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Protein

E3 ubiquitin-protein ligase TRIM23

Gene

Trim23

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Acts as an E3 ubiquitin-protein ligase (By similarity). The C-terminus can act as an allosteric activator of the cholera toxin catalytic subunit.By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri31 – 7646RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri122 – 16847B box-type; degeneratePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi411 – 4188GTPBy similarity
Nucleotide bindingi454 – 4585GTPBy similarity
Nucleotide bindingi513 – 5164GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

GTP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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
Tripartite motif-containing protein 23
Gene namesi
Name:Trim23
Synonyms:Ard-1, Ard1, Arfd1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621587. Trim23.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 573573E3 ubiquitin-protein ligase TRIM23PRO_0000207485Add
BLAST

Proteomic databases

PaxDbiP36407.
PRIDEiP36407.

Interactioni

Subunit structurei

Interacts with PSCD1.By similarity

Protein-protein interaction databases

BioGridi249495. 1 interaction.
STRINGi10116.ENSRNOP00000016647.

Structurei

3D structure databases

ProteinModelPortaliP36407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 573184ARF-likeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili351 – 37828Sequence analysisAdd
BLAST

Domaini

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

Sequence similaritiesi

In the C-terminal section; belongs to the small GTPase superfamily. Arf family.Curated
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri31 – 7646RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri122 – 16847B box-type; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG0070. Eukaryota.
KOG4185. Eukaryota.
ENOG410ZGPK. LUCA.
HOVERGENiHBG000551.
InParanoidiP36407.
KOiK07963.
PhylomeDBiP36407.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003649. 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]
PfamiPF00025. Arf. 1 hit.
PF00643. zf-B_box. 1 hit.
PF14634. zf-RING_5. 1 hit.
[Graphical view]
PRINTSiPR00328. SAR1GTPBP.
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51417. ARF. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P36407-1) [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
MAALAVNKPG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL
60 70 80 90 100
CGHTVCHDCL TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE
110 120 130 140 150
RLQNGHIGQY GAAEEALGIS GESIIRCDED EAHVASVYCT VCATHLCSEC
160 170 180 190 200
SQVTHSTKTL AKHRRVPLAD KPHEKTMCCQ HQVHAIEFVC LEEACQTSPL
210 220 230 240 250
MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF TEEISDYSRK
260 270 280 290 300
LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCVRA YFSDLHETLC
310 320 330 340 350
RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSQVSTACL HCKTLQQDDC
360 370 380 390 400
RVVLAKQEIT RLLETLQKQQ QQFTEVADHI QLDASIPVTF TKDNRVYHGP
410 420 430 440 450
KMEIRVVTLG LDGAGKTTIL FKLKQDEFMQ PIPTIGFNVE TVEYKNLKFT
460 470 480 490 500
IWDVGGKHKL RPLWKHYYLN TQAVVFVVDS SHRDRISEAH SELAKLLTEK
510 520 530 540 550
ELRDALLLIF ANKQDVAGAL SVEEITELLS LHKLCCGRSW YIQGCDARSG
560 570
MGLYEGLDWL SRQLVAAGVL DVA
Length:573
Mass (Da):63,892
Last modified:August 10, 2010 - v2
Checksum:i62263E1DE6C2C909
GO
Isoform 2 (identifier: P36407-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     216-276: Missing.

Show »
Length:512
Mass (Da):57,098
Checksum:i79B2CFF27AAF5814
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611T → S in AAA41301 (PubMed:15057822).Curated
Sequence conflicti342 – 3421C → CE in AAA41301 (PubMed:15057822).Curated
Sequence conflicti398 – 3981H → Y in AAA41301 (PubMed:15057822).Curated
Sequence conflicti456 – 4561G → E in AAA41301 (PubMed:15057822).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei216 – 27661Missing in isoform 2. CuratedVSP_039562Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04760 mRNA. Translation: AAA41301.1.
RefSeqiNP_001094107.1. NM_001100637.1.
UniGeneiRn.6763.

Genome annotation databases

GeneIDi81002.
KEGGirno:81002.
UCSCiRGD:621587. rat. [P36407-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04760 mRNA. Translation: AAA41301.1.
RefSeqiNP_001094107.1. NM_001100637.1.
UniGeneiRn.6763.

3D structure databases

ProteinModelPortaliP36407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249495. 1 interaction.
STRINGi10116.ENSRNOP00000016647.

Proteomic databases

PaxDbiP36407.
PRIDEiP36407.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81002.
KEGGirno:81002.
UCSCiRGD:621587. rat. [P36407-1]

Organism-specific databases

CTDi373.
RGDi621587. Trim23.

Phylogenomic databases

eggNOGiKOG0070. Eukaryota.
KOG4185. Eukaryota.
ENOG410ZGPK. LUCA.
HOVERGENiHBG000551.
InParanoidiP36407.
KOiK07963.
PhylomeDBiP36407.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiP36407.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003649. 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]
PfamiPF00025. Arf. 1 hit.
PF00643. zf-B_box. 1 hit.
PF14634. zf-RING_5. 1 hit.
[Graphical view]
PRINTSiPR00328. SAR1GTPBP.
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51417. ARF. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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] OF 21-573 (ISOFORM 1).

Entry informationi

Entry nameiTRI23_RAT
AccessioniPrimary (citable) accession number: P36407
Secondary accession number(s): D3ZT39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: August 10, 2010
Last modified: July 6, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.