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Q5SHN9

- RL4_THET8

UniProt

Q5SHN9 - RL4_THET8

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Protein

50S ribosomal protein L4

Gene

rplD

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).By similarity
Forms part of the polypeptide exit tunnel.By similarity
This protein can be incorporated into E.coli ribosomes in vivo, which resulted in decreased peptidyltransferase (Ptase) activity of the hybrid ribosomes. The hybrid 50S subunits associate less well with 30S subunits to form the ribosome.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1730-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L4
Alternative name(s):
L1e
Gene namesi
Name:rplD
Ordered Locus Names:TTHA1691
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 551G → A: Increases Ptase activity of hybrid ribosomes to a value greater than that of pure E.coli ribosomes. Increases binding of a tRNA analog to the P site. 1 Publication
Mutagenesisi55 – 551G → S: No effect on Ptase activity of hybrid ribosomes. No change in binding of a tRNA analog to the A or P site. 1 Publication
Mutagenesisi56 – 561E → A: Further decreases Ptase activity in E.coli hybrid ribosomes. Significantly decreases binding of a tRNA analog to the A or P site. 1 Publication
Mutagenesisi56 – 561E → Q: Restores Ptase activity of hybrid ribosomes to that of pure E.coli ribosomes. Significantly increases binding of a tRNA analog to the P site. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21021050S ribosomal protein L4PRO_0000129300Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

STRINGi300852.TTHA1691.

Structurei

Secondary structure

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 126Combined sources
Beta strandi14 – 163Combined sources
Beta strandi18 – 225Combined sources
Beta strandi24 – 263Combined sources
Helixi30 – 4314Combined sources
Turni54 – 563Combined sources
Beta strandi57 – 593Combined sources
Beta strandi67 – 726Combined sources
Beta strandi78 – 803Combined sources
Beta strandi83 – 864Combined sources
Beta strandi88 – 903Combined sources
Helixi103 – 11917Combined sources
Beta strandi123 – 1275Combined sources
Helixi136 – 14510Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi154 – 1574Combined sources
Helixi161 – 1688Combined sources
Beta strandi173 – 1764Combined sources
Helixi178 – 1803Combined sources
Helixi183 – 1886Combined sources
Beta strandi189 – 1957Combined sources
Helixi196 – 20510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GIYX-ray5.50F1-210[»]
1TWVmodel-D1-210[»]
1VVMX-ray3.22F1-210[»]
1VVOX-ray3.22F1-210[»]
1VVQX-ray3.90F1-210[»]
1VVSX-ray3.90F1-210[»]
1VVUX-ray3.90F1-210[»]
1VVWX-ray3.90F1-210[»]
1VVYX-ray3.92F1-210[»]
1VW0X-ray3.92F1-210[»]
1VX9X-ray2.94F1-210[»]
1VXJX-ray2.94F1-210[»]
1VXLX-ray3.48F1-210[»]
1VXNX-ray3.48F1-210[»]
1VXQX-ray3.14F1-210[»]
1VXTX-ray3.14F1-210[»]
1VY1X-ray3.68F1-210[»]
1VY3X-ray3.68F1-210[»]
1YL3X-ray5.50F1-210[»]
2HGJX-ray5.00F1-210[»]
2HGQX-ray5.50F1-210[»]
2HGUX-ray4.51F1-210[»]
2J01X-ray2.80F1-210[»]
2J03X-ray2.80F1-210[»]
2V47X-ray3.80F1-210[»]
2V49X-ray3.80F1-210[»]
2WDIX-ray3.30F1-210[»]
2WDJX-ray3.30F1-210[»]
2WDLX-ray3.50F1-210[»]
2WDNX-ray3.50F1-210[»]
2WH2X-ray3.45F1-210[»]
2WH4X-ray3.45F1-210[»]
2WRJX-ray3.60F1-210[»]
2WRLX-ray3.60F1-210[»]
2WROX-ray3.60F1-210[»]
2WRRX-ray3.60F1-210[»]
2X9SX-ray3.10F1-210[»]
2X9UX-ray3.10F1-210[»]
2XG0X-ray3.20F1-210[»]
2XG2X-ray3.20F1-210[»]
2XQEX-ray3.10F1-210[»]
2XTGelectron microscopy7.80F1-210[»]
2XUXelectron microscopy7.60F1-210[»]
2Y0VX-ray3.10F1-210[»]
2Y0XX-ray3.10F1-210[»]
2Y0ZX-ray3.10F1-210[»]
2Y11X-ray3.10F1-210[»]
2Y13X-ray3.10F1-210[»]
2Y15X-ray3.10F1-210[»]
2Y17X-ray3.10F1-210[»]
2Y19X-ray3.10F1-210[»]
3F1FX-ray3.00F1-210[»]
3F1HX-ray3.00F1-210[»]
3FINelectron microscopy6.40F1-208[»]
3HUXX-ray3.10F1-210[»]
3HUZX-ray3.10F1-210[»]
3I8FX-ray3.10F1-210[»]
3I8IX-ray3.10F1-210[»]
3I9CX-ray3.50F1-210[»]
3I9EX-ray3.50F1-210[»]
3KIRX-ray3.30F1-210[»]
3KITX-ray3.30F1-210[»]
3KIWX-ray3.60F1-210[»]
3KIYX-ray3.60F1-210[»]
3KNIX-ray3.00F1-210[»]
3KNKX-ray3.00F1-210[»]
3KNMX-ray3.45F1-210[»]
3KNOX-ray3.45F1-210[»]
3OHJX-ray3.00F1-210[»]
3OHZX-ray3.00F1-210[»]
3OI5X-ray3.10F1-210[»]
3TVEX-ray3.10F6-207[»]
3TVHX-ray3.10F1-208[»]
3UXQX-ray3.20F6-210[»]
3UXRX-ray3.20F6-210[»]
3UYEX-ray3.00F1-210[»]
3UYGX-ray3.00F1-210[»]
3UZ1X-ray3.30F1-210[»]
3UZ2X-ray3.30F1-210[»]
3UZ8X-ray3.00F1-210[»]
3UZ9X-ray3.00F1-210[»]
3UZFX-ray3.30F1-210[»]
3UZHX-ray3.30F1-210[»]
3UZKX-ray3.30F1-210[»]
3UZNX-ray3.30F1-210[»]
3V23X-ray3.00F1-210[»]
3V25X-ray3.00F1-210[»]
3V27X-ray3.10F1-210[»]
3V29X-ray3.10F1-210[»]
3V2DX-ray2.70F1-210[»]
3V2FX-ray2.70F1-210[»]
3V6WX-ray3.90F1-210[»]
3V6XX-ray3.90F1-210[»]
3ZN9X-ray3.10F1-210[»]
3ZNEX-ray3.10F1-210[»]
3ZVPX-ray3.80F1-210[»]
4ABSX-ray3.10F1-210[»]
4B8GX-ray3.70F1-210[»]
4B8IX-ray3.70F1-210[»]
4BTDX-ray2.95F1-210[»]
4BYCX-ray3.35F1-210[»]
4BYEX-ray3.35F1-210[»]
4DHAX-ray3.20F1-210[»]
4DHCX-ray3.20F1-210[»]
4EJBX-ray3.52F1-210[»]
4EJCX-ray3.52F1-210[»]
4G5LX-ray3.30F1-210[»]
4G5NX-ray3.30F1-210[»]
4G5UX-ray3.10F1-210[»]
4G5WX-ray3.10F1-210[»]
4JUXX-ray2.86F1-210[»]
4K0MX-ray3.30F1-207[»]
4K0QX-ray3.30F1-207[»]
4KX0X-ray3.44F1-210[»]
4KX2X-ray3.44F1-210[»]
4NVVX-ray3.00F1-210[»]
4NVXX-ray3.00F1-210[»]
4NVZX-ray3.10F1-210[»]
4NW1X-ray3.10F1-210[»]
4QCNX-ray2.60F1-210[»]
4QCPX-ray2.60F1-210[»]
4QCRX-ray2.55F1-210[»]
4QCTX-ray2.55F1-210[»]
4QCVX-ray2.90F1-210[»]
4QCXX-ray2.90F1-210[»]
4QCZX-ray2.80F1-210[»]
4QD1X-ray2.80F1-210[»]
4QJSX-ray2.90F6-210[»]
4W2BX-ray3.60E1-210[»]
4W2DX-ray3.60E1-210[»]
ProteinModelPortaliQ5SHN9.
SMRiQ5SHN9. Positions 3-210.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHN9.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L4P family.Curated

Phylogenomic databases

eggNOGiCOG0088.
HOGENOMiHOG000248767.
KOiK02926.
OMAiRSIMANQ.
OrthoDBiEOG6M0T9G.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
HAMAPiMF_01328_B. Ribosomal_L4_B.
InterProiIPR002136. Ribosomal_L4/L1e.
IPR013005. Ribosomal_L4/L1e_bac-type.
IPR023574. Ribosomal_L4_dom.
[Graphical view]
PANTHERiPTHR10746. PTHR10746. 1 hit.
PfamiPF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
TIGRFAMsiTIGR03953. rplD_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5SHN9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKEVAVYQIP VLSPSGRREL AADLPAEINP HLLWEVVRWQ LAKRRRGTAS
60 70 80 90 100
TKTRGEVAYS GRKIWPQKHT GRARHGDIGA PIFVGGGVVF GPKPRDYSYT
110 120 130 140 150
LPKKVRKKGL AMAVADRARE GKLLLVEAFA GVNGKTKEFL AWAKEAGLDG
160 170 180 190 200
SESVLLVTGN ELVRRAARNL PWVVTLAPEG LNVYDIVRTE RLVMDLDAWE
210
VFQNRIGGEA
Length:210
Mass (Da):23,235
Last modified:December 21, 2004 - v1
Checksum:iBFB99AC179C110B4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 202EL → DV in AAA97862. (PubMed:8566766)Curated

Mass spectrometryi

Molecular mass is 22724 Da from positions 1 - 210. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36480 Genomic DNA. Translation: AAA97862.1.
AP008226 Genomic DNA. Translation: BAD71514.1.
RefSeqiYP_144957.2. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71514; BAD71514; BAD71514.
GeneIDi3167923.
KEGGittj:TTHA1691.
PATRICi23958337. VBITheThe93045_1661.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36480 Genomic DNA. Translation: AAA97862.1 .
AP008226 Genomic DNA. Translation: BAD71514.1 .
RefSeqi YP_144957.2. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GIY X-ray 5.50 F 1-210 [» ]
1TWV model - D 1-210 [» ]
1VVM X-ray 3.22 F 1-210 [» ]
1VVO X-ray 3.22 F 1-210 [» ]
1VVQ X-ray 3.90 F 1-210 [» ]
1VVS X-ray 3.90 F 1-210 [» ]
1VVU X-ray 3.90 F 1-210 [» ]
1VVW X-ray 3.90 F 1-210 [» ]
1VVY X-ray 3.92 F 1-210 [» ]
1VW0 X-ray 3.92 F 1-210 [» ]
1VX9 X-ray 2.94 F 1-210 [» ]
1VXJ X-ray 2.94 F 1-210 [» ]
1VXL X-ray 3.48 F 1-210 [» ]
1VXN X-ray 3.48 F 1-210 [» ]
1VXQ X-ray 3.14 F 1-210 [» ]
1VXT X-ray 3.14 F 1-210 [» ]
1VY1 X-ray 3.68 F 1-210 [» ]
1VY3 X-ray 3.68 F 1-210 [» ]
1YL3 X-ray 5.50 F 1-210 [» ]
2HGJ X-ray 5.00 F 1-210 [» ]
2HGQ X-ray 5.50 F 1-210 [» ]
2HGU X-ray 4.51 F 1-210 [» ]
2J01 X-ray 2.80 F 1-210 [» ]
2J03 X-ray 2.80 F 1-210 [» ]
2V47 X-ray 3.80 F 1-210 [» ]
2V49 X-ray 3.80 F 1-210 [» ]
2WDI X-ray 3.30 F 1-210 [» ]
2WDJ X-ray 3.30 F 1-210 [» ]
2WDL X-ray 3.50 F 1-210 [» ]
2WDN X-ray 3.50 F 1-210 [» ]
2WH2 X-ray 3.45 F 1-210 [» ]
2WH4 X-ray 3.45 F 1-210 [» ]
2WRJ X-ray 3.60 F 1-210 [» ]
2WRL X-ray 3.60 F 1-210 [» ]
2WRO X-ray 3.60 F 1-210 [» ]
2WRR X-ray 3.60 F 1-210 [» ]
2X9S X-ray 3.10 F 1-210 [» ]
2X9U X-ray 3.10 F 1-210 [» ]
2XG0 X-ray 3.20 F 1-210 [» ]
2XG2 X-ray 3.20 F 1-210 [» ]
2XQE X-ray 3.10 F 1-210 [» ]
2XTG electron microscopy 7.80 F 1-210 [» ]
2XUX electron microscopy 7.60 F 1-210 [» ]
2Y0V X-ray 3.10 F 1-210 [» ]
2Y0X X-ray 3.10 F 1-210 [» ]
2Y0Z X-ray 3.10 F 1-210 [» ]
2Y11 X-ray 3.10 F 1-210 [» ]
2Y13 X-ray 3.10 F 1-210 [» ]
2Y15 X-ray 3.10 F 1-210 [» ]
2Y17 X-ray 3.10 F 1-210 [» ]
2Y19 X-ray 3.10 F 1-210 [» ]
3F1F X-ray 3.00 F 1-210 [» ]
3F1H X-ray 3.00 F 1-210 [» ]
3FIN electron microscopy 6.40 F 1-208 [» ]
3HUX X-ray 3.10 F 1-210 [» ]
3HUZ X-ray 3.10 F 1-210 [» ]
3I8F X-ray 3.10 F 1-210 [» ]
3I8I X-ray 3.10 F 1-210 [» ]
3I9C X-ray 3.50 F 1-210 [» ]
3I9E X-ray 3.50 F 1-210 [» ]
3KIR X-ray 3.30 F 1-210 [» ]
3KIT X-ray 3.30 F 1-210 [» ]
3KIW X-ray 3.60 F 1-210 [» ]
3KIY X-ray 3.60 F 1-210 [» ]
3KNI X-ray 3.00 F 1-210 [» ]
3KNK X-ray 3.00 F 1-210 [» ]
3KNM X-ray 3.45 F 1-210 [» ]
3KNO X-ray 3.45 F 1-210 [» ]
3OHJ X-ray 3.00 F 1-210 [» ]
3OHZ X-ray 3.00 F 1-210 [» ]
3OI5 X-ray 3.10 F 1-210 [» ]
3TVE X-ray 3.10 F 6-207 [» ]
3TVH X-ray 3.10 F 1-208 [» ]
3UXQ X-ray 3.20 F 6-210 [» ]
3UXR X-ray 3.20 F 6-210 [» ]
3UYE X-ray 3.00 F 1-210 [» ]
3UYG X-ray 3.00 F 1-210 [» ]
3UZ1 X-ray 3.30 F 1-210 [» ]
3UZ2 X-ray 3.30 F 1-210 [» ]
3UZ8 X-ray 3.00 F 1-210 [» ]
3UZ9 X-ray 3.00 F 1-210 [» ]
3UZF X-ray 3.30 F 1-210 [» ]
3UZH X-ray 3.30 F 1-210 [» ]
3UZK X-ray 3.30 F 1-210 [» ]
3UZN X-ray 3.30 F 1-210 [» ]
3V23 X-ray 3.00 F 1-210 [» ]
3V25 X-ray 3.00 F 1-210 [» ]
3V27 X-ray 3.10 F 1-210 [» ]
3V29 X-ray 3.10 F 1-210 [» ]
3V2D X-ray 2.70 F 1-210 [» ]
3V2F X-ray 2.70 F 1-210 [» ]
3V6W X-ray 3.90 F 1-210 [» ]
3V6X X-ray 3.90 F 1-210 [» ]
3ZN9 X-ray 3.10 F 1-210 [» ]
3ZNE X-ray 3.10 F 1-210 [» ]
3ZVP X-ray 3.80 F 1-210 [» ]
4ABS X-ray 3.10 F 1-210 [» ]
4B8G X-ray 3.70 F 1-210 [» ]
4B8I X-ray 3.70 F 1-210 [» ]
4BTD X-ray 2.95 F 1-210 [» ]
4BYC X-ray 3.35 F 1-210 [» ]
4BYE X-ray 3.35 F 1-210 [» ]
4DHA X-ray 3.20 F 1-210 [» ]
4DHC X-ray 3.20 F 1-210 [» ]
4EJB X-ray 3.52 F 1-210 [» ]
4EJC X-ray 3.52 F 1-210 [» ]
4G5L X-ray 3.30 F 1-210 [» ]
4G5N X-ray 3.30 F 1-210 [» ]
4G5U X-ray 3.10 F 1-210 [» ]
4G5W X-ray 3.10 F 1-210 [» ]
4JUX X-ray 2.86 F 1-210 [» ]
4K0M X-ray 3.30 F 1-207 [» ]
4K0Q X-ray 3.30 F 1-207 [» ]
4KX0 X-ray 3.44 F 1-210 [» ]
4KX2 X-ray 3.44 F 1-210 [» ]
4NVV X-ray 3.00 F 1-210 [» ]
4NVX X-ray 3.00 F 1-210 [» ]
4NVZ X-ray 3.10 F 1-210 [» ]
4NW1 X-ray 3.10 F 1-210 [» ]
4QCN X-ray 2.60 F 1-210 [» ]
4QCP X-ray 2.60 F 1-210 [» ]
4QCR X-ray 2.55 F 1-210 [» ]
4QCT X-ray 2.55 F 1-210 [» ]
4QCV X-ray 2.90 F 1-210 [» ]
4QCX X-ray 2.90 F 1-210 [» ]
4QCZ X-ray 2.80 F 1-210 [» ]
4QD1 X-ray 2.80 F 1-210 [» ]
4QJS X-ray 2.90 F 6-210 [» ]
4W2B X-ray 3.60 E 1-210 [» ]
4W2D X-ray 3.60 E 1-210 [» ]
ProteinModelPortali Q5SHN9.
SMRi Q5SHN9. Positions 3-210.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1691.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71514 ; BAD71514 ; BAD71514 .
GeneIDi 3167923.
KEGGi ttj:TTHA1691.
PATRICi 23958337. VBITheThe93045_1661.

Phylogenomic databases

eggNOGi COG0088.
HOGENOMi HOG000248767.
KOi K02926.
OMAi RSIMANQ.
OrthoDBi EOG6M0T9G.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-1730-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5SHN9.

Family and domain databases

Gene3Di 3.40.1370.10. 1 hit.
HAMAPi MF_01328_B. Ribosomal_L4_B.
InterProi IPR002136. Ribosomal_L4/L1e.
IPR013005. Ribosomal_L4/L1e_bac-type.
IPR023574. Ribosomal_L4_dom.
[Graphical view ]
PANTHERi PTHR10746. PTHR10746. 1 hit.
Pfami PF00573. Ribosomal_L4. 1 hit.
[Graphical view ]
SUPFAMi SSF52166. SSF52166. 1 hit.
TIGRFAMsi TIGR03953. rplD_bact. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Direct linkage of str-, S10- and spc-related gene clusters in Thermus thermophilus HB8, and sequences of ribosomal proteins L4 and S10."
    Pfeiffer T., Jorcke D., Feltens R., Hartmann R.K.
    Gene 167:141-145(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus."
    Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T.
    Biol. Chem. 381:1079-1087(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 6-17, BLOCKAGE OF N-TERMINUS.
  4. "On the structural and functional importance of the highly conserved Glu56 of Thermus thermophilus L4 ribosomal protein."
    Leontiadou F., Xaplanteri M.A., Papadopoulos G., Gerassimou C., Kalpaxis D.L., Choli-Papadopoulou T.
    J. Mol. Biol. 332:73-84(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-55 AND GLU-56.
  5. "Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry."
    Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.
    Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  6. "The path of messenger RNA through the ribosome."
    Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.
    Cell 106:233-241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.

Entry informationi

Entry nameiRL4_THET8
AccessioniPrimary (citable) accession number: Q5SHN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: November 26, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3