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P27635 (RL10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L10
Alternative name(s):
Laminin receptor homolog
Protein QM
Tumor suppressor QM
Gene names
Name:RPL10
Synonyms:DXS648E, QM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S).

Developmental stage

Down-regulated during adipocyte, kidney, and heart differentiation.

Post-translational modification

Citrullinated by PADI4 By similarity.

Involvement in disease

Autism, X-linked 5 (AUTSX5) [MIM:300847]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. RPL10 is involved in autism only in rare cases. Two hypomorphic variants affecting the translation process have been found in families with autism spectrum disorders, suggesting that aberrant translation may play a role in disease mechanisms. Ref.18 Ref.19

Sequence similarities

Belongs to the ribosomal protein L10e family.

Sequence caution

The sequence AAB22173.1 differs from that shown. Reason: Frameshift at position 124.

The sequence CAM45852.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAM45853.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMCitrullination
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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 Ref.15. 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_componentcytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay Ref.15. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay. Source: LIFEdb

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16741966. Source: IntAct

structural constituent of ribosome

Non-traceable author statement Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SRCP129316EBI-352398,EBI-621482

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 21421360S ribosomal protein L10
PRO_0000147105

Amino acid modifications

Modified residue321Citrulline By similarity
Cross-link188Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Natural variant2021N → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.14
Corresponds to variant rs12012747 [ dbSNP | Ensembl ].
VAR_006922
Natural variant2061L → M in AUTSX5. Ref.18
VAR_027795
Natural variant2131H → Q in AUTSX5. Ref.18 Ref.19
VAR_027796

Experimental info

Sequence conflict231Missing in AAL88713. Ref.5
Sequence conflict1571F → L in BAD97029. Ref.8

Secondary structure

..................... 214
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27635 [UniParc].

Last modified June 12, 2007. Version 4.
Checksum: 0860CECC91DF74FE

FASTA21424,604
        10         20         30         40         50         60 
MGRRPARCYR YCKNKPYPKS RFCRGVPDAK IRIFDLGRKK AKVDEFPLCG HMVSDEYEQL 

        70         80         90        100        110        120 
SSEALEAARI CANKYMVKSC GKDGFHIRVR LHPFHVIRIN KMLSCAGADR LQTGMRGAFG 

       130        140        150        160        170        180 
KPQGTVARVH IGQVIMSIRT KLQNKEHVIE ALRRAKFKFP GRQKIHISKK WGFTKFNADE 

       190        200        210 
FEDMVAEKRL IPDGCGVKYI PNRGPLDKWR ALHS 

« Hide

References

« Hide 'large scale' references
[1]"The isolation and characterization of a novel cDNA demonstrating an altered mRNA level in nontumorigenic Wilms' microcell hybrid cells."
Dowdy S.F., Lai K.M., Weissman B.E., Matsui Y., Hogan B.L.M., Stanbridge E.S.
Nucleic Acids Res. 19:5763-5769(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202.
[2]"Identification and characterization of a new gene in the human Xq28 region."
van den Ouweland A.M.W., Kioschis P., Verdijk M., Tamanini F., Toniolo D., Poustka A., van Oost B.A.
Hum. Mol. Genet. 1:269-273(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-202.
[3]"Sequence analysis of a novel gene expressed in normal and in tumor-derived tissue."
Kroepelin M.
Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202.
Tissue: Mammary gland.
[4]"Genomic organization of a cDNA (QM) demonstrating an altered mRNA level in nontumorigenic Wilms' microcell hybrid cells and its localization to Xq28."
Kaneko K., Kobayashi H., Onodera O., Miyatake T., Tsuji S.
Hum. Mol. Genet. 1:529-533(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-202.
[5]"QM, a putative tumor suppressor, regulates proto-oncogene c-Yes."
Oh H.S., Kwon H., Sun S.K., Yang C.-H.
J. Biol. Chem. 277:36489-36498(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Loss of heterozygosity and microsatellite instability at the Xq28 and the A/G heterozygosity of the QM gene are associated with ovarian cancer."
Shen X.J., Ali-Fehmi R., Weng C.R., Sarkar F.H., Grignon D., Liao D.J.
Cancer Biol. Ther. 5:523-528(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202.
Tissue: Mammary cancer, Ovarian carcinoma, Pancreatic cancer and Prostatic carcinoma.
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-202.
[8]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-202.
Tissue: Thymus.
[9]"Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."
Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.
Hum. Mol. Genet. 5:659-668(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-202.
[11]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"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], VARIANT SER-202.
Tissue: Brain, Mammary gland and Placenta.
[13]"cDNA cloning and genomic analysis of a new multigene family sharing common phylogenetic and expression profiles with the laminin receptor gene."
Bignon C., Roux-Dosseto M., Zeigler M.E., Wicha M.S., Martin P.M.
Biochem. Biophys. Res. Commun. 184:1165-1172(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-147.
[14]"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 135-214, VARIANT SER-202.
[15]"Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"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].
[17]"Crystal structure of human ribosomal protein L10 core domain reveals eukaryote-specific motifs in addition to the conserved fold."
Nishimura M., Kaminishi T., Takemoto C., Kawazoe M., Yoshida T., Tanaka A., Sugano S., Shirouzu M., Ohkubo T., Yokoyama S., Kobayashi Y.
J. Mol. Biol. 377:421-430(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-182.
[18]"Mutations in the ribosomal protein gene RPL10 suggest a novel modulating disease mechanism for autism."
Klauck S.M., Felder B., Kolb-Kokocinski A., Schuster C., Chiocchetti A., Schupp I., Wellenreuther R., Schmoetzer G., Poustka F., Breitenbach-Koller L., Poustka A.
Mol. Psychiatry 11:1073-1084(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO AUTISM, VARIANTS AUTSX5 MET-206 AND GLN-213.
[19]"Mutation and expression analyses of the ribosomal protein gene RPL10 in an extended German sample of patients with autism spectrum disorder."
Chiocchetti A., Pakalapati G., Duketis E., Wiemann S., Poustka A., Poustka F., Klauck S.M.
Am. J. Med. Genet. A 155:1472-1475(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AUTSX5 GLN-213.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64241 mRNA. Translation: AAA63253.1.
M81806 Genomic DNA. Translation: AAA36021.1.
M73791 mRNA. Translation: AAA36378.1.
S64169, S64168 Genomic DNA. Translation: AAB27665.1.
AF486812 mRNA. Translation: AAL88713.1.
DQ369703 mRNA. Translation: ABC88559.1.
DQ369704 mRNA. Translation: ABC88560.1.
DQ369705 mRNA. Translation: ABC88561.1.
DQ369706 mRNA. Translation: ABC88562.1.
DQ369707 mRNA. Translation: ABC88563.1.
DQ369708 mRNA. Translation: ABC88564.1.
DQ369709 mRNA. Translation: ABC88565.1.
DQ369710 mRNA. Translation: ABC88566.1.
DQ369711 mRNA. Translation: ABC88567.1.
DQ369712 mRNA. Translation: ABC88568.1.
DQ369713 mRNA. Translation: ABC88569.1.
DQ369714 mRNA. Translation: ABC88570.1.
DQ369715 mRNA. Translation: ABC88571.1.
DQ369716 mRNA. Translation: ABC88572.1.
CR456797 mRNA. Translation: CAG33078.1.
CR542069 mRNA. Translation: CAG46866.1.
AK223309 mRNA. Translation: BAD97029.1.
L44140 Genomic DNA. Translation: AAA92646.1.
BX936347, BX936346 Genomic DNA. Translation: CAI43214.1.
BX936346, BX936347 Genomic DNA. Translation: CAI43230.1.
BX936347, BX936346 Genomic DNA. Translation: CAM45852.1. Sequence problems.
BX936346, BX936347 Genomic DNA. Translation: CAM45853.1. Sequence problems.
CH471172 Genomic DNA. Translation: EAW72737.1.
CH471172 Genomic DNA. Translation: EAW72739.1.
BC003358 mRNA. Translation: AAH03358.1.
BC026276 mRNA. Translation: AAH26276.1.
BC071918 mRNA. Translation: AAH71918.1.
S35960 mRNA. Translation: AAB22173.1. Frameshift.
AB007170 Genomic DNA. Translation: BAA28595.1.
CCDSCCDS14746.1.
PIRA42735.
RefSeqNP_001243506.1. NM_001256577.1.
NP_001243509.1. NM_001256580.1.
NP_006004.2. NM_006013.3.
UniGeneHs.534404.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PA2X-ray2.50A/B34-182[»]
ProteinModelPortalP27635.
SMRP27635. Positions 2-214.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112054. 83 interactions.
DIPDIP-1133N.
IntActP27635. 16 interactions.
MINTMINT-1153266.
STRING9606.ENSP00000341730.

PTM databases

PhosphoSiteP27635.

Polymorphism databases

DMDM148887414.

Proteomic databases

MaxQBP27635.
PaxDbP27635.
PRIDEP27635.

Protocols and materials databases

DNASU6134.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344746; ENSP00000341730; ENSG00000147403.
ENST00000369817; ENSP00000358832; ENSG00000147403.
ENST00000424325; ENSP00000413436; ENSG00000147403.
ENST00000595651; ENSP00000470743; ENSG00000268963.
ENST00000606463; ENSP00000475602; ENSG00000268963.
ENST00000607648; ENSP00000475930; ENSG00000268963.
GeneID6134.
KEGGhsa:6134.
UCSCuc004fkm.2. human.

Organism-specific databases

CTD6134.
GeneCardsGC0XP153618.
GeneReviewsRPL10.
H-InvDBHIX0017152.
HIX0202878.
HGNCHGNC:10298. RPL10.
HPACAB010339.
HPA011311.
MIM300847. phenotype.
312173. gene.
neXtProtNX_P27635.
Orphanet106. Autism.
PharmGKBPA34660.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0197.
HOVERGENHBG002287.
KOK02866.
OMAIMSMRCK.
PhylomeDBP27635.
TreeFamTF300082.

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

ArrayExpressP27635.
BgeeP27635.
CleanExHS_RPL10.
GenevestigatorP27635.

Family and domain databases

Gene3D3.90.1170.10. 1 hit.
InterProIPR001197. Ribosomal_L10e.
IPR016180. Ribosomal_L10e/L16.
IPR018255. Ribosomal_L10e_CS.
[Graphical view]
PfamPF00252. Ribosomal_L16. 1 hit.
[Graphical view]
PIRSFPIRSF005590. Ribosomal_L10. 1 hit.
SUPFAMSSF54686. SSF54686. 1 hit.
TIGRFAMsTIGR00279. L10e. 1 hit.
PROSITEPS01257. RIBOSOMAL_L10E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL10. human.
EvolutionaryTraceP27635.
GeneWikiRPL10.
GenomeRNAi6134.
NextBio23827.
PMAP-CutDBP27635.
PROP27635.
SOURCESearch...

Entry information

Entry nameRL10_HUMAN
AccessionPrimary (citable) accession number: P27635
Secondary accession number(s): A3KQT0 expand/collapse secondary AC list , D3DWW6, Q16470, Q2HXT7, Q53FH7, Q6FGN8, Q8TDA5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 12, 2007
Last modified: July 9, 2014
This is version 150 of the entry and version 4 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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