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Center for Computational Systems Medicine
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Protein Summary

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AS Summary

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Protein Functional Features

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Gene Isoform Structures and Expression Levels

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Protein Structures

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pLDDT Score Distribution

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Ramachandran Plot of Protein Structures

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Potential Active Site Information

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Protein Structure and Feature Comparision

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Protein-Protein Interaction

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Related Drugs

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Related Diseases

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Clinically Important Variants

Protein:MIA3

Protein Summary

check button Gene summary
Gene name: MIA3
ASpdb.0 ID: 375056
Gene
Gene symbol

MIA3

Gene ID

375056

Gene nameMIA SH3 domain ER export factor 3
SynonymsARNT|D320|ODCD2|TANGO|TANGO1|UNQ6077
Cytomap

1q41

Type of geneprotein-coding
Descriptiontransport and Golgi organization protein 1 homologC219-reactive peptideMIA family member 3, ER export factormelanoma inhibitory activity family, member 3melanoma inhibitory activity protein 3
Modification date20240411
UniProtAcc

Q5JRA6


check button Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
GeneMIA3

GO:0002687

positive regulation of leukocyte migration

17726152

GeneMIA3

GO:0005789

endoplasmic reticulum membrane

19269366

GeneMIA3

GO:0007162

negative regulation of cell adhesion

17726152

GeneMIA3

GO:0016020

membrane

19269366

GeneMIA3

GO:0030336

negative regulation of cell migration

17044017

GeneMIA3

GO:0042060

wound healing

17044017

GeneMIA3

GO:0043231

intracellular membrane-bounded organelle

-

GeneMIA3

GO:0070971

endoplasmic reticulum exit site

21525241|25202031|28442536



AS Summary

check button Information of the canonical protein with experimentally identified structure from PDB (2023).
UniProt AccFile namePDB IDMethodResolutionChainStartEnd
Q5JRA6-1Q5JRA6-1_5kyn_C.pdb5KYNX-ray2.55C18011803

check button ASpdb's canonical and alternatively spliced isoform information.
accession_idgene_namecanonical_idalternative_idcanonical_lengthalternative_lengthcanonical_startcanonical_endtypeoriginalSEQvariationSEQalternative_startalternative_end
Q5JRA6MIA3Q5JRA6-1Q5JRA6-31907500493500SubstitutionMTVHSSVHFKTEPIKL493500
Q5JRA6MIA3Q5JRA6-1Q5JRA6-319075005011907Deletionnonenone500500
Q5JRA6MIA3Q5JRA6-1Q5JRA6-4190778511122Deletionnonenone00
Q5JRA6MIA3Q5JRA6-1Q5JRA6-4190778511231159SubstitutionIDANKQPETAAEEPASVTPLENAILLIYSFMFYLTKSMDSVPATVPSIAATPGDPELVGPLSVLYAAFIAKLLE137

check buttonMultiple sequence alignment of our canonical and alternatively spliced MIA3

check button Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of MIA3
UniProt-idENSGENSTENSP
Q5JRA6-1ENSG00000154305.18ENST00000344922.10ENSP00000340900.5
Q5JRA6-4ENSG00000154305.18ENST00000340535.11ENSP00000345866.7

UniProt-idNM IDNP ID
Q5JRA6-1NM_198551.3NP_940953.2
Q5JRA6-4NM_001300867.1NP_001287796.1

check buttonAmino acid sequences of our canonical and alternatively spliced MIA3
accession_idProtein sequence
Q5JRA6-1MAAAPGLLVWLLVLRLPWRVPGQLDPSTGRRFSEHKLCADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARGWPEVWAGSV
GRTFGYFPKDLIQVVHEYTKEELQVPTDETDFVCFDGGRDDFHNYNVEELLGFLELYNSAATDSEKAVEKTLQDMEKNPELSKEREPEPE
PVEANSEESDSVFSENTEDLQEQFTTQKHHSHANSQANHAQGEQASFESFEEMLQDKLKVPESENNKTSNSSQVSNEQDKIDAYKLLKKE
MTLDLKTKFGSTADALVSDDETTRLVTSLEDDFDEELDTEYYAVGKEDEENQEDFDELPLLTFTDGEDMKTPAKSGVEKYPTDKEQNSNE
EDKVQLTVPPGIKNDDKNILTTWGDTIFSIVTGGEETRDTMDLESSSSEEEKEDDDDALVPDSKQGKPQSATDYSDPDNVDDGLFIVDIP
KTNNDKEVNAEHHIKGKGRGVQESKRGLVQDKTELEDENQEGMTVHSSVHSNNLNSMPAAEKGKDTLKSAYDDTENDLKGAAIHISKGML
HEEKPGEQILEGGSESESAQKAAGNQMNDRKIQQESLGSAPLMGDDHPNASRDSVEGDALVNGAKLHTLSVEHQREELKEELVLKTQNQP
RFSSPDEIDLPRELEDEVPILGRNLPWQQERDVAATASKQMSEKIRLSEGEAKEDSLDEEFFHHKAMQGTEVGQTDQTDSTGGPAFLSKV
EEDDYPSEELLEDENAINAKRSKEKNPGNQGRQFDVNLQVPDRAVLGTIHPDPEIEESKQETSMILDSEKTSETAAKGVNTGGREPNTMV
EKERPLADKKAQRPFERSDFSDSIKIQTPELGEVFQNKDSDYLKNDNPEEHLKTSGLAGEPEGELSKEDHENTEKYMGTESQGSAAAEPE
DDSFHWTPHTSVEPGHSDKREDLLIISSFFKEQQSLQRFQKYFNVHELEALLQEMSSKLKSAQQESLPYNMEKVLDKVFRASESQILSIA
EKMLDTRVAENRDLGMNENNIFEEAAVLDDIQDLIYFVRYKHSTAEETATLVMAPPLEEGLGGAMEEMQPLHEDNFSREKTAELNVQVPE
EPTHLDQRVIGDTHASEVSQKPNTEKDLDPGPVTTEDTPMDAIDANKQPETAAEEPASVTPLENAILLIYSFMFYLTKSLVATLPDDVQP
GPDFYGLPWKPVFITAFLGIASFAIFLWRTVLVVKDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSD
EAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQ
EENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVG
GDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQK
EMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAA
NLRHKLLELTQKMAMLQEEPVIVKPMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDGP
LPHPRWSAEASGKPSPSDPGSGTATMMNSSSRGSSPTRVLDEGKVNMAPKGPPPFPGVPLMSTPMGGPVPPPIRYGPPPQLCGPFGPRPL
PPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREYFIPGTRLPPPTHGPQEYPPPPAVRDLLPSGSRDEPPP
Q5JRA6-3MAAAPGLLVWLLVLRLPWRVPGQLDPSTGRRFSEHKLCADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARGWPEVWAGSV
GRTFGYFPKDLIQVVHEYTKEELQVPTDETDFVCFDGGRDDFHNYNVEELLGFLELYNSAATDSEKAVEKTLQDMEKNPELSKEREPEPE
PVEANSEESDSVFSENTEDLQEQFTTQKHHSHANSQANHAQGEQASFESFEEMLQDKLKVPESENNKTSNSSQVSNEQDKIDAYKLLKKE
MTLDLKTKFGSTADALVSDDETTRLVTSLEDDFDEELDTEYYAVGKEDEENQEDFDELPLLTFTDGEDMKTPAKSGVEKYPTDKEQNSNE
EDKVQLTVPPGIKNDDKNILTTWGDTIFSIVTGGEETRDTMDLESSSSEEEKEDDDDALVPDSKQGKPQSATDYSDPDNVDDGLFIVDIP
Q5JRA6-4MDSVPATVPSIAATPGDPELVGPLSVLYAAFIAKLLELVATLPDDVQPGPDFYGLPWKPVFITAFLGIASFAIFLWRTVLVVKDRVYQVT
EQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQD
LISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLE
VALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASV
STKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRR
IEEMEDELQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEEPVIVKPMPGKPNTQNPPRRGPLS
QNGSFGPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGKPSPSDPGSGTATMMNSSSRGSSPTRVLDE
GKVNMAPKGPPPFPGVPLMSTPMGGPVPPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGFLPGHAPF

Protein Functional Features

check buttonMain function of this protein. (from UniProt)
MIA3 (go to UniProt):Q5JRA6

check buttonRetention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at

download page

* Minus value of BPloci means that the break pointn is located before the CDS.
- Retained protein feature among the 13 regional features.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
Q5JRA6Topological domain231144Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=493;End=500
Q5JRA6Topological domain231144Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=501;End=1907
Q5JRA6Topological domain231144Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=1;End=1122
Q5JRA6Topological domain231144Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=1123;End=1159
Q5JRA6Intramembrane11451165Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=501;End=1907
Q5JRA6Intramembrane11451165Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=1123;End=1159
Q5JRA6Topological domain11661176Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=501;End=1907
Q5JRA6Transmembrane11771197Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=501;End=1907
Q5JRA6Topological domain11981907Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=501;End=1907
Q5JRA6Domain45107Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192Type=Deletion;Start=1;End=1122
Q5JRA6Region155258Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Region314378Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Region390601Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=493;End=500
Q5JRA6Region390601Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Region390601Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Region659918Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Region659918Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Region10931121Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Region10931121Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Region12111650Note=Mediates interaction with MIA2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21525241;Dbxref=PMID:21525241Type=Deletion;Start=501;End=1907
Q5JRA6Region14201443Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Region16421907Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Region17511907"Note=Proline-rich domain (PRD)%3B mediates interaction with the COPII coat subunits SEC23A and SEC23B;Ontology_term=ECO:0000269ECO:0000269
Q5JRA6Region17881847Note=SEC16A-interacting region (SIR)%3B required for its localization to endoplasmic reticulum exit sites and for its interaction with SEC16A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28442536;Dbxref=PMID:28442536Type=Deletion;Start=501;End=1907
Q5JRA6Coiled coil471531Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=493;End=500
Q5JRA6Coiled coil471531Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=501;End=1907
Q5JRA6Coiled coil471531Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=1;End=1122
Q5JRA6Coiled coil12141396Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=501;End=1907
Q5JRA6Coiled coil14871639Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=501;End=1907
Q5JRA6Compositional bias157182Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias187225Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias244258Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias341361Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias454493Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=493;End=500
Q5JRA6Compositional bias454493Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias494509Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Substitution;Start=493;End=500
Q5JRA6Compositional bias494509Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias494509Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias515550Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias515550Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias553575Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias553575Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias674696Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias674696Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias700714Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias700714Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias733748Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias733748Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias769786Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias769786Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias807830Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias807830Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias847886Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias847886Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias902918Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias902918Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=1;End=1122
Q5JRA6Compositional bias16551671Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias17241747Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias17591809Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias18561878Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907
Q5JRA6Compositional bias18871907Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=501;End=1907


Gene Isoform Structures and Expression Levels for MIA3

check buttonGene structures of our canonical and alternative spliced genes of MIA3
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
gene isoform structure of MIA3

check button Expression levels of gene isoforms across GTEx.
gtex expression

check button Expression levels of gene isoforms across TCGA.
tcga expression


Protein Structures

check button PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.
3D view using mol* of Q5JRA6-1
3D view using mol* of Q5JRA6-3
3D view using mol* of Q5JRA6-4


pLDDT Score Distribution

check button pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.
pLDDT distribution across the protein length of Q5JRA6-1
all structure
pLDDT distribution across the protein length of Q5JRA6-3
all structure
pLDDT distribution across the protein length of Q5JRA6-4
all structure


Ramachandran Plot of Protein Structures


check button Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.
Ramachandran plot of Q5JRA6-1
all structure
Ramachandran plot of Q5JRA6-3
all structure

Potential Active Site Information


check button The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.
UniProt-idSite scoreSizeD scoreVolumeExposureEnclosureContactPhobicPhilicBalanceDon/AccResidues
Q5JRA6-10.953870.935228.4380.4970.7010.930.8221.1130.7390.544914,916,917,918,919,920,923,927,930,931,932,933,93
6,937,940,944,945,946
Q5JRA6-30.645330.612128.9680.8210.5770.6630.2790.8420.3321.09928,31,32,33,34,35,79,80,81,82,135,136,137,138
Q5JRA6-40.834350.8966.8850.6070.6460.8283.0020.16518.2246.42228,31,32,35,58,61,62,64,65,66

Protein Structure and Feature Comparision


check button Protein Structure Comparision Using Template Modeling Scores (TM-score).
all structure

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)
3D view using mol* of Q5JRA6-1_Q5JRA6-1_5kyn_C.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of Q5JRA6-1_5kyn_C_Q5JRA6-3.pdb
3D view using mol* of Q5JRA6-1_5kyn_C_Q5JRA6-4.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of Q5JRA6-1_Q5JRA6-3.pdb
3D view using mol* of Q5JRA6-1_Q5JRA6-4.pdb

check button Protein Feature Comparison of the protein sequendary structures among the protiens.
./stats/secondary_structure/figure/Q5JRA6-1_vs_Q5JRA6-3.png
all structure<
./stats/secondary_structure/figure/Q5JRA6-1_vs_Q5JRA6-4.png
all structure<

check button Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.
./stats/relative_asa/Q5JRA6-1_vs_Q5JRA6-3.png
all structure<
./stats/relative_asa/Q5JRA6-1_vs_Q5JRA6-4.png
all structure<


Protein-Protein Interaction


check button Interactors from UniProt.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
Q5JRA6Region12111650Note=Mediates interaction with MIA2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21525241;Dbxref=PMID:21525241Type=Deletion;Start=501;End=1907
Q5JRA6Region17511907"Note=Proline-rich domain (PRD)%3B mediates interaction with the COPII coat subunits SEC23A and SEC23B;Ontology_term=ECO:0000269ECO:0000269
Q5JRA6Region17881847Note=SEC16A-interacting region (SIR)%3B required for its localization to endoplasmic reticulum exit sites and for its interaction with SEC16A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28442536;Dbxref=PMID:28442536Type=Deletion;Start=501;End=1907


check button Interactors from STRING.
Gene nameInteractors


Related Drugs to MIA3


check button Drugs targeting this gene/protein.
(DrugBank)
UniProt accessionGene nameDrugBank IDDrug nameDrug groupActions

Related Diseases to MIA3


check button Previous studies relating to the alternative splicing of MIA3 and disease information from the MeSH term (PubMed)
GenePMIDTitleAbstractMeSH IDMeSH term


Clinically important variants in MIA3


check button (ClinVar, 04/20/2024)
accession_iduniprot_idgene_nameTypeVariantClinical_significance