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P05386 (RLA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 139. 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.
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

P1 and P2 exist as dimers at the large ribosomal subunit.

Sequence similarities

Belongs to the ribosomal protein L12P family.

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

Chain1 – 11411460S acidic ribosomal protein P1 HAMAP-Rule MF_01478
PRO_0000157686

Amino acid modifications

Modified residue1011Phosphoserine Ref.6 Ref.7
Modified residue1041Phosphoserine By similarity

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, MASS SPECTROMETRY.
Tissue: Pituitary.
[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].
+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.
IPIIPI00008527.
IPI00412779.
PIRR6HUP1. B27125.
RefSeqNP_000994.1. NM_001003.2.
NP_998890.1. NM_213725.1.
UniGeneHs.356502.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LBFNMR-A1-69[»]
ProteinModelPortalP05386.
ModBaseSearch...

Protein-protein interaction databases

IntActP05386. 37 interactions.
MINTMINT-193188.
STRING9606.ENSP00000346037.

PTM databases

PhosphoSiteP05386.

Polymorphism databases

DMDM133051.

Proteomic databases

PaxDbP05386.
PRIDEP05386.

Protocols and materials databases

DNASU6176.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260379; ENSP00000346037; ENSG00000137818.
ENST00000357790; ENSP00000350437; ENSG00000137818.
GeneID6176.
KEGGhsa:6176.
UCSCuc002asd.1. human.
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.
OMADVEPYWP.
OrthoDBEOG44J2KS.
PhylomeDBP05386.

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

ArrayExpressP05386.
BgeeP05386.
CleanExHS_RPLP1.
HS_RRP1.
GenevestigatorP05386.
GermOnlineENSG00000137818. Homo sapiens.

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.
GenomeRNAi6176.
NextBio23995.
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: May 29, 2013
This is version 139 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

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 15

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families