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O15344

- TRI18_HUMAN

UniProt

O15344 - TRI18_HUMAN

Protein

E3 ubiquitin-protein ligase Midline-1

Gene

MID1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    1. ligase activity Source: UniProtKB-KW
    2. microtubule binding Source: UniProt
    3. phosphoprotein binding Source: UniProt
    4. protein heterodimerization activity Source: UniProt
    5. protein homodimerization activity Source: UniProt
    6. ubiquitin protein ligase binding Source: UniProtKB
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. microtubule cytoskeleton organization Source: ProtInc
    2. pattern specification process Source: ProtInc
    3. positive regulation of stress-activated MAPK cascade Source: UniProtKB
    4. protein localization to microtubule Source: UniProt

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    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: Chromosome X

    Organism-specific databases

    HGNCiHGNC:7095. MID1.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication
    Note: Microtubule-associated. It is associated with microtubules throughout the cell cycle, co-localizing with cytoplasmic fibers in interphase and with the mitotic spindle and midbodies during mitosis and cytokinesis.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. microtubule Source: UniProt
    3. microtubule associated complex Source: ProtInc
    4. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Opitz GBBB syndrome 1 (OGS1) [MIM:300000]: A 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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. MID1 mutations produce proteins with a decreased affinity for microtubules.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti266 – 2661C → R in OGS1. 1 Publication
    VAR_013758
    Natural varianti295 – 2951L → P in OGS1. 1 Publication
    VAR_025495
    Natural varianti391 – 3922LC → R in OGS1.
    VAR_025496
    Natural varianti438 – 4381Missing in OGS1. 1 Publication
    VAR_013759
    Natural varianti534 – 5341V → VFIDSGRHL in OGS1.
    VAR_013760
    Natural varianti536 – 5361I → T in OGS1. 1 Publication
    VAR_013761
    Natural varianti626 – 6261L → P in OGS1. 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.

    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 – 921Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated on serine and threonine residues.2 Publications

    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

    ArrayExpressiO15344.
    BgeeiO15344.
    CleanExiHS_MID1.
    GenevestigatoriO15344.

    Organism-specific databases

    HPAiHPA003715.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi110427. 31 interactions.
    IntActiO15344. 13 interactions.
    STRINGi9606.ENSP00000312678.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DQ5NMR-A168-214[»]
    2FFWNMR-A87-164[»]
    2JUNNMR-A114-214[»]
    ProteinModelPortaliO15344.
    SMRiO15344. Positions 2-64, 87-361, 376-642.
    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.
    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.
    IPR008985. ConA-like_lec_gl_sf.
    IPR017903. COS_domain.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR027727. MID1.
    IPR006574. PRY.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    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. Align

    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

    METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNESVES    50
    ITAFQCPTCR HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET 100
    RRERAFDANT MTSAEKVLCQ FCDQDPAQDA VKTCVTCEVS YCDECLKATH 150
    PNKKPFTGHR LIEPIPDSHI RGLMCLEHED EKVNMYCVTD DQLICALCKL 200
    VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL LAKLIQTCQH 250
    VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVM RLRKLAQQIA 300
    NCKQCIERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI 350
    PEINLNDTFD TFALDFSREK KLLECLDYLT APNPPTIREE LCTASYDTIT 400
    VHWTSDDEFS VVSYELQYTI FTGQANVVSL CNSADSWMIV PNIKQNHYTV 450
    HGLQSGTKYI FMVKAINQAG SRSSEPGKLK TNSQPFKLDP KSAHRKLKVS 500
    HDNLTVERDE SSSKKSHTPE RFTSQGSYGV AGNVFIDSGR HYWEVVISGS 550
    TWYAIGLAYK SAPKHEWIGK NSASWALCRC NNNWVVRHNS KEIPIEPAPH 600
    LRRVGILLDY DNGSIAFYDA LNSIHLYTFD VAFAQPVCPT FTVWNKCLTI 650
    ITGLPIPDHL DCTEQLP 667
    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 OGS1. 1 Publication
    VAR_013758
    Natural varianti295 – 2951L → P in OGS1. 1 Publication
    VAR_025495
    Natural varianti391 – 3922LC → R in OGS1.
    VAR_025496
    Natural varianti438 – 4381Missing in OGS1. 1 Publication
    VAR_013759
    Natural varianti534 – 5341V → VFIDSGRHL in OGS1.
    VAR_013760
    Natural varianti536 – 5361I → T in OGS1. 1 Publication
    VAR_013761
    Natural varianti626 – 6261L → P in OGS1. 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14138.1. [O15344-1 ]
    PIRi T09482.
    RefSeqi NP_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 ]
    UniGenei Hs.27695.
    Hs.460482.
    Hs.689953.
    Hs.738954.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DQ5 NMR - A 168-214 [» ]
    2FFW NMR - A 87-164 [» ]
    2JUN NMR - A 114-214 [» ]
    ProteinModelPortali O15344.
    SMRi O15344. Positions 2-64, 87-361, 376-642.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110427. 31 interactions.
    IntActi O15344. 13 interactions.
    STRINGi 9606.ENSP00000312678.

    PTM databases

    PhosphoSitei O15344.

    Proteomic databases

    MaxQBi O15344.
    PaxDbi O15344.
    PRIDEi O15344.

    Protocols and materials databases

    DNASUi 4281.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317552 ; 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 ]
    GeneIDi 4281.
    KEGGi hsa:4281.
    UCSCi uc004ctc.4. human. [O15344-1 ]

    Organism-specific databases

    CTDi 4281.
    GeneCardsi GC0XM010373.
    GeneReviewsi MID1.
    HGNCi HGNC:7095. MID1.
    HPAi HPA003715.
    MIMi 300000. phenotype.
    300552. gene.
    neXtProti NX_O15344.
    Orphaneti 306597. X-linked Opitz G/BBB syndrome.
    PharmGKBi PA30816.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG253961.
    HOGENOMi HOG000049193.
    HOVERGENi HBG056432.
    InParanoidi O15344.
    KOi K08285.
    OMAi RERAFDS.
    OrthoDBi EOG7MH0XH.
    PhylomeDBi O15344.
    TreeFami TF333654.

    Miscellaneous databases

    EvolutionaryTracei O15344.
    GeneWikii MID1.
    GenomeRNAii 4281.
    NextBioi 16837.
    PROi O15344.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15344.
    Bgeei O15344.
    CleanExi HS_MID1.
    Genevestigatori O15344.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.30.40.10. 2 hits.
    4.10.45.10. 1 hit.
    InterProi IPR001870. B30.2/SPRY.
    IPR003649. Bbox_C.
    IPR003879. Butyrophylin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR017903. COS_domain.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR027727. MID1.
    IPR006574. PRY.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    IPR000315. Znf_B-box.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    PANTHERi PTHR24103:SF26. PTHR24103:SF26. 1 hit.
    Pfami PF00041. fn3. 1 hit.
    PF13765. PRY. 1 hit.
    PF00622. SPRY. 1 hit.
    PF00643. zf-B_box. 1 hit.
    [Graphical view ]
    PRINTSi PR01407. BUTYPHLNCDUF.
    SMARTi SM00502. 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 ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF49899. SSF49899. 1 hit.
    PROSITEi PS50188. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS OGS1 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 OGS1 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. "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.
    19. "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 OGS1 ARG-266 AND THR-536.
    20. Cited for: VARIANTS OGS1 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: October 1, 2014
    This is version 159 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