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Protein

60S ribosomal protein L38

Gene

RPL38

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

Functioni

GO - Molecular functioni

  • 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 L38
Gene namesi
Name:RPL38
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10349. RPL38.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • eukaryotic 80S initiation complex Source: Ensembl
  • focal adhesion Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34741.

Polymorphism and mutation databases

DMDMi52783779.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 706960S ribosomal protein L38PRO_0000215434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysine1 Publication
Modified residuei67 – 671N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP63173.
PaxDbiP63173.
PRIDEiP63173.

PTM databases

PhosphoSiteiP63173.

Expressioni

Gene expression databases

BgeeiP63173.
CleanExiHS_RPL38.
ExpressionAtlasiP63173. baseline and differential.
GenevisibleiP63173. HS.

Organism-specific databases

HPAiHPA052543.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NME2P223921EBI-359141,EBI-713693
RIPK2O433531EBI-359141,EBI-358522
TFE3P195321EBI-359141,EBI-1048957

Protein-protein interaction databases

BioGridi112088. 76 interactions.
IntActiP63173. 12 interactions.
MINTiMINT-5002686.
STRINGi9606.ENSP00000309830.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Ck1-70[»]
5AJ0electron microscopy3.50Ak1-70[»]
ProteinModelPortaliP63173.
SMRiP63173. Positions 2-70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L38e family.Curated

Phylogenomic databases

eggNOGiNOG323549.
GeneTreeiENSGT00390000003718.
HOGENOMiHOG000188979.
HOVERGENiHBG001013.
InParanoidiP63173.
KOiK02923.
OMAiLYTLVIQ.
OrthoDBiEOG79W98H.
PhylomeDBiP63173.
TreeFamiTF300215.

Family and domain databases

InterProiIPR002675. Ribosomal_L38e.
[Graphical view]
PANTHERiPTHR10965. PTHR10965. 1 hit.
PfamiPF01781. Ribosomal_L38e. 1 hit.
[Graphical view]
ProDomiPD010361. Ribosomal_L38e. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

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

P63173-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRKIEEIKD FLLTARRKDA KSVKIKKNKD NVKFKVRCSR YLYTLVITDK
60 70
EKAEKLKQSL PPGLAVKELK
Length:70
Mass (Da):8,218
Last modified:January 23, 2007 - v2
Checksum:iFDD9A107BC98DBBA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26876 mRNA. Translation: CAA81488.1.
AK312119 mRNA. Translation: BAG35055.1.
CH471099 Genomic DNA. Translation: EAW89137.1.
BC000603 mRNA. Translation: AAH00603.1.
AB007185 Genomic DNA. Translation: BAA25844.1.
CCDSiCCDS11696.1.
PIRiS38385.
RefSeqiNP_000990.1. NM_000999.3.
NP_001030335.1. NM_001035258.1.
UniGeneiHs.380953.

Genome annotation databases

EnsembliENST00000311111; ENSP00000309830; ENSG00000172809.
ENST00000439590; ENSP00000390279; ENSG00000172809.
ENST00000533498; ENSP00000434243; ENSG00000172809.
GeneIDi6169.
KEGGihsa:6169.
UCSCiuc002jjz.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26876 mRNA. Translation: CAA81488.1.
AK312119 mRNA. Translation: BAG35055.1.
CH471099 Genomic DNA. Translation: EAW89137.1.
BC000603 mRNA. Translation: AAH00603.1.
AB007185 Genomic DNA. Translation: BAA25844.1.
CCDSiCCDS11696.1.
PIRiS38385.
RefSeqiNP_000990.1. NM_000999.3.
NP_001030335.1. NM_001035258.1.
UniGeneiHs.380953.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Ck1-70[»]
5AJ0electron microscopy3.50Ak1-70[»]
ProteinModelPortaliP63173.
SMRiP63173. Positions 2-70.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112088. 76 interactions.
IntActiP63173. 12 interactions.
MINTiMINT-5002686.
STRINGi9606.ENSP00000309830.

PTM databases

PhosphoSiteiP63173.

Polymorphism and mutation databases

DMDMi52783779.

Proteomic databases

MaxQBiP63173.
PaxDbiP63173.
PRIDEiP63173.

Protocols and materials databases

DNASUi6169.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311111; ENSP00000309830; ENSG00000172809.
ENST00000439590; ENSP00000390279; ENSG00000172809.
ENST00000533498; ENSP00000434243; ENSG00000172809.
GeneIDi6169.
KEGGihsa:6169.
UCSCiuc002jjz.3. human.

Organism-specific databases

CTDi6169.
GeneCardsiGC17P072202.
HGNCiHGNC:10349. RPL38.
HPAiHPA052543.
MIMi604182. gene.
neXtProtiNX_P63173.
PharmGKBiPA34741.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG323549.
GeneTreeiENSGT00390000003718.
HOGENOMiHOG000188979.
HOVERGENiHBG001013.
InParanoidiP63173.
KOiK02923.
OMAiLYTLVIQ.
OrthoDBiEOG79W98H.
PhylomeDBiP63173.
TreeFamiTF300215.

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

ChiTaRSiRPL38. human.
GeneWikii60S_ribosomal_protein_L38.
GenomeRNAii6169.
NextBioi23965.
PROiP63173.
SOURCEiSearch...

Gene expression databases

BgeeiP63173.
CleanExiHS_RPL38.
ExpressionAtlasiP63173. baseline and differential.
GenevisibleiP63173. HS.

Family and domain databases

InterProiIPR002675. Ribosomal_L38e.
[Graphical view]
PANTHERiPTHR10965. PTHR10965. 1 hit.
PfamiPF01781. Ribosomal_L38e. 1 hit.
[Graphical view]
ProDomiPD010361. Ribosomal_L38e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary sequence of the human, lysine-rich, ribosomal protein RPL38 and detection of an unusual RPL38 processed pseudogene in the promoter region of the type-1 angiotensin II receptor gene."
    Espinosa L., Martin M., Nicolas A., Fabre M., Navarro E.
    Biochim. Biophys. Acta 1354:58-64(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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: Skin.
  5. "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 34-70.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL38_HUMAN
AccessioniPrimary (citable) accession number: P63173
Secondary accession number(s): B2R5A8, P23411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 107 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, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. 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.