Skip Header

Contribute Send feedback
Read comments (?) or add your own

P61927 (RL37_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 87. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L37
Alternative name(s):
G1.16
Gene names
Name:RPL37
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length97 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the 23S rRNA By similarity.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Sequence similarities

Belongs to the ribosomal protein L37e family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DDX56Q9NY931EBI-2105843,EBI-372376

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 979660S ribosomal protein L37
PRO_0000139705

Regions

Zinc finger19 – 3719C4-type Potential

Sites

Metal binding191Zinc By similarity
Metal binding221Zinc By similarity
Metal binding341Zinc By similarity
Metal binding371Zinc By similarity

Amino acid modifications

Modified residue101N6-acetyllysine Ref.11
Modified residue961Phosphoserine Ref.14
Modified residue971Phosphoserine Ref.12 Ref.14

Natural variations

Natural variant811G → E.
Corresponds to variant rs14898 [ dbSNP | Ensembl ].
VAR_014606

Experimental info

Sequence conflict651R → S in AAB47039. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P61927 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F565A11E983027C9

FASTA9711,078
        10         20         30         40         50         60 
MTKGTSSFGK RRNKTHTLCR RCGSKAYHLQ KSTCGKCGYP AKRKRKYNWS AKAKRRNTTG 

        70         80         90 
TGRMRHLKIV YRRFRHGFRE GTTPKPKRAA VAASSSS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"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].
[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, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00220871.
PIRS47646.
RefSeqNP_000988.1. NM_000997.4.
UniGeneHs.447582.
Hs.558601.
Hs.731513.

3D structure databases

ProteinModelPortalP61927.
ModBaseSearch...

Protein-protein interaction databases

IntActP61927. 5 interactions.
MINTMINT-3022842.
STRING9606.ENSP00000274242.

PTM databases

PhosphoSiteP61927.

Polymorphism databases

DMDM48429090.

Proteomic databases

PaxDbP61927.
PRIDEP61927.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274242; ENSP00000274242; ENSG00000145592.
GeneID6167.
KEGGhsa:6167.
UCSCuc003jme.1. human.

Organism-specific databases

CTD6167.
GeneCardsGC05M040825.
HGNCHGNC:10347. RPL37.
MIM604181. gene.
neXtProtNX_P61927.
PharmGKBPA34736.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2126.
HOGENOMHOG000111076.
HOVERGENHBG004454.
KOK02922.
OrthoDBEOG4VX26R.

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

ArrayExpressP61927.
BgeeP61927.
CleanExHS_RPL37.
GenevestigatorP61927.
GermOnlineENSG00000145592. Homo sapiens.

Family and domain databases

Gene3D2.20.25.30. 1 hit.
InterProIPR011331. Ribosomal_L37ae/L37e.
IPR001569. Ribosomal_L37e.
IPR018267. Ribosomal_L37e_CS.
IPR011332. Ribosomal_zn-bd_dom.
[Graphical view]
PANTHERPTHR10768. PTHR10768. 1 hit.
PfamPF01907. Ribosomal_L37e. 1 hit.
[Graphical view]
ProDomPD005132. Ribosomal_L37e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF57829. Ribosomal_zn-bd. 1 hit.
PROSITEPS01077. RIBOSOMAL_L37E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL37. human.
GenomeRNAi6167.
NextBio23957.
SOURCESearch...

Entry information

Entry nameRL37_HUMAN
AccessionPrimary (citable) accession number: P61927
Secondary accession number(s): B2R4H2 expand/collapse secondary AC list , P02403, Q6IBB4, Q99883
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 87 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

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families