SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O15344

- TRI18_HUMAN

UniProt

O15344 - TRI18_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

E3 ubiquitin-protein ligase Midline-1

Gene
MID1, FXY, RNF59, TRIM18, XPRF
Organism
Homo sapiens (Human)
Status
Reviewed - 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-typeAdd
BLAST
Zinc fingeri116 – 16550B box-type 1Add
BLAST
Zinc fingeri172 – 21241B box-type 2Add
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
Complete GO annotation...

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. Cytoplasmcytoskeleton. Cytoplasmcytoskeletonspindle
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.1 Publication

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. MID1 mutations produce proteins with a decreased affinity for microtubules.4 Publications
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 – 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

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.

Miscellaneous databases

EvolutionaryTraceiO15344.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini320 – 37960COSAdd
BLAST
Domaini381 – 484104Fibronectin type-IIIAdd
BLAST
Domaini482 – 659178B30.2/SPRYAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili205 – 26460 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Belongs to the TRIM/RBCC family.
Contains 1 B30.2/SPRY domain.
Contains 1 COS domain.

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

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. VSP_005735Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281T → P in AAC32999. 1 Publication
Sequence conflicti484 – 4841Q → P in AAC32998. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 158 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