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P05386

- RLA1_HUMAN

UniProt

P05386 - RLA1_HUMAN

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Protein
60S acidic ribosomal protein P1
Gene
RPLP1, RRP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays an important role in the elongation step of protein synthesis.UniRule annotation

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. protein binding Source: UniProtKB
  3. structural constituent of ribosome Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  3. cellular protein metabolic process Source: Reactome
  4. gene expression Source: Reactome
  5. mRNA metabolic process Source: Reactome
  6. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  7. translation Source: UniProtKB
  8. translational elongation Source: Reactome
  9. translational initiation Source: Reactome
  10. translational termination Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
  13. viral transcription Source: Reactome
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 acidic ribosomal protein P1
Gene namesi
Name:RPLP1
Synonyms:RRP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:10372. RPLP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. cytosolic large ribosomal subunit Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34775.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11411360S acidic ribosomal protein P1UniRule annotation
PRO_0000157686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei101 – 1011Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05386.
PaxDbiP05386.
PRIDEiP05386.

PTM databases

PhosphoSiteiP05386.

Expressioni

Gene expression databases

BgeeiP05386.
CleanExiHS_RPLP1.
HS_RRP1.
GenevestigatoriP05386.

Organism-specific databases

HPAiHPA003368.

Interactioni

Subunit structurei

Heterodimer with RPLP2 at the lateral ribosomal stalk of the large ribosomal subunit.1 Publication

Protein-protein interaction databases

BioGridi112095. 96 interactions.
IntActiP05386. 49 interactions.
MINTiMINT-193188.
STRINGi9606.ENSP00000346037.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1916
Helixi25 – 3511
Helixi42 – 509
Turni51 – 533
Helixi56 – 605
Turni61 – 644

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LBFNMR-A1-69[»]
3J3Belectron microscopy5.00s/t1-114[»]
4BEHNMR-A1-114[»]
ProteinModelPortaliP05386.
SMRiP05386. Positions 1-114.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2058.
HOGENOMiHOG000229898.
HOVERGENiHBG002291.
InParanoidiP05386.
KOiK02942.
OMAiTSELACI.
OrthoDBiEOG7M0NVC.
PhylomeDBiP05386.
TreeFamiTF312932.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR001813. Ribosomal_L10/L12.
IPR027534. Ribosomal_L12.
[Graphical view]
PfamiPF00428. Ribosomal_60s. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P05386-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MASVSELACI YSALILHDDE VTVTEDKINA LIKAAGVNVE PFWPGLFAKA    50
LANVNIGSLI CNVGAGGPAP AAGAAPAGGP APSTAAAPAE EKKVEAKKEE 100
SEESDDDMGF GLFD 114
Length:114
Mass (Da):11,514
Last modified:November 1, 1988 - v1
Checksum:i4C282AB8DCA079C8
GO
Isoform 2 (identifier: P05386-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     25-49: Missing.

Note: No experimental confirmation available.

Show »
Length:89
Mass (Da):8,804
Checksum:iB84B9045B930348B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei25 – 4925Missing in isoform 2.
VSP_045244Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M17886 mRNA. Translation: AAA36471.1.
AB061836 Genomic DNA. Translation: BAB79474.1.
AC027237 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77845.1.
BC003369 mRNA. Translation: AAH03369.1.
BC007590 mRNA. Translation: AAH07590.1.
CD388103 mRNA. No translation available.
CCDSiCCDS10233.1. [P05386-1]
CCDS10234.1. [P05386-2]
PIRiB27125. R6HUP1.
RefSeqiNP_000994.1. NM_001003.2. [P05386-1]
NP_998890.1. NM_213725.1. [P05386-2]
UniGeneiHs.356502.

Genome annotation databases

EnsembliENST00000260379; ENSP00000346037; ENSG00000137818. [P05386-1]
ENST00000357790; ENSP00000350437; ENSG00000137818. [P05386-2]
GeneIDi6176.
KEGGihsa:6176.
UCSCiuc002asd.1. human. [P05386-1]
uc002ase.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M17886 mRNA. Translation: AAA36471.1 .
AB061836 Genomic DNA. Translation: BAB79474.1 .
AC027237 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77845.1 .
BC003369 mRNA. Translation: AAH03369.1 .
BC007590 mRNA. Translation: AAH07590.1 .
CD388103 mRNA. No translation available.
CCDSi CCDS10233.1. [P05386-1 ]
CCDS10234.1. [P05386-2 ]
PIRi B27125. R6HUP1.
RefSeqi NP_000994.1. NM_001003.2. [P05386-1 ]
NP_998890.1. NM_213725.1. [P05386-2 ]
UniGenei Hs.356502.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LBF NMR - A 1-69 [» ]
3J3B electron microscopy 5.00 s/t 1-114 [» ]
4BEH NMR - A 1-114 [» ]
ProteinModelPortali P05386.
SMRi P05386. Positions 1-114.
ModBasei Search...

Protein-protein interaction databases

BioGridi 112095. 96 interactions.
IntActi P05386. 49 interactions.
MINTi MINT-193188.
STRINGi 9606.ENSP00000346037.

PTM databases

PhosphoSitei P05386.

Proteomic databases

MaxQBi P05386.
PaxDbi P05386.
PRIDEi P05386.

Protocols and materials databases

DNASUi 6176.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260379 ; ENSP00000346037 ; ENSG00000137818 . [P05386-1 ]
ENST00000357790 ; ENSP00000350437 ; ENSG00000137818 . [P05386-2 ]
GeneIDi 6176.
KEGGi hsa:6176.
UCSCi uc002asd.1. human. [P05386-1 ]
uc002ase.1. human.

Organism-specific databases

CTDi 6176.
GeneCardsi GC15P069745.
HGNCi HGNC:10372. RPLP1.
HPAi HPA003368.
MIMi 180520. gene.
neXtProti NX_P05386.
PharmGKBi PA34775.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2058.
HOGENOMi HOG000229898.
HOVERGENi HBG002291.
InParanoidi P05386.
KOi K02942.
OMAi TSELACI.
OrthoDBi EOG7M0NVC.
PhylomeDBi P05386.
TreeFami TF312932.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi RpLP1. human.
GeneWikii RPLP1.
GenomeRNAii 6176.
NextBioi 23995.
PROi P05386.
SOURCEi Search...

Gene expression databases

Bgeei P05386.
CleanExi HS_RPLP1.
HS_RRP1.
Genevestigatori P05386.

Family and domain databases

HAMAPi MF_01478. Ribosomal_L12_arch.
InterProi IPR001813. Ribosomal_L10/L12.
IPR027534. Ribosomal_L12.
[Graphical view ]
Pfami PF00428. Ribosomal_60s. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly."
    Rich B.E., Steitz J.A.
    Mol. Cell. Biol. 7:4065-4074(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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].
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Eye, Placenta and Trophoblast.
  6. "Identification and characterization of phosphorylated proteins in the human pituitary."
    Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.
    Proteomics 4:587-598(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-101.
    Tissue: Pituitary.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex."
    Lee K.M., Yu C.W., Chiu T.Y., Sze K.H., Shaw P.C., Wong K.B.
    Nucleic Acids Res. 40:3172-3182(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-69, SUBUNIT.
  12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRLA1_HUMAN
AccessioniPrimary (citable) accession number: P05386
Secondary accession number(s): A6NIB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: September 3, 2014
This is version 152 of the entry and version 1 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 15
    Human chromosome 15: 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

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