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Q9R1R2

- TRIM3_MOUSE

UniProt

Q9R1R2 - TRIM3_MOUSE

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Protein

Tripartite motif-containing protein 3

Gene
Trim3, Hac1, Rnf22
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Regions

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

GO - Molecular functioni

  1. protein binding 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 – 11Removed By similarity
Chaini2 – 744743Tripartite motif-containing protein 3PRO_0000056198Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9R1R2.
PaxDbiQ9R1R2.
PRIDEiQ9R1R2.

PTM databases

PhosphoSiteiQ9R1R2.

Expressioni

Gene expression databases

ArrayExpressiQ9R1R2.
BgeeiQ9R1R2.
CleanExiMM_TRIM3.
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.

Protein-protein interaction databases

BioGridi207763. 3 interactions.
IntActiQ9R1R2. 4 interactions.
MINTiMINT-4138575.

Structurei

3D structure databases

ProteinModelPortaliQ9R1R2.
SMRiQ9R1R2. Positions 18-63, 290-419, 475-744.

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 – 22472 Reviewed predictionAdd
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.
Contains 1 filamin repeat.
Contains 6 NHL repeats.

Zinc finger

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

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG3391.
GeneTreeiENSGT00550000074377.
HOGENOMiHOG000220817.
HOVERGENiHBG054843.
InParanoidiQ9R1R2.
KOiK11997.
OMAiINTTAEP.
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

MAKREDSPGP EVQPMDKQFL VCSICLDRYR CPKVLPCLHT FCERCLQNYI    50
PPQSLTLSCP VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPEGAHDPE 100
DPHPLSAVAG RPLSCPNHEG KTMEFYCEAC ETAMCGECRA GEHREHGTVL 150
LRDVVEQHKA ALQRQLEAVR GRLPQLSAAI ALVGGISQQL QERKAEALAQ 200
ISAAFEDLEQ ALQQRKQALV SDLESICGAK QKVLQTQLDT LRQGQEHIGS 250
SCSFAEQALR LGSAPEVLLV RKHMRERLAA LAAQAFPERP HENAQLELVL 300
EVDGLRRSVL NLGALLTTSA TAHETVATGE GLRQALVGQP ASLTVTTKDK 350
DGRLVRTGSA ELCAEITGPD GVRLAVPVVD HKNGTYELVY TARTEGDLLL 400
SVLLYGQPVR GSPFRVRALR PGDLPPSPDD VKRRVKSPGG PGSHVRQKAV 450
RRPSSMYSTG GKRKDNPIED ELVFRVGSRG REKGEFTNLQ GVSAASSGRI 500
VVADSNNQCI QVFSNEGQFK FRFGVRGRSP GQLQRPTGVA VDTNGDIIVA 550
DYDNRWVSIF SPEGKFKTKI GAGRLMGPKG VAVDRNGHII VVDNKSCCVF 600
TFQPNGKLVG RFGGRGATDR HFAGPHFVAV NNKNEIVVTD FHNHSVKVYS 650
ADGEFLFKFG SHGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDSSG 700
SFLSYINTSA EPLYGPQGLA LTSDGHVVVA DAGNHCFKAY RYLQ 744
Length:744
Mass (Da):80,774
Last modified:May 1, 2000 - v1
Checksum:iD9AEF4FA264BA168
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS21655.1.
RefSeqi NP_001272799.1. NM_001285870.1.
NP_001272800.1. NM_001285871.1.
NP_001272802.1. NM_001285873.1.
NP_061368.1. NM_018880.3.
UniGenei Mm.29290.

3D structure databases

ProteinModelPortali Q9R1R2.
SMRi Q9R1R2. Positions 18-63, 290-419, 475-744.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207763. 3 interactions.
IntActi Q9R1R2. 4 interactions.
MINTi MINT-4138575.

PTM databases

PhosphoSitei Q9R1R2.

Proteomic databases

MaxQBi Q9R1R2.
PaxDbi Q9R1R2.
PRIDEi Q9R1R2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000057525 ; ENSMUSP00000053384 ; ENSMUSG00000036989 .
ENSMUST00000106789 ; ENSMUSP00000102401 ; ENSMUSG00000036989 .
GeneIDi 55992.
KEGGi mmu:55992.
UCSCi uc009iym.1. mouse.

Organism-specific databases

CTDi 10612.
MGIi MGI:1860040. Trim3.

Phylogenomic databases

eggNOGi COG3391.
GeneTreei ENSGT00550000074377.
HOGENOMi HOG000220817.
HOVERGENi HBG054843.
InParanoidi Q9R1R2.
KOi K11997.
OMAi INTTAEP.
PhylomeDBi Q9R1R2.
TreeFami TF331018.

Miscellaneous databases

ChiTaRSi TRIM3. mouse.
NextBioi 311722.
PROi Q9R1R2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9R1R2.
Bgeei Q9R1R2.
CleanExi MM_TRIM3.
Genevestigatori Q9R1R2.

Family and domain databases

Gene3Di 2.120.10.30. 1 hit.
2.60.40.10. 1 hit.
3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProi IPR011042. 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 ]
Pfami PF00630. Filamin. 1 hit.
PF01436. NHL. 6 hits.
PF00643. zf-B_box. 1 hit.
PF14634. zf-RING_5. 1 hit.
[Graphical view ]
SMARTi SM00502. BBC. 1 hit.
SM00336. BBOX. 1 hit.
SM00557. IG_FLMN. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF81296. SSF81296. 1 hit.
PROSITEi PS50194. 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 ]
ProtoNeti Search...

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: September 3, 2014
This is version 127 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