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Protein

E3 ubiquitin-protein ligase TRIM33

Gene

TRIM33

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

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 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
  • R-SMAD binding Source: BHF-UCL
  • ubiquitin-protein transferase activity Source: Reactome
  • zinc ion binding Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Repressor, Transferase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
SignaLinkiQ9UPN9
SIGNORiQ9UPN9
UniPathwayi
UPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM33 (EC:2.3.2.27)
Alternative name(s):
Ectodermin homolog
RET-fused gene 7 protein
Short name:
Protein Rfg7
RING-type E3 ubiquitin transferase TRIM33Curated
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

EuPathDBiHostDB:ENSG00000197323.10
HGNCiHGNC:16290 TRIM33
MIMi605769 gene
neXtProtiNX_Q9UPN9

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

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.1 Publication

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-linki329Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki334Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki504Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei515Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei515Omega-N-methylarginine; alternateCombined sources1
Cross-linki527Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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-linki774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki776Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki776Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined 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
Cross-linki796Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined 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
Cross-linki1043Glycyl 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
ProteomicsDBi85392
85393 [Q9UPN9-2]

PTM databases

iPTMnetiQ9UPN9
PhosphoSitePlusiQ9UPN9

Miscellaneous databases

PMAP-CutDBiQ9UPN9

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 Expressed in 242 organ(s), highest expression level in endometrium epithelium
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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi119625, 87 interactors
CORUMiQ9UPN9
DIPiDIP-54262N
IntActiQ9UPN9, 55 interactors
MINTiQ9UPN9
STRINGi9606.ENSP00000351250

Chemistry databases

BindingDBiQ9UPN9

Structurei

Secondary structure

11127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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
GeneTreeiENSGT00920000148978
HOVERGENiHBG054599
InParanoidiQ9UPN9
KOiK08883
OMAiPVRSLMH
OrthoDBiEOG091G01KK
PhylomeDBiQ9UPN9
TreeFamiTF106455

Family and domain databases

CDDicd00021 BBOX, 1 hit
Gene3Di1.20.920.10, 1 hit
3.30.40.10, 2 hits
InterProiView protein in InterPro
IPR003649 Bbox_C
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
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
PfamiView protein in Pfam
PF00439 Bromodomain, 1 hit
PF00628 PHD, 1 hit
PF00643 zf-B_box, 1 hit
PF13445 zf-RING_UBOX, 1 hit
PRINTSiPR00503 BROMODOMAIN
SMARTiView protein in SMART
SM00502 BBC, 1 hit
SM00336 BBOX, 2 hits
SM00297 BROMO, 1 hit
SM00249 PHD, 2 hits
SM00184 RING, 2 hits
SUPFAMiSSF47370 SSF47370, 1 hit
SSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS50014 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

Sequences (2+)i

Sequence statusi: Complete.

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

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y612H0Y612_HUMAN
E3 ubiquitin-protein ligase TRIM33
TRIM33
888Annotation score:

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

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 dbSNP:rs6691166Ensembl.1
Natural variantiVAR_042376580M → I in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_042377696L → S1 PublicationCorresponds to variant dbSNP:rs56151583Ensembl.1
Natural variantiVAR_042378811E → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_024616840I → T4 PublicationsCorresponds to variant dbSNP:rs6537825Ensembl.1
Natural variantiVAR_042379885P → S in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_042380961V → M1 PublicationCorresponds to variant dbSNP:rs55688622Ensembl.1
Natural variantiVAR_0423811090P → T1 PublicationCorresponds to variant dbSNP:rs55784699Ensembl.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.
AL035410 Genomic DNA No translation available.
AL390241 Genomic DNA No translation available.
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

Similar proteinsi

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.
AL035410 Genomic DNA No translation available.
AL390241 Genomic DNA No translation available.
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[»]
5MR8X-ray1.74A882-1090[»]
ProteinModelPortaliQ9UPN9
SMRiQ9UPN9
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119625, 87 interactors
CORUMiQ9UPN9
DIPiDIP-54262N
IntActiQ9UPN9, 55 interactors
MINTiQ9UPN9
STRINGi9606.ENSP00000351250

Chemistry databases

BindingDBiQ9UPN9
ChEMBLiCHEMBL2176772

PTM databases

iPTMnetiQ9UPN9
PhosphoSitePlusiQ9UPN9

Polymorphism and mutation databases

BioMutaiTRIM33
DMDMi313104270

Proteomic databases

EPDiQ9UPN9
PaxDbiQ9UPN9
PeptideAtlasiQ9UPN9
PRIDEiQ9UPN9
ProteomicsDBi85392
85393 [Q9UPN9-2]

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
EuPathDBiHostDB:ENSG00000197323.10
GeneCardsiTRIM33
H-InvDBiHIX0000910
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
GeneTreeiENSGT00920000148978
HOVERGENiHBG054599
InParanoidiQ9UPN9
KOiK08883
OMAiPVRSLMH
OrthoDBiEOG091G01KK
PhylomeDBiQ9UPN9
TreeFamiTF106455

Enzyme and pathway databases

UniPathwayi
UPA00143

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

Miscellaneous databases

ChiTaRSiTRIM33 human
GeneWikiiTRIM33
GenomeRNAii51592
PMAP-CutDBiQ9UPN9
PROiPR:Q9UPN9
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197323 Expressed in 242 organ(s), highest expression level in endometrium epithelium
CleanExiHS_TRIM33
ExpressionAtlasiQ9UPN9 baseline and differential
GenevisibleiQ9UPN9 HS

Family and domain databases

CDDicd00021 BBOX, 1 hit
Gene3Di1.20.920.10, 1 hit
3.30.40.10, 2 hits
InterProiView protein in InterPro
IPR003649 Bbox_C
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
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
PfamiView protein in Pfam
PF00439 Bromodomain, 1 hit
PF00628 PHD, 1 hit
PF00643 zf-B_box, 1 hit
PF13445 zf-RING_UBOX, 1 hit
PRINTSiPR00503 BROMODOMAIN
SMARTiView protein in SMART
SM00502 BBC, 1 hit
SM00336 BBOX, 2 hits
SM00297 BROMO, 1 hit
SM00249 PHD, 2 hits
SM00184 RING, 2 hits
SUPFAMiSSF47370 SSF47370, 1 hit
SSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS50014 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
ProtoNetiSearch...

Entry informationi

Entry nameiTRI33_HUMAN
AccessioniPrimary (citable) accession number: Q9UPN9
Secondary accession number(s): O95855
, Q5TG72, Q5TG73, Q5TG74, Q9C017, Q9UJ79
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 30, 2010
Last modified: September 12, 2018
This is version 186 of the entry and version 3 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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