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Protein

E3 ubiquitin-protein ligase Midline-1

Gene

MID1

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

Functioni

Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi119 – 1191Zinc 1
Metal bindingi122 – 1221Zinc 1
Metal bindingi134 – 1341Zinc 2
Metal bindingi137 – 1371Zinc 2
Metal bindingi142 – 1421Zinc 1
Metal bindingi145 – 1451Zinc 1
Metal bindingi150 – 1501Zinc 2
Metal bindingi159 – 1591Zinc 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri10 – 6051RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri116 – 16550B box-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri172 – 21241B box-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  • cytokine-mediated signaling pathway Source: Reactome
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • microtubule cytoskeleton organization Source: ProtInc
  • negative regulation of microtubule depolymerization Source: Ensembl
  • pattern specification process Source: ProtInc
  • positive regulation of stress-activated MAPK cascade Source: UniProtKB
  • protein localization to microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_25078. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase Midline-1 (EC:6.3.2.-)
Alternative name(s):
Midin
Putative transcription factor XPRF
RING finger protein 59
RING finger protein Midline-1
Tripartite motif-containing protein 18
Gene namesi
Name:MID1
Synonyms:FXY, RNF59, TRIM18, XPRF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:7095. MID1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • microtubule Source: UniProtKB
  • microtubule associated complex Source: ProtInc
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Opitz GBBB syndrome 1 (GBBB1)4 Publications

The disease is caused by mutations affecting the gene represented in this entry. MID1 mutations produce proteins with a decreased affinity for microtubules.

Disease descriptionA congenital midline malformation syndrome characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, cleft lip/palate, laryngotracheoesophageal abnormalities, imperforate anus, developmental delay and congenital heart defects.

See also OMIM:300000
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti266 – 2661C → R in GBBB1. 1 Publication
VAR_013758
Natural varianti295 – 2951L → P in GBBB1. 1 Publication
VAR_025495
Natural varianti391 – 3922LC → R in GBBB1. 1 Publication
VAR_025496
Natural varianti438 – 4381Missing in GBBB1. 1 Publication
VAR_013759
Natural varianti534 – 5341V → VFIDSGRHL in GBBB1.
VAR_013760
Natural varianti536 – 5361I → T in GBBB1. 1 Publication
VAR_013761
Natural varianti626 – 6261L → P in GBBB1. 1 Publication
Corresponds to variant rs28934611 [ dbSNP | Ensembl ].
VAR_013762

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi300000. phenotype.
Orphaneti306597. X-linked Opitz G/BBB syndrome.
PharmGKBiPA30816.

Polymorphism and mutation databases

BioMutaiMID1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 667667E3 ubiquitin-protein ligase Midline-1PRO_0000056227Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei92 – 921Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine and threonine residues.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO15344.
PaxDbiO15344.
PRIDEiO15344.

PTM databases

PhosphoSiteiO15344.

Expressioni

Tissue specificityi

In the fetus, highest expression found in kidney, followed by brain and lung. Expressed at low levels in fetal liver. In the adult, most abundant in heart, placenta and brain.

Inductioni

A retroviral element acts as an alternative tissue-specific promoter for this gene. The LTR of an HERV-E element enhances the expression in placenta and embryonic kidney.

Gene expression databases

BgeeiO15344.
CleanExiHS_MID1.
ExpressionAtlasiO15344. baseline and differential.
GenevisibleiO15344. HS.

Organism-specific databases

HPAiHPA003715.

Interactioni

Subunit structurei

Homodimer or heterodimer with MID2. Interacts with IGBP1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-2340316,EBI-2340316
BYSLQ138953EBI-2340316,EBI-358049
DYRK4Q9NR203EBI-2340316,EBI-3914009
EHHADHQ084263EBI-2340316,EBI-2339219
FKBP1AQ0VDC63EBI-2340316,EBI-10226858
FLJ13057Q53SE73EBI-2340316,EBI-10172181
MEOX1P502213EBI-2340316,EBI-2864512
MID2Q9UJV3-23EBI-2340316,EBI-10172526
OTUB2Q96DC93EBI-2340316,EBI-746259
PKN1Q165123EBI-2340316,EBI-602382
TCEANCQ8N8B73EBI-2340316,EBI-954696
UBE2D1P516684EBI-2340316,EBI-743540
UBE2D3P610774EBI-2340316,EBI-348268
UBE2E2Q96LR55EBI-2340316,EBI-2129763
UBE2E3Q969T44EBI-2340316,EBI-348496
UBTD1Q9HAC83EBI-2340316,EBI-745871

Protein-protein interaction databases

BioGridi110427. 46 interactions.
IntActiO15344. 25 interactions.
STRINGi9606.ENSP00000312678.

Structurei

Secondary structure

1
667
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi112 – 1143Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi132 – 1343Combined sources
Turni135 – 1384Combined sources
Beta strandi139 – 1413Combined sources
Helixi143 – 1497Combined sources
Beta strandi154 – 1563Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi185 – 1873Combined sources
Turni188 – 1914Combined sources
Beta strandi192 – 1943Combined sources
Helixi196 – 2005Combined sources
Beta strandi205 – 2073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DQ5NMR-A168-214[»]
2FFWNMR-A87-164[»]
2JUNNMR-A114-214[»]
ProteinModelPortaliO15344.
SMRiO15344. Positions 1-343, 376-655.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15344.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini320 – 37960COSPROSITE-ProRule annotationAdd
BLAST
Domaini381 – 484104Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST
Domaini482 – 659178B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili205 – 26460Sequence AnalysisAdd
BLAST

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 fingeri10 – 6051RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri116 – 16550B box-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri172 – 21241B box-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG253961.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000049193.
HOVERGENiHBG056432.
InParanoidiO15344.
KOiK08285.
OMAiRERAFDS.
OrthoDBiEOG7MH0XH.
PhylomeDBiO15344.
TreeFamiTF333654.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.40.10. 2 hits.
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.
IPR027727. MID1.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR24103:SF26. PTHR24103:SF26. 1 hit.
PfamiPF00041. fn3. 1 hit.
PF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00060. FN3. 1 hit.
SM00589. PRY. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15344-1) [UniParc]FASTAAdd to basket

Also known as: Alpha

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
METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNESVES
60 70 80 90 100
ITAFQCPTCR HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET
110 120 130 140 150
RRERAFDANT MTSAEKVLCQ FCDQDPAQDA VKTCVTCEVS YCDECLKATH
160 170 180 190 200
PNKKPFTGHR LIEPIPDSHI RGLMCLEHED EKVNMYCVTD DQLICALCKL
210 220 230 240 250
VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL LAKLIQTCQH
260 270 280 290 300
VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVM RLRKLAQQIA
310 320 330 340 350
NCKQCIERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI
360 370 380 390 400
PEINLNDTFD TFALDFSREK KLLECLDYLT APNPPTIREE LCTASYDTIT
410 420 430 440 450
VHWTSDDEFS VVSYELQYTI FTGQANVVSL CNSADSWMIV PNIKQNHYTV
460 470 480 490 500
HGLQSGTKYI FMVKAINQAG SRSSEPGKLK TNSQPFKLDP KSAHRKLKVS
510 520 530 540 550
HDNLTVERDE SSSKKSHTPE RFTSQGSYGV AGNVFIDSGR HYWEVVISGS
560 570 580 590 600
TWYAIGLAYK SAPKHEWIGK NSASWALCRC NNNWVVRHNS KEIPIEPAPH
610 620 630 640 650
LRRVGILLDY DNGSIAFYDA LNSIHLYTFD VAFAQPVCPT FTVWNKCLTI
660
ITGLPIPDHL DCTEQLP
Length:667
Mass (Da):75,251
Last modified:January 1, 1998 - v1
Checksum:i673C5120018BA619
GO
Isoform 2 (identifier: O15344-2) [UniParc]FASTAAdd to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     553-667: Missing.

Show »
Length:552
Mass (Da):62,288
Checksum:iFD4D4C0EA5915DB2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281T → P in AAC32999 (PubMed:9722948).Curated
Sequence conflicti484 – 4841Q → P in AAC32998 (PubMed:9722948).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti266 – 2661C → R in GBBB1. 1 Publication
VAR_013758
Natural varianti295 – 2951L → P in GBBB1. 1 Publication
VAR_025495
Natural varianti391 – 3922LC → R in GBBB1. 1 Publication
VAR_025496
Natural varianti438 – 4381Missing in GBBB1. 1 Publication
VAR_013759
Natural varianti534 – 5341V → VFIDSGRHL in GBBB1.
VAR_013760
Natural varianti536 – 5361I → T in GBBB1. 1 Publication
VAR_013761
Natural varianti626 – 6261L → P in GBBB1. 1 Publication
Corresponds to variant rs28934611 [ dbSNP | Ensembl ].
VAR_013762

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei553 – 667115Missing in isoform 2. 2 PublicationsVSP_005735Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13667 mRNA. Translation: CAA74018.1.
AF035360 mRNA. Translation: AAB99951.1.
AF041206 mRNA. Translation: AAC32998.1.
AF041207 mRNA. Translation: AAC32999.1.
AF041208 mRNA. Translation: AAC33000.1.
AF041209 mRNA. Translation: AAC33001.1.
AF041210 mRNA. Translation: AAC33002.1.
AF230976 mRNA. Translation: AAG50191.1.
AF230977 mRNA. Translation: AAG50192.1.
AF269101 mRNA. Translation: AAG33130.1.
AK315095 mRNA. Translation: BAG37559.1.
CH471074 Genomic DNA. Translation: EAW98780.1.
BC053626 mRNA. Translation: AAH53626.1.
CCDSiCCDS14138.1. [O15344-1]
PIRiT09482.
RefSeqiNP_000372.1. NM_000381.3. [O15344-1]
NP_001092094.1. NM_001098624.2. [O15344-1]
NP_001180206.1. NM_001193277.1. [O15344-1]
NP_001180207.1. NM_001193278.1.
NP_001180208.1. NM_001193279.1.
NP_001180209.1. NM_001193280.1.
NP_001180210.1. NM_001193281.1.
NP_150632.1. NM_033290.3. [O15344-1]
UniGeneiHs.27695.
Hs.460482.
Hs.689953.
Hs.738954.

Genome annotation databases

EnsembliENST00000317552; ENSP00000312678; ENSG00000101871. [O15344-1]
ENST00000380779; ENSP00000370156; ENSG00000101871. [O15344-1]
ENST00000380780; ENSP00000370157; ENSG00000101871. [O15344-1]
ENST00000380782; ENSP00000370159; ENSG00000101871. [O15344-2]
ENST00000380785; ENSP00000370162; ENSG00000101871. [O15344-1]
ENST00000380787; ENSP00000370164; ENSG00000101871. [O15344-1]
ENST00000453318; ENSP00000414521; ENSG00000101871. [O15344-1]
GeneIDi4281.
KEGGihsa:4281.
UCSCiuc004ctc.4. human. [O15344-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13667 mRNA. Translation: CAA74018.1.
AF035360 mRNA. Translation: AAB99951.1.
AF041206 mRNA. Translation: AAC32998.1.
AF041207 mRNA. Translation: AAC32999.1.
AF041208 mRNA. Translation: AAC33000.1.
AF041209 mRNA. Translation: AAC33001.1.
AF041210 mRNA. Translation: AAC33002.1.
AF230976 mRNA. Translation: AAG50191.1.
AF230977 mRNA. Translation: AAG50192.1.
AF269101 mRNA. Translation: AAG33130.1.
AK315095 mRNA. Translation: BAG37559.1.
CH471074 Genomic DNA. Translation: EAW98780.1.
BC053626 mRNA. Translation: AAH53626.1.
CCDSiCCDS14138.1. [O15344-1]
PIRiT09482.
RefSeqiNP_000372.1. NM_000381.3. [O15344-1]
NP_001092094.1. NM_001098624.2. [O15344-1]
NP_001180206.1. NM_001193277.1. [O15344-1]
NP_001180207.1. NM_001193278.1.
NP_001180208.1. NM_001193279.1.
NP_001180209.1. NM_001193280.1.
NP_001180210.1. NM_001193281.1.
NP_150632.1. NM_033290.3. [O15344-1]
UniGeneiHs.27695.
Hs.460482.
Hs.689953.
Hs.738954.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DQ5NMR-A168-214[»]
2FFWNMR-A87-164[»]
2JUNNMR-A114-214[»]
ProteinModelPortaliO15344.
SMRiO15344. Positions 1-343, 376-655.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110427. 46 interactions.
IntActiO15344. 25 interactions.
STRINGi9606.ENSP00000312678.

PTM databases

PhosphoSiteiO15344.

Polymorphism and mutation databases

BioMutaiMID1.

Proteomic databases

MaxQBiO15344.
PaxDbiO15344.
PRIDEiO15344.

Protocols and materials databases

DNASUi4281.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317552; ENSP00000312678; ENSG00000101871. [O15344-1]
ENST00000380779; ENSP00000370156; ENSG00000101871. [O15344-1]
ENST00000380780; ENSP00000370157; ENSG00000101871. [O15344-1]
ENST00000380782; ENSP00000370159; ENSG00000101871. [O15344-2]
ENST00000380785; ENSP00000370162; ENSG00000101871. [O15344-1]
ENST00000380787; ENSP00000370164; ENSG00000101871. [O15344-1]
ENST00000453318; ENSP00000414521; ENSG00000101871. [O15344-1]
GeneIDi4281.
KEGGihsa:4281.
UCSCiuc004ctc.4. human. [O15344-1]

Organism-specific databases

CTDi4281.
GeneCardsiGC0XM010373.
GeneReviewsiMID1.
HGNCiHGNC:7095. MID1.
HPAiHPA003715.
MIMi300000. phenotype.
300552. gene.
neXtProtiNX_O15344.
Orphaneti306597. X-linked Opitz G/BBB syndrome.
PharmGKBiPA30816.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG253961.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000049193.
HOVERGENiHBG056432.
InParanoidiO15344.
KOiK08285.
OMAiRERAFDS.
OrthoDBiEOG7MH0XH.
PhylomeDBiO15344.
TreeFamiTF333654.

Enzyme and pathway databases

ReactomeiREACT_25078. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiMID1. human.
EvolutionaryTraceiO15344.
GeneWikiiMID1.
GenomeRNAii4281.
NextBioi16837.
PROiO15344.
SOURCEiSearch...

Gene expression databases

BgeeiO15344.
CleanExiHS_MID1.
ExpressionAtlasiO15344. baseline and differential.
GenevisibleiO15344. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.40.10. 2 hits.
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.
IPR027727. MID1.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR24103:SF26. PTHR24103:SF26. 1 hit.
PfamiPF00041. fn3. 1 hit.
PF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00060. FN3. 1 hit.
SM00589. PRY. 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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GBBB1 MET-438 DEL AND PHE-ILE-ASP-SER-GLY-ARG-HIS-LEU-534 INS.
    Tissue: Neuron.
  2. "The human FXY gene is located within Xp22.3: implications for evolution of the mammalian X chromosome."
    Perry J., Feather S., Smith A., Palmer S., Ashworth A.
    Hum. Mol. Genet. 7:299-305(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  3. "Characterization and physical mapping in human and mouse of a novel RING finger gene in Xp22."
    Van den Veyver I.B., Cormier T.A., Jurecic V., Baldini A., Zoghbi H.Y.
    Genomics 51:251-261(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal kidney.
  4. "New mutations in MID1 provide support for loss of function as the cause of X-linked Opitz syndrome."
    Cox T.C., Allen L.R., Cox L.L., Hopwood B., Goodwin B., Haan E., Suthers G.K.
    Hum. Mol. Genet. 9:2553-2562(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GBBB1 PRO-626.
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Skin.
  9. "Functional characterization of the Opitz syndrome gene product (midin): evidence for homodimerization and association with microtubules throughout the cell cycle."
    Cainarca S., Messali S., Ballabio A., Meroni G.
    Hum. Mol. Genet. 8:1387-1396(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: SUBCELLULAR LOCATION.
  11. "MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation."
    Trockenbacher A., Suckow V., Foerster J., Winter J., Krauss S., Ropers H.H., Schneider R., Schweiger S.
    Nat. Genet. 29:287-294(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-associated protein phosphorylation."
    Watkins G.R., Wang N., Mazalouskas M.D., Gomez R.J., Guthrie C.R., Kraemer B.C., Schweiger S., Spiller B.W., Wadzinski B.E.
    J. Biol. Chem. 287:24207-24215(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box with a RING."
    Massiah M.A., Simmons B.N., Short K.M., Cox T.C.
    J. Mol. Biol. 358:532-545(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 87-164.
  20. "Opitz G/BBB syndrome in Xp22: mutations in the MID1 gene cluster in the carboxy-terminal domain."
    Gaudenz K., Roessler E., Quaderi N.A., Franco B., Feldman G.J., Gasser D.L., Wittwer B., Horst J., Montini E., Opitz J.M., Ballabio A., Muenke M.
    Am. J. Hum. Genet. 63:703-710(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GBBB1 ARG-266 AND THR-536.
  21. Cited for: VARIANTS GBBB1 PRO-295 AND 391-LEU-CYS-392 DELINS ARG.

Entry informationi

Entry nameiTRI18_HUMAN
AccessioniPrimary (citable) accession number: O15344
Secondary accession number(s): B2RCG2, O75361, Q9BZX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: January 1, 1998
Last modified: June 24, 2015
This is version 168 of the entry and version 1 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 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.