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UniProtKB - P36406 (TRI23_HUMAN)

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Protein

E3 ubiquitin-protein ligase TRIM23

Gene

TRIM23

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

Functioni

Acts as an E3 ubiquitin-protein ligase. Plays an essential role in autophagy activation during viral infection. Mechanistically, activates TANK-binding kinase 1/TBK1 by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor SQSTM1. In order to achieve this function, TRIM23 mediates 'Lys-27'-linked auto-ubiquitination of its ADP-ribosylation factor (ARF) domain to induce its GTPase activity and its recruitment to autophagosomes (PubMed:28871090).2 Publications
(Microbial infection) Mediates TRAF6 auto-ubiquitination in the presence of human cytomegalovirus protein UL144, resulting in the virally controlled activation of NF-kappa-B stimulation at early times of HCMV infection.1 Publication

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 76RING-type; degeneratePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri122 – 168B box-type; degeneratePROSITE-ProRule annotationAdd BLAST47
Nucleotide bindingi411 – 418GTPBy similarity8
Nucleotide bindingi454 – 458GTPBy similarity5
Nucleotide bindingi513 – 516GTPBy similarity4

GO - Molecular functioni

  • enzyme activator activity Source: ProtInc
  • GDP binding Source: HGNC
  • GTPase activity Source: HGNC
  • GTP binding Source: HGNC
  • identical protein binding Source: IntAct
  • nucleic acid binding Source: InterPro
  • ubiquitin-protein transferase activity Source: HGNC
  • zinc ion binding Source: InterPro
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • innate immune response Source: UniProtKB-KW
  • protein ubiquitination Source: HGNC
  • viral process Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionTransferase
Biological processHost-virus interaction, Immunity, Innate immunity, Ubl conjugation pathway
LigandGTP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM23 (EC:2.3.2.27)
Alternative name(s):
ADP-ribosylation factor domain-containing protein 1
GTP-binding protein ARD-1
RING finger protein 46
RING-type E3 ubiquitin transferase TRIM23Curated
Tripartite motif-containing protein 23
Gene namesi
Name:TRIM23
Synonyms:ARD1, ARFD1, RNF46
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000113595.14
HGNCiHGNC:660 TRIM23
MIMi601747 gene
neXtProtiNX_P36406

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi34C → A: Loss of E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi53H → A: Loss of E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi418T → N: Maintains GTPase activity. Increases interaction with PSCD1. 1 Publication1
Mutagenesisi458K → I: Suppresses GTPase activity. Decreases interaction with PSCD1. 1 Publication1

Organism-specific databases

DisGeNETi373
OpenTargetsiENSG00000113595
PharmGKBiPA24943

Polymorphism and mutation databases

BioMutaiTRIM23
DMDMi543839

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002074831 – 574E3 ubiquitin-protein ligase TRIM23Add BLAST574

Proteomic databases

EPDiP36406
MaxQBiP36406
PaxDbiP36406
PeptideAtlasiP36406
PRIDEiP36406
ProteomicsDBi55200
55201 [P36406-2]
55202 [P36406-3]

PTM databases

iPTMnetiP36406
PhosphoSitePlusiP36406

Expressioni

Gene expression databases

BgeeiENSG00000113595
CleanExiHS_TRIM23
ExpressionAtlasiP36406 baseline and differential
GenevisibleiP36406 HS

Organism-specific databases

HPAiHPA039605

Interactioni

Subunit structurei

Homodimer. Interacts with PSCD1. Interacts with UBE2D2 (PubMed:28681414). Interacts with TBK1 (via N-terminal kinase domain) and p62/SQSTM1.3 Publications
(Microbial infection) Interacts with human cytomegalovirus protein UL144; this interaction might cause autoubiquitination of TRAF6, leading to NF-kappa-B activation.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-740098,EBI-740098
G2XKQ03EBI-740098,EBI-10175576
ACTN4A0A0S2Z3G13EBI-740098,EBI-16430749
ANKRD36BP1Q96IX93EBI-740098,EBI-744859
AQP1P299725EBI-740098,EBI-745213
ARFGAP1Q8N6T33EBI-740098,EBI-716933
ARHGEF3Q9NR813EBI-740098,EBI-10312733
ATPAF2Q8N5M16EBI-740098,EBI-1166928
BAG1Q999335EBI-740098,EBI-1030678
C19orf57Q0VDD74EBI-740098,EBI-741210
C8orf33Q9H7E93EBI-740098,EBI-715389
CARD9Q9H2573EBI-740098,EBI-751319
CCDC146Q8IYE0-23EBI-740098,EBI-10247802
CCDC25Q86WR03EBI-740098,EBI-2690264
CDC20BQ86Y333EBI-740098,EBI-10260504
CDR2Q018505EBI-740098,EBI-1181367
CFAP53Q96M913EBI-740098,EBI-742422
COX5BP106064EBI-740098,EBI-1053725
CREB5Q02930-33EBI-740098,EBI-10192698
CXCL14O957153EBI-740098,EBI-2798068
DCXO436023EBI-740098,EBI-8646694
DMC1Q145653EBI-740098,EBI-930865
DMRT3Q9NQL93EBI-740098,EBI-9679045
DOCK2Q926083EBI-740098,EBI-448771
EAF2Q96CJ13EBI-740098,EBI-1245604
EXOC3-AS1Q8N2X65EBI-740098,EBI-749333
FAM103A1Q9BTL35EBI-740098,EBI-744023
FAM110AQ9BQ895EBI-740098,EBI-1752811
FAM133AQ8N9E05EBI-740098,EBI-10268158
FAM193BQ96PV7-23EBI-740098,EBI-10292648
FAM208BQ5VWN6-23EBI-740098,EBI-10172380
FAM83AQ86UY53EBI-740098,EBI-1384254
FAM90A1Q86YD75EBI-740098,EBI-6658203
FBF1Q8TES7-63EBI-740098,EBI-10244131
FLJ38668C0H5X23EBI-740098,EBI-10176227
GAD1A0A0S2Z4D93EBI-740098,EBI-16430771
GATA2P237693EBI-740098,EBI-2806671
GEMP550405EBI-740098,EBI-744104
GMCL2Q8NEA93EBI-740098,EBI-745707
GPANK1O958725EBI-740098,EBI-751540
GPKOWQ929173EBI-740098,EBI-746309
HAUS1Q96CS23EBI-740098,EBI-2514791
Hoxa1P090222EBI-740098,EBI-3957603From Mus musculus.
HOXB5P090675EBI-740098,EBI-3893317
HSPB7Q9UBY93EBI-740098,EBI-739361
IQUBQ8NA545EBI-740098,EBI-10220600
JOSD1Q150403EBI-740098,EBI-2510602
KAT5Q929933EBI-740098,EBI-399080
KIFC3Q9BVG83EBI-740098,EBI-2125614
KLHL42Q9P2K65EBI-740098,EBI-739890
KRT6AP025388EBI-740098,EBI-702198
LGALS8O002143EBI-740098,EBI-740058
LINC00526Q96FQ73EBI-740098,EBI-10286106
LMO2P257913EBI-740098,EBI-739696
MORN4Q8NDC45EBI-740098,EBI-10269566
MRP4P329023EBI-740098,EBI-16248From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
MRPL4Q9BYD33EBI-740098,EBI-721368
MRPL45Q9BRJ23EBI-740098,EBI-2514313
MTFR2Q6P4443EBI-740098,EBI-10252703
NEK6Q9HC983EBI-740098,EBI-740364
NFU1Q9UMS03EBI-740098,EBI-725252
NXT2Q9NPJ83EBI-740098,EBI-752122
PHF1O431893EBI-740098,EBI-530034
PIAS2O759283EBI-740098,EBI-348555
PIK3R2O004593EBI-740098,EBI-346930
PKP4Q995693EBI-740098,EBI-726447
POLLQ9UGP5-23EBI-740098,EBI-10320765
PPIL2Q133563EBI-740098,EBI-7705988
PPP1R18Q6NYC83EBI-740098,EBI-2557469
PSMA1P257865EBI-740098,EBI-359352
RNF213Q63HN8-63EBI-740098,EBI-10248548
RNF6A0A0S2Z4G93EBI-740098,EBI-16428950
RSRC2Q7L4I2-23EBI-740098,EBI-10256202
RTP5Q14D333EBI-740098,EBI-10217913
SH2D4AQ9H7883EBI-740098,EBI-747035
SH2D4AQ9H788-23EBI-740098,EBI-10308083
SIAH1Q8IUQ43EBI-740098,EBI-747107
SLC25A6P122363EBI-740098,EBI-356254
SMG9Q9H0W85EBI-740098,EBI-2872322
SNAI1O958635EBI-740098,EBI-1045459
SNAI2O436233EBI-740098,EBI-9876238
SNRPBP14678-23EBI-740098,EBI-372475
SORBS3O605045EBI-740098,EBI-741237
SPG21Q9NZD83EBI-740098,EBI-742688
STK19B7ZLI83EBI-740098,EBI-10176124
TBC1D22BQ9NU195EBI-740098,EBI-8787464
TMSB4XQ0P5Q03EBI-740098,EBI-10226570
TNFAIP3P215805EBI-740098,EBI-527670
TRAF1Q130773EBI-740098,EBI-359224
TRIM29Q0P6H73EBI-740098,EBI-10226710
TRIM29Q141343EBI-740098,EBI-702370
TRIM42Q8IWZ53EBI-740098,EBI-5235829
TROAPQ128155EBI-740098,EBI-2349743
TSHZ3Q63HK53EBI-740098,EBI-9053916
TXNDC5Q86UY03EBI-740098,EBI-2825190
UBE2IQ7KZS03EBI-740098,EBI-10180829
USP20Q9Y2K63EBI-740098,EBI-2511991
UTP23Q9BRU93EBI-740098,EBI-5457544
WDR25Q64LD23EBI-740098,EBI-744560
ZC2HC1CQ53FD03EBI-740098,EBI-740767
ZNF564Q8TBZ85EBI-740098,EBI-10273713
ZNF581Q9P0T46EBI-740098,EBI-745520
ZNF688A0A0S2Z5X43EBI-740098,EBI-16429014
ZNF688A0A0S2Z6P03EBI-740098,EBI-16429989

GO - Molecular functioni

  • identical protein binding Source: IntAct
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi106868, 161 interactors
CORUMiP36406
IntActiP36406, 208 interactors
MINTiP36406
STRINGi9606.ENSP00000231524

Structurei

Secondary structure

1574
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni32 – 34Combined sources3
Beta strandi40 – 42Combined sources3
Beta strandi46 – 48Combined sources3
Beta strandi54 – 56Combined sources3
Helixi57 – 62Combined sources6
Beta strandi69 – 71Combined sources3
Turni73 – 75Combined sources3
Beta strandi78 – 80Combined sources3
Helixi85 – 88Combined sources4
Helixi93 – 103Combined sources11

3D structure databases

ProteinModelPortaliP36406
SMRiP36406
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni390 – 574ARF-likeAdd BLAST185

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili352 – 379Sequence analysisAdd BLAST28

Domaini

The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity. This domain is catalytically active as a dimer.1 Publication

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 76RING-type; degeneratePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri122 – 168B box-type; degeneratePROSITE-ProRule annotationAdd BLAST47

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG0070 Eukaryota
KOG4185 Eukaryota
ENOG410ZGPK LUCA
GeneTreeiENSGT00780000121855
HOGENOMiHOG000008208
HOVERGENiHBG000551
InParanoidiP36406
KOiK07963
OMAiCVRAYFS
OrthoDBiEOG091G05L6
PhylomeDBiP36406
TreeFamiTF320703

Family and domain databases

CDDicd00021 BBOX, 1 hit
Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR003649 Bbox_C
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR024156 Small_GTPase_ARF
IPR006689 Small_GTPase_ARF/SAR
IPR027370 Znf-RING_LisH
IPR000315 Znf_B-box
IPR013087 Znf_C2H2_type
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF00025 Arf, 1 hit
PF00643 zf-B_box, 1 hit
PF13445 zf-RING_UBOX, 1 hit
PRINTSiPR00328 SAR1GTPBP
SMARTiView protein in SMART
SM00502 BBC, 1 hit
SM00336 BBOX, 2 hits
SM00184 RING, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51417 ARF, 1 hit
PS50119 ZF_BBOX, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha (identifier: P36406-1) [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
MATLVVNKLG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL 
        60         70         80         90        100
CGHTVCHDCL TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE 
       110        120        130        140        150
RLQNGPIGQY GAAEESIGIS GESIIRCDED EAHLASVYCT VCATHLCSEC 
       160        170        180        190        200
SQVTHSTKTL AKHRRVPLAD KPHEKTMCSQ HQVHAIEFVC LEEGCQTSPL 
       210        220        230        240        250
MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF TEEISDYSRK 
       260        270        280        290        300
LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCIRA YFYDLHETLC 
       310        320        330        340        350
RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSEVSAACL HCEKTLQQDD 
       360        370        380        390        400
CRVVLAKQEI TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG 
       410        420        430        440        450
PKMEIRVVTL GLDGAGKTTI LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF 
       460        470        480        490        500
TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD SSHRDRISEA HSELAKLLTE 
       510        520        530        540        550
KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS WYIQGCDARS 
       560        570 
GMGLYEGLDW LSRQLVAAGV LDVA
Length:574
Mass (Da):64,067
Last modified:June 1, 1994 - v1
Checksum:iCB85923B29BF0320
GO
Isoform Beta (identifier: P36406-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     551-574: GMGLYEGLDWLSRQLVAAGVLDVA → VFQIICDQYTGKEVVTEKG

Show »
Length:569
Mass (Da):63,690
Checksum:i21399953A4224B7A
GO
Isoform Gamma (identifier: P36406-3) [UniParc]FASTAAdd to basket

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

Show »
Length:546
Mass (Da):61,068
Checksum:iD21D92EED6E967A2
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_048320480D → N. Corresponds to variant dbSNP:rs34046496Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000297541 – 574WYIQG…VLDVA → CFSDNM in isoform Gamma. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_000296551 – 574GMGLY…VLDVA → VFQIICDQYTGKEVVTEKG in isoform Beta. 1 PublicationAdd BLAST24

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS3986.1 [P36406-3]
CCDS3987.1 [P36406-1]
CCDS43322.1 [P36406-2]
PIRiA46054
RefSeqiNP_001647.1, NM_001656.3 [P36406-1]
NP_150230.1, NM_033227.2 [P36406-2]
NP_150231.1, NM_033228.2 [P36406-3]
XP_016864933.1, XM_017009444.1 [P36406-2]
UniGeneiHs.792

Genome annotation databases

EnsembliENST00000231524; ENSP00000231524; ENSG00000113595 [P36406-1]
ENST00000274327; ENSP00000274327; ENSG00000113595 [P36406-3]
ENST00000381018; ENSP00000370406; ENSG00000113595 [P36406-2]
GeneIDi373
KEGGihsa:373
UCSCiuc003jtw.4 human [P36406-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTRI23_HUMAN
AccessioniPrimary (citable) accession number: P36406
Secondary accession number(s): Q9BZY4, Q9BZY5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 18, 2018
This is version 181 of the entry and version 1 of the sequence. See 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 5
    Human chromosome 5: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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