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O15344 (TRI18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MID1
Synonyms:FXY, RNF59, TRIM18, XPRF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length667 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.17

Subunit structure

Homodimer or heterodimer with MID2. Interacts with IGBP1. Ref.12 Ref.17

Subcellular location

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. Ref.10

Tissue specificity

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.

Induction

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.

Post-translational modification

Phosphorylated on serine and threonine residues. Ref.12

Involvement in disease

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. Ref.1 Ref.4 Ref.19 Ref.21

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 2 B box-type zinc fingers.

Contains 1 B30.2/SPRY domain.

Contains 1 COS domain.

Contains 1 fibronectin type-III domain.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmicrotubule cytoskeleton organization

Traceable author statement Ref.10. Source: ProtInc

pattern specification process

Traceable author statement Ref.1. Source: ProtInc

positive regulation of stress-activated MAPK cascade

Inferred from mutant phenotype PubMed 17438131. Source: UniProtKB

protein localization to microtubule

Inferred from mutant phenotype Ref.12. Source: UniProt

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from direct assay Ref.12. Source: UniProt

microtubule associated complex

Traceable author statement Ref.10. Source: ProtInc

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule binding

Inferred from mutant phenotype Ref.12. Source: UniProt

phosphoprotein binding

Inferred from physical interaction Ref.12. Source: UniProt

protein heterodimerization activity

Inferred from direct assay Ref.12. Source: UniProt

protein homodimerization activity

Inferred from direct assay Ref.12. Source: UniProt

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 17438131. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15344-1)

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.
Isoform 2 (identifier: O15344-2)

Also known as: Beta;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 667667E3 ubiquitin-protein ligase Midline-1
PRO_0000056227

Regions

Domain320 – 37960COS
Domain381 – 484104Fibronectin type-III
Domain482 – 659178B30.2/SPRY
Zinc finger10 – 6051RING-type
Zinc finger116 – 16550B box-type 1
Zinc finger172 – 21241B box-type 2
Coiled coil205 – 26460 Potential

Sites

Metal binding1191Zinc 1
Metal binding1221Zinc 1
Metal binding1341Zinc 2
Metal binding1371Zinc 2
Metal binding1421Zinc 1
Metal binding1451Zinc 1
Metal binding1501Zinc 2
Metal binding1591Zinc 2

Amino acid modifications

Modified residue921Phosphoserine Ref.16

Natural variations

Alternative sequence553 – 667115Missing in isoform 2.
VSP_005735
Natural variant2661C → R in OGS1. Ref.19
VAR_013758
Natural variant2951L → P in OGS1. Ref.21
VAR_025495
Natural variant391 – 3922LC → R in OGS1.
VAR_025496
Natural variant4381Missing in OGS1. Ref.1
VAR_013759
Natural variant5341V → VFIDSGRHL in OGS1.
VAR_013760
Natural variant5361I → T in OGS1. Ref.19
VAR_013761
Natural variant6261L → P in OGS1. Ref.4
Corresponds to variant rs28934611 [ dbSNP | Ensembl ].
VAR_013762

Experimental info

Sequence conflict2281T → P in AAC32999. Ref.3
Sequence conflict4841Q → P in AAC32998. Ref.3

Secondary structure

......................... 667
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 673C5120018BA619

FASTA66775,251
        10         20         30         40         50         60 
METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNESVES ITAFQCPTCR 

        70         80         90        100        110        120 
HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERAFDANT MTSAEKVLCQ 

       130        140        150        160        170        180 
FCDQDPAQDA VKTCVTCEVS YCDECLKATH PNKKPFTGHR LIEPIPDSHI RGLMCLEHED 

       190        200        210        220        230        240 
EKVNMYCVTD DQLICALCKL VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL 

       250        260        270        280        290        300 
LAKLIQTCQH VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVM RLRKLAQQIA 

       310        320        330        340        350        360 
NCKQCIERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI PEINLNDTFD 

       370        380        390        400        410        420 
TFALDFSREK KLLECLDYLT APNPPTIREE LCTASYDTIT VHWTSDDEFS VVSYELQYTI 

       430        440        450        460        470        480 
FTGQANVVSL CNSADSWMIV PNIKQNHYTV HGLQSGTKYI FMVKAINQAG SRSSEPGKLK 

       490        500        510        520        530        540 
TNSQPFKLDP KSAHRKLKVS HDNLTVERDE SSSKKSHTPE RFTSQGSYGV AGNVFIDSGR 

       550        560        570        580        590        600 
HYWEVVISGS TWYAIGLAYK SAPKHEWIGK NSASWALCRC NNNWVVRHNS KEIPIEPAPH 

       610        620        630        640        650        660 
LRRVGILLDY DNGSIAFYDA LNSIHLYTFD VAFAQPVCPT FTVWNKCLTI ITGLPIPDHL 


DCTEQLP 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: FD4D4C0EA5915DB2
Show »

FASTA55262,288

References

« Hide 'large scale' references
[1]"Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22."
Quaderi N.A., Schweiger S., Gaudenz K., Franco B., Rugarli E.I., Berger W., Feldman G.J., Volta M., Andolfi G., Gilgenkrantz S., Marion R.W., Hennekam R.C.M., Opitz J.M., Muenke M., Ropers H.-H., Ballabio A.
Nat. Genet. 17:285-291(1997) [PubMed] [Europe PMC] [Abstract]
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]"The tripartite motif family identifies cell compartments."
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A.
EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The Opitz syndrome gene product, MID1, associates with microtubules."
Schweiger S., Foerster J., Lehmann T., Suckow V., Muller Y.A., Walter G., Davies T., Porter H., van Bokhoven H., Lunt P.W., Traub P., Ropers H.H.
Proc. Natl. Acad. Sci. U.S.A. 96:2794-2799(1999) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]Erratum
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. 63:1571-1571(1998)
[21]"Mild phenotypes in a series of patients with Opitz GBBB syndrome with MID1 mutations."
So J., Suckow V., Kijas Z., Kalscheuer V., Moser B., Winter J., Baars M., Firth H., Lunt P., Hamel B.C.J., Meinecke P., Moraine C., Odent S., Schinzel A., van der Smagt J.J., Devriendt K., Albrecht B., Gillessen-Kaesbach G. expand/collapse author list , van der Burgt I., Petrij F., Faivre L., McGaughran J., McKenzie F., Opitz J.M., Cox T., Schweiger S.
Am. J. Med. Genet. A 132:1-7(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OGS1 PRO-295 AND 391-LEU-CYS-392 DELINS ARG.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT09482.
RefSeqNP_000372.1. NM_000381.3.
NP_001092094.1. NM_001098624.2.
NP_001180206.1. NM_001193277.1.
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.
UniGeneHs.27695.
Hs.689953.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DQ5NMR-A168-214[»]
2FFWNMR-A87-164[»]
2JUNNMR-A114-214[»]
ProteinModelPortalO15344.
SMRO15344. Positions 1-84, 87-214, 376-642.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110427. 31 interactions.
IntActO15344. 13 interactions.
STRING9606.ENSP00000312678.

PTM databases

PhosphoSiteO15344.

Proteomic databases

PaxDbO15344.
PRIDEO15344.

Protocols and materials databases

DNASU4281.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317552; 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]
GeneID4281.
KEGGhsa:4281.
UCSCuc004ctc.4. human. [O15344-1]

Organism-specific databases

CTD4281.
GeneCardsGC0XM010373.
HGNCHGNC:7095. MID1.
HPAHPA003715.
MIM300000. phenotype.
300552. gene.
neXtProtNX_O15344.
Orphanet306597. X-linked Opitz G/BBB syndrome.
PharmGKBPA30816.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253961.
HOGENOMHOG000049193.
HOVERGENHBG056432.
InParanoidO15344.
KOK08285.
OMACIERSTS.
OrthoDBEOG7MH0XH.
PhylomeDBO15344.
TreeFamTF333654.

Gene expression databases

ArrayExpressO15344.
BgeeO15344.
CleanExHS_MID1.
GenevestigatorO15344.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.30.40.10. 2 hits.
4.10.45.10. 1 hit.
InterProIPR001870. 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/MID2.
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]
PANTHERPTHR24103:SF148. PTHR24103:SF148. 1 hit.
PfamPF00041. fn3. 1 hit.
PF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSPR01407. BUTYPHLNCDUF.
SMARTSM00502. 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]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEPS50188. 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]
ProtoNetSearch...

Other

EvolutionaryTraceO15344.
GeneWikiMID1.
GenomeRNAi4281.
NextBio16837.
PROO15344.
SOURCESearch...

Entry information

Entry nameTRI18_HUMAN
AccessionPrimary (citable) accession number: O15344
Secondary accession number(s): B2RCG2, O75361, Q9BZX5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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Human chromosome X

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