ligand4Fe-4S
ATP-binding
Iron
Iron-sulfur
Metal-binding
Nucleotide-binding
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell growth

Inferred from mutant phenotype Ref.4. Source: UniProtKB

cellular iron ion homeostasis

Inferred from mutant phenotype Ref.4. Source: UniProtKB

centrosome localization

Inferred from electronic annotation. Source: Ensembl

iron-sulfur cluster assembly

Inferred from mutant phenotype Ref.4. Source: UniProtKB

negative regulation of centrosome duplication

Inferred from electronic annotation. Source: Ensembl

protein localization to cell cortex

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.4. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

iron-sulfur cluster binding

Inferred from direct assay Ref.4. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

nucleotide binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P53384-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P53384-2)

The sequence of this isoform differs from the canonical sequence as follows:
     110-120: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320Cytosolic Fe-S cluster assembly factor NUBP1 HAMAP-Rule MF_03038
PRO_0000184943

Regions

Nucleotide binding62 – 698ATP Potential

Sites

Metal binding81Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding221Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding251Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding311Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding2351Iron-sulfur 2 (4Fe-4S); shared with dimeric partner By similarity
Metal binding2381Iron-sulfur 2 (4Fe-4S); shared with dimeric partner By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5 Ref.7 Ref.8

Natural variations

Alternative sequence110 – 12011Missing in isoform 2.
VSP_029043
Natural variant391P → A. Ref.2 Ref.3
Corresponds to variant rs2233531 [ dbSNP | Ensembl ].
VAR_020359

Experimental info

Sequence conflict2041V → L in AAA61932. Ref.1
Sequence conflict2321G → P in AAA61932. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: 346E1C694224E437

FASTA32034,534
        10         20         30         40         50         60 
MEEVPHDCPG ADSAQAGRGA SCQGCPNQRL CASGAGATPD TAIEEIKEKM KTVKHKILVL 

        70         80         90        100        110        120 
SGKGGVGKST FSAHLAHGLA EDENTQIALL DIDICGPSIP KIMGLEGEQV HQSGSGWSPV 

       130        140        150        160        170        180 
YVEDNLGVMS VGFLLSSPDD AVIWRGPKKN GMIKQFLRDV DWGEVDYLIV DTPPGTSDEH 

       190        200        210        220        230        240 
LSVVRYLATA HIDGAVIITT PQEVSLQDVR KEINFCRKVK LPIIGVVENM SGFICPKCKK 

       250        260        270        280        290        300 
ESQIFPPTTG GAELMCQDLE VPLLGRVPLD PLIGKNCDKG QSFFIDAPDS PATLAYRSII 

       310        320 
QRIQEFCNLH QSKEENLISS 

« Hide

Isoform 2 [UniParc].

Checksum: 1A2201FF81478FFE
Show »

FASTA30933,412

References

« Hide 'large scale' references
[1]"Cloning of a human cDNA encoding a putative nucleotide-binding protein related to Escherichia coli MinD."
Shahrestanifar M., Saha D.P., Scala L.A., Basu A., Howells R.D.
Gene 147:281-285(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-39.
Tissue: Spleen.
[3]"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] (ISOFORMS 1 AND 2), VARIANT ALA-39.
Tissue: Eye.
[4]"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: FUNCTION, INTERACTION WITH NUBP2, SUBCELLULAR LOCATION, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
[5]"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].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01833 mRNA. Translation: AAA61932.1.
AK223204 mRNA. Translation: BAD96924.1.
BC100290 mRNA. Translation: AAI00291.1.
BC109322 mRNA. Translation: AAI09323.1.
BC109323 mRNA. Translation: AAI09324.1.
PIRJC4010.
RefSeqNP_001265435.1. NM_001278506.1.
NP_002475.2. NM_002484.3.
UniGeneHs.81469.

3D structure databases

ProteinModelPortalP53384.
SMRP53384. Positions 44-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110762. 19 interactions.
IntActP53384. 1 interaction.
MINTMINT-3019860.
STRING9606.ENSP00000283027.

PTM databases

PhosphoSiteP53384.

Polymorphism databases

DMDM257050984.

Proteomic databases

PaxDbP53384.
PRIDEP53384.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283027; ENSP00000283027; ENSG00000103274. [P53384-1]
ENST00000433392; ENSP00000409654; ENSG00000103274. [P53384-2]
GeneID4682.
KEGGhsa:4682.
UCSCuc002daa.1. human. [P53384-1]
uc002dab.1. human. [P53384-2]

Organism-specific databases

CTD4682.
GeneCardsGC16P010837.
H-InvDBHIX0038641.
HGNCHGNC:8041. NUBP1.
HPAHPA041656.
HPA041799.
MIM600280. gene.
neXtProtNX_P53384.
PharmGKBPA31823.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0489.
HOGENOMHOG000079916.
HOVERGENHBG051027.
InParanoidP53384.
OMAQDLEVPL.
PhylomeDBP53384.
TreeFamTF300755.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP53384.
BgeeP53384.
CleanExHS_NUBP1.
GenevestigatorP53384.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_03038. NUBP1.
InterProIPR003593. AAA+_ATPase.
IPR025723. Anion-transp_ATPase-like_dom.
IPR019591. ATPase-like_ParA/MinD.
IPR000808. Mrp_CS.
IPR028601. NUBP1/Nbp35.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF02374. ArsA_ATPase. 1 hit.
PF10609. ParA. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS01215. MRP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi4682.
NextBio18050.
PROP53384.
SOURCESearch...

Entry information

Entry nameNUBP1_HUMAN
AccessionPrimary (citable) accession number: P53384
Secondary accession number(s): Q32M30, Q498A9, Q53FS7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM