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P53384

- NUBP1_HUMAN

UniProt

P53384 - NUBP1_HUMAN

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Protein

Cytosolic Fe-S cluster assembly factor NUBP1

Gene

NUBP1

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

Functioni

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.By similarity1 Publication

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 bindingi8 – 81Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi22 – 221Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi25 – 251Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi31 – 311Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi235 – 2351Iron-sulfur 2 (4Fe-4S); shared with dimeric partnerUniRule annotation
Metal bindingi238 – 2381Iron-sulfur 2 (4Fe-4S); shared with dimeric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi62 – 698ATPUniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-KW
  3. iron-sulfur cluster binding Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. nucleotide binding Source: ProtInc

GO - Biological processi

  1. cell growth Source: UniProtKB
  2. cellular iron ion homeostasis Source: UniProtKB
  3. centrosome localization Source: Ensembl
  4. iron-sulfur cluster assembly Source: UniProtKB
  5. negative regulation of centrosome duplication Source: Ensembl
  6. protein localization to cell cortex Source: Ensembl
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_160176. Cytosolic iron-sulfur cluster assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic Fe-S cluster assembly factor NUBP1UniRule annotation
Alternative name(s):
Nucleotide-binding protein 1UniRule annotation
Short name:
NBP 1UniRule annotation
Gene namesi
Name:NUBP1UniRule annotation
Synonyms:NBP, NBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:8041. NUBP1.

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31823.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320Cytosolic Fe-S cluster assembly factor NUBP1PRO_0000184943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP53384.
PaxDbiP53384.
PRIDEiP53384.

PTM databases

PhosphoSiteiP53384.

Expressioni

Gene expression databases

BgeeiP53384.
CleanExiHS_NUBP1.
ExpressionAtlasiP53384. baseline and differential.
GenevestigatoriP53384.

Organism-specific databases

HPAiHPA041656.
HPA041799.

Interactioni

Subunit structurei

Heterotetramer of 2 NUBP1 and 2 NUBP2 chains. Interacts with KIFC1 (By similarity). Interacts with NUBP2.1 PublicationUniRule annotation

Protein-protein interaction databases

BioGridi110762. 20 interactions.
IntActiP53384. 1 interaction.
MINTiMINT-3019860.
STRINGi9606.ENSP00000283027.

Structurei

3D structure databases

ProteinModelPortaliP53384.
SMRiP53384. Positions 44-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0489.
GeneTreeiENSGT00390000009735.
HOGENOMiHOG000079916.
HOVERGENiHBG051027.
InParanoidiP53384.
OMAiMCREMGV.
PhylomeDBiP53384.
TreeFamiTF300755.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_03038. NUBP1.
InterProiIPR003593. AAA+_ATPase.
IPR025723. Anion-transp_ATPase-like_dom.
IPR019591. Mrp/NBP35_ATP-bd.
IPR000808. Mrp_CS.
IPR028601. NUBP1/Nbp35.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23264. PTHR23264. 1 hit.
PfamiPF02374. ArsA_ATPase. 1 hit.
PF10609. ParA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS01215. MRP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P53384-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MEEVPHDCPG ADSAQAGRGA SCQGCPNQRL CASGAGATPD TAIEEIKEKM
60 70 80 90 100
KTVKHKILVL SGKGGVGKST FSAHLAHGLA EDENTQIALL DIDICGPSIP
110 120 130 140 150
KIMGLEGEQV HQSGSGWSPV YVEDNLGVMS VGFLLSSPDD AVIWRGPKKN
160 170 180 190 200
GMIKQFLRDV DWGEVDYLIV DTPPGTSDEH LSVVRYLATA HIDGAVIITT
210 220 230 240 250
PQEVSLQDVR KEINFCRKVK LPIIGVVENM SGFICPKCKK ESQIFPPTTG
260 270 280 290 300
GAELMCQDLE VPLLGRVPLD PLIGKNCDKG QSFFIDAPDS PATLAYRSII
310 320
QRIQEFCNLH QSKEENLISS
Length:320
Mass (Da):34,534
Last modified:September 1, 2009 - v2
Checksum:i346E1C694224E437
GO
Isoform 2 (identifier: P53384-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     110-120: Missing.

Note: No experimental confirmation available.

Show »
Length:309
Mass (Da):33,412
Checksum:i1A2201FF81478FFE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041V → L in AAA61932. (PubMed:7926816)Curated
Sequence conflicti232 – 2321G → P in AAA61932. (PubMed:7926816)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391P → A.2 Publications
Corresponds to variant rs2233531 [ dbSNP | Ensembl ].
VAR_020359

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei110 – 12011Missing in isoform 2. 1 PublicationVSP_029043Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10543.1. [P53384-1]
CCDS61839.1. [P53384-2]
PIRiJC4010.
RefSeqiNP_001265435.1. NM_001278506.1. [P53384-2]
NP_002475.2. NM_002484.3. [P53384-1]
UniGeneiHs.81469.

Genome annotation databases

EnsembliENST00000283027; ENSP00000283027; ENSG00000103274. [P53384-1]
ENST00000433392; ENSP00000409654; ENSG00000103274. [P53384-2]
GeneIDi4682.
KEGGihsa:4682.
UCSCiuc002daa.1. human. [P53384-1]
uc002dab.1. human. [P53384-2]

Polymorphism databases

DMDMi257050984.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS10543.1. [P53384-1 ]
CCDS61839.1. [P53384-2 ]
PIRi JC4010.
RefSeqi NP_001265435.1. NM_001278506.1. [P53384-2 ]
NP_002475.2. NM_002484.3. [P53384-1 ]
UniGenei Hs.81469.

3D structure databases

ProteinModelPortali P53384.
SMRi P53384. Positions 44-309.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110762. 20 interactions.
IntActi P53384. 1 interaction.
MINTi MINT-3019860.
STRINGi 9606.ENSP00000283027.

PTM databases

PhosphoSitei P53384.

Polymorphism databases

DMDMi 257050984.

Proteomic databases

MaxQBi P53384.
PaxDbi P53384.
PRIDEi P53384.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000283027 ; ENSP00000283027 ; ENSG00000103274 . [P53384-1 ]
ENST00000433392 ; ENSP00000409654 ; ENSG00000103274 . [P53384-2 ]
GeneIDi 4682.
KEGGi hsa:4682.
UCSCi uc002daa.1. human. [P53384-1 ]
uc002dab.1. human. [P53384-2 ]

Organism-specific databases

CTDi 4682.
GeneCardsi GC16P010837.
H-InvDB HIX0038641.
HGNCi HGNC:8041. NUBP1.
HPAi HPA041656.
HPA041799.
MIMi 600280. gene.
neXtProti NX_P53384.
PharmGKBi PA31823.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0489.
GeneTreei ENSGT00390000009735.
HOGENOMi HOG000079916.
HOVERGENi HBG051027.
InParanoidi P53384.
OMAi MCREMGV.
PhylomeDBi P53384.
TreeFami TF300755.

Enzyme and pathway databases

Reactomei REACT_160176. Cytosolic iron-sulfur cluster assembly.

Miscellaneous databases

GenomeRNAii 4682.
NextBioi 18050.
PROi P53384.
SOURCEi Search...

Gene expression databases

Bgeei P53384.
CleanExi HS_NUBP1.
ExpressionAtlasi P53384. baseline and differential.
Genevestigatori P53384.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_03038. NUBP1.
InterProi IPR003593. AAA+_ATPase.
IPR025723. Anion-transp_ATPase-like_dom.
IPR019591. Mrp/NBP35_ATP-bd.
IPR000808. Mrp_CS.
IPR028601. NUBP1/Nbp35.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR23264. PTHR23264. 1 hit.
Pfami PF02374. ArsA_ATPase. 1 hit.
PF10609. ParA. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS01215. MRP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNUBP1_HUMAN
AccessioniPrimary (citable) accession number: P53384
Secondary accession number(s): Q32M30, Q498A9, Q53FS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 1, 2009
Last modified: November 26, 2014
This is version 121 of the entry and version 2 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, 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

External Data

Dasty 3