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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

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L21
Gene namesi
Name:RPL21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:10313. RPL21.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: HPA
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321R → Q in HYPT12; autosomal dominant. 1 Publication
VAR_066030

Keywords - Diseasei

Disease mutation, Hypotrichosis

Organism-specific databases

MIMi615885. phenotype.
Orphaneti55654. Hypotrichosis simplex.
PharmGKBiPA34683.

Polymorphism and mutation databases

BioMutaiRPL21.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 16015960S ribosomal protein L21PRO_0000149669Add
BLAST

Proteomic databases

MaxQBiP46778.
PaxDbiP46778.
PRIDEiP46778.

2D gel databases

SWISS-2DPAGEP46778.

PTM databases

PhosphoSiteiP46778.

Expressioni

Gene expression databases

BgeeiP46778.
CleanExiHS_RPL21.
ExpressionAtlasiP46778. baseline.
GenevisibleiP46778. HS.

Organism-specific databases

HPAiHPA047252.

Interactioni

Protein-protein interaction databases

BioGridi112064. 118 interactions.
IntActiP46778. 28 interactions.
MINTiMINT-3016420.
STRINGi9606.ENSP00000346027.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CT1-160[»]
ProteinModelPortaliP46778.
SMRiP46778. Positions 4-99.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L21e family.Curated

Phylogenomic databases

eggNOGiCOG2139.
HOVERGENiHBG001518.
InParanoidiP46778.
KOiK02889.
OMAiGTGTIQK.
PhylomeDBiP46778.
TreeFamiTF314640.

Family and domain databases

Gene3Di2.30.30.70. 1 hit.
InterProiIPR001147. Ribosomal_L21e.
IPR018259. Ribosomal_L21e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR20981. PTHR20981. 1 hit.
PfamiPF01157. Ribosomal_L21e. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
PROSITEiPS01171. RIBOSOMAL_L21E. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721V → A in AAA93231 (PubMed:7581362).Curated
Sequence conflicti78 – 781K → E in AAA93231 (PubMed:7581362).Curated
Sequence conflicti104 – 1041S → N in AAA93231 (PubMed:7581362).Curated
Sequence conflicti112 – 1121N → D in AAA93231 (PubMed:7581362).Curated
Sequence conflicti115 – 1151K → E in AAA93231 (PubMed:7581362).Curated
Sequence conflicti120 – 1201K → Q in AAA93231 (PubMed:7581362).Curated
Sequence conflicti131 – 1311Q → H in AAA80462 (PubMed:7951316).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151F → S.
Corresponds to variant rs17085349 [ dbSNP | Ensembl ].
VAR_034459
Natural varianti32 – 321R → Q in HYPT12; autosomal dominant. 1 Publication
VAR_066030

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.
UCSCiuc001uqz.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CT1-160[»]
ProteinModelPortaliP46778.
SMRiP46778. Positions 4-99.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112064. 118 interactions.
IntActiP46778. 28 interactions.
MINTiMINT-3016420.
STRINGi9606.ENSP00000346027.

PTM databases

PhosphoSiteiP46778.

Polymorphism and mutation databases

BioMutaiRPL21.

2D gel databases

SWISS-2DPAGEP46778.

Proteomic databases

MaxQBiP46778.
PaxDbiP46778.
PRIDEiP46778.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272274; ENSP00000351021; ENSG00000122026.
ENST00000311549; ENSP00000346027; ENSG00000122026.
ENST00000319826; ENSP00000370574; ENSG00000122026.
ENST00000326092; ENSP00000370569; ENSG00000122026.
GeneIDi6144.
KEGGihsa:6144.
UCSCiuc001uqz.1. human.

Organism-specific databases

CTDi6144.
GeneCardsiGC13P027827.
H-InvDBHIX0096689.
HGNCiHGNC:10313. RPL21.
HPAiHPA047252.
MIMi603636. gene.
615885. phenotype.
neXtProtiNX_P46778.
Orphaneti55654. Hypotrichosis simplex.
PharmGKBiPA34683.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2139.
HOVERGENiHBG001518.
InParanoidiP46778.
KOiK02889.
OMAiGTGTIQK.
PhylomeDBiP46778.
TreeFamiTF314640.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPL21. human.
GeneWikiiRPL21.
GenomeRNAii6144.
NextBioi23871.
PROiP46778.
SOURCEiSearch...

Gene expression databases

BgeeiP46778.
CleanExiHS_RPL21.
ExpressionAtlasiP46778. baseline.
GenevisibleiP46778. HS.

Family and domain databases

Gene3Di2.30.30.70. 1 hit.
InterProiIPR001147. Ribosomal_L21e.
IPR018259. Ribosomal_L21e_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR20981. PTHR20981. 1 hit.
PfamiPF01157. Ribosomal_L21e. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
PROSITEiPS01171. RIBOSOMAL_L21E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: INVOLVEMENT IN HYPT12, VARIANT HYPT12 GLN-32.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL21_HUMAN
AccessioniPrimary (citable) accession number: P46778
Secondary accession number(s): Q16699
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 159 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

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 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.