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Protein
Submitted name:

RNA polymerase I-specific transcription initiation factor RRN3

Gene

RRN3

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Submitted name:
RNA polymerase I-specific transcription initiation factor RRN3Imported
Gene namesi
Name:RRN3Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:30346. RRN3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

PeptideAtlasiF5H148.

Expressioni

Gene expression databases

BgeeiF5H148.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000198767.

Family & Domainsi

Phylogenomic databases

eggNOGiKOG2434. Eukaryota.
ENOG410XRJJ. LUCA.
GeneTreeiENSGT00390000001488.

Family and domain databases

InterProiIPR007991. RNA_pol_I_trans_ini_fac_RRN3.
[Graphical view]
PANTHERiPTHR12790. PTHR12790. 1 hit.
PfamiPF05327. RRN3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

F5H148-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPLLHTRL PGDAAASSSA VKKLGASRTG ISNMRALEND FFNSPPRKTV
60 70 80 90 100
RFGGTVTEVL LKYKKGETND FELLKNQLLD PDIKRLPWLN RSQTVVEEYL
110 120 130 140 150
AFLGNLVSAQ TVFLRPCLSM IASHFVPPRV IIKEGDVDVS DSDDEDDNLP
160 170 180 190 200
ANFDTCHRAL QIIARYVPST PWFLMPILVE KFPFVRKSER TLECYVHNLL
210 220 230 240 250
RISVYFPTLR HEILELIIEK LLKLDVNASR QGIEDAEETA TQTCGGTDST
260 270 280 290 300
EGLFNMDEDE ETEHETKAGP ERLDQMVHPV AERLDILMSL VLSYMKDVCY
310 320 330 340 350
VDGKVDNGKT KDLYRDLINI FDKLLLPTHA SCHVQFFMFY LCSFKLGFAE
360 370 380 390 400
AFLEHLWKKL QDPSNPAIIR QAAGNYIGSF LARAKFIPLI TVKSCLDLLV
410 420 430 440 450
NWLHIYLNNQ DSGTKAFCDV ALHGPFYSAC QAVFYTFVFR HKQLLSGNLK
460 470 480 490 500
EGLQYLQSLN FERIVMSQLN PLKICLPSVV NFFAAITNKY QLVFCYTIIE
510 520 530 540 550
RNNRQMLPVI RSTAGGDSVQ ICTNPLDTFF PFDPCVLKRS KKFIDPIYQV
560 570 580 590 600
WEDMSAEELQ EFKKPMKKDI VEDEDDDFLK GEVPQNDTVI GITPSSFDTH
610 620
FRSPSSSVGS PPVLYMQPSP L
Length:621
Mass (Da):70,467
Last modified:June 28, 2011 - v1
Checksum:i244350779B812955
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC139256 Genomic DNA. No translation available.
AC243651 Genomic DNA. No translation available.
RefSeqiNP_001287993.1. NM_001301064.1.
UniGeneiHs.460078.
Hs.720348.

Genome annotation databases

EnsembliENST00000429751; ENSP00000402027; ENSG00000085721.
ENST00000631800; ENSP00000487970; ENSG00000278494.
GeneIDi54700.
UCSCiuc010uzq.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC139256 Genomic DNA. No translation available.
AC243651 Genomic DNA. No translation available.
RefSeqiNP_001287993.1. NM_001301064.1.
UniGeneiHs.460078.
Hs.720348.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000198767.

Proteomic databases

PeptideAtlasiF5H148.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000429751; ENSP00000402027; ENSG00000085721.
ENST00000631800; ENSP00000487970; ENSG00000278494.
GeneIDi54700.
UCSCiuc010uzq.3. human.

Organism-specific databases

CTDi54700.
HGNCiHGNC:30346. RRN3.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2434. Eukaryota.
ENOG410XRJJ. LUCA.
GeneTreeiENSGT00390000001488.

Miscellaneous databases

GenomeRNAii54700.

Gene expression databases

BgeeiF5H148.

Family and domain databases

InterProiIPR007991. RNA_pol_I_trans_ini_fac_RRN3.
[Graphical view]
PANTHERiPTHR12790. PTHR12790. 1 hit.
PfamiPF05327. RRN3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "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].
  5. "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].
  6. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  7. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Ensembl
    Submitted (AUG-2015) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiF5H148_HUMAN
AccessioniPrimary (citable) accession number: F5H148
Entry historyi
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: July 6, 2016
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.