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Protein

60S ribosomal protein L36a

Gene

RPL36A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • 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

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L36a
Alternative name(s):
60S ribosomal protein L44
Cell growth-inhibiting gene 15 protein
Cell migration-inducing gene 6 protein
Gene namesi
Name:RPL36A
Synonyms:RPL44
ORF Names:GIG15, MIG6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:10359. RPL36A.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • ribosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164742367.

Polymorphism and mutation databases

DMDMi47117731.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10610660S ribosomal protein L36aPRO_0000149117Add
BLAST

Proteomic databases

EPDiP83881.
MaxQBiP83881.
PaxDbiP83881.
PRIDEiP83881.
TopDownProteomicsiP83881.

PTM databases

iPTMnetiP83881.
PhosphoSiteiP83881.
SwissPalmiP83881.

Expressioni

Gene expression databases

BgeeiP83881.
CleanExiHS_RPL36A.
ExpressionAtlasiP83881. baseline and differential.

Interactioni

Protein-protein interaction databases

BioGridi112092. 14 interactions.
IntActiP83881. 10 interactions.
MINTiMINT-3023791.
STRINGi9606.ENSP00000404375.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-Lo1-106[»]
4V6Xelectron microscopy5.00Co1-106[»]
5AJ0electron microscopy3.50Ao1-106[»]
ProteinModelPortaliP83881.
SMRiP83881. Positions 2-96.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L44e family.Curated

Phylogenomic databases

eggNOGiKOG3464. Eukaryota.
COG1631. LUCA.
GeneTreeiENSGT00390000018085.
HOGENOMiHOG000224989.
HOVERGENiHBG056127.
InParanoidiP83881.
KOiK02929.
PhylomeDBiP83881.

Family and domain databases

Gene3Di3.10.450.80. 1 hit.
InterProiIPR000552. Ribosomal_L44e.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR10369. PTHR10369. 1 hit.
PfamiPF00935. Ribosomal_L44. 1 hit.
[Graphical view]
ProDomiPD002841. Ribosomal_L44e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01172. RIBOSOMAL_L44E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83881-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNVPKTRRT FCKKCGKHQP HKVTQYKKGK DSLYAQGKRR YDRKQSGYGG
60 70 80 90 100
QTKPIFRKKA KTTKKIVLRL ECVEPNCRSK RMLAIKRCKH FELGGDKKRK

GQVIQF
Length:106
Mass (Da):12,441
Last modified:January 23, 2007 - v2
Checksum:iAE3308265D70BD26
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78027 Genomic DNA. Translation: AAB64204.1.
AY305871 mRNA. Translation: AAQ95213.1.
CR542198 mRNA. Translation: CAG46995.1.
AY927233 mRNA. Translation: AAX08138.1.
AL035422 Genomic DNA. Translation: CAI42360.1.
CH471115 Genomic DNA. Translation: EAX02860.1.
BC001781 mRNA. Translation: AAH01781.1.
BC031015 mRNA. Translation: AAH31015.1.
BC062219 mRNA. Translation: AAH62219.1.
BC070204 mRNA. Translation: AAH70204.1.
RefSeqiNP_066357.2. NM_021029.5.
UniGeneiHs.432485.
Hs.655348.

Genome annotation databases

EnsembliENST00000553110; ENSP00000446503; ENSG00000241343.
GeneIDi6173.
KEGGihsa:6173.
UCSCiuc065agx.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78027 Genomic DNA. Translation: AAB64204.1.
AY305871 mRNA. Translation: AAQ95213.1.
CR542198 mRNA. Translation: CAG46995.1.
AY927233 mRNA. Translation: AAX08138.1.
AL035422 Genomic DNA. Translation: CAI42360.1.
CH471115 Genomic DNA. Translation: EAX02860.1.
BC001781 mRNA. Translation: AAH01781.1.
BC031015 mRNA. Translation: AAH31015.1.
BC062219 mRNA. Translation: AAH62219.1.
BC070204 mRNA. Translation: AAH70204.1.
RefSeqiNP_066357.2. NM_021029.5.
UniGeneiHs.432485.
Hs.655348.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-Lo1-106[»]
4V6Xelectron microscopy5.00Co1-106[»]
5AJ0electron microscopy3.50Ao1-106[»]
ProteinModelPortaliP83881.
SMRiP83881. Positions 2-96.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112092. 14 interactions.
IntActiP83881. 10 interactions.
MINTiMINT-3023791.
STRINGi9606.ENSP00000404375.

PTM databases

iPTMnetiP83881.
PhosphoSiteiP83881.
SwissPalmiP83881.

Polymorphism and mutation databases

DMDMi47117731.

Proteomic databases

EPDiP83881.
MaxQBiP83881.
PaxDbiP83881.
PRIDEiP83881.
TopDownProteomicsiP83881.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000553110; ENSP00000446503; ENSG00000241343.
GeneIDi6173.
KEGGihsa:6173.
UCSCiuc065agx.1. human.

Organism-specific databases

CTDi6173.
GeneCardsiRPL36A.
H-InvDBHIX0016927.
HIX0056232.
HGNCiHGNC:10359. RPL36A.
MIMi300902. gene.
neXtProtiNX_P83881.
PharmGKBiPA164742367.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3464. Eukaryota.
COG1631. LUCA.
GeneTreeiENSGT00390000018085.
HOGENOMiHOG000224989.
HOVERGENiHBG056127.
InParanoidiP83881.
KOiK02929.
PhylomeDBiP83881.

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRPL36A. human.
GeneWikiiRPL36A.
GenomeRNAii6173.
PROiP83881.
SOURCEiSearch...

Gene expression databases

BgeeiP83881.
CleanExiHS_RPL36A.
ExpressionAtlasiP83881. baseline and differential.

Family and domain databases

Gene3Di3.10.450.80. 1 hit.
InterProiIPR000552. Ribosomal_L44e.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR10369. PTHR10369. 1 hit.
PfamiPF00935. Ribosomal_L44. 1 hit.
[Graphical view]
ProDomiPD002841. Ribosomal_L44e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01172. RIBOSOMAL_L44E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Large-scale comparative sequence analysis of the human and murine Bruton's tyrosine kinase loci reveals conserved regulatory domains."
    Oeltjen J.C., Malley T.M., Muzny D.M., Miller W., Gibbs R.A., Belmont J.W.
    Genome Res. 7:315-329(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of a migration-inducing gene."
    Kim J.W.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
  4. "Identification of cell growth-inhibiting gene."
    Kim J.W., Kim H.K.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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.
    , 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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Eye, Lung and Testis.
  8. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL36A_HUMAN
AccessioniPrimary (citable) accession number: P83881
Secondary accession number(s): P09896
, P10661, Q08ES5, Q5J9I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 129 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, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

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 one 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.