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P46778 (RL21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
60S ribosomal protein L21
Gene names
Name:RPL21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Involvement in disease

Defects in RPL21 are a cause of generalized hypotrichosis simplex (HTS). A rare form of non-syndromic hereditary hypotrichosis without characteristic hair shaft anomalies. Affected individuals typically show normal hair at birth, but hair loss and thinning of the hair shaft start during early childhood and progress with age. Ref.11

Sequence similarities

Belongs to the ribosomal protein L21e family.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Hypotrichosis
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

translation

Non-traceable author statement Ref.7. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay Ref.7. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

structural constituent of ribosome

Non-traceable author statement Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 16015960S ribosomal protein L21
PRO_0000149669

Natural variations

Natural variant151F → S.
Corresponds to variant rs17085349 [ dbSNP | Ensembl ].
VAR_034459
Natural variant321R → Q in HTS. Ref.11
VAR_066030

Experimental info

Sequence conflict721V → A in AAA93231. Ref.2
Sequence conflict781K → E in AAA93231. Ref.2
Sequence conflict1041S → N in AAA93231. Ref.2
Sequence conflict1121N → D in AAA93231. Ref.2
Sequence conflict1151K → E in AAA93231. Ref.2
Sequence conflict1201K → Q in AAA93231. Ref.2
Sequence conflict1311Q → H in AAA80462. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P46778 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C51D0B5E8EB9D69E

FASTA16018,565
        10         20         30         40         50         60 
MTNTKGKRRG TRYMFSRPFR KHGVVPLATY MRIYKKGDIV DIKGMGTVQK GMPHKCYHGK 

        70         80         90        100        110        120 
TGRVYNVTQH AVGIVVNKQV KGKILAKRIN VRIEHIKHSK SRDSFLKRVK ENDQKKKEAK 

       130        140        150        160 
EKGTWVQLKR QPAPPREAHF VRTNGKEPEL LEPIPYEFMA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Colon.
[2]"Comparison of the positional cloning methods used to isolate the BRCA1 gene."
Harshman K., Bell R., Rosenthal J., Katcher H., Miki Y., Swenson J., Gholami Z., Frye C., Ding W., Dayananth P., Eddington K., Norris F.H., Bristow P.K., Phelps R., Hattier T., Stone S., Shaffer D., Bayer S. expand/collapse author list , Hussey C., Tran T., Lai M., Rosteck P.R. Jr., Skolnick M.H., Shattuck-Eidens D., Kamb A.
Hum. Mol. Genet. 4:1259-1266(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [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].
Tissue: Brain, Lymph, Muscle, Pancreas, Prostate and Testis.
[5]"A physical map and candidate genes in the BRCA1 region on chromosome 17q12-21."
Albertsen H.M., Smith S.A., Mazoyer S., Fujimoto E., Stevens J., Williams B., Rodriguez P., Cropp C.S., Slijepcevic P., Carlson M., Robertson M., Bradley P., Lawrence E., Harrington T., Sheng Z.M., Hoopes R., Sternberg N., Brothman A. expand/collapse author list , Callahan R., Ponder B.A.J., White R.
Nat. Genet. 7:472-479(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-160.
Tissue: Brain.
[6]"A map of 75 human ribosomal protein genes."
Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 124-154.
[7]"Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-15, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
[11]"Mutation in ribosomal protein L21 underlies hereditary hypotrichosis simplex."
Zhou C., Zang D., Jin Y., Wu H., Liu Z., Du J., Zhang J.
Hum. Mutat. 32:710-714(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HTS GLN-32.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS55913.
RefSeqNP_000973.2. NM_000982.3.
UniGeneHs.381123.
Hs.535873.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00T1-160[»]
ProteinModelPortalP46778.
SMRP46778. Positions 2-160.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112064. 118 interactions.
IntActP46778. 27 interactions.
MINTMINT-3016420.
STRING9606.ENSP00000346027.

PTM databases

PhosphoSiteP46778.

2D gel databases

SWISS-2DPAGEP46778.

Proteomic databases

PaxDbP46778.
PRIDEP46778.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272274; ENSP00000351021; ENSG00000122026.
ENST00000311549; ENSP00000346027; ENSG00000122026.
ENST00000319826; ENSP00000370574; ENSG00000122026.
ENST00000326092; ENSP00000370569; ENSG00000122026.
GeneID6144.
KEGGhsa:6144.
UCSCuc001uqz.1. human.

Organism-specific databases

CTD6144.
GeneCardsGC13P027827.
H-InvDBHIX0096689.
HGNCHGNC:10313. RPL21.
HPAHPA047252.
MIM603636. gene.
neXtProtNX_P46778.
Orphanet55654. Hypotrichosis simplex.
PharmGKBPA34683.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2139.
HOVERGENHBG001518.
InParanoidP46778.
KOK02889.
OMAGTGTIQK.
PhylomeDBP46778.
TreeFamTF314640.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

BgeeP46778.
CleanExHS_RPL21.
GenevestigatorP46778.

Family and domain databases

Gene3D2.30.30.70. 1 hit.
InterProIPR001147. Ribosomal_L21e.
IPR018259. Ribosomal_L21e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERPTHR20981. PTHR20981. 1 hit.
PfamPF01157. Ribosomal_L21e. 1 hit.
[Graphical view]
SUPFAMSSF50104. SSF50104. 1 hit.
PROSITEPS01171. RIBOSOMAL_L21E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL21. human.
GeneWikiRPL21.
GenomeRNAi6144.
NextBio23871.
PROP46778.
SOURCESearch...

Entry information

Entry nameRL21_HUMAN
AccessionPrimary (citable) accession number: P46778
Secondary accession number(s): Q16699
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 148 of the entry and version 2 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

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 13

Human chromosome 13: entries, gene names and cross-references to MIM