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P61927

- RL37_HUMAN

UniProt

P61927 - RL37_HUMAN

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Protein

60S ribosomal protein L37

Gene
RPL37
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds to the 23S rRNA By similarity.UniRule annotation

Cofactori

Binds 1 zinc ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi19 – 191Zinc By similarity
Metal bindingi22 – 221Zinc By similarity
Metal bindingi34 – 341Zinc By similarity
Metal bindingi37 – 371Zinc By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri19 – 3719C4-type Reviewed predictionAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB
  3. rRNA binding Source: UniProtKB-KW
  4. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  7. translation Source: UniProtKB
  8. translational elongation Source: Reactome
  9. translational initiation Source: Reactome
  10. translational termination Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
  13. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, RNA-binding, rRNA-binding, Zinc

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 L37
Alternative name(s):
G1.16
Gene namesi
Name:RPL37
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:10347. RPL37.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34736.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 979660S ribosomal protein L37UniRule annotationPRO_0000139705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101N6-acetyllysine1 Publication
Modified residuei96 – 961Phosphoserine1 Publication
Modified residuei97 – 971Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP61927.
PaxDbiP61927.
PRIDEiP61927.

PTM databases

PhosphoSiteiP61927.

Expressioni

Gene expression databases

ArrayExpressiP61927.
BgeeiP61927.
CleanExiHS_RPL37.
GenevestigatoriP61927.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX56Q9NY931EBI-2105843,EBI-372376

Protein-protein interaction databases

BioGridi112086. 14 interactions.
IntActiP61927. 5 interactions.
MINTiMINT-3022842.
STRINGi9606.ENSP00000274242.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00j1-97[»]
ProteinModelPortaliP61927.
SMRiP61927. Positions 2-91.

Family & Domainsi

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri19 – 3719C4-type Reviewed predictionAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG2126.
HOGENOMiHOG000111076.
HOVERGENiHBG004454.
KOiK02922.
OMAiYLANIRV.
OrthoDBiEOG7RJPTP.
PhylomeDBiP61927.
TreeFamiTF300260.

Family and domain databases

Gene3Di2.20.25.30. 1 hit.
HAMAPiMF_00547. Ribosomal_L37e.
InterProiIPR011331. Ribosomal_L37ae/L37e.
IPR001569. Ribosomal_L37e.
IPR018267. Ribosomal_L37e_CS.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR10768. PTHR10768. 1 hit.
PfamiPF01907. Ribosomal_L37e. 1 hit.
[Graphical view]
ProDomiPD005132. Ribosomal_L37e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01077. RIBOSOMAL_L37E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P61927-1 [UniParc]FASTAAdd to Basket

« Hide

MTKGTSSFGK RRNKTHTLCR RCGSKAYHLQ KSTCGKCGYP AKRKRKYNWS   50
AKAKRRNTTG TGRMRHLKIV YRRFRHGFRE GTTPKPKRAA VAASSSS 97
Length:97
Mass (Da):11,078
Last modified:January 23, 2007 - v2
Checksum:iF565A11E983027C9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811G → E.
Corresponds to variant rs14898 [ dbSNP | Ensembl ].
VAR_014606

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651R → S in AAB47039. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D23661 mRNA. Translation: BAA04888.1.
L11567 mRNA. Translation: AAA62148.1.
S79979 mRNA. Translation: AAB47039.2.
AB061834 Genomic DNA. Translation: BAB79472.1.
CR456890 mRNA. Translation: CAG33171.1.
AK311827 mRNA. Translation: BAG34769.1.
BC079477 mRNA. Translation: AAH79477.1.
BC084576 mRNA. Translation: AAH84576.1.
AB007184 Genomic DNA. Translation: BAA25843.1.
AB007183 Genomic DNA. Translation: BAA25842.1.
CCDSiCCDS3934.1.
PIRiS47646.
RefSeqiNP_000988.1. NM_000997.4.
UniGeneiHs.447582.
Hs.558601.
Hs.731513.

Genome annotation databases

EnsembliENST00000274242; ENSP00000274242; ENSG00000145592.
GeneIDi6167.
KEGGihsa:6167.
UCSCiuc003jme.1. human.

Polymorphism databases

DMDMi48429090.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D23661 mRNA. Translation: BAA04888.1 .
L11567 mRNA. Translation: AAA62148.1 .
S79979 mRNA. Translation: AAB47039.2 .
AB061834 Genomic DNA. Translation: BAB79472.1 .
CR456890 mRNA. Translation: CAG33171.1 .
AK311827 mRNA. Translation: BAG34769.1 .
BC079477 mRNA. Translation: AAH79477.1 .
BC084576 mRNA. Translation: AAH84576.1 .
AB007184 Genomic DNA. Translation: BAA25843.1 .
AB007183 Genomic DNA. Translation: BAA25842.1 .
CCDSi CCDS3934.1.
PIRi S47646.
RefSeqi NP_000988.1. NM_000997.4.
UniGenei Hs.447582.
Hs.558601.
Hs.731513.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3B electron microscopy 5.00 j 1-97 [» ]
ProteinModelPortali P61927.
SMRi P61927. Positions 2-91.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112086. 14 interactions.
IntActi P61927. 5 interactions.
MINTi MINT-3022842.
STRINGi 9606.ENSP00000274242.

PTM databases

PhosphoSitei P61927.

Polymorphism databases

DMDMi 48429090.

Proteomic databases

MaxQBi P61927.
PaxDbi P61927.
PRIDEi P61927.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274242 ; ENSP00000274242 ; ENSG00000145592 .
GeneIDi 6167.
KEGGi hsa:6167.
UCSCi uc003jme.1. human.

Organism-specific databases

CTDi 6167.
GeneCardsi GC05M040825.
HGNCi HGNC:10347. RPL37.
MIMi 604181. gene.
neXtProti NX_P61927.
PharmGKBi PA34736.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2126.
HOGENOMi HOG000111076.
HOVERGENi HBG004454.
KOi K02922.
OMAi YLANIRV.
OrthoDBi EOG7RJPTP.
PhylomeDBi P61927.
TreeFami TF300260.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi RPL37. human.
GeneWikii RPL37.
GenomeRNAii 6167.
NextBioi 23957.
PROi P61927.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61927.
Bgeei P61927.
CleanExi HS_RPL37.
Genevestigatori P61927.

Family and domain databases

Gene3Di 2.20.25.30. 1 hit.
HAMAPi MF_00547. Ribosomal_L37e.
InterProi IPR011331. Ribosomal_L37ae/L37e.
IPR001569. Ribosomal_L37e.
IPR018267. Ribosomal_L37e_CS.
IPR011332. Ribosomal_zn-bd.
[Graphical view ]
PANTHERi PTHR10768. PTHR10768. 1 hit.
Pfami PF01907. Ribosomal_L37e. 1 hit.
[Graphical view ]
ProDomi PD005132. Ribosomal_L37e. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF57829. SSF57829. 1 hit.
PROSITEi PS01077. RIBOSOMAL_L37E. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human ribosomal protein L37 cDNA."
    Kato S.
    Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoma.
  2. "Human ribosomal protein L37 has motifs predicting serine/threonine phosphorylation and a zinc-finger domain."
    Barnard G.F., Staniunas R.J., Puder M., Steele G.D. Jr., Chen L.B.
    Biochim. Biophys. Acta 1218:425-428(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon.
  3. "Cell cycle, differentiation and tissue-independent expression of ribosomal protein L37."
    Su S., Bird R.C.
    Eur. J. Biochem. 232:789-797(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
    Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
    Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "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].
  6. "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].
    Tissue: Trachea.
  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: Lung and Ovary.
  8. "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 48-74 AND 76-97.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRL37_HUMAN
AccessioniPrimary (citable) accession number: P61927
Secondary accession number(s): B2R4H2
, P02403, Q6IBB4, Q99883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 99 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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