
titin
Sign in to saveAlso known as rhabdomyosarcoma antigen MU-RMS-40.14, connectin, Ttn, TTN
<!-- DO NOT ADD THE FULL CHEMICAL NAME OF TITIN INTO THIS ARTICLE.
OverviewAI-generated
Titin is a protein encoded by the TTN gene in Homo sapiens. It has a length of 34350 and a mass of 3816030. The protein is associated with keywords including 3D-structure, Alternative splicing, ATP-binding, Calcium, and Calmodulin-binding. Its existence is supported by evidence at the protein level, and it is classified under the EC enzyme number 2.7.11.1.
The chemical formula for titin is listed as C₁₆₉₇₂₃H₂₇₀₄₆₄N₄₅₆₈₈O₅₂₂₄₃S₉₁1123fr. In scientific literature, there are 4057 PubMed records and 4 ClinicalTrials.gov entries associated with the query "titin". The subject is referenced by 727 other encyclopedia articles.
Synthesized by Vinony from 17 facts across 5 sources: Wikidata, PubMed, ClinicalTrials.gov, UniProt, Vinony graph. Generated from structured data (not the Wikipedia text) and checked against those facts — may still contain errors.
Key facts
- Protein family.Pfam
- PF06582
- Protein family.Name
- Titin repeat
- Protein family.Symbol
- Titin_Ig-rpts
- Protein family.InterPro
- IPR010939
via Wikipedia infobox
Protein · UniProt
Titin
- Gene
- TTN
- Organism
- Homo sapiens (Human)
- Length
- 34,350 aa
- Molecular mass
- 3,816,030 Da
- Evidence
- 1: Evidence at protein level
Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase
Swiss-Prot (reviewed) · via UniProt
Research
4,057 papers- Titin (TTN): from molecule to modifications, mechanics, and medical significance.Cardiovascular research · 2022
- Discovery of Titin and Its Role in Heart Function and Disease.Circulation research · 2025
- Titin N2A Domain and Its Interactions at the Sarcomere.International journal of molecular sciences · 2021
- The giant titin: how to evaluate its role in cardiomyopathies.Journal of muscle research and cell motility · 2019
- Titin fragment in urine: A noninvasive biomarker of muscle degradation.Advances in clinical chemistry · 2019
via PubMed
Clinical Trials
4 registered- ENROLLING_BY_INVITATIONThe Validity of Urinary Titin and Skeletal Muscle Index as Predictor of Muscle Weakness in Critically Ill Patients. A Prospective Cohort StudyZagazig University · NCT06487728
- PHASE2TERMINATEDExploratory Study of Danicamtiv in Patients With Primary Dilated Cardiomyopathy (DCM) Due to Genetic Variants or Other CausalitiesBristol-Myers Squibb · NCT04572893
- RECRUITINGCongenital Muscle Disease Study of Patient and Family Reported Medical InformationCure CMD · NCT01403402
- NARECRUITINGUrinary Titin Biomarker in DMDChildren's Hospital of Philadelphia · NCT07332013
Wikidata facts
Show 4 more facts
- chemical formula
- C₁₆₉₇₂₃H₂₇₀₄₆₄N₄₅₆₈₈O₅₂₂₄₃S₉₁1123fr
- EC enzyme number
- 2.7.11.1
- found in taxon
- Homo sapiens
- Commons category
- Titin
via Wikidata · CC0
~13 min read
Encyclopedic overview
13 sectionsContents
- Discovery
- Genetics
- Isoforms
- Structure
- Evolution
- Function
- Clinical relevance
- Interactions
- Linguistic significance
- See also
- References
- Further reading
- External links
thumb|Cardiac#Microanatomy|Cardiac sarcomere structure, featuring titin thumb|Reconstruction of the thin (green) and thick filament from mammalian cardiac tissue. Myosin is in blue, MyBP-C is in yellow, and titin is in two shades of red (dark red for titin-alpha and light red for titin-beta).
Titin (; also called connectin) is a protein that in humans is encoded by the TTN gene. The protein, which is over 1 μm in length, functions as a molecular spring that is responsible for the passive elasticity of muscle. It comprises 244 individually folded protein domains connected by unstructured peptide sequences. These domains unfold when the protein is stretched and refold when the tension is removed.
Excerpted from Wikipedia’s “titin” article, available under the CC BY-SA 4.0 licence.