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Protein

Probable E3 ubiquitin-protein ligase MID2

Gene

Mid2

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

Functioni

May play a role in microtubule stabilization.By similarity

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 fingeri30 – 8051RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri137 – 18448B box-type 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri190 – 23243B box-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable E3 ubiquitin-protein ligase MID2 (EC:6.3.2.-)
Alternative name(s):
Midline defect 2
Midline-2
Tripartite motif-containing protein 1
Gene namesi
Name:Mid2
Synonyms:Fxy2, Trim1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1344333. Mid2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 705705Probable E3 ubiquitin-protein ligase MID2PRO_0000056194Add
BLAST

Post-translational modificationi

Phosphorylated on serine and threonine residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9QUS6.
PaxDbiQ9QUS6.
PRIDEiQ9QUS6.

PTM databases

iPTMnetiQ9QUS6.
PhosphoSiteiQ9QUS6.

Expressioni

Tissue specificityi

Low abundance in brain and lung, with even lower levels in heart, liver, and kidney.

Developmental stagei

At E10.5, a very low level is mostly confined to the central nervous system and the developing heart and kidney, while at later stages it is present in other organ systems.

Gene expression databases

BgeeiQ9QUS6.
CleanExiMM_MID2.

Interactioni

Subunit structurei

Homodimer or heterodimer with MID1. Interacts with IGBP1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000108617.

Structurei

3D structure databases

ProteinModelPortaliQ9QUS6.
SMRiQ9QUS6. Positions 24-104, 107-252, 396-663.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini340 – 39960COSPROSITE-ProRule annotationAdd
BLAST
Domaini404 – 504101Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST
Domaini486 – 679194B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili233 – 30169Sequence analysisAdd
BLAST

Domaini

The tripartite motif (RBCC; RING- and B box-type zinc fingers and coiled coil domains) mediates dimerization.By similarity
Associates with microtubules in a manner that is dependent on the C-terminal B30.2 domain.

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 2 B box-type zinc fingers.PROSITE-ProRule annotation
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 COS domain.PROSITE-ProRule annotation
Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri30 – 8051RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri137 – 18448B box-type 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri190 – 23243B box-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITF1. Eukaryota.
ENOG410YTG8. LUCA.
HOGENOMiHOG000049193.
HOVERGENiHBG056432.
InParanoidiQ9QUS6.
KOiK10647.
PhylomeDBiQ9QUS6.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003649. Bbox_C.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR017903. COS_domain.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR003877. SPRY_dom.
IPR027370. Znf-RING_LisH.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00060. FN3. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS51262. COS. 1 hit.
PS50853. FN3. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QUS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGESPASAVL NASAGLFSLK METLESELTC PICLELFEDP LLLPCAHSLC
60 70 80 90 100
FSCAHRILVS SCSSGESIEP ITAFQCPTCR YVISLNHRGL DGLKRNVTLQ
110 120 130 140 150
NIIDRFQKAS VSGPNSPSES RRERTYRPSS AMSSERIACQ FCEQDPPRDA
160 170 180 190 200
VKTCITCEVS YCDRCLRATH PNKKPFTSHR LVEPVSDTHL RGITCLDHEN
210 220 230 240 250
EKVNMYCVSD DQLICALCKL VGRHRDHQVA SLNDRFEKLK QTLEMNLTNL
260 270 280 290 300
VKRNSELENQ MAKLIQICQQ VEVNTAMHEA KLMEECDELV EIIQQRKQMI
310 320 330 340 350
AVKIKETKVM KLRKLAQQVA NCRQCLERST VLINQAEHIL KENDQARFLQ
360 370 380 390 400
SAKNIAERVA MATASSQVLI PDINFNDAFE NFALDFSREK KLLEGLDYLT
410 420 430 440 450
APNPPSIREE LCTASHDTIT VHWISDDEFS ISSYELQYTI FTGQANFISL
460 470 480 490 500
YNSVDSWMIV PNIKQNHYTV HGLQSGTRYI FIVKAINQAG SRNSEPTRLK
510 520 530 540 550
TNSQPFKLDP KMTHKKLKIS NDGLQMEKDE SSLKKSHTPE RFSGTGCYGA
560 570 580 590 600
AGNIFIDSGC HYWEVVMGSS TWYAIGIAYK SAPKNEWIGK NASSWVFSRC
610 620 630 640 650
NSNFVVRHNN KEMLVDVPPQ LKRLGVLLDY DNNMLSFYDP ANSLHLHTFD
660 670 680 690 700
VTFILPVCPT FTIWNKSLMI LSGLPAPDFI DYPERQECNC RPQESPYVSG

MKACH
Length:705
Mass (Da):79,774
Last modified:April 20, 2010 - v2
Checksum:i141D80291912FA6B
GO

Sequence cautioni

The sequence AAF07340.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB56170.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18881 mRNA. Translation: CAB56170.1. Different initiation.
AF196480 mRNA. Translation: AAF07340.1. Different initiation.
RefSeqiNP_035975.1. NM_011845.2.
XP_006528586.1. XM_006528523.2.
UniGeneiMm.131097.

Genome annotation databases

GeneIDi23947.
KEGGimmu:23947.
UCSCiuc009uld.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18881 mRNA. Translation: CAB56170.1. Different initiation.
AF196480 mRNA. Translation: AAF07340.1. Different initiation.
RefSeqiNP_035975.1. NM_011845.2.
XP_006528586.1. XM_006528523.2.
UniGeneiMm.131097.

3D structure databases

ProteinModelPortaliQ9QUS6.
SMRiQ9QUS6. Positions 24-104, 107-252, 396-663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000108617.

PTM databases

iPTMnetiQ9QUS6.
PhosphoSiteiQ9QUS6.

Proteomic databases

MaxQBiQ9QUS6.
PaxDbiQ9QUS6.
PRIDEiQ9QUS6.

Protocols and materials databases

DNASUi23947.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi23947.
KEGGimmu:23947.
UCSCiuc009uld.1. mouse.

Organism-specific databases

CTDi11043.
MGIiMGI:1344333. Mid2.

Phylogenomic databases

eggNOGiENOG410ITF1. Eukaryota.
ENOG410YTG8. LUCA.
HOGENOMiHOG000049193.
HOVERGENiHBG056432.
InParanoidiQ9QUS6.
KOiK10647.
PhylomeDBiQ9QUS6.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiMid2. mouse.
PROiQ9QUS6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QUS6.
CleanExiMM_MID2.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003649. Bbox_C.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR017903. COS_domain.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR003877. SPRY_dom.
IPR027370. Znf-RING_LisH.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00060. FN3. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS51262. COS. 1 hit.
PS50853. FN3. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "MID2, a homologue of the Opitz syndrome gene MID1: similarities in a sub-cellular localization and differences in expression during development."
    Buchner G., Montini E., Andolfi G., Quaderi N., Cainarca S., Messali S., Bassi M.T., Ballabio A., Meroni G., Franco B.
    Hum. Mol. Genet. 8:1397-1407(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "FXY2/MID2, a gene related to the X-linked Opitz syndrome gene FXY/MID1, maps to Xq22 and encodes a FNIII domain-containing protein that associates with microtubules."
    Perry J., Short K.M., Romer J.T., Swift S., Cox T.C., Ashworth A.
    Genomics 62:385-394(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-705.

Entry informationi

Entry nameiTRIM1_MOUSE
AccessioniPrimary (citable) accession number: Q9QUS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: April 20, 2010
Last modified: June 8, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-21 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.