Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

60S ribosomal protein L36a

Gene

RPL36A

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

Functioni

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. cytoplasmic translation Source: GO_Central
  3. gene expression Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  6. RNA metabolic process Source: Reactome
  7. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  8. translation Source: UniProtKB
  9. translational elongation Source: Reactome
  10. translational initiation Source: Reactome
  11. translational termination Source: Reactome
  12. viral life cycle Source: Reactome
  13. viral process Source: Reactome
  14. viral transcription Source: Reactome
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 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
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:10359. RPL36A.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic large ribosomal subunit Source: UniProtKB
  3. ribosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164742367.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301N6-succinyllysineBy similarity

Proteomic databases

MaxQBiP83881.
PaxDbiP83881.
PRIDEiP83881.

PTM databases

PhosphoSiteiP83881.

Expressioni

Gene expression databases

BgeeiP83881.
CleanExiHS_RPL36A.
ExpressionAtlasiP83881. baseline and differential.
GenevestigatoriP83881.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MAGEB2O154791EBI-1054835,EBI-1057615
PSTPIP1O435861EBI-1054835,EBI-1050964

Protein-protein interaction databases

BioGridi112092. 9 interactions.
IntActiP83881. 5 interactions.
MINTiMINT-3023791.
STRINGi9606.ENSP00000404375.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00o1-106[»]
ProteinModelPortaliP83881.
SMRiP83881. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L44e family.Curated

Phylogenomic databases

eggNOGiCOG1631.
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.

Polymorphism databases

DMDMi47117731.

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
4V6Xelectron microscopy5.00o1-106[»]
ProteinModelPortaliP83881.
SMRiP83881. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112092. 9 interactions.
IntActiP83881. 5 interactions.
MINTiMINT-3023791.
STRINGi9606.ENSP00000404375.

PTM databases

PhosphoSiteiP83881.

Polymorphism databases

DMDMi47117731.

Proteomic databases

MaxQBiP83881.
PaxDbiP83881.
PRIDEiP83881.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000553110; ENSP00000446503; ENSG00000241343.
GeneIDi6173.
KEGGihsa:6173.

Organism-specific databases

CTDi6173.
GeneCardsiGC0XP100645.
H-InvDBHIX0016927.
HIX0056232.
HGNCiHGNC:10359. RPL36A.
MIMi300902. gene.
neXtProtiNX_P83881.
PharmGKBiPA164742367.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1631.
GeneTreeiENSGT00390000018085.
HOGENOMiHOG000224989.
HOVERGENiHBG056127.
InParanoidiP83881.
KOiK02929.
PhylomeDBiP83881.

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

ChiTaRSiRPL36A. human.
GeneWikiiRPL36A.
GenomeRNAii6173.
NextBioi23983.
PROiP83881.
SOURCEiSearch...

Gene expression databases

BgeeiP83881.
CleanExiHS_RPL36A.
ExpressionAtlasiP83881. baseline and differential.
GenevestigatoriP83881.

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: February 4, 2015
This is version 114 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

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.