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Protein

Tripartite motif-containing protein 3

Gene

Trim3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri22 – 6342RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri110 – 15142B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ubiquitin protein ligase activity Source: MGI
  2. ubiquitin-protein transferase activity Source: FlyBase
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
  2. protein ubiquitination Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Tripartite motif-containing protein 3
Alternative name(s):
RING finger protein 22
RING finger protein HAC1
Gene namesi
Name:Trim3
Synonyms:Hac1, Rnf22
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1860040. Trim3.

Subcellular locationi

Cytoplasm By similarity. Early endosome By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. early endosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 744743Tripartite motif-containing protein 3PRO_0000056198Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei7 – 71Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9R1R2.
PaxDbiQ9R1R2.
PRIDEiQ9R1R2.

PTM databases

PhosphoSiteiQ9R1R2.

Expressioni

Gene expression databases

BgeeiQ9R1R2.
CleanExiMM_TRIM3.
ExpressionAtlasiQ9R1R2. baseline and differential.
GenevestigatoriQ9R1R2.

Interactioni

Subunit structurei

Associates with myosin-Vb (MYO5B) and alpha-actinin-4 (ACTN4). Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Interacts with ZFYVE28/LST2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi207763. 4 interactions.
IntActiQ9R1R2. 4 interactions.
MINTiMINT-4138575.

Structurei

3D structure databases

ProteinModelPortaliQ9R1R2.
SMRiQ9R1R2. Positions 9-92, 290-419, 475-744.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati317 – 418102FilaminAdd
BLAST
Repeati473 – 51644NHL 1Add
BLAST
Repeati520 – 56344NHL 2Add
BLAST
Repeati564 – 60542NHL 3Add
BLAST
Repeati609 – 65244NHL 4Add
BLAST
Repeati656 – 69944NHL 5Add
BLAST
Repeati700 – 74344NHL 6Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili153 – 22472Sequence AnalysisAdd
BLAST

Domaini

The interaction with MYO5B is dependent upon its NHL repeats, which form a beta-propeller (NHL) domain containing six blades.By similarity

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 filamin repeat.PROSITE-ProRule annotation
Contains 6 NHL repeats.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri22 – 6342RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri110 – 15142B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG3391.
GeneTreeiENSGT00550000074377.
HOGENOMiHOG000220817.
HOVERGENiHBG054843.
InParanoidiQ9R1R2.
KOiK11997.
OMAiNRWVSVF.
PhylomeDBiQ9R1R2.
TreeFamiTF331018.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
2.60.40.10. 1 hit.
3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR003649. Bbox_C.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00630. Filamin. 1 hit.
PF01436. NHL. 6 hits.
PF00643. zf-B_box. 1 hit.
PF14634. zf-RING_5. 1 hit.
[Graphical view]
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 1 hit.
SM00557. IG_FLMN. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
PROSITEiPS50194. FILAMIN_REPEAT. 1 hit.
PS51125. NHL. 6 hits.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R1R2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKREDSPGP EVQPMDKQFL VCSICLDRYR CPKVLPCLHT FCERCLQNYI
60 70 80 90 100
PPQSLTLSCP VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPEGAHDPE
110 120 130 140 150
DPHPLSAVAG RPLSCPNHEG KTMEFYCEAC ETAMCGECRA GEHREHGTVL
160 170 180 190 200
LRDVVEQHKA ALQRQLEAVR GRLPQLSAAI ALVGGISQQL QERKAEALAQ
210 220 230 240 250
ISAAFEDLEQ ALQQRKQALV SDLESICGAK QKVLQTQLDT LRQGQEHIGS
260 270 280 290 300
SCSFAEQALR LGSAPEVLLV RKHMRERLAA LAAQAFPERP HENAQLELVL
310 320 330 340 350
EVDGLRRSVL NLGALLTTSA TAHETVATGE GLRQALVGQP ASLTVTTKDK
360 370 380 390 400
DGRLVRTGSA ELCAEITGPD GVRLAVPVVD HKNGTYELVY TARTEGDLLL
410 420 430 440 450
SVLLYGQPVR GSPFRVRALR PGDLPPSPDD VKRRVKSPGG PGSHVRQKAV
460 470 480 490 500
RRPSSMYSTG GKRKDNPIED ELVFRVGSRG REKGEFTNLQ GVSAASSGRI
510 520 530 540 550
VVADSNNQCI QVFSNEGQFK FRFGVRGRSP GQLQRPTGVA VDTNGDIIVA
560 570 580 590 600
DYDNRWVSIF SPEGKFKTKI GAGRLMGPKG VAVDRNGHII VVDNKSCCVF
610 620 630 640 650
TFQPNGKLVG RFGGRGATDR HFAGPHFVAV NNKNEIVVTD FHNHSVKVYS
660 670 680 690 700
ADGEFLFKFG SHGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDSSG
710 720 730 740
SFLSYINTSA EPLYGPQGLA LTSDGHVVVA DAGNHCFKAY RYLQ
Length:744
Mass (Da):80,774
Last modified:May 1, 2000 - v1
Checksum:iD9AEF4FA264BA168
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030912 mRNA. Translation: BAA83343.1.
AF220019 mRNA. Translation: AAG53473.1.
AK019165 mRNA. Translation: BAB31580.1.
AK144674 mRNA. Translation: BAE26003.1.
BC034263 mRNA. Translation: AAH34263.1.
CCDSiCCDS21655.1.
RefSeqiNP_001272799.1. NM_001285870.1.
NP_001272800.1. NM_001285871.1.
NP_001272802.1. NM_001285873.1.
NP_061368.1. NM_018880.3.
UniGeneiMm.29290.

Genome annotation databases

EnsembliENSMUST00000057525; ENSMUSP00000053384; ENSMUSG00000036989.
ENSMUST00000106789; ENSMUSP00000102401; ENSMUSG00000036989.
GeneIDi55992.
KEGGimmu:55992.
UCSCiuc009iym.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030912 mRNA. Translation: BAA83343.1.
AF220019 mRNA. Translation: AAG53473.1.
AK019165 mRNA. Translation: BAB31580.1.
AK144674 mRNA. Translation: BAE26003.1.
BC034263 mRNA. Translation: AAH34263.1.
CCDSiCCDS21655.1.
RefSeqiNP_001272799.1. NM_001285870.1.
NP_001272800.1. NM_001285871.1.
NP_001272802.1. NM_001285873.1.
NP_061368.1. NM_018880.3.
UniGeneiMm.29290.

3D structure databases

ProteinModelPortaliQ9R1R2.
SMRiQ9R1R2. Positions 9-92, 290-419, 475-744.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207763. 4 interactions.
IntActiQ9R1R2. 4 interactions.
MINTiMINT-4138575.

PTM databases

PhosphoSiteiQ9R1R2.

Proteomic databases

MaxQBiQ9R1R2.
PaxDbiQ9R1R2.
PRIDEiQ9R1R2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057525; ENSMUSP00000053384; ENSMUSG00000036989.
ENSMUST00000106789; ENSMUSP00000102401; ENSMUSG00000036989.
GeneIDi55992.
KEGGimmu:55992.
UCSCiuc009iym.1. mouse.

Organism-specific databases

CTDi10612.
MGIiMGI:1860040. Trim3.

Phylogenomic databases

eggNOGiCOG3391.
GeneTreeiENSGT00550000074377.
HOGENOMiHOG000220817.
HOVERGENiHBG054843.
InParanoidiQ9R1R2.
KOiK11997.
OMAiNRWVSVF.
PhylomeDBiQ9R1R2.
TreeFamiTF331018.

Miscellaneous databases

ChiTaRSiTrim3. mouse.
NextBioi311722.
PROiQ9R1R2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R1R2.
CleanExiMM_TRIM3.
ExpressionAtlasiQ9R1R2. baseline and differential.
GenevestigatoriQ9R1R2.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
2.60.40.10. 1 hit.
3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR003649. Bbox_C.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00630. Filamin. 1 hit.
PF01436. NHL. 6 hits.
PF00643. zf-B_box. 1 hit.
PF14634. zf-RING_5. 1 hit.
[Graphical view]
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 1 hit.
SM00557. IG_FLMN. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
PROSITEiPS50194. FILAMIN_REPEAT. 1 hit.
PS51125. NHL. 6 hits.
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. "Cloning of a new co-activator with ring finger motif."
    Yanai K., Shimamoto Y., Hirota K., Fukamizu A.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Lung.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Retina.
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiTRIM3_MOUSE
AccessioniPrimary (citable) accession number: Q9R1R2
Secondary accession number(s): Q3UMU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: May 1, 2000
Last modified: March 4, 2015
This is version 133 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.