P43243 · MATR3_HUMAN
- ProteinMatrin-3
- GeneMATR3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids847 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947).
May bind to specific miRNA hairpins (PubMed:28431233).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | nuclear inner membrane | |
Cellular Component | nuclear matrix | |
Cellular Component | nucleus | |
Molecular Function | identical protein binding | |
Molecular Function | miRNA binding | |
Molecular Function | RNA binding | |
Molecular Function | structural molecule activity | |
Molecular Function | zinc ion binding | |
Biological Process | activation of innate immune response | |
Biological Process | blastocyst formation | |
Biological Process | heart valve development | |
Biological Process | innate immune response | |
Biological Process | post-transcriptional regulation of gene expression | |
Biological Process | ventricular septum development |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMatrin-3
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP43243
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Amyotrophic lateral sclerosis 21 (ALS21)
- Note
- DescriptionA neurodegenerative disorder affecting upper and lower motor neurons, resulting in muscle weakness and respiratory failure. Some patients may develop myopathic features or dementia.
- See alsoMIM:606070
Natural variants in ALS21
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_074067 | 72 | A>T | in ALS21; uncertain significance | |
VAR_063421 | 85 | S>C | in ALS21; results in increased interaction with TARDBP; dbSNP:rs121434591 | |
VAR_071078 | 115 | F>C | in ALS21; dbSNP:rs587777300 | |
VAR_078513 | 147 | R>W | in ALS21; uncertain significance | |
VAR_071079 | 154 | P>S | in ALS21; uncertain significance; dbSNP:rs587777302 | |
VAR_071080 | 622 | T>A | in ALS21; dbSNP:rs587777301 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_074067 | 72 | in ALS21; uncertain significance | |||
Sequence: A → T | ||||||
Natural variant | VAR_063421 | 85 | in ALS21; results in increased interaction with TARDBP; dbSNP:rs121434591 | |||
Sequence: S → C | ||||||
Natural variant | VAR_074068 | 89 | in dbSNP:rs528548235 | |||
Sequence: I → V | ||||||
Natural variant | VAR_071078 | 115 | in ALS21; dbSNP:rs587777300 | |||
Sequence: F → C | ||||||
Natural variant | VAR_078513 | 147 | in ALS21; uncertain significance | |||
Sequence: R → W | ||||||
Natural variant | VAR_071079 | 154 | in ALS21; uncertain significance; dbSNP:rs587777302 | |||
Sequence: P → S | ||||||
Natural variant | VAR_071080 | 622 | in ALS21; dbSNP:rs587777301 | |||
Sequence: T → A | ||||||
Natural variant | VAR_074069 | 664 | in dbSNP:rs139589527 | |||
Sequence: E → A | ||||||
Natural variant | VAR_074070 | 787 | in dbSNP:rs148402819 | |||
Sequence: N → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 815 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, modified residue (large scale data), chain, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000081622 | 2-847 | UniProt | Matrin-3 | |||
Sequence: SKSFQQSSLSRDSQGHGRDLSAAGIGLLAAATQSLSMPASLGRMNQGTARLASLMNLGMSSSLNQQGAHSALSSASTSSHNLQSIFNIGSRGPLPLSSQHRGDADQASNILASFGLSARDLDELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRSATREPPYRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHGSRSQESGYYDRMDYEDDRLRDGERCRDDSFFGETSHNYHKFDSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPKGYPHLCSICDLPVHSNKEWSQHINGASHSRRCQLLLEIYPEWNPDNDTGHTMGDPFMLQQSTNPAPGILGPPPPSFHLGGPAVGPRGNLGAGNGNLQGPRHMQKGRVETSRVVHIMDFQRGKNLRYQLLQLVEPFGVISNHLILNKINEAFIEMATTEDAQAAVDYYTTTPALVFGKPVRVHLSQKYKRIKKPEGKPDQKFDQKQELGRVIHLSNLPHSGYSDSAVLKLAEPYGKIKNYILMRMKSQAFIEMETREDAMAMVDHCLKKALWFQGRCVKVDLSEKYKKLVLRIPNRGIDLLKKDKSRKRSYSPDGKESPSDKKSKTDGSQKTESSTEGKEQEEKSGEDGEKDTKDDQTEQEPNMLLESEDELLVDEEEAAALLESGSSVGDETDLANLGDVASDGKKEPSDKAVKKDGSASAAAKKKLKKVDKIEELDQENEAALENGIKNEENTEPGAESSENADDPNKDTSENADGQSDENKDDYTIPDEYRIGPYQPNVPVGIDYVIPKTGFYCKLCSLFYTNEEVAKNTHCSSLPHYQKLKKFLNKLAEERRQKKET | |||||||
Modified residue | 3 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 3 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 4 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 9 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 11 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 14 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 22 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 35 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 41 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 99 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 118 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 126 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 132 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 134 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 146 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 150 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 150 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 157 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 157 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 158 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 164 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 164 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 166 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 188 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 188 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 195 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 195 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 202 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 206 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 206 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 208 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 211 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 213 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 219 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 219 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 234 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 239 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 245 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 248 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 264 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 264 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 269 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 275 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 478 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 487 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 491 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 501 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 509 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 509 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 511 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 511 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 515 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 522 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 522 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 533 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 533 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 541 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 554 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 555 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 571 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 596 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 596 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 597 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 598 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 598 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 604 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 604 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 606 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 606 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 615 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 617 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 618 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 621 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 630 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 631 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 654 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 671 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 673 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 674 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 679 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 689 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 719 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 736 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 741 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 741 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 747 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 747 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 748 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 759 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 759 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 766 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 766 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 770 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 773 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 836 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 836 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with FUS. Interacts with IGF2BP1; the interaction is enhanced by SEPIN14P20 peptide RBPR (PubMed:29476152, PubMed:32245947).
Interacts with IGF2BP2 and IGF2BP3 (PubMed:29476152).
Interacts with RBPMS (PubMed:37548402).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P43243 | DISC1 Q9NRI5 | 3 | EBI-352602, EBI-529989 | |
BINARY | P43243 | HNRNPK P61978 | 4 | EBI-352602, EBI-304185 | |
BINARY | P43243 | HNRNPK P61978-2 | 4 | EBI-352602, EBI-7060731 | |
BINARY | P43243 | HTR7 P34969 | 2 | EBI-352602, EBI-2625020 | |
BINARY | P43243 | HTT P42858 | 4 | EBI-352602, EBI-466029 | |
BINARY | P43243 | KRT27 Q7Z3Y8 | 3 | EBI-352602, EBI-3044087 | |
BINARY | P43243 | KRT34 O76011 | 3 | EBI-352602, EBI-1047093 | |
BINARY | P43243 | MATR3 P43243 | 4 | EBI-352602, EBI-352602 | |
BINARY | P43243 | NR4A1 P22736 | 2 | EBI-352602, EBI-721550 | |
BINARY | P43243 | PCBP3 P57721-2 | 3 | EBI-352602, EBI-11983983 | |
BINARY | P43243 | PLEKHG4 Q58EX7 | 3 | EBI-352602, EBI-949255 | |
BINARY | P43243 | PTBP2 Q9UKA9-2 | 3 | EBI-352602, EBI-12255608 | |
BINARY | P43243 | RASD1 Q9Y272 | 6 | EBI-352602, EBI-740818 | |
BINARY | P43243 | RBM45 Q8IUH3 | 5 | EBI-352602, EBI-2512147 | |
BINARY | P43243 | TARDBP Q13148 | 6 | EBI-352602, EBI-372899 | |
BINARY | P43243 | TRAF1 Q13077 | 3 | EBI-352602, EBI-359224 | |
BINARY | P43243 | TSGA10 Q9BZW7 | 3 | EBI-352602, EBI-744794 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, motif, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 146-174 | Disordered | ||||
Sequence: KRRRTEEGPTLSYGRDGRSATREPPYRVP | ||||||
Region | 187-214 | Disordered | ||||
Sequence: DSFDDRGPSLNPVLDYDHGSRSQESGYY | ||||||
Region | 342-394 | Disordered | ||||
Sequence: PFMLQQSTNPAPGILGPPPPSFHLGGPAVGPRGNLGAGNGNLQGPRHMQKGRV | ||||||
Domain | 398-473 | RRM 1 | ||||
Sequence: RVVHIMDFQRGKNLRYQLLQLVEPFGVISNHLILNKINEAFIEMATTEDAQAAVDYYTTTPALVFGKPVRVHLSQK | ||||||
Domain | 496-571 | RRM 2 | ||||
Sequence: RVIHLSNLPHSGYSDSAVLKLAEPYGKIKNYILMRMKSQAFIEMETREDAMAMVDHCLKKALWFQGRCVKVDLSEK | ||||||
Compositional bias | 588-647 | Basic and acidic residues | ||||
Sequence: KKDKSRKRSYSPDGKESPSDKKSKTDGSQKTESSTEGKEQEEKSGEDGEKDTKDDQTEQE | ||||||
Region | 588-786 | Disordered | ||||
Sequence: KKDKSRKRSYSPDGKESPSDKKSKTDGSQKTESSTEGKEQEEKSGEDGEKDTKDDQTEQEPNMLLESEDELLVDEEEAAALLESGSSVGDETDLANLGDVASDGKKEPSDKAVKKDGSASAAAKKKLKKVDKIEELDQENEAALENGIKNEENTEPGAESSENADDPNKDTSENADGQSDENKDDYTIPDEYRIGPYQP | ||||||
Compositional bias | 648-664 | Acidic residues | ||||
Sequence: PNMLLESEDELLVDEEE | ||||||
Compositional bias | 690-735 | Basic and acidic residues | ||||
Sequence: DGKKEPSDKAVKKDGSASAAAKKKLKKVDKIEELDQENEAALENGI | ||||||
Motif | 710-718 | Nuclear localization signal | ||||
Sequence: AKKKLKKVD | ||||||
Compositional bias | 749-777 | Basic and acidic residues | ||||
Sequence: ENADDPNKDTSENADGQSDENKDDYTIPD | ||||||
Zinc finger | 801-832 | Matrin-type | ||||
Sequence: FYCKLCSLFYTNEEVAKNTHCSSLPHYQKLKK |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P43243-1
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.
- Name1
- Length847
- Mass (Da)94,623
- Last updated2001-01-24 v2
- Checksum530AA49214BC1611
P43243-2
- Name2
- Differences from canonical
- 1-304: MSKSFQQSSLSRDSQGHGRDLSAAGIGLLAAATQSLSMPASLGRMNQGTARLASLMNLGMSSSLNQQGAHSALSSASTSSHNLQSIFNIGSRGPLPLSSQHRGDADQASNILASFGLSARDLDELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRSATREPPYRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHGSRSQESGYYDRMDYEDDRLRDGERCRDDSFFGETSHNYHKFDSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPKGYPHLCSICDLPVHSNK → MLGAQWRRNQPSRAAE
Computationally mapped potential isoform sequences
There are 20 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A8MXP9 | A8MXP9_HUMAN | MATR3 | 895 | ||
A0A0R4J2E8 | A0A0R4J2E8_HUMAN | MATR3 | 847 | ||
D6REK4 | D6REK4_HUMAN | MATR3 | 100 | ||
D6REM6 | D6REM6_HUMAN | MATR3 | 794 | ||
D6RIA2 | D6RIA2_HUMAN | MATR3 | 172 | ||
D6RBS2 | D6RBS2_HUMAN | MATR3 | 87 | ||
D6RBI2 | D6RBI2_HUMAN | MATR3 | 109 | ||
D6RBK5 | D6RBK5_HUMAN | MATR3 | 121 | ||
D6RB45 | D6RB45_HUMAN | MATR3 | 47 | ||
D6RAY2 | D6RAY2_HUMAN | MATR3 | 86 | ||
D6RAM9 | D6RAM9_HUMAN | MATR3 | 81 | ||
D6RE02 | D6RE02_HUMAN | MATR3 | 124 | ||
D6RCM3 | D6RCM3_HUMAN | MATR3 | 99 | ||
D6R9N0 | D6R9N0_HUMAN | MATR3 | 25 | ||
D6R9F3 | D6R9F3_HUMAN | MATR3 | 78 | ||
D6R8Z5 | D6R8Z5_HUMAN | MATR3 | 107 | ||
D6R991 | D6R991_HUMAN | MATR3 | 433 | ||
A0A1B0GX04 | A0A1B0GX04_HUMAN | MATR3 | 77 | ||
H0Y8T4 | H0Y8T4_HUMAN | MATR3 | 334 | ||
B3KM87 | B3KM87_HUMAN | MATR3 | 509 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_042624 | 1-304 | in isoform 2 | |||
Sequence: MSKSFQQSSLSRDSQGHGRDLSAAGIGLLAAATQSLSMPASLGRMNQGTARLASLMNLGMSSSLNQQGAHSALSSASTSSHNLQSIFNIGSRGPLPLSSQHRGDADQASNILASFGLSARDLDELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRSATREPPYRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHGSRSQESGYYDRMDYEDDRLRDGERCRDDSFFGETSHNYHKFDSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPKGYPHLCSICDLPVHSNK → MLGAQWRRNQPSRAAE | ||||||
Sequence conflict | 257 | in Ref. 2; AAF17217 | ||||
Sequence: P → S | ||||||
Sequence conflict | 274 | in Ref. 2; AAF17217 | ||||
Sequence: P → S | ||||||
Sequence conflict | 572 | in Ref. 2; AAF17217 and 8; M63483 | ||||
Sequence: Y → C | ||||||
Compositional bias | 588-647 | Basic and acidic residues | ||||
Sequence: KKDKSRKRSYSPDGKESPSDKKSKTDGSQKTESSTEGKEQEEKSGEDGEKDTKDDQTEQE | ||||||
Compositional bias | 648-664 | Acidic residues | ||||
Sequence: PNMLLESEDELLVDEEE | ||||||
Compositional bias | 690-735 | Basic and acidic residues | ||||
Sequence: DGKKEPSDKAVKKDGSASAAAKKKLKKVDKIEELDQENEAALENGI | ||||||
Sequence conflict | 691 | in Ref. 8; M63483 | ||||
Sequence: G → P | ||||||
Sequence conflict | 703 | in Ref. 8; M63483 | ||||
Sequence: D → H | ||||||
Compositional bias | 749-777 | Basic and acidic residues | ||||
Sequence: ENADDPNKDTSENADGQSDENKDDYTIPD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB018266 EMBL· GenBank· DDBJ | BAA34443.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF117236 EMBL· GenBank· DDBJ | AAF17217.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK316420 EMBL· GenBank· DDBJ | BAH14791.1 EMBL· GenBank· DDBJ | mRNA | ||
AC011404 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471062 EMBL· GenBank· DDBJ | EAW62114.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62115.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC015031 EMBL· GenBank· DDBJ | AAH15031.1 EMBL· GenBank· DDBJ | mRNA | ||
M63483 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |