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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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri125 – 15430RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri212 – 25948B box-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri271 – 31242B box-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri887 – 93448PHD-typePROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi125 – 1251C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-128. 1 Publication
Mutagenesisi128 – 1281C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-125. 1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei964 – 9652Breakpoint for translocation to form TRIM33-RET oncogene

Organism-specific databases

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

Chemistry

ChEMBLiCHEMBL2176772.

Polymorphism and mutation databases

BioMutaiTRIM33.
DMDMi313104270.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11271127E3 ubiquitin-protein ligase TRIM33PRO_0000056395Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki334 – 334Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei763 – 7631N6-acetyllysine; alternateCombined sources
Cross-linki763 – 763Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei769 – 7691N6-acetyllysine; alternateCombined sources
Cross-linki769 – 769Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki776 – 776Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki776 – 776Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei793 – 7931N6-acetyllysine; alternateBy similarity
Cross-linki793 – 793Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki793 – 793Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei803 – 8031PhosphoserineBy similarity
Modified residuei815 – 8151PhosphothreonineBy similarity
Cross-linki861 – 861Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei862 – 8621PhosphoserineCombined sources
Modified residuei951 – 9511N6-acetyllysineBy similarity
Modified residuei953 – 9531N6-acetyllysine; alternateCombined sources
Cross-linki953 – 953Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki1007 – 1007Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1051 – 10511PhosphothreonineCombined sources
Cross-linki1057 – 1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1102 – 11021PhosphothreonineCombined sources
Modified residuei1105 – 11051PhosphoserineCombined sources
Cross-linki1118 – 1118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1119 – 11191PhosphoserineCombined sources

Post-translational modificationi

Sumoylated with SUMO1.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UPN9.
MaxQBiQ9UPN9.
PaxDbiQ9UPN9.
PeptideAtlasiQ9UPN9.
PRIDEiQ9UPN9.

PTM databases

iPTMnetiQ9UPN9.
PhosphoSiteiQ9UPN9.

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. 75 interactions.
DIPiDIP-54262N.
IntActiQ9UPN9. 49 interactions.
MINTiMINT-2822547.
STRINGi9606.ENSP00000351250.

Chemistry

BindingDBiQ9UPN9.

Structurei

Secondary structure

1
1127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi888 – 8903Combined sources
Turni891 – 8933Combined sources
Beta strandi897 – 9015Combined sources
Beta strandi903 – 9064Combined sources
Turni911 – 9133Combined sources
Beta strandi914 – 9163Combined sources
Beta strandi918 – 9203Combined sources
Turni929 – 9313Combined sources
Beta strandi934 – 9363Combined sources
Helixi944 – 9474Combined sources
Helixi960 – 97415Combined sources
Helixi980 – 9823Combined sources
Helixi993 – 9964Combined sources
Helixi1003 – 10108Combined sources
Beta strandi1011 – 10133Combined sources
Helixi1021 – 104525Combined sources
Helixi1061 – 108020Combined sources
Beta strandi1081 – 10833Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 270-314, 883-1087.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini974 – 104673BromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 147147Necessary for E3 ubiquitin-protein ligase activity and repression of SMAD4 signaling and transcriptional repressionAdd
BLAST
Regioni299 – 401103Necessary for oligomerizationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili299 – 401103Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 186Poly-Gly
Compositional biasi44 – 496Poly-Glu
Compositional biasi545 – 5506Poly-Thr

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri125 – 15430RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri212 – 25948B box-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri271 – 31242B box-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri887 – 93448PHD-typePROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891V → E in CAB55313 (PubMed:10439047).Curated
Sequence conflicti451 – 4533PAA → LLH in CAB55313 (PubMed:10439047).Curated
Sequence conflicti909 – 9091F → S in CAB55313 (PubMed:10439047).Curated
Sequence conflicti1037 – 10371R → T in AAD17259 (PubMed:10022127).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671V → A.
Corresponds to variant rs6691166 [ dbSNP | Ensembl ].
VAR_029494
Natural varianti580 – 5801M → I in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_042376
Natural varianti696 – 6961L → S.1 Publication
Corresponds to variant rs56151583 [ dbSNP | Ensembl ].
VAR_042377
Natural varianti811 – 8111E → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042378
Natural varianti840 – 8401I → T.4 Publications
Corresponds to variant rs6537825 [ dbSNP | Ensembl ].
VAR_024616
Natural varianti885 – 8851P → S in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_042379
Natural varianti961 – 9611V → M.1 Publication
Corresponds to variant rs55688622 [ dbSNP | Ensembl ].
VAR_042380
Natural varianti1090 – 10901P → T.1 Publication
Corresponds to variant rs55784699 [ dbSNP | Ensembl ].
VAR_042381

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1041 – 105717Missing in isoform Beta. 2 PublicationsVSP_005774Add
BLAST

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
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. Positions 270-314, 883-1087.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119625. 75 interactions.
DIPiDIP-54262N.
IntActiQ9UPN9. 49 interactions.
MINTiMINT-2822547.
STRINGi9606.ENSP00000351250.

Chemistry

BindingDBiQ9UPN9.
ChEMBLiCHEMBL2176772.

PTM databases

iPTMnetiQ9UPN9.
PhosphoSiteiQ9UPN9.

Polymorphism and mutation databases

BioMutaiTRIM33.
DMDMi313104270.

Proteomic databases

EPDiQ9UPN9.
MaxQBiQ9UPN9.
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.
GeneCardsiTRIM33.
H-InvDBHIX0000910.
HGNCiHGNC:16290. TRIM33.
HPAiHPA004345.
MalaCardsiTRIM33.
MIMi605769. gene.
neXtProtiNX_Q9UPN9.
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: September 7, 2016
This is version 170 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.