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Protein

60S ribosomal protein L35

Gene

RPL35

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

Functioni

GO - Molecular functioni

  • mRNA binding Source: ProtInc
  • poly(A) RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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 L35
Gene namesi
Name:RPL35
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:10344. RPL35.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34727.

Polymorphism and mutation databases

BioMutaiRPL35.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12312260S ribosomal protein L35PRO_0000130533Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191N6-acetyllysine1 Publication
Modified residuei43 – 431N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP42766.
PaxDbiP42766.
PRIDEiP42766.

2D gel databases

SWISS-2DPAGEP42766.

PTM databases

PhosphoSiteiP42766.

Expressioni

Gene expression databases

BgeeiP42766.
CleanExiHS_RPL35.
ExpressionAtlasiP42766. baseline and differential.
GenevisibleiP42766. HS.

Organism-specific databases

HPAiHPA006047.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PSTPIP1O435861EBI-356819,EBI-1050964

Protein-protein interaction databases

BioGridi116392. 66 interactions.
IntActiP42766. 20 interactions.
MINTiMINT-5000320.
STRINGi9606.ENSP00000259469.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Ch1-123[»]
5AJ0electron microscopy3.50Ah1-123[»]
ProteinModelPortaliP42766.
SMRiP42766. Positions 2-66.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L29P family.Curated

Phylogenomic databases

eggNOGiCOG0255.
GeneTreeiENSGT00390000016384.
HOVERGENiHBG000862.
InParanoidiP42766.
KOiK02918.
OMAiPIRKYAV.
PhylomeDBiP42766.
TreeFamiTF314951.

Family and domain databases

Gene3Di1.10.287.310. 1 hit.
HAMAPiMF_00374. Ribosomal_L29.
InterProiIPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]
PfamiPF00831. Ribosomal_L29. 1 hit.
[Graphical view]
SUPFAMiSSF46561. SSF46561. 1 hit.
TIGRFAMsiTIGR00012. L29. 1 hit.
PROSITEiPS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42766-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKIKARDLR GKKKEELLKQ LDDLKVELSQ LRVAKVTGGA ASKLSKIRVV
60 70 80 90 100
RKSIARVLTV INQTQKENLR KFYKGKKYKP LDLRPKKTRA MRRRLNKHEE
110 120
NLKTKKQQRK ERLYPLRKYA VKA
Length:123
Mass (Da):14,551
Last modified:January 23, 2007 - v2
Checksum:i92B7694A97AC725D
GO

Sequence cautioni

The sequence CAI39638.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221K → R in AAH10919 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12465 mRNA. Translation: AAA51648.1.
CR456877 mRNA. Translation: CAG33158.1.
AK291072 mRNA. Translation: BAF83761.1.
AL354928 Genomic DNA. Translation: CAI39638.1. Sequence problems.
AL354928 Genomic DNA. Translation: CAI39639.1.
BC000348 mRNA. Translation: AAH00348.1.
BC010919 mRNA. Translation: AAH10919.1.
BC071915 mRNA. Translation: AAH71915.1.
BC094828 mRNA. Translation: AAH94828.1.
AB046409 Genomic DNA. Translation: BAB21255.1.
CCDSiCCDS6858.1.
PIRiG01477.
RefSeqiNP_009140.1. NM_007209.3.
UniGeneiHs.182825.

Genome annotation databases

EnsembliENST00000348462; ENSP00000259469; ENSG00000136942.
GeneIDi11224.
KEGGihsa:11224.
UCSCiuc004boy.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12465 mRNA. Translation: AAA51648.1.
CR456877 mRNA. Translation: CAG33158.1.
AK291072 mRNA. Translation: BAF83761.1.
AL354928 Genomic DNA. Translation: CAI39638.1. Sequence problems.
AL354928 Genomic DNA. Translation: CAI39639.1.
BC000348 mRNA. Translation: AAH00348.1.
BC010919 mRNA. Translation: AAH10919.1.
BC071915 mRNA. Translation: AAH71915.1.
BC094828 mRNA. Translation: AAH94828.1.
AB046409 Genomic DNA. Translation: BAB21255.1.
CCDSiCCDS6858.1.
PIRiG01477.
RefSeqiNP_009140.1. NM_007209.3.
UniGeneiHs.182825.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Ch1-123[»]
5AJ0electron microscopy3.50Ah1-123[»]
ProteinModelPortaliP42766.
SMRiP42766. Positions 2-66.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116392. 66 interactions.
IntActiP42766. 20 interactions.
MINTiMINT-5000320.
STRINGi9606.ENSP00000259469.

PTM databases

PhosphoSiteiP42766.

Polymorphism and mutation databases

BioMutaiRPL35.

2D gel databases

SWISS-2DPAGEP42766.

Proteomic databases

MaxQBiP42766.
PaxDbiP42766.
PRIDEiP42766.

Protocols and materials databases

DNASUi11224.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000348462; ENSP00000259469; ENSG00000136942.
GeneIDi11224.
KEGGihsa:11224.
UCSCiuc004boy.1. human.

Organism-specific databases

CTDi11224.
GeneCardsiGC09M127620.
HGNCiHGNC:10344. RPL35.
HPAiHPA006047.
neXtProtiNX_P42766.
PharmGKBiPA34727.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0255.
GeneTreeiENSGT00390000016384.
HOVERGENiHBG000862.
InParanoidiP42766.
KOiK02918.
OMAiPIRKYAV.
PhylomeDBiP42766.
TreeFamiTF314951.

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

ChiTaRSiRPL35. human.
GeneWikii60S_ribosomal_protein_L35.
GenomeRNAii11224.
NextBioi42722.
PROiP42766.

Gene expression databases

BgeeiP42766.
CleanExiHS_RPL35.
ExpressionAtlasiP42766. baseline and differential.
GenevisibleiP42766. HS.

Family and domain databases

Gene3Di1.10.287.310. 1 hit.
HAMAPiMF_00374. Ribosomal_L29.
InterProiIPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]
PfamiPF00831. Ribosomal_L29. 1 hit.
[Graphical view]
SUPFAMiSSF46561. SSF46561. 1 hit.
TIGRFAMsiTIGR00012. L29. 1 hit.
PROSITEiPS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human cDNA sequence of ribosomal protein L35."
    Patel S.K., Chandraratna R., Nagpal S.
    Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
  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].
    Tissue: Brain, Lung, Muscle and Prostate.
  6. "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 2-13, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders."
    Uechi T., Tanaka T., Kenmochi N.
    Genomics 72:223-230(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-63.
  8. "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-19 AND LYS-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL35_HUMAN
AccessioniPrimary (citable) accession number: P42766
Secondary accession number(s): A8K4V7
, Q4VBY5, Q5JTN5, Q6IBC7, Q96QJ7, Q9BYF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 138 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. 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.