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Protein

60S ribosomal protein L21

Gene

RPL21

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

Functioni

Component of the large ribosomal subunit.1 Publication

GO - Molecular functioni

  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-9010553. Regulation of expression of SLITs and ROBOs.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L21
Alternative name(s):
Large ribosomal subunit protein eL211 Publication
Gene namesi
Name:RPL21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

EuPathDBiHostDB:ENSG00000122026.10.
HGNCiHGNC:10313. RPL21.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Involvement in diseasei

Hypotrichosis 12 (HYPT12)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of hypotrichosis, a condition characterized by the presence of less than the normal amount of hair and abnormal hair follicles and shafts, which are thin and atrophic. The extent of scalp and body hair involvement can be very variable, within as well as between families. HYPT12 patients have normal scalp hair density at birth. Hair loss begins during the first 6 months of life and gradually progresses to nearly complete loss of scalp hair. The remaining hairs grow slowly and are thin, sparse, dry, and fragile. Body hair, axillary and pubic hair, eyebrows and eyelashes are also sparse or absent.
See also OMIM:615885
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06603032R → Q in HYPT12; autosomal dominant. 1 PublicationCorresponds to variant dbSNP:rs587777527Ensembl.1

Keywords - Diseasei

Disease mutation, Hypotrichosis

Organism-specific databases

DisGeNETi6144.
MalaCardsiRPL21.
MIMi615885. phenotype.
OpenTargetsiENSG00000122026.
Orphaneti55654. Hypotrichosis simplex.
PharmGKBiPA34683.

Polymorphism and mutation databases

BioMutaiRPL21.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001496692 – 16060S ribosomal protein L21Add BLAST159

Proteomic databases

EPDiP46778.
PaxDbiP46778.
PeptideAtlasiP46778.
PRIDEiP46778.
TopDownProteomicsiP46778.

2D gel databases

SWISS-2DPAGEiP46778.

PTM databases

iPTMnetiP46778.
PhosphoSitePlusiP46778.
SwissPalmiP46778.

Expressioni

Gene expression databases

BgeeiENSG00000122026.
CleanExiHS_RPL21.
ExpressionAtlasiP46778. baseline and differential.
GenevisibleiP46778. HS.

Organism-specific databases

HPAiHPA047252.

Interactioni

Subunit structurei

Component of the large ribosomal subunit.1 Publication

Protein-protein interaction databases

BioGridi112064. 144 interactors.
CORUMiP46778.
IntActiP46778. 47 interactors.
MINTiMINT-3016420.
STRINGi9606.ENSP00000346027.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LT1-160[»]
4V6Xelectron microscopy5.00CT1-160[»]
5AJ0electron microscopy3.50AT1-160[»]
5LKSelectron microscopy3.60LT1-160[»]
5T2Celectron microscopy3.60N1-160[»]
ProteinModelPortaliP46778.
SMRiP46778.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1732. Eukaryota.
COG2139. LUCA.
GeneTreeiENSGT00390000001293.
HOVERGENiHBG001518.
InParanoidiP46778.
KOiK02889.
OMAiHVKHSKS.
OrthoDBiEOG091G0SNM.
PhylomeDBiP46778.
TreeFamiTF314640.

Family and domain databases

Gene3Di2.30.30.70. 1 hit.
InterProiView protein in InterPro
IPR036948. Ribosomal_L21_sf.
IPR001147. Ribosomal_L21e.
IPR018259. Ribosomal_L21e_CS.
IPR008991. Translation_prot_SH3-like_sf.
PANTHERiPTHR20981. PTHR20981. 1 hit.
PfamiView protein in Pfam
PF01157. Ribosomal_L21e. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
PROSITEiView protein in PROSITE
PS01171. RIBOSOMAL_L21E. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P46778-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNTKGKRRG TRYMFSRPFR KHGVVPLATY MRIYKKGDIV DIKGMGTVQK
60 70 80 90 100
GMPHKCYHGK TGRVYNVTQH AVGIVVNKQV KGKILAKRIN VRIEHIKHSK
110 120 130 140 150
SRDSFLKRVK ENDQKKKEAK EKGTWVQLKR QPAPPREAHF VRTNGKEPEL
160
LEPIPYEFMA
Length:160
Mass (Da):18,565
Last modified:January 23, 2007 - v2
Checksum:iC51D0B5E8EB9D69E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti72V → A in AAA93231 (PubMed:7581362).Curated1
Sequence conflicti78K → E in AAA93231 (PubMed:7581362).Curated1
Sequence conflicti104S → N in AAA93231 (PubMed:7581362).Curated1
Sequence conflicti112N → D in AAA93231 (PubMed:7581362).Curated1
Sequence conflicti115K → E in AAA93231 (PubMed:7581362).Curated1
Sequence conflicti120K → Q in AAA93231 (PubMed:7581362).Curated1
Sequence conflicti131Q → H in AAA80462 (PubMed:7951316).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03445915F → S. Corresponds to variant dbSNP:rs17085349Ensembl.1
Natural variantiVAR_06603032R → Q in HYPT12; autosomal dominant. 1 PublicationCorresponds to variant dbSNP:rs587777527Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89401 mRNA. Translation: CAA61582.1.
U14967 mRNA. Translation: AAA85655.1.
AB061826 Genomic DNA. Translation: BAB79464.1.
BC001603 mRNA. Translation: AAH01603.1.
BC007505 mRNA. Translation: AAH07505.1.
BC062981 mRNA. Translation: AAH62981.1.
BC070184 mRNA. Translation: AAH70184.1.
BC070323 mRNA. Translation: AAH70323.1.
BC070330 mRNA. Translation: AAH70330.1.
U25789 mRNA. Translation: AAA93231.1.
L38826 Genomic DNA. Translation: AAA80462.1.
AB007176 Genomic DNA. Translation: BAA25835.1.
CCDSiCCDS9320.1.
PIRiS55913.
RefSeqiNP_000973.2. NM_000982.3.
UniGeneiHs.381123.
Hs.535873.

Genome annotation databases

EnsembliENST00000272274; ENSP00000351021; ENSG00000122026.
ENST00000311549; ENSP00000346027; ENSG00000122026.
ENST00000319826; ENSP00000370574; ENSG00000122026.
ENST00000326092; ENSP00000370569; ENSG00000122026.
GeneIDi6144.
KEGGihsa:6144.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRL21_HUMAN
AccessioniPrimary (citable) accession number: P46778
Secondary accession number(s): Q16699
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 184 of the entry and version 2 of the sequence. See 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 13
    Human chromosome 13: 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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families