Q13061 · TRDN_HUMAN
- ProteinTriadin
- GeneTRDN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids729 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for normal skeletal muscle strength. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats
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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Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTriadin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13061
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-47 | Cytoplasmic | ||||
Sequence: MTEITAEGNASTTTTVIDSKNGSVPKSPGKVLKRTVTEDIVTTFSSP | ||||||
Transmembrane | 48-68 | Helical | ||||
Sequence: AAWLLVIALIITWSAVAIVMF | ||||||
Topological domain | 69-729 | Lumenal | ||||
Sequence: DLVDYKNFSASSIAKIGSDPLKLVRDAMEETTDWIYGFFSLLSDIISSEDEEDDDGDEDTDKGEIDEPPLRKKEIHKDKTEKQEKPERKIQTKVTHKEKEKGKEKVREKEKPEKKATHKEKIEKKEKPETKTLAKEQKKAKTAEKSEEKTKKEVKGGKQEKVKQTAAKVKEVQKTPSKPKEKEDKEKAAVSKHEQKDQYAFCRYMIDIFVHGDLKPGQSPAIPPPLPTEQASRPTPASPALEEKEGEKKKAEKKVTSETKKKEKEDIKKKSEKETAIDVEKKEPGKASETKQGTVKIAAQAAAKKDEKKEDSKKTKKPAEVEQPKGKKQEKKEKHVEPAKSPKKEHSVPSDKQVKAKTERAKEEIGAVSIKKAVPGKKEEKTTKTVEQEIRKEKSGKTSSILKDKEPIKGKEEKVPASLKEKEPETKKDEKMSKAGKEVKPKPPQLQGKKEEKPEPQIKKEAKPAISEKVQIHKQDIVKPEKTVSHGKPEEKVLKQVKAVTIEKTAKPKPTKKAEHREREPPSIKTDKPKPTPKGTSEVTESGKKKTEISEKESKEKADMKHLREEKVSTRKESLQLHNVTKAEKPARVSKDVEDVPASKKAKEGTEDVSPTKQKSPISFFQCVYLDGYNGYGFQFPFTPADRPGESSGQANSPGQKQQGQ |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cardiac arrhythmia syndrome, with or without skeletal muscle weakness (CARDAR)
- Note
- DescriptionAn autosomal recessive cardiac disorder characterized by stress-induced arrhythmias in infancy or early childhood. Patients present with recurrent syncope or cardiac arrest after physical activity or emotional stress. Sudden death may occur in early childhood. Some patients have muscle weakness.
- See alsoMIM:615441
Natural variants in CARDAR
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067350 | 59 | T>R | in CARDAR; results in intracellular retention and degradation of the mutant protein; dbSNP:rs397515459 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_067350 | 59 | in CARDAR; results in intracellular retention and degradation of the mutant protein; dbSNP:rs397515459 | |||
Sequence: T → R | ||||||
Natural variant | VAR_057008 | 128 | in dbSNP:rs9490809 | |||
Sequence: T → S | ||||||
Natural variant | VAR_065263 | 201 | in dbSNP:rs6902416 | |||
Sequence: L → V | ||||||
Natural variant | VAR_057009 | 339 | in dbSNP:rs35766971 | |||
Sequence: S → N | ||||||
Natural variant | VAR_065264 | 396 | in dbSNP:rs6901953 | |||
Sequence: K → N | ||||||
Natural variant | VAR_057010 | 404 | in dbSNP:rs28494009 | |||
Sequence: V → G | ||||||
Natural variant | VAR_057011 | 419 | in dbSNP:rs17737379 | |||
Sequence: D → E | ||||||
Natural variant | VAR_065265 | 438 | in dbSNP:rs2873479 | |||
Sequence: I → S | ||||||
Natural variant | VAR_057012 | 470 | in dbSNP:rs6569336 | |||
Sequence: L → M | ||||||
Natural variant | VAR_057013 | 540 | in dbSNP:rs7771303 | |||
Sequence: I → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,056 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 chain, glycosylation, disulfide bond, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000065626 | 1-729 | UniProt | Triadin | |||
Sequence: MTEITAEGNASTTTTVIDSKNGSVPKSPGKVLKRTVTEDIVTTFSSPAAWLLVIALIITWSAVAIVMFDLVDYKNFSASSIAKIGSDPLKLVRDAMEETTDWIYGFFSLLSDIISSEDEEDDDGDEDTDKGEIDEPPLRKKEIHKDKTEKQEKPERKIQTKVTHKEKEKGKEKVREKEKPEKKATHKEKIEKKEKPETKTLAKEQKKAKTAEKSEEKTKKEVKGGKQEKVKQTAAKVKEVQKTPSKPKEKEDKEKAAVSKHEQKDQYAFCRYMIDIFVHGDLKPGQSPAIPPPLPTEQASRPTPASPALEEKEGEKKKAEKKVTSETKKKEKEDIKKKSEKETAIDVEKKEPGKASETKQGTVKIAAQAAAKKDEKKEDSKKTKKPAEVEQPKGKKQEKKEKHVEPAKSPKKEHSVPSDKQVKAKTERAKEEIGAVSIKKAVPGKKEEKTTKTVEQEIRKEKSGKTSSILKDKEPIKGKEEKVPASLKEKEPETKKDEKMSKAGKEVKPKPPQLQGKKEEKPEPQIKKEAKPAISEKVQIHKQDIVKPEKTVSHGKPEEKVLKQVKAVTIEKTAKPKPTKKAEHREREPPSIKTDKPKPTPKGTSEVTESGKKKTEISEKESKEKADMKHLREEKVSTRKESLQLHNVTKAEKPARVSKDVEDVPASKKAKEGTEDVSPTKQKSPISFFQCVYLDGYNGYGFQFPFTPADRPGESSGQANSPGQKQQGQ | |||||||
Glycosylation | 75 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 270 | UniProt | Interchain | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 415 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 642 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 647 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 678 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 691 | UniProt | Interchain | ||||
Sequence: C |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with CASQ1 and RYR1 in skeletal muscle. Interacts with CASQ2
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q13061-2 | KCNE4 Q8WWG9 | 3 | EBI-17257686, EBI-11750916 | |
BINARY | Q13061-2 | PPIB P23284 | 3 | EBI-17257686, EBI-359252 | |
BINARY | Q13061-2 | PTPRN Q16849-3 | 3 | EBI-17257686, EBI-10200782 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MTEITAEGNASTTTTVIDSKNG | ||||||
Region | 1-28 | Disordered | ||||
Sequence: MTEITAEGNASTTTTVIDSKNGSVPKSP | ||||||
Compositional bias | 117-131 | Acidic residues | ||||
Sequence: EDEEDDDGDEDTDKG | ||||||
Region | 117-265 | Disordered | ||||
Sequence: EDEEDDDGDEDTDKGEIDEPPLRKKEIHKDKTEKQEKPERKIQTKVTHKEKEKGKEKVREKEKPEKKATHKEKIEKKEKPETKTLAKEQKKAKTAEKSEEKTKKEVKGGKQEKVKQTAAKVKEVQKTPSKPKEKEDKEKAAVSKHEQKD | ||||||
Compositional bias | 132-265 | Basic and acidic residues | ||||
Sequence: EIDEPPLRKKEIHKDKTEKQEKPERKIQTKVTHKEKEKGKEKVREKEKPEKKATHKEKIEKKEKPETKTLAKEQKKAKTAEKSEEKTKKEVKGGKQEKVKQTAAKVKEVQKTPSKPKEKEDKEKAAVSKHEQKD | ||||||
Region | 281-682 | Disordered | ||||
Sequence: DLKPGQSPAIPPPLPTEQASRPTPASPALEEKEGEKKKAEKKVTSETKKKEKEDIKKKSEKETAIDVEKKEPGKASETKQGTVKIAAQAAAKKDEKKEDSKKTKKPAEVEQPKGKKQEKKEKHVEPAKSPKKEHSVPSDKQVKAKTERAKEEIGAVSIKKAVPGKKEEKTTKTVEQEIRKEKSGKTSSILKDKEPIKGKEEKVPASLKEKEPETKKDEKMSKAGKEVKPKPPQLQGKKEEKPEPQIKKEAKPAISEKVQIHKQDIVKPEKTVSHGKPEEKVLKQVKAVTIEKTAKPKPTKKAEHREREPPSIKTDKPKPTPKGTSEVTESGKKKTEISEKESKEKADMKHLREEKVSTRKESLQLHNVTKAEKPARVSKDVEDVPASKKAKEGTEDVSPTKQ | ||||||
Compositional bias | 286-300 | Pro residues | ||||
Sequence: QSPAIPPPLPTEQAS | ||||||
Compositional bias | 308-357 | Basic and acidic residues | ||||
Sequence: ALEEKEGEKKKAEKKVTSETKKKEKEDIKKKSEKETAIDVEKKEPGKASE | ||||||
Compositional bias | 369-566 | Basic and acidic residues | ||||
Sequence: AAAKKDEKKEDSKKTKKPAEVEQPKGKKQEKKEKHVEPAKSPKKEHSVPSDKQVKAKTERAKEEIGAVSIKKAVPGKKEEKTTKTVEQEIRKEKSGKTSSILKDKEPIKGKEEKVPASLKEKEPETKKDEKMSKAGKEVKPKPPQLQGKKEEKPEPQIKKEAKPAISEKVQIHKQDIVKPEKTVSHGKPEEKVLKQVK | ||||||
Compositional bias | 573-678 | Basic and acidic residues | ||||
Sequence: TAKPKPTKKAEHREREPPSIKTDKPKPTPKGTSEVTESGKKKTEISEKESKEKADMKHLREEKVSTRKESLQLHNVTKAEKPARVSKDVEDVPASKKAKEGTEDVS | ||||||
Region | 705-729 | Disordered | ||||
Sequence: PFTPADRPGESSGQANSPGQKQQGQ | ||||||
Compositional bias | 713-729 | Polar residues | ||||
Sequence: GESSGQANSPGQKQQGQ |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q13061-1
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
- Length729
- Mass (Da)81,595
- Last updated2011-06-28 v4
- Checksum0D9653203D52FA05
Q13061-2
- Name2
Q13061-3
- Name3
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H9ME53 | H9ME53_HUMAN | TRDN | 286 | ||
A0AAQ5BHC7 | A0AAQ5BHC7_HUMAN | TRDN | 97 | ||
A0AAQ5BHD4 | A0AAQ5BHD4_HUMAN | TRDN | 143 | ||
A0AAQ5BHB9 | A0AAQ5BHB9_HUMAN | TRDN | 202 | ||
A0AAQ5BH94 | A0AAQ5BH94_HUMAN | TRDN | 183 | ||
A0AAQ5BH97 | A0AAQ5BH97_HUMAN | TRDN | 176 | ||
H0Y6P0 | H0Y6P0_HUMAN | TRDN | 119 | ||
A0A590UJV0 | A0A590UJV0_HUMAN | TRDN | 461 | ||
H7BY47 | H7BY47_HUMAN | TRDN | 246 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MTEITAEGNASTTTTVIDSKNG | ||||||
Compositional bias | 117-131 | Acidic residues | ||||
Sequence: EDEEDDDGDEDTDKG | ||||||
Compositional bias | 132-265 | Basic and acidic residues | ||||
Sequence: EIDEPPLRKKEIHKDKTEKQEKPERKIQTKVTHKEKEKGKEKVREKEKPEKKATHKEKIEKKEKPETKTLAKEQKKAKTAEKSEEKTKKEVKGGKQEKVKQTAAKVKEVQKTPSKPKEKEDKEKAAVSKHEQKD | ||||||
Alternative sequence | VSP_045561 | 162-167 | in isoform 3 | |||
Sequence: VTHKEK → EVGHSS | ||||||
Alternative sequence | VSP_045562 | 168-729 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_045563 | 265-284 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 286-300 | Pro residues | ||||
Sequence: QSPAIPPPLPTEQAS | ||||||
Compositional bias | 308-357 | Basic and acidic residues | ||||
Sequence: ALEEKEGEKKKAEKKVTSETKKKEKEDIKKKSEKETAIDVEKKEPGKASE | ||||||
Alternative sequence | VSP_045564 | 311-317 | in isoform 2 | |||
Sequence: EKEGEKK → GKYFFFS | ||||||
Alternative sequence | VSP_045565 | 318-729 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 369-566 | Basic and acidic residues | ||||
Sequence: AAAKKDEKKEDSKKTKKPAEVEQPKGKKQEKKEKHVEPAKSPKKEHSVPSDKQVKAKTERAKEEIGAVSIKKAVPGKKEEKTTKTVEQEIRKEKSGKTSSILKDKEPIKGKEEKVPASLKEKEPETKKDEKMSKAGKEVKPKPPQLQGKKEEKPEPQIKKEAKPAISEKVQIHKQDIVKPEKTVSHGKPEEKVLKQVK | ||||||
Compositional bias | 573-678 | Basic and acidic residues | ||||
Sequence: TAKPKPTKKAEHREREPPSIKTDKPKPTPKGTSEVTESGKKKTEISEKESKEKADMKHLREEKVSTRKESLQLHNVTKAEKPARVSKDVEDVPASKKAKEGTEDVS | ||||||
Compositional bias | 713-729 | Polar residues | ||||
Sequence: GESSGQANSPGQKQQGQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U18985 EMBL· GenBank· DDBJ | AAA75315.1 EMBL· GenBank· DDBJ | mRNA | ||
AL133257 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL357352 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL445259 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL603902 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL603911 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC070290 EMBL· GenBank· DDBJ | AAH70290.1 EMBL· GenBank· DDBJ | mRNA | ||
BC139910 EMBL· GenBank· DDBJ | AAI39911.1 EMBL· GenBank· DDBJ | mRNA |