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P05386 (RLA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S acidic ribosomal protein P1
Gene names
Name:RPLP1
Synonyms:RRP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length114 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the elongation step of protein synthesis. HAMAP-Rule MF_01478

Subunit structure

Heterodimer with RPLP2 at the lateral ribosomal stalk of the large ribosomal subunit. Ref.11

Sequence similarities

Belongs to the ribosomal protein L12P family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
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 PubMed 12962325. 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 PubMed 12962325. Source: UniProtKB

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 12054647. Source: UniProtKB

structural constituent of ribosome

Non-traceable author statement PubMed 12962325. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05386-1)

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.
Isoform 2 (identifier: P05386-2)

The sequence of this isoform differs from the canonical sequence as follows:
     25-49: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 11411360S acidic ribosomal protein P1 HAMAP-Rule MF_01478
PRO_0000157686

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.10
Modified residue1011Phosphoserine Ref.6 Ref.7

Natural variations

Alternative sequence25 – 4925Missing in isoform 2.
VSP_045244

Secondary structure

........... 114
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 4C282AB8DCA079C8

FASTA11411,514
        10         20         30         40         50         60 
MASVSELACI YSALILHDDE VTVTEDKINA LIKAAGVNVE PFWPGLFAKA LANVNIGSLI 

        70         80         90        100        110 
CNVGAGGPAP AAGAAPAGGP APSTAAAPAE EKKVEAKKEE SEESDDDMGF GLFD 

« Hide

Isoform 2 [UniParc].

Checksum: B84B9045B930348B
Show »

FASTA898,804

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
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]"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].
[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]"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) OF 80S RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10233.1. [P05386-1]
CCDS10234.1. [P05386-2]
PIRR6HUP1. B27125.
RefSeqNP_000994.1. NM_001003.2. [P05386-1]
NP_998890.1. NM_213725.1. [P05386-2]
UniGeneHs.356502.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LBFNMR-A1-69[»]
3J3Belectron microscopy5.00s/t1-114[»]
4BEHNMR-A1-114[»]
ProteinModelPortalP05386.
SMRP05386. Positions 1-114.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112095. 103 interactions.
IntActP05386. 49 interactions.
MINTMINT-193188.
STRING9606.ENSP00000346037.

PTM databases

PhosphoSiteP05386.

Proteomic databases

MaxQBP05386.
PaxDbP05386.
PRIDEP05386.

Protocols and materials databases

DNASU6176.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260379; ENSP00000346037; ENSG00000137818. [P05386-1]
ENST00000357790; ENSP00000350437; ENSG00000137818. [P05386-2]
GeneID6176.
KEGGhsa:6176.
UCSCuc002asd.1. human. [P05386-1]
uc002ase.1. human.

Organism-specific databases

CTD6176.
GeneCardsGC15P069745.
HGNCHGNC:10372. RPLP1.
HPAHPA003368.
MIM180520. gene.
neXtProtNX_P05386.
PharmGKBPA34775.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2058.
HOGENOMHOG000229898.
HOVERGENHBG002291.
InParanoidP05386.
KOK02942.
OMATSELACI.
OrthoDBEOG7M0NVC.
PhylomeDBP05386.
TreeFamTF312932.

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

BgeeP05386.
CleanExHS_RPLP1.
HS_RRP1.
GenevestigatorP05386.

Family and domain databases

HAMAPMF_01478. Ribosomal_L12_arch.
InterProIPR001813. Ribosomal_L10/L12.
IPR027534. Ribosomal_L12.
[Graphical view]
PfamPF00428. Ribosomal_60s. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRpLP1. human.
GeneWikiRPLP1.
GenomeRNAi6176.
NextBio23995.
PROP05386.
SOURCESearch...

Entry information

Entry nameRLA1_HUMAN
AccessionPrimary (citable) accession number: P05386
Secondary accession number(s): A6NIB2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: July 9, 2014
This is version 151 of the entry and version 1 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 chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM