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Protein

NFU1 iron-sulfur cluster scaffold homolog, mitochondrial

Gene

Nfu1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Iron-sulfur cluster scaffold protein which can assemble [4Fe-2S] clusters and deliver them to target proteins.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
Alternative name(s):
HIRA-interacting protein 5
Short name:
mHIRIP5
Gene namesi
Name:Nfu1
Synonyms:Hirip5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1913290. Nfu1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionSequence analysisAdd
BLAST
Chaini30 – 255226NFU1 iron-sulfur cluster scaffold homolog, mitochondrialPRO_0000166192Add
BLAST

Proteomic databases

EPDiQ9QZ23.
MaxQBiQ9QZ23.
PaxDbiQ9QZ23.
PRIDEiQ9QZ23.

PTM databases

SwissPalmiQ9QZ23.

Expressioni

Gene expression databases

BgeeiQ9QZ23.
ExpressionAtlasiQ9QZ23. baseline and differential.

Interactioni

Subunit structurei

Interacts with HIRA and EPM2A/laforin.By similarity

Protein-protein interaction databases

IntActiQ9QZ23. 1 interaction.
MINTiMINT-1853650.
STRINGi10090.ENSMUSP00000032060.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi168 – 17912Combined sources
Helixi182 – 1887Combined sources
Beta strandi194 – 1985Combined sources
Beta strandi201 – 2044Combined sources
Helixi214 – 2196Combined sources
Helixi221 – 23111Combined sources
Beta strandi238 – 2403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VEHNMR-A163-241[»]
ProteinModelPortaliQ9QZ23.
SMRiQ9QZ23. Positions 57-153, 169-241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QZ23.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 24169NifUAdd
BLAST

Sequence similaritiesi

Belongs to the NifU family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2358. Eukaryota.
COG0694. LUCA.
GeneTreeiENSGT00390000011296.
HOGENOMiHOG000023557.
HOVERGENiHBG054438.
InParanoidiQ9QZ23.
OrthoDBiEOG7SXW47.
PhylomeDBiQ9QZ23.
TreeFamiTF315076.

Family and domain databases

Gene3Di3.30.1370.70. 1 hit.
InterProiIPR014824. Nfu/NifU_N.
IPR017065. NFU1.
IPR001075. NIF_FeS_clus_asmbl_NifU_C.
[Graphical view]
PANTHERiPTHR11178:SF1. PTHR11178:SF1. 1 hit.
PfamiPF08712. Nfu_N. 1 hit.
PF01106. NifU. 1 hit.
[Graphical view]
ProDomiPD002830. NIF_FeS_clus_asmbl_NifU_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00932. Nfu_N. 1 hit.
[Graphical view]
SUPFAMiSSF110836. SSF110836. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QZ23-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAERAWGA AVGVVRLCRR FCHVATPHTF KKQPLHQYVR RPLFPLRAPL
60 70 80 90 100
CNTVRFMFIQ TQDTPNPNSL KFIPGKPVLE TRTMDFPTPA AAFRSPLARQ
110 120 130 140 150
LFRIEGVKSV FFGPDFITVT KENEELDWNL LKPDIYATIM DFFASGLPLV
160 170 180 190 200
TEETPPPPGE AGSEEDDEVV AMIKELLDTR IRPTVQEDGG DVIYRGFEDG
210 220 230 240 250
IVRLKLQGSC TSCPSSIITL KSGIQNMLQF YIPEVEGVEQ VMDDDESDEK

EANSS
Length:255
Mass (Da):28,568
Last modified:July 22, 2008 - v2
Checksum:iE7DA6A0333E2EB5E
GO

Sequence cautioni

The sequence AAH18355.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC24985.1 differs from that shown. Reason: Frameshift at positions 33 and 48. Curated
The sequence CAB57314.1 differs from that shown. Reason: Frameshift at positions 5, 8 and 50. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 122AV → TS in AAQ73785 (PubMed:12915448).Curated
Sequence conflicti19 – 191R → K in CAB57314 (PubMed:11342215).Curated
Sequence conflicti39 – 391V → A in CAB57314 (PubMed:11342215).Curated
Sequence conflicti39 – 391V → A in AAH18355 (PubMed:15489334).Curated
Sequence conflicti39 – 391V → A in AAQ73785 (PubMed:12915448).Curated
Sequence conflicti48 – 481A → H in CAB57314 (PubMed:11342215).Curated
Sequence conflicti163 – 1631S → SS in BAC24985 (PubMed:16141072).Curated
Sequence conflicti163 – 1631S → SS in BAE26508 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002244 mRNA. Translation: BAC24985.1. Frameshift.
AK003730 mRNA. Translation: BAB22965.1.
AK145558 mRNA. Translation: BAE26508.1.
AJ132616 mRNA. Translation: CAB57314.1. Frameshift.
BC018355 mRNA. Translation: AAH18355.1. Different initiation.
AY335195 mRNA. Translation: AAQ73785.1.
RefSeqiNP_001164062.1. NM_001170591.1.
NP_064429.2. NM_020045.3.
XP_006506482.1. XM_006506419.1.
XP_006506483.1. XM_006506420.1.
UniGeneiMm.23809.

Genome annotation databases

EnsembliENSMUST00000117583; ENSMUSP00000113332; ENSMUSG00000029993.
GeneIDi56748.
KEGGimmu:56748.
UCSCiuc009csv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002244 mRNA. Translation: BAC24985.1. Frameshift.
AK003730 mRNA. Translation: BAB22965.1.
AK145558 mRNA. Translation: BAE26508.1.
AJ132616 mRNA. Translation: CAB57314.1. Frameshift.
BC018355 mRNA. Translation: AAH18355.1. Different initiation.
AY335195 mRNA. Translation: AAQ73785.1.
RefSeqiNP_001164062.1. NM_001170591.1.
NP_064429.2. NM_020045.3.
XP_006506482.1. XM_006506419.1.
XP_006506483.1. XM_006506420.1.
UniGeneiMm.23809.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VEHNMR-A163-241[»]
ProteinModelPortaliQ9QZ23.
SMRiQ9QZ23. Positions 57-153, 169-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QZ23. 1 interaction.
MINTiMINT-1853650.
STRINGi10090.ENSMUSP00000032060.

PTM databases

SwissPalmiQ9QZ23.

Proteomic databases

EPDiQ9QZ23.
MaxQBiQ9QZ23.
PaxDbiQ9QZ23.
PRIDEiQ9QZ23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000117583; ENSMUSP00000113332; ENSMUSG00000029993.
GeneIDi56748.
KEGGimmu:56748.
UCSCiuc009csv.2. mouse.

Organism-specific databases

CTDi27247.
MGIiMGI:1913290. Nfu1.

Phylogenomic databases

eggNOGiKOG2358. Eukaryota.
COG0694. LUCA.
GeneTreeiENSGT00390000011296.
HOGENOMiHOG000023557.
HOVERGENiHBG054438.
InParanoidiQ9QZ23.
OrthoDBiEOG7SXW47.
PhylomeDBiQ9QZ23.
TreeFamiTF315076.

Miscellaneous databases

EvolutionaryTraceiQ9QZ23.
PROiQ9QZ23.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZ23.
ExpressionAtlasiQ9QZ23. baseline and differential.

Family and domain databases

Gene3Di3.30.1370.70. 1 hit.
InterProiIPR014824. Nfu/NifU_N.
IPR017065. NFU1.
IPR001075. NIF_FeS_clus_asmbl_NifU_C.
[Graphical view]
PANTHERiPTHR11178:SF1. PTHR11178:SF1. 1 hit.
PfamiPF08712. Nfu_N. 1 hit.
PF01106. NifU. 1 hit.
[Graphical view]
ProDomiPD002830. NIF_FeS_clus_asmbl_NifU_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00932. Nfu_N. 1 hit.
[Graphical view]
SUPFAMiSSF110836. SSF110836. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Blastocyst, Kidney and Testis.
  2. "Identification of human and mouse HIRA-interacting protein-5 (HIRIP5), two mammalian representatives in a family of phylogenetically conserved proteins with a role in the biogenesis of Fe/S proteins."
    Lorain S., Lecluse Y., Scamps C., Mattei M.-G., Lipinski M.
    Biochim. Biophys. Acta 1517:376-383(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-255.
  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] OF 6-255.
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain."
    Ganesh S., Tsurutani N., Suzuki T., Ueda K., Agarwala K.L., Osada H., Delgado-Escueta A.V., Yamakawa K.
    Hum. Mol. Genet. 12:2359-2368(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-255.
    Strain: ICR.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "Solution structure of RSGI RUH-018, a NIFU-like domain of HIRIP5 protein from mouse."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 162-241.

Entry informationi

Entry nameiNFU1_MOUSE
AccessioniPrimary (citable) accession number: Q9QZ23
Secondary accession number(s): Q3ULE0
, Q6VNZ7, Q8CF80, Q9D1B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: July 22, 2008
Last modified: June 8, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.