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P18077 (RL35A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. 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 L35a
Alternative name(s):
Cell growth-inhibiting gene 33 protein
Gene names
Name:RPL35A
ORF Names:GIG33
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length110 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the proliferation and viability of hematopoietic cells. Plays a role in 60S ribosomal subunit formation. The protein was found to bind to both initiator and elongator tRNAs and consequently was assigned to the P site or P and A site. Ref.6

Involvement in disease

Diamond-Blackfan anemia 5 (DBA5) [MIM:612528]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Miscellaneous

Knockdown of RPL35A in hematopoietic cell lines results in decreased cell proliferation, increased apoptosis, decreased biogenesis of mature 60S ribosomal subunit, and abnormal processing of large ribosomal subunit rRNA.

Sequence similarities

Belongs to the ribosomal protein L35Ae family.

Ontologies

Keywords
   DiseaseDiamond-Blackfan anemia
Disease mutation
   LigandRNA-binding
tRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
   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

rRNA processing

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

ribosomal large subunit biogenesis

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

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_componentcytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay PubMed 12962325. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

   Molecular_functionpoly(A) RNA binding

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

structural constituent of ribosome

Non-traceable author statement PubMed 12962325. Source: UniProtKB

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CNBPP626331EBI-353383,EBI-1047529
PSTPIP1O435861EBI-353383,EBI-1050964

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11011060S ribosomal protein L35a
PRO_0000192796

Amino acid modifications

Modified residue81N6-acetyllysine Ref.7
Modified residue631N6-acetyllysine; alternate By similarity
Modified residue631N6-succinyllysine; alternate By similarity

Natural variations

Natural variant271Missing in DBA5. Ref.6
VAR_055446
Natural variant331V → I in DBA5; may result in aberrant splicing. Ref.6
VAR_055447

Experimental info

Sequence conflict851R → L in CAA37138. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P18077 [UniParc].

Last modified July 26, 2002. Version 2.
Checksum: F32E4A26A25E79E8

FASTA11012,538
        10         20         30         40         50         60 
MSGRLWSKAI FAGYKRGLRN QREHTALLKI EGVYARDETE FYLGKRCAYV YKAKNNTVTP 

        70         80         90        100        110 
GGKPNKTRVI WGKVTRAHGN SGMVRAKFRS NLPAKAIGHR IRVMLYPSRI 

« Hide

References

« Hide 'large scale' references
[1]"cDNA encoding the human homologue of rat ribosomal protein L35a."
Herzog H., Hfferer L., Schneider R., Schweiger M.
Nucleic Acids Res. 18:4600-4600(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification of a cell growth-inhibiting gene."
Kim J.W., Kim H.K.
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Bone marrow, Colon, Ovary and Placenta.
[5]"The human L35a ribosomal protein (RPL35A) gene is located at chromosome band 3q29-qter."
Colombo P., Read M., Fried M.
Genomics 32:148-150(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[6]"Abnormalities of the large ribosomal subunit protein, Rpl35a, in Diamond-Blackfan anemia."
Farrar J.E., Nater M., Caywood E., McDevitt M.A., Kowalski J., Takemoto C.M., Talbot C.C. Jr., Meltzer P., Esposito D., Beggs A.H., Schneider H.E., Grabowska A., Ball S.E., Niewiadomska E., Sieff C.A., Vlachos A., Atsidaftos E., Ellis S.R. expand/collapse author list , Lipton J.M., Gazda H.T., Arceci R.J.
Blood 112:1582-1592(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANTS DBA5 LEU-27 DEL AND ILE-33.
[7]"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-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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].
[9]"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
X52966 mRNA. Translation: CAA37138.1.
AY871273 mRNA. Translation: AAX11429.1.
CH471252 Genomic DNA. Translation: EAW92249.1.
BC001037 mRNA. Translation: AAH01037.1.
BC010949 mRNA. Translation: AAH10949.1.
BC017093 mRNA. Translation: AAH17093.1.
BC061890 mRNA. Translation: AAH61890.1.
X94619 Genomic DNA. Translation: CAA64325.1.
CCDSCCDS33930.1.
PIRR5HU35. S12710.
RefSeqNP_000987.2. NM_000996.2.
XP_005269408.1. XM_005269351.1.
UniGeneHs.529631.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00f1-110[»]
ProteinModelPortalP18077.
SMRP18077. Positions 2-110.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112084. 19 interactions.
IntActP18077. 10 interactions.
MINTMINT-1163509.
STRING9606.ENSP00000393393.

PTM databases

PhosphoSiteP18077.

2D gel databases

SWISS-2DPAGEP18077.

Proteomic databases

MaxQBP18077.
PaxDbP18077.
PRIDEP18077.

Protocols and materials databases

DNASU6165.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000448864; ENSP00000393393; ENSG00000182899.
ENST00000464167; ENSP00000419117; ENSG00000182899.
GeneID6165.
KEGGhsa:6165.
UCSCuc003fyr.3. human.

Organism-specific databases

CTD6165.
GeneCardsGC03P197676.
GeneReviewsRPL35A.
H-InvDBHIX0005661.
HIX0163429.
HIX0170318.
HIX0170319.
HGNCHGNC:10345. RPL35A.
MIM180468. gene.
612528. phenotype.
neXtProtNX_P18077.
Orphanet124. Blackfan-Diamond anemia.
PharmGKBPA34728.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2451.
HOGENOMHOG000195636.
HOVERGENHBG054581.
InParanoidP18077.
KOK02917.
OMASTRLYSK.
OrthoDBEOG741Z4R.
PhylomeDBP18077.
TreeFamTF300104.

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

ArrayExpressP18077.
BgeeP18077.
CleanExHS_RPL35A.
GenevestigatorP18077.

Family and domain databases

InterProIPR001780. Ribosomal_L35A.
IPR018266. Ribosomal_L35Ae_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERPTHR10902. PTHR10902. 1 hit.
PfamPF01247. Ribosomal_L35Ae. 1 hit.
[Graphical view]
ProDomPD012670. Ribosomal_L35Ae. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF50447. SSF50447. 1 hit.
PROSITEPS01105. RIBOSOMAL_L35AE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRPL35A.
GenomeRNAi6165.
NextBio23949.
PROP18077.
SOURCESearch...

Entry information

Entry nameRL35A_HUMAN
AccessionPrimary (citable) accession number: P18077
Secondary accession number(s): Q08ES9, Q9BVN7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 26, 2002
Last modified: July 9, 2014
This is version 130 of the entry and version 2 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 3

Human chromosome 3: entries, gene names and cross-references to MIM