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Protein

60S ribosomal protein L14

Gene

RPL14

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. ribosomal large subunit biogenesis Source: UniProtKB
  6. RNA metabolic process Source: Reactome
  7. rRNA processing Source: UniProtKB
  8. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  9. translation Source: UniProtKB
  10. translational elongation Source: Reactome
  11. translational initiation Source: Reactome
  12. translational termination Source: Reactome
  13. viral life cycle Source: Reactome
  14. viral process Source: Reactome
  15. 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 L14
Alternative name(s):
CAG-ISL 7
Gene namesi
Name:RPL14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:10305. RPL14.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34673.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 21521460S ribosomal protein L14PRO_0000132031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791N6-acetyllysine1 Publication
Modified residuei85 – 851N6-acetyllysine; alternate1 Publication
Modified residuei85 – 851N6-succinyllysine; alternateBy similarity
Modified residuei139 – 1391Phosphoserine7 Publications
Modified residuei204 – 2041N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP50914.
PaxDbiP50914.
PeptideAtlasiP50914.
PRIDEiP50914.

2D gel databases

SWISS-2DPAGEP50914.

PTM databases

PhosphoSiteiP50914.

Expressioni

Gene expression databases

BgeeiP50914.
CleanExiHS_RPL14.
ExpressionAtlasiP50914. baseline.
GenevestigatoriP50914.

Organism-specific databases

HPAiHPA004136.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0072EBI-356746,EBI-5323863
PHLDA1Q8WV242EBI-356746,EBI-738731

Protein-protein interaction databases

BioGridi114507. 198 interactions.
IntActiP50914. 21 interactions.
MINTiMINT-1156434.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00M1-215[»]
ProteinModelPortaliP50914.
SMRiP50914. Positions 1-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati171 – 17551-1
Repeati176 – 18051-2
Repeati181 – 18551-3
Repeati186 – 19051-4
Repeati193 – 19532-1
Repeati196 – 19832-2

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni171 – 190204 X 5 AA tandem repeats of Q-K-A-[PAS]-XAdd
BLAST
Regioni193 – 19862 X 3 AA tandem repeats of K-[GA]-Q

Sequence similaritiesi

Belongs to the ribosomal protein L14e family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2163.
GeneTreeiENSGT00390000007888.
HOVERGENiHBG005187.
InParanoidiP50914.
KOiK02875.
OMAiSWAKKIE.
OrthoDBiEOG7MD4S6.
PhylomeDBiP50914.
TreeFamiTF314356.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR014722. Rib_L2_dom2.
IPR002784. Ribosomal_L14.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF01929. Ribosomal_L14e. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P50914-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVFRRFVEVG RVAYVSFGPH AGKLVAIVDV IDQNRALVDG PCTQVRRQAM
60 70 80 90 100
PFKCMQLTDF ILKFPHSAHQ KYVRQAWQKA DINTKWAATR WAKKIEARER
110 120 130 140 150
KAKMTDFDRF KVMKAKKMRN RIIKNEVKKL QKAALLKASP KKAPGTKGTA
160 170 180 190 200
AAAAAAAAAK VPAKKITAAS KKAPAQKVPA QKATGQKAAP APKAQKGQKA
210
PAQKAPAPKA SGKKA
Length:215
Mass (Da):23,432
Last modified:November 4, 2008 - v4
Checksum:i4C63DE4FC8E687FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651P → L in BAA13443. (PubMed:9480843)Curated

Polymorphismi

The poly-Ala stretch is highly polymorphic.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381A → S.
VAR_013633
Natural varianti158 – 1592Missing.2 Publications
VAR_047109
Natural varianti159 – 1591A → AA.
VAR_013634
Natural varianti159 – 1591A → AAA.
VAR_014070
Natural varianti159 – 1591A → AAAA.
VAR_013635
Natural varianti159 – 1591A → AAAAA.
VAR_013636
Natural varianti159 – 1591A → AAAAAA.3 Publications
VAR_006923
Natural varianti159 – 1591A → AAAAAAAA.
VAR_013637

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16738 mRNA. Translation: AAC16021.1.
D87735 mRNA. Translation: BAA13443.1.
AB061822 Genomic DNA. Translation: BAB79460.1.
DQ118667 mRNA. Translation: AAZ38460.1.
AK223111 mRNA. Translation: BAD96831.1.
AC104186 Genomic DNA. No translation available.
BC000606 mRNA. Translation: AAH00606.1.
BC005134 mRNA. Translation: AAH05134.1.
BC009294 mRNA. Translation: AAH09294.1.
BC019651 mRNA. Translation: AAH19651.1.
BC022805 mRNA. Translation: AAH22805.1.
BC029036 mRNA. Translation: AAH29036.1.
AB046407 Genomic DNA. Translation: BAB21253.1.
CCDSiCCDS33739.1.
CCDS43070.1.
RefSeqiNP_001030168.1. NM_001034996.2.
NP_003964.3. NM_003973.4.
UniGeneiHs.446522.

Genome annotation databases

EnsembliENST00000338970; ENSP00000345156; ENSG00000188846.
ENST00000396203; ENSP00000379506; ENSG00000188846.
GeneIDi9045.
KEGGihsa:9045.
UCSCiuc003ckg.4. human.

Polymorphism databases

DMDMi212276521.

Keywords - Coding sequence diversityi

Polymorphism, Triplet repeat expansion

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16738 mRNA. Translation: AAC16021.1.
D87735 mRNA. Translation: BAA13443.1.
AB061822 Genomic DNA. Translation: BAB79460.1.
DQ118667 mRNA. Translation: AAZ38460.1.
AK223111 mRNA. Translation: BAD96831.1.
AC104186 Genomic DNA. No translation available.
BC000606 mRNA. Translation: AAH00606.1.
BC005134 mRNA. Translation: AAH05134.1.
BC009294 mRNA. Translation: AAH09294.1.
BC019651 mRNA. Translation: AAH19651.1.
BC022805 mRNA. Translation: AAH22805.1.
BC029036 mRNA. Translation: AAH29036.1.
AB046407 Genomic DNA. Translation: BAB21253.1.
CCDSiCCDS33739.1.
CCDS43070.1.
RefSeqiNP_001030168.1. NM_001034996.2.
NP_003964.3. NM_003973.4.
UniGeneiHs.446522.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00M1-215[»]
ProteinModelPortaliP50914.
SMRiP50914. Positions 1-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114507. 198 interactions.
IntActiP50914. 21 interactions.
MINTiMINT-1156434.

PTM databases

PhosphoSiteiP50914.

Polymorphism databases

DMDMi212276521.

2D gel databases

SWISS-2DPAGEP50914.

Proteomic databases

MaxQBiP50914.
PaxDbiP50914.
PeptideAtlasiP50914.
PRIDEiP50914.

Protocols and materials databases

DNASUi9045.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338970; ENSP00000345156; ENSG00000188846.
ENST00000396203; ENSP00000379506; ENSG00000188846.
GeneIDi9045.
KEGGihsa:9045.
UCSCiuc003ckg.4. human.

Organism-specific databases

CTDi9045.
GeneCardsiGC03P040501.
H-InvDBHIX0003196.
HIX0036844.
HGNCiHGNC:10305. RPL14.
HPAiHPA004136.
neXtProtiNX_P50914.
PharmGKBiPA34673.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2163.
GeneTreeiENSGT00390000007888.
HOVERGENiHBG005187.
InParanoidiP50914.
KOiK02875.
OMAiSWAKKIE.
OrthoDBiEOG7MD4S6.
PhylomeDBiP50914.
TreeFamiTF314356.

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

ChiTaRSiRPL14. human.
GeneWikii60S_ribosomal_protein_L14.
GenomeRNAii9045.
NextBioi33879.
PROiP50914.

Gene expression databases

BgeeiP50914.
CleanExiHS_RPL14.
ExpressionAtlasiP50914. baseline.
GenevestigatoriP50914.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR014722. Rib_L2_dom2.
IPR002784. Ribosomal_L14.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF01929. Ribosomal_L14e. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of trinucleotide repeat-containing genes in human pancreatic islets."
    Aoki M., Koranyi L., Riggs A.C., Wasson J., Chiu K.C., Vaxillaire M., Froguel P., Gough S., Liu L., Donis-Keller H., Permutt M.A.
    Diabetes 45:157-164(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT 158-ALA-ALA-159 DEL.
    Tissue: Pancreas.
  2. "Triplet repeat-containing ribosomal protein L14 gene in immortalized human endothelial cell line (t-HUE4)."
    Tanaka M., Tanaka T., Harata M., Suzuki T., Mitsui Y.
    Biochem. Biophys. Res. Commun. 243:531-537(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-ALA-ALA-ALA-ALA-159 INS.
    Tissue: Umbilical vein.
  3. "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], VARIANT ALA-ALA-ALA-ALA-ALA-159 INS.
  4. Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Wen S., Li H., Yang S.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-ALA-ALA-ALA-ALA-159 INS.
  6. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    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], POLYMORPHISM OF POLY-ALA REGION.
    Tissue: Brain, Kidney, Muscle, Ovary and Skin.
  8. "A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders."
    Uechi T., Tanaka T., Kenmochi N.
    Genomics 72:223-230(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-116.
  9. "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
    Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
    J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, IDENTIFICATION BY MASS SPECTROMETRY.
  10. Bienvenut W.V.
    Submitted (AUG-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 12-46; 80-85; 104-109; 148-158 AND 188-193, VARIANT 158-ALA-ALA-159 DEL, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  11. "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-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-79 AND LYS-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL14_HUMAN
AccessioniPrimary (citable) accession number: P50914
Secondary accession number(s): Q45RF0
, Q53G20, Q8TBD5, Q8WUT0, Q92579, Q96GR0, Q9BSB8, Q9BW65, Q9BYF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 4, 2008
Last modified: February 4, 2015
This is version 154 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Ribosomal proteins
    Ribosomal proteins families and list of entries
  6. 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.