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Protein

Probable E3 ubiquitin-protein ligase MID2

Gene

MID2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in microtubule stabilization.1 Publication

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

  • ligase activity Source: UniProtKB-KW
  • microtubule binding Source: UniProtKB
  • phosphoprotein binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • innate immune response Source: UniProtKB
  • negative regulation of viral entry into host cell Source: UniProtKB
  • negative regulation of viral release from host cell Source: UniProtKB
  • negative regulation of viral transcription Source: UniProtKB
  • positive regulation of autophagy Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • protein localization to microtubule Source: UniProtKB
  • protein ubiquitination Source: UniProtKB-UniPathway
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):
Midin-2
Midline defect 2
Midline-2
RING finger protein 60
Tripartite motif-containing protein 1
Gene namesi
Name:MID2
Synonyms:FXY2, RNF60, TRIM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:7096. MID2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked 101 (MRX101)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. MRX101 clinical features include global developmental delay, hyperactivity often with aggressive outbursts, and seizures in some patients. Several affected individuals have long face, prominent ears, and squint or strabismus.
See also OMIM:300928
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti347 – 3471R → Q in MRX101; the mutant is abnormally localized in aggregates or enclosed in cytoplasmic vesicles rather than being bound to microtubules. 1 Publication
Corresponds to variant rs587777605 [ dbSNP | Ensembl ].
VAR_071836

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MalaCardsiMID2.
MIMi300928. phenotype.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA30817.

Polymorphism and mutation databases

BioMutaiMID2.
DMDMi294862489.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Probable E3 ubiquitin-protein ligase MID2PRO_0000056193Add
BLAST

Post-translational modificationi

Phosphorylated on serine and threonine residues.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UJV3.
PaxDbiQ9UJV3.
PeptideAtlasiQ9UJV3.
PRIDEiQ9UJV3.

PTM databases

iPTMnetiQ9UJV3.
PhosphoSiteiQ9UJV3.

Expressioni

Tissue specificityi

Low level in fetal kidney and lung, and in adult prostate, ovary and small intestine.

Gene expression databases

BgeeiQ9UJV3.
CleanExiHS_MID2.
ExpressionAtlasiQ9UJV3. baseline and differential.
GenevisibleiQ9UJV3. HS.

Organism-specific databases

HPAiHPA029077.

Interactioni

Subunit structurei

Homodimer or heterodimer with MID1. Interacts with IGBP1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
B3KPU63EBI-10172526,EBI-10175879
ADAMTSL4Q6UY14-33EBI-10172526,EBI-10173507
AENQ8WTP83EBI-10172526,EBI-8637627
AQP1P299723EBI-10172526,EBI-745213
ATRIPQ8WXE13EBI-10172526,EBI-747353
BCL6BA8KA133EBI-10172526,EBI-10174813
BRMS1LQ5PSV43EBI-10172526,EBI-5666615
BYSLQ138955EBI-10172526,EBI-358049
CALCOCO2Q131373EBI-10172526,EBI-739580
CBX8Q9HC523EBI-10172526,EBI-712912
CCDC120Q96HB5-43EBI-10172526,EBI-10185348
CCDC42Q96M953EBI-10172526,EBI-747041
CCHCR1Q8TD31-33EBI-10172526,EBI-10175300
CEP57L1Q8IYX83EBI-10172526,EBI-1104570
CEP57L1Q8IYX8-23EBI-10172526,EBI-10181988
CHD2O146473EBI-10172526,EBI-1210503
CTSZQ9UBR23EBI-10172526,EBI-8636823
DCXO436023EBI-10172526,EBI-8646694
DGCR6LQ9BY273EBI-10172526,EBI-742953
DIEXFQ68CQ43EBI-10172526,EBI-747711
DMRT3Q9NQL93EBI-10172526,EBI-9679045
FAM107AO95990-33EBI-10172526,EBI-10192902
FAM161AQ3B8203EBI-10172526,EBI-719941
FAM214AQ32MH53EBI-10172526,EBI-2866142
FAM90A1Q86YD73EBI-10172526,EBI-6658203
FARS2O953633EBI-10172526,EBI-2513774
FBF1Q8TES7-63EBI-10172526,EBI-10244131
FBXL18Q96D163EBI-10172526,EBI-744419
FLJ13057Q53SE73EBI-10172526,EBI-10172181
FRMD6Q96NE93EBI-10172526,EBI-741729
GOLGA2Q083793EBI-10172526,EBI-618309
GORASP2Q9H8Y83EBI-10172526,EBI-739467
HOXB9P174823EBI-10172526,EBI-745290
ISCUQ9H1K13EBI-10172526,EBI-1047335
JOSD1Q150403EBI-10172526,EBI-2510602
KIAA1683Q9H0B33EBI-10172526,EBI-745878
KIFC3Q9BVG83EBI-10172526,EBI-2125614
LENG1Q96BZ83EBI-10172526,EBI-726510
LGALS14Q8TCE93EBI-10172526,EBI-10274069
LGALS8O002143EBI-10172526,EBI-740058
MAGOHBQ96A723EBI-10172526,EBI-746778
METTL17Q9H7H03EBI-10172526,EBI-749353
MFAP1P550813EBI-10172526,EBI-1048159
MID1O153443EBI-10172526,EBI-2340316
MID1IP1Q9NPA33EBI-10172526,EBI-750096
MOSP005403EBI-10172526,EBI-1757866
NR1D2Q6NSM03EBI-10172526,EBI-10250949
NXF1Q9UBU93EBI-10172526,EBI-398874
OTUB2Q96DC93EBI-10172526,EBI-746259
PPP1R18Q6NYC83EBI-10172526,EBI-2557469
PRPF31F1T0A53EBI-10172526,EBI-10177194
PSMA1P257863EBI-10172526,EBI-359352
RCOR3Q9P2K33EBI-10172526,EBI-743428
RPH3ALQ9UNE23EBI-10172526,EBI-2855824
RPP25LQ8N5L83EBI-10172526,EBI-10189722
RUNX1T1Q06455-43EBI-10172526,EBI-10224192
RYDENQ9NUL53EBI-10172526,EBI-10313866
SCNM1Q9BWG63EBI-10172526,EBI-748391
SDCBPO005603EBI-10172526,EBI-727004
SLC25A48Q6ZT893EBI-10172526,EBI-10255185
SLC25A6P122363EBI-10172526,EBI-356254
SNAI1O958633EBI-10172526,EBI-1045459
SNAP47Q5SQN13EBI-10172526,EBI-10244848
SPATA24Q86W543EBI-10172526,EBI-3916986
SPG21Q9NZD83EBI-10172526,EBI-742688
SPRY2O435973EBI-10172526,EBI-742487
STX11O755583EBI-10172526,EBI-714135
SYT17Q9BSW73EBI-10172526,EBI-745392
TCEA2Q155603EBI-10172526,EBI-710310
TCEB3Q142413EBI-10172526,EBI-742350
THAP7Q9BT493EBI-10172526,EBI-741350
TOP3BO959853EBI-10172526,EBI-373403
TRIM27P143733EBI-10172526,EBI-719493
TRIM42A1L4B63EBI-10172526,EBI-10172216
TRIM54Q9BYV23EBI-10172526,EBI-2130429
TSGA10Q9BZW73EBI-10172526,EBI-744794
UBE2D1P516683EBI-10172526,EBI-743540
UBE2D4Q9Y2X83EBI-10172526,EBI-745527
UBE2E2Q96LR53EBI-10172526,EBI-2129763
UBTD1Q9HAC83EBI-10172526,EBI-745871
UNC45AQ9H3U13EBI-10172526,EBI-1048763
UTP23Q9BRU93EBI-10172526,EBI-5457544
WT1-ASQ062503EBI-10172526,EBI-10223946
ZBTB24O431673EBI-10172526,EBI-744471
ZC2HC1CQ53FD03EBI-10172526,EBI-740767
ZFABQ9Y2603EBI-10172526,EBI-750052
ZFYVE21Q9BQ243EBI-10172526,EBI-2849569
ZGPATQ8N5A53EBI-10172526,EBI-3439227
ZGPATQ8N5A5-23EBI-10172526,EBI-10183064
ZNF165Q53Z403EBI-10172526,EBI-10186058
ZNF24P170283EBI-10172526,EBI-707773
ZNF250P15622-33EBI-10172526,EBI-10177272
ZNF417Q8TAU33EBI-10172526,EBI-740727
ZNF440Q8IYI83EBI-10172526,EBI-726439
ZNF564Q8TBZ83EBI-10172526,EBI-10273713
ZNF587Q96SQ53EBI-10172526,EBI-6427977
ZNF785A8K8V03EBI-10172526,EBI-3925400
ZNF792Q3KQV33EBI-10172526,EBI-10240849
ZSCAN12O433093EBI-10172526,EBI-1210440

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • phosphoprotein binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi116231. 134 interactions.
IntActiQ9UJV3. 105 interactions.
MINTiMINT-1483459.
STRINGi9606.ENSP00000262843.

Structurei

Secondary structure

1
735
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi199 – 2013Combined sources
Beta strandi205 – 2073Combined sources
Turni208 – 2114Combined sources
Beta strandi212 – 2143Combined sources
Helixi216 – 2205Combined sources
Turni223 – 2264Combined sources
Beta strandi406 – 41510Combined sources
Beta strandi418 – 4247Combined sources
Beta strandi429 – 44214Combined sources
Helixi483 – 4864Combined sources
Beta strandi487 – 4937Combined sources
Beta strandi495 – 5028Combined sources
Beta strandi508 – 51912Combined sources
Beta strandi521 – 5233Combined sources
Beta strandi527 – 5304Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJANMR-A182-252[»]
2DMKNMR-A394-537[»]
ProteinModelPortaliQ9UJV3.
SMRiQ9UJV3. Positions 24-104, 107-252, 396-693.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UJV3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini340 – 39960COSPROSITE-ProRule annotationAdd
BLAST
Domaini398 – 531134Fibronectin type-IIIAdd
BLAST
Domaini516 – 709194B30.2/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.Curated
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.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000049193.
HOVERGENiHBG056432.
InParanoidiQ9UJV3.
KOiK10647.
OMAiTWYAIGV.
OrthoDBiEOG7MH0XH.
PhylomeDBiQ9UJV3.
TreeFamiTF333654.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
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.
IPR033491. MID2.
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]
PANTHERiPTHR24103:SF283. PTHR24103:SF283. 3 hits.
PfamiPF00622. 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. 2 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS51262. COS. 1 hit.
PS50119. ZF_BBOX. 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 1 (identifier: Q9UJV3-1) [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
MGESPASVVL NASGGLFSLK METLESELTC PICLELFEDP LLLPCAHSLC
60 70 80 90 100
FSCAHRILVS SCSSGESIEP ITAFQCPTCR YVISLNHRGL DGLKRNVTLQ
110 120 130 140 150
NIIDRFQKAS VSGPNSPSES RRERTYRPTT AMSSERIACQ FCEQDPPRDA
160 170 180 190 200
VKTCITCEVS YCDRCLRATH PNKKPFTSHR LVEPVPDTHL 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 FTGQANFISK
460 470 480 490 500
SWCSWGLWPE IRKCKEAVSC SRLAGAPRGL YNSVDSWMIV PNIKQNHYTV
510 520 530 540 550
HGLQSGTRYI FIVKAINQAG SRNSEPTRLK TNSQPFKLDP KMTHKKLKIS
560 570 580 590 600
NDGLQMEKDE SSLKKSHTPE RFSGTGCYGA AGNIFIDSGC HYWEVVMGSS
610 620 630 640 650
TWYAIGIAYK SAPKNEWIGK NASSWVFSRC NSNFVVRHNN KEMLVDVPPH
660 670 680 690 700
LKRLGVLLDY DNNMLSFYDP ANSLHLHTFD VTFILPVCPT FTIWNKSLMI
710 720 730
LSGLPAPDFI DYPERQECNC RPQESPYVSG MKTCH
Length:735
Mass (Da):83,210
Last modified:April 20, 2010 - v3
Checksum:i22A0EC26B050EA21
GO
Isoform 2 (identifier: Q9UJV3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     450-479: Missing.

Show »
Length:705
Mass (Da):79,865
Checksum:i130A24684FB5AEC7
GO

Sequence cautioni

The sequence AAF07341.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH17707.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB56154.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAI42073.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAO72053.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti343 – 3431N → S Polymorphism; the protein is normally bound to microtubules. 1 Publication
Corresponds to variant rs551253128 [ dbSNP | Ensembl ].
VAR_071835
Natural varianti347 – 3471R → Q in MRX101; the mutant is abnormally localized in aggregates or enclosed in cytoplasmic vesicles rather than being bound to microtubules. 1 Publication
Corresponds to variant rs587777605 [ dbSNP | Ensembl ].
VAR_071836
Natural varianti378 – 3781A → D.
Corresponds to variant rs12849510 [ dbSNP | Ensembl ].
VAR_052123

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei450 – 47930Missing in isoform 2. 3 PublicationsVSP_009009Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF196481 mRNA. Translation: AAF07341.1. Different initiation.
Y18880 mRNA. Translation: CAB56154.1. Different initiation.
AL034399, AL109946 Genomic DNA. Translation: CAI42073.1. Sequence problems.
AL109946, AL034399 Genomic DNA. Translation: CAO72053.1. Sequence problems.
BC017707 mRNA. Translation: AAH17707.1. Different initiation.
BT006663 mRNA. Translation: AAP35309.1.
CCDSiCCDS14532.2. [Q9UJV3-1]
CCDS14533.2. [Q9UJV3-2]
RefSeqiNP_036348.2. NM_012216.3. [Q9UJV3-1]
NP_438112.2. NM_052817.2. [Q9UJV3-2]
XP_005262119.1. XM_005262062.3.
UniGeneiHs.12256.

Genome annotation databases

EnsembliENST00000262843; ENSP00000262843; ENSG00000080561. [Q9UJV3-1]
ENST00000443968; ENSP00000413976; ENSG00000080561. [Q9UJV3-2]
GeneIDi11043.
KEGGihsa:11043.
UCSCiuc004enk.4. human. [Q9UJV3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF196481 mRNA. Translation: AAF07341.1. Different initiation.
Y18880 mRNA. Translation: CAB56154.1. Different initiation.
AL034399, AL109946 Genomic DNA. Translation: CAI42073.1. Sequence problems.
AL109946, AL034399 Genomic DNA. Translation: CAO72053.1. Sequence problems.
BC017707 mRNA. Translation: AAH17707.1. Different initiation.
BT006663 mRNA. Translation: AAP35309.1.
CCDSiCCDS14532.2. [Q9UJV3-1]
CCDS14533.2. [Q9UJV3-2]
RefSeqiNP_036348.2. NM_012216.3. [Q9UJV3-1]
NP_438112.2. NM_052817.2. [Q9UJV3-2]
XP_005262119.1. XM_005262062.3.
UniGeneiHs.12256.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJANMR-A182-252[»]
2DMKNMR-A394-537[»]
ProteinModelPortaliQ9UJV3.
SMRiQ9UJV3. Positions 24-104, 107-252, 396-693.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116231. 134 interactions.
IntActiQ9UJV3. 105 interactions.
MINTiMINT-1483459.
STRINGi9606.ENSP00000262843.

PTM databases

iPTMnetiQ9UJV3.
PhosphoSiteiQ9UJV3.

Polymorphism and mutation databases

BioMutaiMID2.
DMDMi294862489.

Proteomic databases

MaxQBiQ9UJV3.
PaxDbiQ9UJV3.
PeptideAtlasiQ9UJV3.
PRIDEiQ9UJV3.

Protocols and materials databases

DNASUi11043.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262843; ENSP00000262843; ENSG00000080561. [Q9UJV3-1]
ENST00000443968; ENSP00000413976; ENSG00000080561. [Q9UJV3-2]
GeneIDi11043.
KEGGihsa:11043.
UCSCiuc004enk.4. human. [Q9UJV3-1]

Organism-specific databases

CTDi11043.
GeneCardsiMID2.
HGNCiHGNC:7096. MID2.
HPAiHPA029077.
MalaCardsiMID2.
MIMi300204. gene.
300928. phenotype.
neXtProtiNX_Q9UJV3.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA30817.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITF1. Eukaryota.
ENOG410YTG8. LUCA.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000049193.
HOVERGENiHBG056432.
InParanoidiQ9UJV3.
KOiK10647.
OMAiTWYAIGV.
OrthoDBiEOG7MH0XH.
PhylomeDBiQ9UJV3.
TreeFamiTF333654.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

EvolutionaryTraceiQ9UJV3.
GeneWikiiMID2.
GenomeRNAii11043.
PROiQ9UJV3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJV3.
CleanExiHS_MID2.
ExpressionAtlasiQ9UJV3. baseline and differential.
GenevisibleiQ9UJV3. HS.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
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.
IPR033491. MID2.
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]
PANTHERiPTHR24103:SF283. PTHR24103:SF283. 3 hits.
PfamiPF00622. 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. 2 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS51262. COS. 1 hit.
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. "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] (ISOFORM 2).
  2. "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] (ISOFORM 1).
    Tissue: Fetal brain.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] OF 12-735 (ISOFORM 2).
    Tissue: Kidney.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-735 (ISOFORM 2).
  6. "MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, Alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders."
    Short K.M., Hopwood B., Yi Z., Cox T.C.
    BMC Cell Biol. 3:1-1(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGBP1, PHOSPHORYLATION.
  7. "Targeted deep resequencing identifies MID2 mutation for X-linked intellectual disability with varied disease severity in a large kindred from India."
    Geetha T.S., Michealraj K.A., Kabra M., Kaur G., Juyal R.C., Thelma B.K.
    Hum. Mutat. 35:41-44(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INVOLVEMENT IN MRX101, VARIANT MRX101 GLN-347, VARIANT SER-343, CHARACTERIZATION OF VARIANT MRX101 GLN-347, CHARACTERIZATION OF VARIANT SER-343.
  8. "The solution structure of the FN3 domain of human midline 2 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 394-537.

Entry informationi

Entry nameiTRIM1_HUMAN
AccessioniPrimary (citable) accession number: Q9UJV3
Secondary accession number(s): A6NEL8
, A6PVI5, Q5JYF5, Q8WWK1, Q9UJR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: April 20, 2010
Last modified: July 6, 2016
This is version 160 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

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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.