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Q9NYV6 (RRN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA polymerase I-specific transcription initiation factor RRN3
Alternative name(s):
Transcription initiation factor IA
Short name=TIF-IA
Gene names
Name:RRN3
Synonyms:TIFIA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for efficient transcription initiation by RNA polymerase I. Required for the formation of the competent preinitiation complex (PIC). Dissociates from pol I as a consequence of transcription. In vitro, cannot activate transcription in a subsequent transcription reaction By similarity. Ref.1 Ref.2 Ref.6 Ref.8

Subunit structure

Interacts with TWISTNB, EIF3L, TAF1B and TAF1C. Ref.6 Ref.7

Subcellular location

Nucleusnucleolus Ref.6.

Post-translational modification

Phosphorylation is required for participation in rDNA transcription By similarity. Phosphorylated at Thr-200 by MAPK9/JNK2, which abrogates initiation complex formation. Ref.8

Sequence similarities

Belongs to the RRN3 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from electronic annotation. Source: Ensembl

cytoplasm organization

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

homeostasis of number of cells

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

nucleolus organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of DNA-templated transcription, initiation

Inferred from electronic annotation. Source: Ensembl

ribosome biogenesis

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

   Cellular_componentnucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 651651RNA polymerase I-specific transcription initiation factor RRN3
PRO_0000211426

Regions

Region500 – 651152Interaction with TWISTNB
Region557 – 65195Interaction with EIF3L

Amino acid modifications

Modified residue1701Phosphoserine Ref.9
Modified residue1721Phosphoserine Ref.9
Modified residue2001Phosphothreonine; by MAPK9 Ref.8
Modified residue6401Phosphoserine Ref.9 Ref.10

Natural variations

Natural variant3481I → M.
Corresponds to variant rs2941256 [ dbSNP | Ensembl ].
VAR_051886

Experimental info

Mutagenesis411 – 4155Missing: Abolishes interaction with TAF1B and TAF1C. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q9NYV6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C646DC6677C49895

FASTA65174,107
        10         20         30         40         50         60 
MAAPLLHTRL PGDAAASSSA VKKLGASRTG ISNMRALEND FFNSPPRKTV RFGGTVTEVL 

        70         80         90        100        110        120 
LKYKKGETND FELLKNQLLD PDIKDDQIIN WLLEFRSSIM YLTKDFEQLI SIILRLPWLN 

       130        140        150        160        170        180 
RSQTVVEEYL AFLGNLVSAQ TVFLRPCLSM IASHFVPPRV IIKEGDVDVS DSDDEDDNLP 

       190        200        210        220        230        240 
ANFDTCHRAL QIIARYVPST PWFLMPILVE KFPFVRKSER TLECYVHNLL RISVYFPTLR 

       250        260        270        280        290        300 
HEILELIIEK LLKLDVNASR QGIEDAEETA TQTCGGTDST EGLFNMDEDE ETEHETKAGP 

       310        320        330        340        350        360 
ERLDQMVHPV AERLDILMSL VLSYMKDVCY VDGKVDNGKT KDLYRDLINI FDKLLLPTHA 

       370        380        390        400        410        420 
SCHVQFFMFY LCSFKLGFAE AFLEHLWKKL QDPSNPAIIR QAAGNYIGSF LARAKFIPLI 

       430        440        450        460        470        480 
TVKSCLDLLV NWLHIYLNNQ DSGTKAFCDV ALHGPFYSAC QAVFYTFVFR HKQLLSGNLK 

       490        500        510        520        530        540 
EGLQYLQSLN FERIVMSQLN PLKICLPSVV NFFAAITNKY QLVFCYTIIE RNNRQMLPVI 

       550        560        570        580        590        600 
RSTAGGDSVQ ICTNPLDTFF PFDPCVLKRS KKFIDPIYQV WEDMSAEELQ EFKKPMKKDI 

       610        620        630        640        650 
VEDEDDDFLK GEVPQNDTVI GITPSSFDTH FRSPSSSVGS PPVLYMQPSP L 

« Hide

References

« Hide 'large scale' references
[1]"TIF-IA, the factor mediating growth-dependent control of ribosomal RNA synthesis, is the mammalian homolog of yeast Rrn3p."
Bodem J., Dobreva G., Hoffmann-Rohrer U., Iben S., Zentgraf H., Delius H., Vingron M., Grummt I.
EMBO Rep. 1:171-175(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"RNA polymerase I transcription factor Rrn3 is functionally conserved between yeast and human."
Moorefield B., Greene E.A., Reeder R.H.
Proc. Natl. Acad. Sci. U.S.A. 97:4724-4729(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[3]"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. expand/collapse author list , 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].
Tissue: Hippocampus.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Spleen.
[6]"hRRN3 is essential in the SL1-mediated recruitment of RNA polymerase I to rRNA gene promoters."
Miller G., Panov K.I., Friedrich J.K., Trinkle-Mulcahy L., Lamond A.I., Zomerdijk J.C.B.M.
EMBO J. 20:1373-1382(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TAF1B AND TAF1C.
[7]"Multiple interactions between RNA polymerase I, TIF-IA and TAF(I) subunits regulate preinitiation complex assembly at the ribosomal gene promoter."
Yuan X., Zhao J., Zentgraf H., Hoffmann-Rohrer U., Grummt I.
EMBO Rep. 3:1082-1087(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TWISTNB; EIF3L; TAF1B AND TAF1C, MUTAGENESIS OF 411-LEU--LYS-415.
[8]"The nucleolus as a stress sensor: JNK2 inactivates the transcription factor TIF-IA and down-regulates rRNA synthesis."
Mayer C., Bierhoff H., Grummt I.
Genes Dev. 19:933-941(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-200 BY MAPK9/JNK2, FUNCTION.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-172 AND SER-640, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ272050 mRNA. Translation: CAC07955.1.
AF227156 mRNA. Translation: AAF66160.1.
AK314769 mRNA. Translation: BAG37307.1.
CH471301 Genomic DNA. Translation: EAW54754.1.
BC071868 mRNA. Translation: AAH71868.1.
BC132688 mRNA. Translation: AAI32689.1.
BC132690 mRNA. Translation: AAI32691.1.
CCDSCCDS10559.1.
RefSeqNP_060897.3. NM_018427.3.
UniGeneHs.460078.

3D structure databases

ProteinModelPortalQ9NYV6.
SMRQ9NYV6. Positions 179-585.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120102. 23 interactions.
IntActQ9NYV6. 4 interactions.
MINTMINT-249163.
STRING9606.ENSP00000198767.

PTM databases

PhosphoSiteQ9NYV6.

Polymorphism databases

DMDM74719591.

Proteomic databases

MaxQBQ9NYV6.
PaxDbQ9NYV6.
PRIDEQ9NYV6.

Protocols and materials databases

DNASU54700.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000198767; ENSP00000198767; ENSG00000085721.
GeneID54700.
KEGGhsa:54700.
UCSCuc002dde.3. human.

Organism-specific databases

CTD54700.
GeneCardsGC16M015153.
H-InvDBHIX0012886.
HIX0038660.
HIX0038739.
HGNCHGNC:30346. RRN3.
HPAHPA049837.
MIM605121. gene.
neXtProtNX_Q9NYV6.
PharmGKBPA134878601.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG275643.
HOGENOMHOG000236344.
HOVERGENHBG056994.
InParanoidQ9NYV6.
KOK15216.
OMAFRWRDLT.
OrthoDBEOG7ZGX2R.
PhylomeDBQ9NYV6.
TreeFamTF312979.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9NYV6.
BgeeQ9NYV6.
CleanExHS_RRN3.
GenevestigatorQ9NYV6.

Family and domain databases

InterProIPR007991. RNA_pol_I_trans_ini_fac_RRN3.
[Graphical view]
PANTHERPTHR12790. PTHR12790. 1 hit.
PfamPF05327. RRN3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRRN3.
GenomeRNAi54700.
NextBio57257.
PROQ9NYV6.
SOURCESearch...

Entry information

Entry nameRRN3_HUMAN
AccessionPrimary (citable) accession number: Q9NYV6
Secondary accession number(s): A2RTY9, Q6IPL4, Q9H4F0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 90 of the entry and version 1 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