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Protein

5-methylcytosine rRNA methyltransferase NSUN4

Gene

NSUN4

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

Functioni

Involved in mitochondrial ribosome assembly. 5-methylcytosine rRNA methyltransferase that probably is involved in mitochondrial ribosome small subunit (SSU) maturation by methylation of mitochondrial 12S rRNA; the function is independent of MTERFD2/MTERF4 and assembled mitochondrial ribosome large subunit (LSU). Targeted to LSU by MTERFD2/MTERF4 and probably is involved in a final step in ribosome biogenesis to ensure that SSU and LSU are assembled. In vitro can methylate 16S rRNA of the LSU; the methylation is enhanced by MTERFD/MTERF4.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei237 – 2371S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication
Binding sitei255 – 2551S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication
Active sitei310 – 3101NucleophilePROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  • methyltransferase activity Source: UniProtKB
  • small ribosomal subunit rRNA binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

RNA-binding, rRNA-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
5-methylcytosine rRNA methyltransferase NSUN4 (EC:2.1.1.-)
Alternative name(s):
NOL1/NOP2/Sun domain family member 4
Gene namesi
Name:NSUN4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:31802. NSUN4.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial large ribosomal subunit Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651V → R: Disrupts complex with MTERFD2; when associated with A-136, R-139 and A-141. 1 Publication
Mutagenesisi136 – 1361R → A: Disrupts complex with MTERFD2; when associated with R-65, R-139 and A-141. 1 Publication
Mutagenesisi139 – 1391I → R: Disrupts complex with MTERFD2; when associated with R-65, A-136, and A-141. 1 Publication
Mutagenesisi141 – 1411R → A: Disrupts complex with MTERFD2; when associated with R-65, A-136 and R-139. 1 Publication

Organism-specific databases

PharmGKBiPA134953046.

Polymorphism and mutation databases

BioMutaiNSUN4.
DMDMi152125805.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525Mitochondrion1 PublicationAdd
BLAST
Chaini26 – 3843595-methylcytosine rRNA methyltransferase NSUN4PRO_0000289234Add
BLAST

Proteomic databases

MaxQBiQ96CB9.
PaxDbiQ96CB9.
PRIDEiQ96CB9.

PTM databases

PhosphoSiteiQ96CB9.

Expressioni

Gene expression databases

BgeeiQ96CB9.
CleanExiHS_NSUN4.
ExpressionAtlasiQ96CB9. baseline and differential.
GenevestigatoriQ96CB9.

Organism-specific databases

HPAiHPA027958.
HPA028489.

Interactioni

Protein-protein interaction databases

BioGridi132288. 14 interactions.
DIPiDIP-58104N.
IntActiQ96CB9. 6 interactions.
MINTiMINT-1474456.
STRINGi9606.ENSP00000419740.

Structurei

Secondary structure

1
384
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 5617Combined sources
Helixi57 – 593Combined sources
Helixi60 – 678Combined sources
Beta strandi74 – 774Combined sources
Helixi79 – 813Combined sources
Helixi83 – 9210Combined sources
Helixi98 – 1047Combined sources
Turni105 – 1073Combined sources
Helixi121 – 1244Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi151 – 1588Combined sources
Helixi160 – 1623Combined sources
Helixi163 – 1697Combined sources
Beta strandi175 – 1817Combined sources
Helixi186 – 1938Combined sources
Beta strandi197 – 2037Combined sources
Helixi207 – 22014Combined sources
Turni223 – 2275Combined sources
Beta strandi228 – 2347Combined sources
Helixi238 – 2403Combined sources
Helixi241 – 2444Combined sources
Beta strandi249 – 2557Combined sources
Helixi261 – 2644Combined sources
Helixi275 – 2773Combined sources
Helixi278 – 2825Combined sources
Helixi284 – 29714Combined sources
Beta strandi299 – 31012Combined sources
Turni314 – 3174Combined sources
Helixi318 – 33215Combined sources
Beta strandi336 – 3383Combined sources
Helixi342 – 3487Combined sources
Turni349 – 3513Combined sources
Beta strandi359 – 3657Combined sources
Beta strandi375 – 3828Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FP9X-ray2.90A/C/D/F26-384[»]
4FZVX-ray2.00A26-384[»]
ProteinModelPortaliQ96CB9.
SMRiQ96CB9. Positions 38-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni181 – 1877S-adenosyl-L-methionine binding

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0144.
GeneTreeiENSGT00660000095341.
HOGENOMiHOG000017426.
HOVERGENiHBG106892.
InParanoidiQ96CB9.
OMAiACSPNLR.
OrthoDBiEOG789CB3.
PhylomeDBiQ96CB9.
TreeFamiTF321304.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001678. MeTrfase_RsmB/NOP2.
IPR023267. RCMT.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01189. Nol1_Nop2_Fmu. 1 hit.
[Graphical view]
PRINTSiPR02008. RCMTFAMILY.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96CB9-1) [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
MAALTLRGVR ELLKRVDLAT VPRRHRYKKK WAATEPKFPA VRLALQNFDM
60 70 80 90 100
TYSVQFGDLW PSIRVSLLSE QKYGALVNNF AAWDHVSAKL EQLSAKDFVN
110 120 130 140 150
EAISHWELQS EGGQSAAPSP ASWACSPNLR CFTFDRGDIS RFPPARPGSL
160 170 180 190 200
GVMEYYLMDA ASLLPVLALG LQPGDIVLDL CAAPGGKTLA LLQTGCCRNL
210 220 230 240 250
AANDLSPSRI ARLQKILHSY VPEEIRDGNQ VRVTSWDGRK WGELEGDTYD
260 270 280 290 300
RVLVDVPCTT DRHSLHEEEN NIFKRSRKKE RQILPVLQVQ LLAAGLLATK
310 320 330 340 350
PGGHVVYSTC SLSHLQNEYV VQGAIELLAN QYSIQVQVED LTHFRRVFMD
360 370 380
TFCFFSSCQV GELVIPNLMA NFGPMYFCKM RRLT
Length:384
Mass (Da):43,089
Last modified:May 29, 2007 - v2
Checksum:i4D83B6D55D65C27F
GO
Isoform 2 (identifier: Q96CB9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-384: Missing.

Note: No experimental confirmation available.

Show »
Length:146
Mass (Da):16,507
Checksum:iE49A839AA5937FB5
GO
Isoform 3 (identifier: Q96CB9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-198: Missing.
     199-219: NLAANDLSPSRIARLQKILHS → MLPPCCLFWPSACSLGTSCLT

Note: No experimental confirmation available.

Show »
Length:186
Mass (Da):21,240
Checksum:i4186007A46B086CD
GO
Isoform 4 (identifier: Q96CB9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Note: No experimental confirmation available.

Show »
Length:335
Mass (Da):37,374
Checksum:i85AACD29E9DDB7D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2821Q → R in BAG51912 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511T → A.2 Publications
Corresponds to variant rs3737744 [ dbSNP | Ensembl ].
VAR_032606
Natural varianti128 – 1281N → K.
Corresponds to variant rs17102152 [ dbSNP | Ensembl ].
VAR_032607
Natural varianti325 – 3251I → T.
Corresponds to variant rs13374337 [ dbSNP | Ensembl ].
VAR_032608
Natural varianti365 – 3651I → V.1 Publication
Corresponds to variant rs9865 [ dbSNP | Ensembl ].
VAR_032609

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 198198Missing in isoform 3. 1 PublicationVSP_025971Add
BLAST
Alternative sequencei1 – 4949Missing in isoform 4. 1 PublicationVSP_045053Add
BLAST
Alternative sequencei147 – 384238Missing in isoform 2. 1 PublicationVSP_025972Add
BLAST
Alternative sequencei199 – 21921NLAAN…KILHS → MLPPCCLFWPSACSLGTSCL T in isoform 3. 1 PublicationVSP_025973Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK021577 mRNA. Translation: BAB13847.1.
AK057420 mRNA. Translation: BAG51912.1.
AK291741 mRNA. Translation: BAF84430.1.
AK295003 mRNA. Translation: BAG58065.1.
AL122001 Genomic DNA. Translation: CAI21962.1.
CH471059 Genomic DNA. Translation: EAX06917.1.
BC014441 mRNA. Translation: AAH14441.1.
BC016907 mRNA. Translation: AAH16907.1.
CCDSiCCDS534.1. [Q96CB9-1]
CCDS57996.1. [Q96CB9-4]
RefSeqiNP_001243056.1. NM_001256127.1. [Q96CB9-4]
NP_001243057.1. NM_001256128.1. [Q96CB9-4]
NP_950245.2. NM_199044.3. [Q96CB9-1]
UniGeneiHs.163424.

Genome annotation databases

EnsembliENST00000474844; ENSP00000419740; ENSG00000117481. [Q96CB9-1]
ENST00000537428; ENSP00000437758; ENSG00000117481. [Q96CB9-4]
GeneIDi387338.
KEGGihsa:387338.
UCSCiuc001cpr.2. human. [Q96CB9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK021577 mRNA. Translation: BAB13847.1.
AK057420 mRNA. Translation: BAG51912.1.
AK291741 mRNA. Translation: BAF84430.1.
AK295003 mRNA. Translation: BAG58065.1.
AL122001 Genomic DNA. Translation: CAI21962.1.
CH471059 Genomic DNA. Translation: EAX06917.1.
BC014441 mRNA. Translation: AAH14441.1.
BC016907 mRNA. Translation: AAH16907.1.
CCDSiCCDS534.1. [Q96CB9-1]
CCDS57996.1. [Q96CB9-4]
RefSeqiNP_001243056.1. NM_001256127.1. [Q96CB9-4]
NP_001243057.1. NM_001256128.1. [Q96CB9-4]
NP_950245.2. NM_199044.3. [Q96CB9-1]
UniGeneiHs.163424.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FP9X-ray2.90A/C/D/F26-384[»]
4FZVX-ray2.00A26-384[»]
ProteinModelPortaliQ96CB9.
SMRiQ96CB9. Positions 38-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi132288. 14 interactions.
DIPiDIP-58104N.
IntActiQ96CB9. 6 interactions.
MINTiMINT-1474456.
STRINGi9606.ENSP00000419740.

PTM databases

PhosphoSiteiQ96CB9.

Polymorphism and mutation databases

BioMutaiNSUN4.
DMDMi152125805.

Proteomic databases

MaxQBiQ96CB9.
PaxDbiQ96CB9.
PRIDEiQ96CB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000474844; ENSP00000419740; ENSG00000117481. [Q96CB9-1]
ENST00000537428; ENSP00000437758; ENSG00000117481. [Q96CB9-4]
GeneIDi387338.
KEGGihsa:387338.
UCSCiuc001cpr.2. human. [Q96CB9-1]

Organism-specific databases

CTDi387338.
GeneCardsiGC01P046805.
HGNCiHGNC:31802. NSUN4.
HPAiHPA027958.
HPA028489.
MIMi615394. gene.
neXtProtiNX_Q96CB9.
PharmGKBiPA134953046.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0144.
GeneTreeiENSGT00660000095341.
HOGENOMiHOG000017426.
HOVERGENiHBG106892.
InParanoidiQ96CB9.
OMAiACSPNLR.
OrthoDBiEOG789CB3.
PhylomeDBiQ96CB9.
TreeFamiTF321304.

Miscellaneous databases

GenomeRNAii387338.
NextBioi101304.
PROiQ96CB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ96CB9.
CleanExiHS_NSUN4.
ExpressionAtlasiQ96CB9. baseline and differential.
GenevestigatoriQ96CB9.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001678. MeTrfase_RsmB/NOP2.
IPR023267. RCMT.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01189. Nol1_Nop2_Fmu. 1 hit.
[Graphical view]
PRINTSiPR02008. RCMTFAMILY.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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; 3 AND 4), VARIANTS ALA-51 AND VAL-365.
    Tissue: Brain, Embryo, Placenta and Testis.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-384 (ISOFORM 2), VARIANT ALA-51.
    Tissue: Colon and Duodenum.
  5. Cited for: PARTIAL PROTEIN SEQUENCE, TRANSIT PEPTIDE CLEAVAGE SITE, FUNCTION, INTERACTION WITH MTERF4, SUBCELLULAR LOCATION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Structure of the human MTERF4-NSUN4 protein complex that regulates mitochondrial ribosome biogenesis."
    Spahr H., Habermann B., Gustafsson C.M., Larsson N.G., Hallberg B.M.
    Proc. Natl. Acad. Sci. U.S.A. 109:15253-15258(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-384 IN COMPLEX WITH MTERFD2, ACTIVE SITE, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-65; ARG-136; ILE-139 AND ARG-141.
  9. "Structure of the essential MTERF4:NSUN4 protein complex reveals how an MTERF protein collaborates to facilitate rRNA modification."
    Yakubovskaya E., Guja K.E., Mejia E., Castano S., Hambardjieva E., Choi W.S., Garcia-Diaz M.
    Structure 20:1940-1947(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 26-384 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND MTERFD2, FUNCTION IN METHYLATION OF 16S RRNA, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiNSUN4_HUMAN
AccessioniPrimary (citable) accession number: Q96CB9
Secondary accession number(s): A8K6S6
, B3KQ50, B4DHA4, Q5TDF7, Q96AN8, Q9HAJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: April 29, 2015
This is version 94 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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.