Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E3 ubiquitin-protein ligase TRIM33

Gene

TRIM33

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

Functioni

Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade).By similarity4 Publications

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 fingeri125 – 154RING-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri212 – 259B box-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri271 – 312B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri887 – 934PHD-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

  • co-SMAD binding Source: BHF-UCL
  • DNA binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB-KW
  • R-SMAD binding Source: BHF-UCL
  • ubiquitin-protein transferase activity Source: Reactome
  • zinc ion binding Source: InterPro

GO - Biological processi

  • negative regulation of BMP signaling pathway Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: Reactome
  • protein ubiquitination Source: UniProtKB
  • regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
SignaLinkiQ9UPN9.
SIGNORiQ9UPN9.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM33 (EC:6.3.2.-)
Alternative name(s):
Ectodermin homolog
RET-fused gene 7 protein
Short name:
Protein Rfg7
Transcription intermediary factor 1-gamma
Short name:
TIF1-gamma
Tripartite motif-containing protein 33
Gene namesi
Name:TRIM33
Synonyms:KIAA1113, RFG7, TIF1G
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16290. TRIM33.

Subcellular locationi

GO - Cellular componenti

  • intracellular membrane-bounded organelle Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TRIM33 is found in papillary thyroid carcinomas (PTCs). Translocation t(1;10)(p13;q11) with RET. The translocation generates the TRIM33/RET (PTC7) oncogene.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi125C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-128. 1 Publication1
Mutagenesisi128C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-125. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei964 – 965Breakpoint for translocation to form TRIM33-RET oncogene2

Organism-specific databases

DisGeNETi51592.
MalaCardsiTRIM33.
OpenTargetsiENSG00000197323.
Orphaneti146. Papillary or follicular thyroid carcinoma.
PharmGKBiPA38118.

Chemistry databases

ChEMBLiCHEMBL2176772.

Polymorphism and mutation databases

BioMutaiTRIM33.
DMDMi313104270.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000563951 – 1127E3 ubiquitin-protein ligase TRIM33Add BLAST1127

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki334Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei515Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei515Omega-N-methylarginine; alternateCombined sources1
Modified residuei535Omega-N-methylarginineCombined sources1
Modified residuei577Asymmetric dimethylarginineCombined sources1
Modified residuei591Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei591Omega-N-methylarginine; alternateCombined sources1
Modified residuei598Asymmetric dimethylarginineCombined sources1
Modified residuei604Asymmetric dimethylarginineCombined sources1
Modified residuei763N6-acetyllysine; alternateCombined sources1
Cross-linki763Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei769N6-acetyllysine; alternateCombined sources1
Cross-linki769Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki776Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki776Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei793N6-acetyllysine; alternateBy similarity1
Cross-linki793Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki793Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei803PhosphoserineBy similarity1
Modified residuei815PhosphothreonineBy similarity1
Cross-linki861Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei862PhosphoserineCombined sources1
Modified residuei951N6-acetyllysineBy similarity1
Modified residuei953N6-acetyllysine; alternateCombined sources1
Cross-linki953Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki1007Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1051PhosphothreonineCombined sources1
Cross-linki1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1102PhosphothreonineCombined sources1
Modified residuei1105PhosphoserineCombined sources1
Cross-linki1118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1119PhosphoserineCombined sources1

Post-translational modificationi

Sumoylated with SUMO1.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UPN9.
PaxDbiQ9UPN9.
PeptideAtlasiQ9UPN9.
PRIDEiQ9UPN9.

PTM databases

iPTMnetiQ9UPN9.
PhosphoSitePlusiQ9UPN9.

Miscellaneous databases

PMAP-CutDBQ9UPN9.

Expressioni

Tissue specificityi

Expressed in stem cells at the bottom of the crypts of the colon (at protein level). Expressed in colon adenomas and adenocarcinomas (at protein level). Expressed in brain, lung, liver, spleen, thymus, prostate, kidney, testis, heart, placenta, pancreas, small intestine, ovary, colon, skeletal muscle and hematopoietic progenitors.

Gene expression databases

BgeeiENSG00000197323.
CleanExiHS_TRIM33.
ExpressionAtlasiQ9UPN9. baseline and differential.
GenevisibleiQ9UPN9. HS.

Organism-specific databases

HPAiHPA004345.

Interactioni

Subunit structurei

Homooligomer and heterooligomer with TRIM24 and TRIM28 family members. Interacts with SMAD4 in unstimulated cells. Found in a complex with SMAD2 and SMAD3 upon addition of TGF-beta. Interacts with SMAD2 and SMAD3. Interacts with SMAD4 under basal and induced conditions and, upon TGF-beta signaling, with activated SMAD2. Forms a ternary complex with SMAD4 and SMAD2 upon TGF-beta signaling.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SMAD2Q157966EBI-2214398,EBI-1040141
SMAD4Q134856EBI-2214398,EBI-347263

GO - Molecular functioni

  • co-SMAD binding Source: BHF-UCL
  • R-SMAD binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi119625. 76 interactors.
DIPiDIP-54262N.
IntActiQ9UPN9. 49 interactors.
MINTiMINT-2822547.
STRINGi9606.ENSP00000351250.

Chemistry databases

BindingDBiQ9UPN9.

Structurei

Secondary structure

11127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi888 – 890Combined sources3
Turni891 – 893Combined sources3
Beta strandi897 – 901Combined sources5
Beta strandi903 – 906Combined sources4
Turni911 – 913Combined sources3
Beta strandi914 – 916Combined sources3
Beta strandi918 – 920Combined sources3
Turni929 – 931Combined sources3
Beta strandi934 – 936Combined sources3
Helixi944 – 947Combined sources4
Helixi960 – 974Combined sources15
Helixi980 – 982Combined sources3
Helixi993 – 996Combined sources4
Helixi1003 – 1010Combined sources8
Beta strandi1011 – 1013Combined sources3
Helixi1021 – 1045Combined sources25
Helixi1061 – 1080Combined sources20
Beta strandi1081 – 1083Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3U5MX-ray3.08A/B/C/D/E/F/G/H/I/J/K/L882-1087[»]
3U5NX-ray1.95A/B882-1087[»]
3U5OX-ray2.70A/B/C/D/E/F/G/H882-1087[»]
3U5PX-ray2.80A/B/C/D/E/F/G/H882-1087[»]
ProteinModelPortaliQ9UPN9.
SMRiQ9UPN9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini974 – 1046BromoPROSITE-ProRule annotationAdd BLAST73

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 147Necessary for E3 ubiquitin-protein ligase activity and repression of SMAD4 signaling and transcriptional repressionAdd BLAST147
Regioni299 – 401Necessary for oligomerizationAdd BLAST103

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili299 – 401Sequence analysisAdd BLAST103

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi13 – 18Poly-Gly6
Compositional biasi44 – 49Poly-Glu6
Compositional biasi545 – 550Poly-Thr6

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 2 B box-type zinc fingers.PROSITE-ProRule annotation
Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri125 – 154RING-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri212 – 259B box-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri271 – 312B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri887 – 934PHD-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITFN. Eukaryota.
ENOG410Z421. LUCA.
GeneTreeiENSGT00530000062982.
HOVERGENiHBG054599.
InParanoidiQ9UPN9.
KOiK08883.
OMAiNEMSRII.
OrthoDBiEOG091G01KK.
PhylomeDBiQ9UPN9.
TreeFamiTF106455.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
4.10.45.10. 1 hit.
InterProiIPR003649. Bbox_C.
IPR001487. Bromodomain.
IPR019786. Zinc_finger_PHD-type_CS.
IPR027370. Znf-RING_LisH.
IPR000315. Znf_B-box.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF00643. zf-B_box. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50014. BROMODOMAIN_2. 1 hit.
PS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 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 Alpha (identifier: Q9UPN9-1) [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
MAENKGGGEA ESGGGGSGSA PVTAGAAGPA AQEAEPPLTA VLVEEEEEEG
60 70 80 90 100
GRAGAEGGAA GPDDGGVAAA SSGSAQAASS PAASVGTGVA GGAVSTPAPA
110 120 130 140 150
PASAPAPGPS AGPPPGPPAS LLDTCAVCQQ SLQSRREAEP KLLPCLHSFC
160 170 180 190 200
LRCLPEPERQ LSVPIPGGSN GDIQQVGVIR CPVCRQECRQ IDLVDNYFVK
210 220 230 240 250
DTSEAPSSSD EKSEQVCTSC EDNASAVGFC VECGEWLCKT CIEAHQRVKF
260 270 280 290 300
TKDHLIRKKE DVSESVGASG QRPVFCPVHK QEQLKLFCET CDRLTCRDCQ
310 320 330 340 350
LLEHKEHRYQ FLEEAFQNQK GAIENLLAKL LEKKNYVHFA ATQVQNRIKE
360 370 380 390 400
VNETNKRVEQ EIKVAIFTLI NEINKKGKSL LQQLENVTKE RQMKLLQQQN
410 420 430 440 450
DITGLSRQVK HVMNFTNWAI ASGSSTALLY SKRLITFQLR HILKARCDPV
460 470 480 490 500
PAANGAIRFH CDPTFWAKNV VNLGNLVIES KPAPGYTPNV VVGQVPPGTN
510 520 530 540 550
HISKTPGQIN LAQLRLQHMQ QQVYAQKHQQ LQQMRMQQPP APVPTTTTTT
560 570 580 590 600
QQHPRQAAPQ MLQQQPPRLI SVQTMQRGNM NCGAFQAHQM RLAQNAARIP
610 620 630 640 650
GIPRHSGPQY SMMQPHLQRQ HSNPGHAGPF PVVSVHNTTI NPTSPTTATM
660 670 680 690 700
ANANRGPTSP SVTAIELIPS VTNPENLPSL PDIPPIQLED AGSSSLDNLL
710 720 730 740 750
SRYISGSHLP PQPTSTMNPS PGPSALSPGS SGLSNSHTPV RPPSTSSTGS
760 770 780 790 800
RGSCGSSGRT AEKTSLSFKS DQVKVKQEPG TEDEICSFSG GVKQEKTEDG
810 820 830 840 850
RRSACMLSSP ESSLTPPLST NLHLESELDA LASLENHVKI EPADMNESCK
860 870 880 890 900
QSGLSSLVNG KSPIRSLMHR SARIGGDGNN KDDDPNEDWC AVCQNGGDLL
910 920 930 940 950
CCEKCPKVFH LTCHVPTLLS FPSGDWICTF CRDIGKPEVE YDCDNLQHSK
960 970 980 990 1000
KGKTAQGLSP VDQRKCERLL LYLYCHELSI EFQEPVPASI PNYYKIIKKP
1010 1020 1030 1040 1050
MDLSTVKKKL QKKHSQHYQI PDDFVADVRL IFKNCERFNE MMKVVQVYAD
1060 1070 1080 1090 1100
TQEINLKADS EVAQAGKAVA LYFEDKLTEI YSDRTFAPLP EFEQEEDDGE
1110 1120
VTEDSDEDFI QPRRKRLKSD ERPVHIK
Length:1,127
Mass (Da):122,533
Last modified:November 30, 2010 - v3
Checksum:i7A36013799E9933C
GO
Isoform Beta (identifier: Q9UPN9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1041-1057: Missing.

Show »
Length:1,110
Mass (Da):120,541
Checksum:i1D415E1C620703A8
GO

Sequence cautioni

The sequence AAD17259 differs from that shown. Reason: Frameshift at position 1114.Curated
The sequence BAA83065 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI13548 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI21895 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti89V → E in CAB55313 (PubMed:10439047).Curated1
Sequence conflicti451 – 453PAA → LLH in CAB55313 (PubMed:10439047).Curated3
Sequence conflicti909F → S in CAB55313 (PubMed:10439047).Curated1
Sequence conflicti1037R → T in AAD17259 (PubMed:10022127).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02949467V → A.Corresponds to variant rs6691166dbSNPEnsembl.1
Natural variantiVAR_042376580M → I in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_042377696L → S.1 PublicationCorresponds to variant rs56151583dbSNPEnsembl.1
Natural variantiVAR_042378811E → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_024616840I → T.4 PublicationsCorresponds to variant rs6537825dbSNPEnsembl.1
Natural variantiVAR_042379885P → S in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_042380961V → M.1 PublicationCorresponds to variant rs55688622dbSNPEnsembl.1
Natural variantiVAR_0423811090P → T.1 PublicationCorresponds to variant rs55784699dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0057741041 – 1057Missing in isoform Beta. 2 PublicationsAdd BLAST17

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF119043 mRNA. Translation: AAD17259.1. Frameshift.
AF220136 mRNA. Translation: AAG53509.1.
AF220137 mRNA. Translation: AAG53510.1.
AB029036 mRNA. Translation: BAA83065.1. Different initiation.
AL390241, AL035410 Genomic DNA. Translation: CAI13548.1. Sequence problems.
AL390241, AL035410 Genomic DNA. Translation: CAI13550.1.
AL390241, AL035410 Genomic DNA. Translation: CAI13551.1.
AL035410, AL390241 Genomic DNA. Translation: CAI21895.1. Sequence problems.
AL035410, AL390241 Genomic DNA. Translation: CAI21896.1.
AL035410, AL390241 Genomic DNA. Translation: CAI21897.1.
AJ132948 mRNA. Translation: CAB55313.1.
CCDSiCCDS872.1. [Q9UPN9-1]
CCDS873.1. [Q9UPN9-2]
RefSeqiNP_056990.3. NM_015906.3. [Q9UPN9-1]
NP_148980.2. NM_033020.2. [Q9UPN9-2]
UniGeneiHs.26837.

Genome annotation databases

EnsembliENST00000358465; ENSP00000351250; ENSG00000197323. [Q9UPN9-1]
ENST00000369543; ENSP00000358556; ENSG00000197323. [Q9UPN9-2]
GeneIDi51592.
KEGGihsa:51592.
UCSCiuc001eew.3. human. [Q9UPN9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF119043 mRNA. Translation: AAD17259.1. Frameshift.
AF220136 mRNA. Translation: AAG53509.1.
AF220137 mRNA. Translation: AAG53510.1.
AB029036 mRNA. Translation: BAA83065.1. Different initiation.
AL390241, AL035410 Genomic DNA. Translation: CAI13548.1. Sequence problems.
AL390241, AL035410 Genomic DNA. Translation: CAI13550.1.
AL390241, AL035410 Genomic DNA. Translation: CAI13551.1.
AL035410, AL390241 Genomic DNA. Translation: CAI21895.1. Sequence problems.
AL035410, AL390241 Genomic DNA. Translation: CAI21896.1.
AL035410, AL390241 Genomic DNA. Translation: CAI21897.1.
AJ132948 mRNA. Translation: CAB55313.1.
CCDSiCCDS872.1. [Q9UPN9-1]
CCDS873.1. [Q9UPN9-2]
RefSeqiNP_056990.3. NM_015906.3. [Q9UPN9-1]
NP_148980.2. NM_033020.2. [Q9UPN9-2]
UniGeneiHs.26837.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3U5MX-ray3.08A/B/C/D/E/F/G/H/I/J/K/L882-1087[»]
3U5NX-ray1.95A/B882-1087[»]
3U5OX-ray2.70A/B/C/D/E/F/G/H882-1087[»]
3U5PX-ray2.80A/B/C/D/E/F/G/H882-1087[»]
ProteinModelPortaliQ9UPN9.
SMRiQ9UPN9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119625. 76 interactors.
DIPiDIP-54262N.
IntActiQ9UPN9. 49 interactors.
MINTiMINT-2822547.
STRINGi9606.ENSP00000351250.

Chemistry databases

BindingDBiQ9UPN9.
ChEMBLiCHEMBL2176772.

PTM databases

iPTMnetiQ9UPN9.
PhosphoSitePlusiQ9UPN9.

Polymorphism and mutation databases

BioMutaiTRIM33.
DMDMi313104270.

Proteomic databases

EPDiQ9UPN9.
PaxDbiQ9UPN9.
PeptideAtlasiQ9UPN9.
PRIDEiQ9UPN9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358465; ENSP00000351250; ENSG00000197323. [Q9UPN9-1]
ENST00000369543; ENSP00000358556; ENSG00000197323. [Q9UPN9-2]
GeneIDi51592.
KEGGihsa:51592.
UCSCiuc001eew.3. human. [Q9UPN9-1]

Organism-specific databases

CTDi51592.
DisGeNETi51592.
GeneCardsiTRIM33.
H-InvDBHIX0000910.
HGNCiHGNC:16290. TRIM33.
HPAiHPA004345.
MalaCardsiTRIM33.
MIMi605769. gene.
neXtProtiNX_Q9UPN9.
OpenTargetsiENSG00000197323.
Orphaneti146. Papillary or follicular thyroid carcinoma.
PharmGKBiPA38118.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITFN. Eukaryota.
ENOG410Z421. LUCA.
GeneTreeiENSGT00530000062982.
HOVERGENiHBG054599.
InParanoidiQ9UPN9.
KOiK08883.
OMAiNEMSRII.
OrthoDBiEOG091G01KK.
PhylomeDBiQ9UPN9.
TreeFamiTF106455.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
SignaLinkiQ9UPN9.
SIGNORiQ9UPN9.

Miscellaneous databases

ChiTaRSiTRIM33. human.
GeneWikiiTRIM33.
GenomeRNAii51592.
PMAP-CutDBQ9UPN9.
PROiQ9UPN9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197323.
CleanExiHS_TRIM33.
ExpressionAtlasiQ9UPN9. baseline and differential.
GenevisibleiQ9UPN9. HS.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
4.10.45.10. 1 hit.
InterProiIPR003649. Bbox_C.
IPR001487. Bromodomain.
IPR019786. Zinc_finger_PHD-type_CS.
IPR027370. Znf-RING_LisH.
IPR000315. Znf_B-box.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF00643. zf-B_box. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50014. BROMODOMAIN_2. 1 hit.
PS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRI33_HUMAN
AccessioniPrimary (citable) accession number: Q9UPN9
Secondary accession number(s): O95855
, Q5TG72, Q5TG73, Q5TG74, Q9C017, Q9UJ79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 30, 2010
Last modified: November 2, 2016
This is version 172 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

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.