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Q14657

- LAGE3_HUMAN

UniProt

Q14657 - LAGE3_HUMAN

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Protein

EKC/KEOPS complex subunit LAGE3

Gene

LAGE3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. LAGE3 functions as a dimerization module for the complex (By similarity).By similarity

GO - Biological processi

  1. tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
EKC/KEOPS complex subunit LAGE3
Alternative name(s):
L antigen family member 3
Protein ESO-3
Protein ITBA2
Gene namesi
Name:LAGE3
Synonyms:DXS9879E, ESO3, ITBA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:26058. LAGE3.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394540.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 143143EKC/KEOPS complex subunit LAGE3PRO_0000218924Add
BLAST

Proteomic databases

MaxQBiQ14657.
PaxDbiQ14657.
PeptideAtlasiQ14657.
PRIDEiQ14657.

PTM databases

PhosphoSiteiQ14657.

Miscellaneous databases

PMAP-CutDBQ14657.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

BgeeiQ14657.
CleanExiHS_LAGE3.
ExpressionAtlasiQ14657. baseline and differential.
GenevestigatoriQ14657.

Organism-specific databases

HPAiHPA036122.
HPA036123.

Interactioni

Subunit structurei

Component of the EKC/KEOPS complex composed of at least TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes.1 Publication

Protein-protein interaction databases

BioGridi113888. 35 interactions.
IntActiQ14657. 4 interactions.
MINTiMINT-4719865.
STRINGi9606.ENSP00000349923.

Structurei

3D structure databases

ProteinModelPortaliQ14657.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CTAG/PCC1 family.Curated

Phylogenomic databases

eggNOGiNOG40896.
GeneTreeiENSGT00410000025802.
HOGENOMiHOG000040003.
HOVERGENiHBG052154.
InParanoidiQ14657.
KOiK15902.
OMAiWTAKDPR.
PhylomeDBiQ14657.
TreeFamiTF337064.

Family and domain databases

InterProiIPR015419. EKC/KEOPS_Pcc1.
[Graphical view]
PfamiPF09341. Pcc1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14657-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRDADADAGG GADGGDGRGG HSCRGGVDTA AAPAGGAPPA HAPGPGRDAA
60 70 80 90 100
SAARGSRMRP HIFTLSVPFP TPLEAEIAHG SLAPDAEPHQ RVVGKDLTVS
110 120 130 140
GRILVVRWKA EDCRLLRISV INFLDQLSLV VRTMQRFGPP VSR
Length:143
Mass (Da):14,804
Last modified:October 11, 2004 - v2
Checksum:iAD164559371449F8
GO

Sequence cautioni

The sequence CAA63489.1 differs from that shown. Reason: Frameshift at position 54.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX936365 Genomic DNA. Translation: CAI43195.1.
BC015744 mRNA. Translation: AAH15744.2.
BC062330 mRNA. Translation: AAH62330.1.
X92896 mRNA. Translation: CAA63489.1. Frameshift.
CCDSiCCDS14753.1.
RefSeqiNP_006005.2. NM_006014.4.
UniGeneiHs.444619.

Genome annotation databases

EnsembliENST00000357360; ENSP00000349923; ENSG00000196976.
GeneIDi8270.
KEGGihsa:8270.
UCSCiuc004fln.1. human.

Polymorphism databases

DMDMi54041570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX936365 Genomic DNA. Translation: CAI43195.1 .
BC015744 mRNA. Translation: AAH15744.2 .
BC062330 mRNA. Translation: AAH62330.1 .
X92896 mRNA. Translation: CAA63489.1 . Frameshift.
CCDSi CCDS14753.1.
RefSeqi NP_006005.2. NM_006014.4.
UniGenei Hs.444619.

3D structure databases

ProteinModelPortali Q14657.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113888. 35 interactions.
IntActi Q14657. 4 interactions.
MINTi MINT-4719865.
STRINGi 9606.ENSP00000349923.

PTM databases

PhosphoSitei Q14657.

Polymorphism databases

DMDMi 54041570.

Proteomic databases

MaxQBi Q14657.
PaxDbi Q14657.
PeptideAtlasi Q14657.
PRIDEi Q14657.

Protocols and materials databases

DNASUi 8270.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357360 ; ENSP00000349923 ; ENSG00000196976 .
GeneIDi 8270.
KEGGi hsa:8270.
UCSCi uc004fln.1. human.

Organism-specific databases

CTDi 8270.
GeneCardsi GC0XM153707.
HGNCi HGNC:26058. LAGE3.
HPAi HPA036122.
HPA036123.
MIMi 300060. gene.
neXtProti NX_Q14657.
PharmGKBi PA128394540.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40896.
GeneTreei ENSGT00410000025802.
HOGENOMi HOG000040003.
HOVERGENi HBG052154.
InParanoidi Q14657.
KOi K15902.
OMAi WTAKDPR.
PhylomeDBi Q14657.
TreeFami TF337064.

Miscellaneous databases

GenomeRNAii 8270.
NextBioi 31037.
PMAP-CutDB Q14657.
PROi Q14657.
SOURCEi Search...

Gene expression databases

Bgeei Q14657.
CleanExi HS_LAGE3.
ExpressionAtlasi Q14657. baseline and differential.
Genevestigatori Q14657.

Family and domain databases

InterProi IPR015419. EKC/KEOPS_Pcc1.
[Graphical view ]
Pfami PF09341. Pcc1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "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: Blood and Pancreas.
  3. "Characterization and fine localization of two new genes in Xq28 using the genomic sequence/EST database screening approach."
    Faranda S., Frattini A., Zucchi I., Patrosso C., Milanesi L., Montagna C., Vezzoni P.
    Genomics 34:323-327(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-143, TISSUE SPECIFICITY.
    Tissue: Liver.
  4. "A new member of the NY-ESO-1 gene family is ubiquitously expressed in somatic tissues and evolutionarily conserved."
    Alpen B., Guere A.O., Scanlan M.J., Old L.J., Chen Y.-T.
    Gene 297:141-149(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases by the human tumour antigen PRAME."
    Costessi A., Mahrour N., Sharma V., Stunnenberg R., Stoel M.A., Tijchon E., Conaway J.W., Conaway R.C., Stunnenberg H.G.
    PLoS ONE 7:E42822-E42822(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EKC/KEOPS COMPLEX, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiLAGE3_HUMAN
AccessioniPrimary (citable) accession number: Q14657
Secondary accession number(s): Q5HY39, Q8IZ78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 11, 2004
Last modified: October 29, 2014
This is version 101 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3