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Protein

60S ribosomal protein L31

Gene

RPL31

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. RNA binding Source: ProtInc
  3. 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

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 L31
Gene namesi
Name:RPL31
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:10334. RPL31.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic large ribosomal subunit Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34715.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12512560S ribosomal protein L31PRO_0000153763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei55 – 551N6-succinyllysineBy similarity
Modified residuei70 – 701N6-succinyllysineBy similarity
Modified residuei75 – 751N6-acetyllysine; alternate1 Publication
Modified residuei75 – 751N6-succinyllysine; alternateBy similarity
Modified residuei98 – 981Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62899.
PaxDbiP62899.
PRIDEiP62899.

2D gel databases

SWISS-2DPAGEP62899.

PTM databases

PhosphoSiteiP62899.

Expressioni

Gene expression databases

BgeeiP62899.
CleanExiHS_RPL31.
ExpressionAtlasiP62899. baseline and differential.
GenevestigatoriP62899.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ASF1BQ9NVP21EBI-1053664,EBI-1055650
CNBPP626331EBI-1053664,EBI-1047529
DDX56Q9NY931EBI-1053664,EBI-372376
LYARQ9NX581EBI-1053664,EBI-713507
MAGEB2O154791EBI-1053664,EBI-1057615
PINX1Q96BK51EBI-1053664,EBI-721782
PSTPIP1O435861EBI-1053664,EBI-1050964
WBP5Q9UHQ71EBI-1053664,EBI-1051372
YWHAZP631041EBI-1053664,EBI-347088

Protein-protein interaction databases

BioGridi112079. 125 interactions.
IntActiP62899. 25 interactions.
MINTiMINT-5000327.
STRINGi9606.ENSP00000386717.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00d1-125[»]
ProteinModelPortaliP62899.
SMRiP62899. Positions 18-124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L31e family.Curated

Phylogenomic databases

eggNOGiCOG2097.
GeneTreeiENSGT00390000005200.
HOGENOMiHOG000216660.
HOVERGENiHBG001549.
InParanoidiP62899.
KOiK02910.
OMAiKGLQTEN.
PhylomeDBiP62899.
TreeFamiTF314858.

Family and domain databases

Gene3Di3.10.440.10. 1 hit.
InterProiIPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
IPR023621. Ribosomal_L31e_dom.
[Graphical view]
PANTHERiPTHR10956. PTHR10956. 1 hit.
PfamiPF01198. Ribosomal_L31e. 1 hit.
[Graphical view]
ProDomiPD006030. Ribosomal_L31e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54575. SSF54575. 1 hit.
PROSITEiPS01144. RIBOSOMAL_L31E. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P62899-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPAKKGGEK KKGRSAINEV VTREYTINIH KRIHGVGFKK RAPRALKEIR
60 70 80 90 100
KFAMKEMGTP DVRIDTRLNK AVWAKGIRNV PYRIRVRLSR KRNEDEDSPN
110 120
KLYTLVTYVP VTTFKNLQTV NVDEN
Length:125
Mass (Da):14,463
Last modified:August 31, 2004 - v1
Checksum:iBA9DBE79B9E1C071
GO
Isoform 2 (identifier: P62899-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     116-125: NLQTVNVDEN → ISVLNSVTVAKSP

Note: No experimental confirmation available.

Show »
Length:128
Mass (Da):14,632
Checksum:i73178D90B1AE79A8
GO
Isoform 3 (identifier: P62899-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     116-125: NLQTVNVDEN → SKFSIP

Note: No experimental confirmation available.

Show »
Length:121
Mass (Da):13,995
Checksum:iBAD3547E9019CF61
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei116 – 12510NLQTVNVDEN → ISVLNSVTVAKSP in isoform 2. 1 PublicationVSP_042572
Alternative sequencei116 – 12510NLQTVNVDEN → SKFSIP in isoform 3. 1 PublicationVSP_043224

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15940 mRNA. Translation: CAA34066.1.
AB061830 Genomic DNA. Translation: BAB79468.1.
AK297483 mRNA. Translation: BAH12588.1.
AC016738 Genomic DNA. Translation: AAY14823.1.
CH471127 Genomic DNA. Translation: EAX01826.1.
CH471127 Genomic DNA. Translation: EAX01827.1.
CH471127 Genomic DNA. Translation: EAX01829.1.
BC017343 mRNA. Translation: AAH17343.1.
BC070210 mRNA. Translation: AAH70210.1.
BC070373 mRNA. Translation: AAH70373.1.
X69181 mRNA. Translation: CAA48925.1.
CCDSiCCDS2049.1. [P62899-1]
CCDS46373.1. [P62899-2]
CCDS46374.1. [P62899-3]
PIRiS05576. R5HU31.
RefSeqiNP_000984.1. NM_000993.4. [P62899-1]
NP_001092047.1. NM_001098577.2. [P62899-2]
NP_001093163.1. NM_001099693.1. [P62899-3]
UniGeneiHs.469473.

Genome annotation databases

EnsembliENST00000264258; ENSP00000264258; ENSG00000071082. [P62899-1]
ENST00000409028; ENSP00000386717; ENSG00000071082. [P62899-2]
ENST00000409320; ENSP00000387163; ENSG00000071082. [P62899-3]
ENST00000409733; ENSP00000386681; ENSG00000071082. [P62899-1]
GeneIDi6160.
KEGGihsa:6160.
UCSCiuc002taq.4. human. [P62899-1]
uc002tar.4. human. [P62899-3]
uc010fiu.1. human. [P62899-2]

Polymorphism databases

DMDMi51702807.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15940 mRNA. Translation: CAA34066.1.
AB061830 Genomic DNA. Translation: BAB79468.1.
AK297483 mRNA. Translation: BAH12588.1.
AC016738 Genomic DNA. Translation: AAY14823.1.
CH471127 Genomic DNA. Translation: EAX01826.1.
CH471127 Genomic DNA. Translation: EAX01827.1.
CH471127 Genomic DNA. Translation: EAX01829.1.
BC017343 mRNA. Translation: AAH17343.1.
BC070210 mRNA. Translation: AAH70210.1.
BC070373 mRNA. Translation: AAH70373.1.
X69181 mRNA. Translation: CAA48925.1.
CCDSiCCDS2049.1. [P62899-1]
CCDS46373.1. [P62899-2]
CCDS46374.1. [P62899-3]
PIRiS05576. R5HU31.
RefSeqiNP_000984.1. NM_000993.4. [P62899-1]
NP_001092047.1. NM_001098577.2. [P62899-2]
NP_001093163.1. NM_001099693.1. [P62899-3]
UniGeneiHs.469473.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00d1-125[»]
ProteinModelPortaliP62899.
SMRiP62899. Positions 18-124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112079. 125 interactions.
IntActiP62899. 25 interactions.
MINTiMINT-5000327.
STRINGi9606.ENSP00000386717.

PTM databases

PhosphoSiteiP62899.

Polymorphism databases

DMDMi51702807.

2D gel databases

SWISS-2DPAGEP62899.

Proteomic databases

MaxQBiP62899.
PaxDbiP62899.
PRIDEiP62899.

Protocols and materials databases

DNASUi6160.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264258; ENSP00000264258; ENSG00000071082. [P62899-1]
ENST00000409028; ENSP00000386717; ENSG00000071082. [P62899-2]
ENST00000409320; ENSP00000387163; ENSG00000071082. [P62899-3]
ENST00000409733; ENSP00000386681; ENSG00000071082. [P62899-1]
GeneIDi6160.
KEGGihsa:6160.
UCSCiuc002taq.4. human. [P62899-1]
uc002tar.4. human. [P62899-3]
uc010fiu.1. human. [P62899-2]

Organism-specific databases

CTDi6160.
GeneCardsiGC02P101618.
H-InvDBHIX0017577.
HGNCiHGNC:10334. RPL31.
neXtProtiNX_P62899.
PharmGKBiPA34715.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2097.
GeneTreeiENSGT00390000005200.
HOGENOMiHOG000216660.
HOVERGENiHBG001549.
InParanoidiP62899.
KOiK02910.
OMAiKGLQTEN.
PhylomeDBiP62899.
TreeFamiTF314858.

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

ChiTaRSiRPL31. human.
GeneWikii60S_ribosomal_protein_L31.
GenomeRNAii6160.
NextBioi23923.
PROiP62899.

Gene expression databases

BgeeiP62899.
CleanExiHS_RPL31.
ExpressionAtlasiP62899. baseline and differential.
GenevestigatoriP62899.

Family and domain databases

Gene3Di3.10.440.10. 1 hit.
InterProiIPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
IPR023621. Ribosomal_L31e_dom.
[Graphical view]
PANTHERiPTHR10956. PTHR10956. 1 hit.
PfamiPF01198. Ribosomal_L31e. 1 hit.
[Graphical view]
ProDomiPD006030. Ribosomal_L31e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54575. SSF54575. 1 hit.
PROSITEiPS01144. RIBOSOMAL_L31E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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].
  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] (ISOFORM 2).
    Tissue: Brain.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 3).
    Tissue: Brain, Liver and Prostate.
  7. "Identification of a human ribosomal protein mRNA with increased expression in colorectal tumours."
    Chester K.A., Robson L., Beyent R.H.J., Talbot I.C., Pringle J.H., Primrose L., Macpherson A.J.S., Boxer G., Southhall P., Malcolm A.D.B.
    Biochim. Biophys. Acta 1009:297-300(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-125 (ISOFORM 1).
  8. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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.
  12. "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-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL31_HUMAN
AccessioniPrimary (citable) accession number: P62899
Secondary accession number(s): B7Z4K2
, D3DVJ4, P12947, Q53SQ5, Q6IRZ0, Q6LBJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: February 4, 2015
This is version 112 of the entry and version 1 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 2
    Human chromosome 2: 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.