Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NFU1 iron-sulfur cluster scaffold homolog, mitochondrial

Gene

NFU1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB
  2. iron ion binding Source: UniProtKB

GO - Biological processi

  1. iron-sulfur cluster assembly Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
Alternative name(s):
HIRA-interacting protein 5
Gene namesi
Name:NFU1
Synonyms:HIRIP5
ORF Names:CGI-33
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:16287. NFU1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. mitochondrion Source: UniProtKB
  4. nucleoplasm Source: HPA
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Multiple mitochondrial dysfunctions syndrome 12 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA severe disorder of systemic energy metabolism, resulting in weakness, respiratory failure, lack of neurologic development, lactic acidosis, hyperglycinemia and early death. Some patients show failure to thrive, pulmonary hypertension, hypotonia and irritability. Biochemical features include severe combined deficiency of the 2-oxoacid dehydrogenases, defective lipoic acid synthesis and reduction in activity of mitochondrial respiratory chain complexes.

See also OMIM:605711
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti208 – 2081G → C in MMDS1. 1 Publication
VAR_066639

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi605711. phenotype.
Orphaneti401869. Fatal multiple mitochondrial dysfunction syndrome type 1.
PharmGKBiPA162397454.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 99MitochondrionSequence Analysis
Chaini10 – 254245NFU1 iron-sulfur cluster scaffold homolog, mitochondrialPRO_0000166191Add
BLAST

Proteomic databases

MaxQBiQ9UMS0.
PaxDbiQ9UMS0.
PRIDEiQ9UMS0.

Expressioni

Tissue specificityi

Ubiquitous. Expression in adult lung is weak compared to fetal lung.1 Publication

Developmental stagei

Expressed in embryo and adult.1 Publication

Gene expression databases

BgeeiQ9UMS0.
CleanExiHS_NFU1.
ExpressionAtlasiQ9UMS0. baseline and differential.
GenevestigatoriQ9UMS0.

Organism-specific databases

HPAiHPA035825.

Interactioni

Subunit structurei

Interacts with HIRA and EPM2A/laforin.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ORFQ9Q2G43EBI-725252,EBI-6248094From a different organism.

Protein-protein interaction databases

BioGridi118095. 8 interactions.
IntActiQ9UMS0. 5 interactions.
MINTiMINT-1388264.
STRINGi9606.ENSP00000387219.

Structurei

Secondary structure

1
254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi62 – 643Combined sources
Beta strandi71 – 755Combined sources
Beta strandi80 – 834Combined sources
Beta strandi86 – 883Combined sources
Helixi93 – 964Combined sources
Helixi98 – 1036Combined sources
Beta strandi109 – 1157Combined sources
Beta strandi118 – 1258Combined sources
Helixi130 – 14718Combined sources
Helixi167 – 18822Combined sources
Beta strandi192 – 1987Combined sources
Beta strandi201 – 2066Combined sources
Turni208 – 2125Combined sources
Helixi214 – 23118Combined sources
Beta strandi237 – 2404Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LTMNMR-A59-155[»]
2M5ONMR-A162-247[»]
ProteinModelPortaliQ9UMS0.
SMRiQ9UMS0. Positions 59-155, 164-247.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiCOG0694.
GeneTreeiENSGT00390000011296.
HOVERGENiHBG054438.
InParanoidiQ9UMS0.
OMAiEETSWDY.
OrthoDBiEOG7SXW47.
PhylomeDBiQ9UMS0.
TreeFamiTF315076.

Family and domain databases

Gene3Di3.30.1370.70. 1 hit.
InterProiIPR017065. HIRA-interacting_protein_5.
IPR014824. Nfu/NifU_N.
IPR001075. NIF_FeS_clus_asmbl_NifU_C.
[Graphical view]
PfamiPF08712. Nfu_N. 1 hit.
PF01106. NifU. 1 hit.
[Graphical view]
PIRSFiPIRSF036773. HIRIP5. 1 hit.
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.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UMS0-1) [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
MAATARRGWG AAAVAAGLRR RFCHMLKNPY TIKKQPLHQF VQRPLFPLPA
60 70 80 90 100
AFYHPVRYMF IQTQDTPNPN SLKFIPGKPV LETRTMDFPT PAAAFRSPLA
110 120 130 140 150
RQLFRIEGVK SVFFGPDFIT VTKENEELDW NLLKPDIYAT IMDFFASGLP
160 170 180 190 200
LVTEETPSGE AGSEEDDEVV AMIKELLDTR IRPTVQEDGG DVIYKGFEDG
210 220 230 240 250
IVQLKLQGSC TSCPSSIITL KNGIQNMLQF YIPEVEGVEQ VMDDESDEKE

ANSP
Length:254
Mass (Da):28,463
Last modified:September 2, 2008 - v2
Checksum:iE84B7F47A4A282CF
GO
Isoform 2 (identifier: Q9UMS0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-141: Missing.

Note: No experimental confirmation available.

Show »
Length:113
Mass (Da):12,347
Checksum:iC46A36AEC7E4C515
GO
Isoform 3 (identifier: Q9UMS0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.

Show »
Length:230
Mass (Da):25,924
Checksum:i2B953543B3A68DCC
GO

Sequence cautioni

The sequence AAD27742.1 differs from that shown. Reason: Frameshift at positions 5, 16, 115 and 117. Curated
The sequence AAY14828.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAG36716.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB53015.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581S → P in AAD27742. (PubMed:10810093)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251M → K.2 Publications
Corresponds to variant rs4453725 [ dbSNP | Ensembl ].
VAR_044429
Natural varianti208 – 2081G → C in MMDS1. 1 Publication
VAR_066639

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 141141Missing in isoform 2. 1 PublicationVSP_041224Add
BLAST
Alternative sequencei1 – 2424Missing in isoform 3. 3 PublicationsVSP_041225Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132584 mRNA. Translation: CAB53015.1. Different initiation.
AY335194 mRNA. Translation: AAQ73784.1.
AY286306 mRNA. Translation: AAP92372.1.
AY286307 mRNA. Translation: AAP92373.1.
AF132967 mRNA. Translation: AAD27742.1. Frameshift.
AK314004 mRNA. Translation: BAG36716.1. Different initiation.
AK300700 mRNA. Translation: BAG62381.1.
DB304061 mRNA. No translation available.
AC114772 Genomic DNA. Translation: AAY14828.1. Sequence problems.
CH471053 Genomic DNA. Translation: EAW99849.1.
CH471053 Genomic DNA. Translation: EAW99850.1.
BC113692 mRNA. Translation: AAI13693.1.
BC113694 mRNA. Translation: AAI13695.1.
CCDSiCCDS33217.1. [Q9UMS0-1]
CCDS42694.1. [Q9UMS0-2]
CCDS46315.1. [Q9UMS0-3]
RefSeqiNP_001002755.1. NM_001002755.2. [Q9UMS0-1]
NP_001002756.1. NM_001002756.2. [Q9UMS0-2]
NP_056515.2. NM_015700.3. [Q9UMS0-3]
XP_006712051.1. XM_006711988.1. [Q9UMS0-3]
UniGeneiHs.430439.

Genome annotation databases

EnsembliENST00000303698; ENSP00000306965; ENSG00000169599. [Q9UMS0-3]
ENST00000394305; ENSP00000377842; ENSG00000169599. [Q9UMS0-2]
ENST00000410022; ENSP00000387219; ENSG00000169599. [Q9UMS0-1]
ENST00000462320; ENSP00000418598; ENSG00000169599. [Q9UMS0-2]
GeneIDi27247.
KEGGihsa:27247.
UCSCiuc002sfj.3. human. [Q9UMS0-1]
uc002sfl.3. human. [Q9UMS0-2]

Polymorphism databases

DMDMi205371805.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132584 mRNA. Translation: CAB53015.1. Different initiation.
AY335194 mRNA. Translation: AAQ73784.1.
AY286306 mRNA. Translation: AAP92372.1.
AY286307 mRNA. Translation: AAP92373.1.
AF132967 mRNA. Translation: AAD27742.1. Frameshift.
AK314004 mRNA. Translation: BAG36716.1. Different initiation.
AK300700 mRNA. Translation: BAG62381.1.
DB304061 mRNA. No translation available.
AC114772 Genomic DNA. Translation: AAY14828.1. Sequence problems.
CH471053 Genomic DNA. Translation: EAW99849.1.
CH471053 Genomic DNA. Translation: EAW99850.1.
BC113692 mRNA. Translation: AAI13693.1.
BC113694 mRNA. Translation: AAI13695.1.
CCDSiCCDS33217.1. [Q9UMS0-1]
CCDS42694.1. [Q9UMS0-2]
CCDS46315.1. [Q9UMS0-3]
RefSeqiNP_001002755.1. NM_001002755.2. [Q9UMS0-1]
NP_001002756.1. NM_001002756.2. [Q9UMS0-2]
NP_056515.2. NM_015700.3. [Q9UMS0-3]
XP_006712051.1. XM_006711988.1. [Q9UMS0-3]
UniGeneiHs.430439.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LTMNMR-A59-155[»]
2M5ONMR-A162-247[»]
ProteinModelPortaliQ9UMS0.
SMRiQ9UMS0. Positions 59-155, 164-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118095. 8 interactions.
IntActiQ9UMS0. 5 interactions.
MINTiMINT-1388264.
STRINGi9606.ENSP00000387219.

Polymorphism databases

DMDMi205371805.

Proteomic databases

MaxQBiQ9UMS0.
PaxDbiQ9UMS0.
PRIDEiQ9UMS0.

Protocols and materials databases

DNASUi27247.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303698; ENSP00000306965; ENSG00000169599. [Q9UMS0-3]
ENST00000394305; ENSP00000377842; ENSG00000169599. [Q9UMS0-2]
ENST00000410022; ENSP00000387219; ENSG00000169599. [Q9UMS0-1]
ENST00000462320; ENSP00000418598; ENSG00000169599. [Q9UMS0-2]
GeneIDi27247.
KEGGihsa:27247.
UCSCiuc002sfj.3. human. [Q9UMS0-1]
uc002sfl.3. human. [Q9UMS0-2]

Organism-specific databases

CTDi27247.
GeneCardsiGC02M069622.
HGNCiHGNC:16287. NFU1.
HPAiHPA035825.
MIMi605711. phenotype.
608100. gene.
neXtProtiNX_Q9UMS0.
Orphaneti401869. Fatal multiple mitochondrial dysfunction syndrome type 1.
PharmGKBiPA162397454.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0694.
GeneTreeiENSGT00390000011296.
HOVERGENiHBG054438.
InParanoidiQ9UMS0.
OMAiEETSWDY.
OrthoDBiEOG7SXW47.
PhylomeDBiQ9UMS0.
TreeFamiTF315076.

Miscellaneous databases

ChiTaRSiNFU1. human.
GenomeRNAii27247.
NextBioi50161.
PROiQ9UMS0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UMS0.
CleanExiHS_NFU1.
ExpressionAtlasiQ9UMS0. baseline and differential.
GenevestigatoriQ9UMS0.

Family and domain databases

Gene3Di3.30.1370.70. 1 hit.
InterProiIPR017065. HIRA-interacting_protein_5.
IPR014824. Nfu/NifU_N.
IPR001075. NIF_FeS_clus_asmbl_NifU_C.
[Graphical view]
PfamiPF08712. Nfu_N. 1 hit.
PF01106. NifU. 1 hit.
[Graphical view]
PIRSFiPIRSF036773. HIRIP5. 1 hit.
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. "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] (ISOFORM 3).
    Tissue: Myeloid leukemia cell.
  2. "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] (ISOFORM 1), INTERACTION WITH EPM2A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANT LYS-25.
    Tissue: Brain.
  3. "Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster."
    Tong W.-H., Jameson G.N.L., Huynh B.H., Rouault T.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:9762-9767(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR LOCATION.
  4. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  5. "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] (ISOFORMS 1 AND 2), VARIANT LYS-25.
    Tissue: Skeletal muscle.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Cerebellum.
  9. "Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes."
    Cameron J.M., Janer A., Levandovskiy V., Mackay N., Rouault T.A., Tong W.H., Ogilvie I., Shoubridge E.A., Robinson B.H.
    Am. J. Hum. Genet. 89:486-495(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INVOLVEMENT IN MMDS1.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Solution NMR structure of NFU1 iron-sulfur cluster scaffold homolog from Homo sapiens, Northeast structural genomics consortium (NESG) target HR2876B."
    Northeast structural genomics consortium (NESG)
    Submitted (AUG-2012) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 59-155.
  12. Cited for: VARIANT MMDS1 CYS-208.

Entry informationi

Entry nameiNFU1_HUMAN
AccessioniPrimary (citable) accession number: Q9UMS0
Secondary accession number(s): B4DUL9
, Q53QE5, Q6VNZ8, Q7Z5B1, Q7Z5B2, Q9Y322
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: September 2, 2008
Last modified: February 4, 2015
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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.