Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P36406 (TRI23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase TRIM23

EC=6.3.2.-
Alternative name(s):
ADP-ribosylation factor domain-containing protein 1
GTP-binding protein ARD-1
RING finger protein 46
Tripartite motif-containing protein 23
Gene names
Name:TRIM23
Synonyms:ARD1, ARFD1, RNF46
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as an E3 ubiquitin-protein ligase. In the presence of the human cytomegalovirus (HCMV) protein UL144, participates in 'Lys-63'-linked auto-ubiquitination of TRAF6 resulting in the virally controlled activation of NF-kappa-B at early time of infection. The C-terminus can act as an allosteric activator of the cholera toxin catalytic subunit. Ref.6

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with PSCD1. Interacts with human cytomegalovirus protein UL144; this interaction might causes auto-ubiquitination of TRAF6, leading to NF-kappaB activation. Ref.5 Ref.7

Subcellular location

Endomembrane system. Golgi apparatus membrane. Lysosome membrane. Note: Membrane-associated with the Golgi complex and lysosomal structures. Ref.4

Domain

The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity.

Sequence similarities

In the C-terminal section; belongs to the small GTPase superfamily. Arf family.

Contains 1 B box-type zinc finger.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processHost-virus interaction
Ubl conjugation pathway
   Cellular componentGolgi apparatus
Lysosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandGTP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay PubMed 8700863. Source: GOC

positive regulation of catalytic activity

Traceable author statement Ref.1. Source: GOC

protein ubiquitination

Inferred from direct assay Ref.6. Source: HGNC

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi membrane

Inferred from direct assay Ref.4. Source: HGNC

lysosomal membrane

Inferred from direct assay Ref.4. Source: HGNC

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGDP binding

Inferred from direct assay PubMed 8700863. Source: HGNC

GTP binding

Inferred from direct assay PubMed 8700863. Source: HGNC

GTPase activity

Inferred from direct assay PubMed 8700863. Source: HGNC

enzyme activator activity

Traceable author statement Ref.1. Source: ProtInc

identical protein binding

Inferred from physical interaction PubMed 16189514PubMed 22493164. Source: IntAct

ubiquitin-protein ligase activity

Inferred from direct assay Ref.6. Source: HGNC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-740098,EBI-740098
GEMP550403EBI-740098,EBI-744104
Hoxa1P090222EBI-740098,EBI-3957603From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: P36406-1)

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.
Isoform Beta (identifier: P36406-2)

The sequence of this isoform differs from the canonical sequence as follows:
     551-574: GMGLYEGLDWLSRQLVAAGVLDVA → VFQIICDQYTGKEVVTEKG
Isoform Gamma (identifier: P36406-3)

The sequence of this isoform differs from the canonical sequence as follows:
     541-574: WYIQGCDARSGMGLYEGLDWLSRQLVAAGVLDVA → CFSDNM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574E3 ubiquitin-protein ligase TRIM23
PRO_0000207483

Regions

Zinc finger31 – 7646RING-type; degenerate
Zinc finger122 – 16847B box-type; degenerate
Nucleotide binding411 – 4188GTP By similarity
Nucleotide binding454 – 4585GTP By similarity
Nucleotide binding513 – 5164GTP By similarity
Region390 – 574185ARF-like
Coiled coil352 – 37928 Potential

Natural variations

Alternative sequence541 – 57434WYIQG…VLDVA → CFSDNM in isoform Gamma.
VSP_000297
Alternative sequence551 – 57424GMGLY…VLDVA → VFQIICDQYTGKEVVTEKG in isoform Beta.
VSP_000296
Natural variant4801D → N.
Corresponds to variant rs34046496 [ dbSNP | Ensembl ].
VAR_048320

Experimental info

Mutagenesis341C → A: Loss of E3 ubiquitin-protein ligase activity. Ref.6
Mutagenesis531H → A: Loss of E3 ubiquitin-protein ligase activity. Ref.6
Mutagenesis4181T → N: Maintains GTPase activity. Increases interaction with PSCD1. Ref.5
Mutagenesis4581K → I: Suppresses GTPase activity. Decreases interaction with PSCD1. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: CB85923B29BF0320

FASTA57464,067
        10         20         30         40         50         60 
MATLVVNKLG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL 

        70         80         90        100        110        120 
TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGPIGQY GAAEESIGIS 

       130        140        150        160        170        180 
GESIIRCDED EAHLASVYCT VCATHLCSEC SQVTHSTKTL AKHRRVPLAD KPHEKTMCSQ 

       190        200        210        220        230        240 
HQVHAIEFVC LEEGCQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF 

       250        260        270        280        290        300 
TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCIRA YFYDLHETLC 

       310        320        330        340        350        360 
RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSEVSAACL HCEKTLQQDD CRVVLAKQEI 

       370        380        390        400        410        420 
TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG PKMEIRVVTL GLDGAGKTTI 

       430        440        450        460        470        480 
LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD 

       490        500        510        520        530        540 
SSHRDRISEA HSELAKLLTE KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS 

       550        560        570 
WYIQGCDARS GMGLYEGLDW LSRQLVAAGV LDVA 

« Hide

Isoform Beta [UniParc].

Checksum: 21399953A4224B7A
Show »

FASTA56963,690
Isoform Gamma [UniParc].

Checksum: D21D92EED6E967A2
Show »

FASTA54661,068

References

« Hide 'large scale' references
[1]"ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain."
Mishima K., Tsuchiya M., Nightingale M.S., Moss J., Vaughan M.
J. Biol. Chem. 268:8801-8807(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
[2]"The tripartite motif family identifies cell compartments."
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A.
EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
[3]"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] (ISOFORM ALPHA).
Tissue: Brain.
[4]"Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus."
Vitale N., Horiba K., Ferrans V.J., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 95:8613-8618(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)."
Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W., Moss J., Vaughan M.
J. Biol. Chem. 275:21331-21339(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSCD1, MUTAGENESIS OF THR-418 AND LYS-458.
[6]"E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)."
Vichi A., Payne D.M., Pacheco-Rodriguez G., Moss J., Vaughan M.
Proc. Natl. Acad. Sci. U.S.A. 102:1945-1950(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-34 AND HIS-53.
[7]"Identification of TRIM23 as a cofactor involved in the regulation of NF-kappaB by human cytomegalovirus."
Poole E., Groves I., MacDonald A., Pang Y., Alcami A., Sinclair J.
J. Virol. 83:3581-3590(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL144.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04510 mRNA. Translation: AAA35940.1.
AF230397 mRNA. Translation: AAG50176.1.
AF230398 mRNA. Translation: AAG50177.1.
AF230399 mRNA. Translation: AAG50178.1.
BC022510 mRNA. Translation: AAH22510.1.
PIRA46054.
RefSeqNP_001647.1. NM_001656.3.
NP_150230.1. NM_033227.2.
NP_150231.1. NM_033228.2.
UniGeneHs.792.

3D structure databases

ProteinModelPortalP36406.
SMRP36406. Positions 16-79, 127-219, 371-565.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106868. 55 interactions.
IntActP36406. 44 interactions.
MINTMINT-1442172.
STRING9606.ENSP00000231524.

PTM databases

PhosphoSiteP36406.

Polymorphism databases

DMDM543839.

Proteomic databases

PaxDbP36406.
PRIDEP36406.

Protocols and materials databases

DNASU373.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231524; ENSP00000231524; ENSG00000113595. [P36406-1]
ENST00000274327; ENSP00000274327; ENSG00000113595. [P36406-3]
ENST00000381018; ENSP00000370406; ENSG00000113595. [P36406-2]
GeneID373.
KEGGhsa:373.
UCSCuc003jtw.3. human. [P36406-3]
uc003jtx.3. human. [P36406-2]
uc003jty.3. human. [P36406-1]

Organism-specific databases

CTD373.
GeneCardsGC05M064885.
HGNCHGNC:660. TRIM23.
HPAHPA039605.
MIM601747. gene.
neXtProtNX_P36406.
PharmGKBPA24943.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000008208.
HOVERGENHBG000551.
InParanoidP36406.
KOK07963.
OMARAVRCPF.
OrthoDBEOG76DTS0.
PhylomeDBP36406.
TreeFamTF320703.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressP36406.
BgeeP36406.
CleanExHS_TRIM23.
GenevestigatorP36406.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
3.40.50.300. 1 hit.
InterProIPR003649. Bbox_C.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
IPR000315. Znf_B-box.
IPR007087. Znf_C2H2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00025. Arf. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSPR00328. SAR1GTPBP.
SMARTSM00177. ARF. 1 hit.
SM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51417. ARF. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTRIM23.
GenomeRNAi373.
NextBio1557.
PROP36406.
SOURCESearch...

Entry information

Entry nameTRI23_HUMAN
AccessionPrimary (citable) accession number: P36406
Secondary accession number(s): Q9BZY4, Q9BZY5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 138 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

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