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Protein

60S ribosomal protein L12

Gene

RPL12

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

Functioni

Binds directly to 26S ribosomal RNA.By similarity

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  4. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  5. translation Source: UniProtKB
  6. translational elongation Source: Reactome
  7. translational initiation Source: Reactome
  8. translational termination Source: Reactome
  9. viral life cycle Source: Reactome
  10. viral process Source: Reactome
  11. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding

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 L12
Gene namesi
Name:RPL12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:10302. RPL12.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic large ribosomal subunit Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34665.

Polymorphism and mutation databases

BioMutaiRPL12.
DMDMi266921.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16516560S ribosomal protein L12PRO_0000104456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381Phosphoserine4 Publications
Modified residuei54 – 541N6-acetyllysine1 Publication
Modified residuei83 – 831N6-acetyllysine1 Publication
Modified residuei165 – 1651Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP30050.
PaxDbiP30050.
PRIDEiP30050.

2D gel databases

SWISS-2DPAGEP30050.

PTM databases

PhosphoSiteiP30050.

Expressioni

Gene expression databases

BgeeiP30050.
CleanExiHS_RPL12.
GenevestigatoriP30050.

Organism-specific databases

HPAiHPA003403.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CANXP278243EBI-352743,EBI-355947

Protein-protein interaction databases

BioGridi112056. 112 interactions.
IntActiP30050. 32 interactions.
MINTiMINT-2802291.
STRINGi9606.ENSP00000354739.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CK1-165[»]
ProteinModelPortaliP30050.
SMRiP30050. Positions 1-163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L11P family.Curated

Phylogenomic databases

eggNOGiCOG0080.
GeneTreeiENSGT00390000006922.
HOVERGENiHBG007231.
InParanoidiP30050.
KOiK02870.
OMAiGCTIDGR.
OrthoDBiEOG7JMGG9.
PhylomeDBiP30050.
TreeFamiTF300123.

Family and domain databases

Gene3Di1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPiMF_00736. Ribosomal_L11.
InterProiIPR000911. Ribosomal_L11/L12.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view]
PANTHERiPTHR11661. PTHR11661. 1 hit.
PfamiPF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]
SMARTiSM00649. RL11. 1 hit.
[Graphical view]
SUPFAMiSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
PROSITEiPS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P30050-1) [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

        10         20         30         40         50
MPPKFDPNEI KVVYLRCTGG EVGATSALAP KIGPLGLSPK KVGDDIAKAT
60 70 80 90 100
GDWKGLRITV KLTIQNRQAQ IEVVPSASAL IIKALKEPPR DRKKQKNIKH
110 120 130 140 150
SGNITFDEIV NIARQMRHRS LARELSGTIK EILGTAQSVG CNVDGRHPHD
160
IIDDINSGAV ECPAS
Length:165
Mass (Da):17,819
Last modified:April 1, 1993 - v1
Checksum:i7EFD783A8ED350F9
GO
Isoform 2 (identifier: P30050-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     38-70: Missing.

Note: No experimental confirmation available.

Show »
Length:132
Mass (Da):14,199
Checksum:i1FDF4BEF878AD5D5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei38 – 7033Missing in isoform 2. 1 PublicationVSP_034695Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06505 mRNA. Translation: AAA36157.1.
AL445222 Genomic DNA. Translation: CAH72929.1.
CH471090 Genomic DNA. Translation: EAW87669.1.
BC050644 mRNA. Translation: AAH50644.1.
BC059950 mRNA. Translation: AAH59950.1.
BC094831 mRNA. Translation: AAH94831.1.
BC105603 mRNA. Translation: AAI05604.1.
CCDSiCCDS6872.1. [P30050-1]
PIRiS35531.
RefSeqiNP_000967.1. NM_000976.3. [P30050-1]
UniGeneiHs.408054.

Genome annotation databases

EnsembliENST00000361436; ENSP00000354739; ENSG00000197958. [P30050-1]
ENST00000536368; ENSP00000441179; ENSG00000197958. [P30050-2]
GeneIDi6136.
KEGGihsa:6136.
UCSCiuc004bqy.2. human. [P30050-1]
uc004bqz.2. human. [P30050-2]

Polymorphism and mutation databases

BioMutaiRPL12.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06505 mRNA. Translation: AAA36157.1.
AL445222 Genomic DNA. Translation: CAH72929.1.
CH471090 Genomic DNA. Translation: EAW87669.1.
BC050644 mRNA. Translation: AAH50644.1.
BC059950 mRNA. Translation: AAH59950.1.
BC094831 mRNA. Translation: AAH94831.1.
BC105603 mRNA. Translation: AAI05604.1.
CCDSiCCDS6872.1. [P30050-1]
PIRiS35531.
RefSeqiNP_000967.1. NM_000976.3. [P30050-1]
UniGeneiHs.408054.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CK1-165[»]
ProteinModelPortaliP30050.
SMRiP30050. Positions 1-163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112056. 112 interactions.
IntActiP30050. 32 interactions.
MINTiMINT-2802291.
STRINGi9606.ENSP00000354739.

PTM databases

PhosphoSiteiP30050.

Polymorphism and mutation databases

BioMutaiRPL12.
DMDMi266921.

2D gel databases

SWISS-2DPAGEP30050.

Proteomic databases

MaxQBiP30050.
PaxDbiP30050.
PRIDEiP30050.

Protocols and materials databases

DNASUi6136.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361436; ENSP00000354739; ENSG00000197958. [P30050-1]
ENST00000536368; ENSP00000441179; ENSG00000197958. [P30050-2]
GeneIDi6136.
KEGGihsa:6136.
UCSCiuc004bqy.2. human. [P30050-1]
uc004bqz.2. human. [P30050-2]

Organism-specific databases

CTDi6136.
GeneCardsiGC09M130209.
H-InvDBHIX0170298.
HGNCiHGNC:10302. RPL12.
HPAiHPA003403.
MIMi180475. gene.
neXtProtiNX_P30050.
PharmGKBiPA34665.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0080.
GeneTreeiENSGT00390000006922.
HOVERGENiHBG007231.
InParanoidiP30050.
KOiK02870.
OMAiGCTIDGR.
OrthoDBiEOG7JMGG9.
PhylomeDBiP30050.
TreeFamiTF300123.

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

ChiTaRSiRPL12. human.
GeneWikiiRPL12.
GenomeRNAii6136.
NextBioi23835.
PROiP30050.
SOURCEiSearch...

Gene expression databases

BgeeiP30050.
CleanExiHS_RPL12.
GenevestigatoriP30050.

Family and domain databases

Gene3Di1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPiMF_00736. Ribosomal_L11.
InterProiIPR000911. Ribosomal_L11/L12.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view]
PANTHERiPTHR11661. PTHR11661. 1 hit.
PfamiPF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]
SMARTiSM00649. RL11. 1 hit.
[Graphical view]
SUPFAMiSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
PROSITEiPS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of human ribosomal protein L12."
    Chu W., Presky D.H., Swerlisk R.A., Burns D.K.
    Nucleic Acids Res. 21:749-749(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 2).
    Tissue: Ovary.
  5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-54 AND LYS-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRL12_HUMAN
AccessioniPrimary (citable) accession number: P30050
Secondary accession number(s): Q5VVV2, Q6PB27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 29, 2015
This is version 147 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 9
    Human chromosome 9: 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.