Gene Symbol | TTN |
Entrez ID | 7273 |
Uniprot ID | Q8WZ42 |
Description | titin |
Chromosomal Location | chr2: 178,525,989-178,830,802 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0002576 |
platelet degranulation |
The regulated exocytosis of secretory granules containing preformed mediators such as histamine and serotonin by a platelet. |
TAS |
BP |
GO:0003300 |
cardiac muscle hypertrophy |
The enlargement or overgrowth of all or part of the heart muscle due to an increase in size of cardiac muscle cells without cell division. |
IMP |
BP |
GO:0006936 |
muscle contraction |
A process in which force is generated within muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. |
NAS|TAS |
BP |
GO:0006941 |
striated muscle contraction |
A process in which force is generated within striated muscle tissue, resulting in the shortening of the muscle. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Striated muscle is a type of muscle in which the repeating units (sarcomeres) of the contractile myofibrils are arranged in registry throughout the cell, resulting in transverse or oblique striations observable at the level of the light microscope. |
TAS |
BP |
GO:0007076 |
mitotic chromosome condensation |
The cell cycle process in which chromatin structure is compacted prior to and during mitosis in eukaryotic cells. |
IEP |
BP |
GO:0018108 |
peptidyl-tyrosine phosphorylation |
The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine. |
IEA |
BP |
GO:0030049 |
muscle filament sliding |
The sliding of actin thin filaments and myosin thick filaments past each other in muscle contraction. This involves a process of interaction of myosin located on a thick filament with actin located on a thin filament. During this process ATP is split and forces are generated. |
TAS |
BP |
GO:0030240 |
skeletal muscle thin filament assembly |
The aggregation, arrangement and bonding together of proteins to form the actin-based thin filaments of myofibrils in skeletal muscle. |
IMP |
BP |
GO:0030241 |
skeletal muscle myosin thick filament assembly |
The aggregation, arrangement and bonding together of proteins to form the myosin-based thick filaments of myofibrils in skeletal muscle. |
IMP |
BP |
GO:0035995 |
detection of muscle stretch |
The series of events by which a muscle stretch stimulus is received by a cell and converted into a molecular signal. |
IDA|TAS |
BP |
GO:0045214 |
sarcomere organization |
The myofibril assembly process that results in the organization of muscle actomyosin into sarcomeres. The sarcomere is the repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs. |
IMP |
BP |
GO:0045859 |
regulation of protein kinase activity |
Any process that modulates the frequency, rate or extent of protein kinase activity. |
IMP |
BP |
GO:0048739 |
cardiac muscle fiber development |
The process whose specific outcome is the progression of cardiac muscle fiber over time, from its formation to the mature structure. |
IMP |
BP |
GO:0048769 |
sarcomerogenesis |
The process in which sarcomeres are added in series within a fiber. |
IMP |
BP |
GO:0050790 |
regulation of catalytic activity |
Any process that modulates the activity of an enzyme. |
IMP |
BP |
GO:0051592 |
response to calcium ion |
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a calcium ion stimulus. |
IDA |
BP |
GO:0055003 |
cardiac myofibril assembly |
The process whose specific outcome is the progression of the cardiac myofibril over time, from its formation to the mature structure. A cardiac myofibril is a myofibril specific to cardiac muscle cells. |
IMP |
BP |
GO:0055008 |
cardiac muscle tissue morphogenesis |
The process in which the anatomical structures of cardiac muscle tissue are generated and organized. |
IMP |
BP |
GO:0060048 |
cardiac muscle contraction |
Muscle contraction of cardiac muscle tissue. |
IMP |
CC |
GO:0000794 |
condensed nuclear chromosome |
A highly compacted molecule of DNA and associated proteins resulting in a cytologically distinct nuclear chromosome. |
IDA |
CC |
GO:0005576 |
extracellular region |
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
TAS |
CC |
GO:0005829 |
cytosol |
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
TAS |
CC |
GO:0005859 |
muscle myosin complex |
A filament of myosin found in a muscle cell of any type. |
IBA |
CC |
GO:0030018 |
Z disc |
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached. |
IDA |
CC |
GO:0031674 |
I band |
A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end. |
IDA |
CC |
GO:0070062 |
extracellular exosome |
A membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. |
IDA |
MF |
GO:0002020 |
protease binding |
Interacting selectively and non-covalently with any protease or peptidase. |
IPI |
MF |
GO:0004674 |
protein serine/threonine kinase activity |
Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
IDA |
MF |
GO:0004713 |
protein tyrosine kinase activity |
Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. |
IDA |
MF |
GO:0005509 |
calcium ion binding |
Interacting selectively and non-covalently with calcium ions (Ca2+). |
IDA |
MF |
GO:0005515 |
protein binding |
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). |
IPI |
MF |
GO:0005516 |
calmodulin binding |
Interacting selectively and non-covalently with calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
IPI|TAS |
MF |
GO:0005524 |
ATP binding |
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
IEA |
MF |
GO:0008307 |
structural constituent of muscle |
The action of a molecule that contributes to the structural integrity of a muscle fiber. |
IMP|TAS |
MF |
GO:0019899 |
enzyme binding |
Interacting selectively and non-covalently with any enzyme. |
IPI |
MF |
GO:0019901 |
protein kinase binding |
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
IPI |
MF |
GO:0031433 |
telethonin binding |
Interacting selectively and non-covalently with telethonin, a protein found in the Z disc of striated muscle and which is a substrate of the titin kinase. |
IPI|ISS |
MF |
GO:0042802 |
identical protein binding |
Interacting selectively and non-covalently with an identical protein or proteins. |
IPI |
MF |
GO:0042805 |
actinin binding |
Interacting selectively and non-covalently with actinin, any member of a family of proteins that crosslink F-actin. |
IDA|IPI |
MF |
GO:0043621 |
protein self-association |
Interacting selectively and non-covalently with a domain within the same polypeptide. |
IDA |
MF |
GO:0051015 |
actin filament binding |
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
IDA |
MF |
GO:0051371 |
muscle alpha-actinin binding |
Interacting selectively and non-covalently with muscle isoforms of actinin. Muscle alpha-actinin isoforms are found in skeletal and cardiac muscle and are localized to the Z-disc. |
IPI |
MF |
GO:0097493 |
structural molecule activity conferring elasticity |
The action of a molecule that contributes to the structural integrity of a complex or assembly within or outside a cell, providing elasticity and recoiling. |
TAS |
Domain ID | Description |
---|---|
IPR000719 |
Protein kinase domain |
IPR003598 |
Immunoglobulin subtype 2 |
IPR003599 |
Immunoglobulin subtype |
IPR003961 |
Fibronectin type III |
IPR004168 |
PPAK motif |
IPR007110 |
Immunoglobulin-like domain |
IPR008266 |
Tyrosine-protein kinase, active site |
IPR011009 |
Protein kinase-like domain |
IPR013098 |
Immunoglobulin I-set |
IPR013106 |
Immunoglobulin V-set domain |
IPR013783 |
Immunoglobulin-like fold |
IPR015129 |
Titin, Z repeat |
Pathway ID | Pathway Term | Pathway Source |
---|---|---|
hsa05410 |
Hypertrophic cardiomyopathy (HCM) |
KEGG |
hsa05414 |
Dilated cardiomyopathy |
KEGG |
WP383 |
Striated Muscle Contraction |
WikiPathways |
UMLS CUI | UMLS Term |
---|---|
C0007193 |
Cardiomyopathy, Dilated |
C0026848 |
Myopathy |
C0151786 |
Muscle Weakness |
C0751336 |
Distal Muscular Dystrophies |
C1838244 |
Tibial Muscular Dystrophy, Tardive |
Tissue | Cell Type |
---|---|
heart muscle |
myocytes |
skeletal muscle |
myocytes |
Pubmed ID | Author | Year | Title |
---|---|---|---|
23824412 |
Piltonen et al. |
2013 |
Mesenchymal Stem/Progenitors and Other Endometrial Cell Types From Women With Polycystic Ovary Syndrome (PCOS) Display Inflammatory and Oncogenic Potential |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
MYH9 |
4627 |
P35579 |
0.52 |
SQSTM1 |
8878 |
Q13501 |
0.52 |
ACTA1 |
58 |
P68133 |
0.63 |
ACTN3 |
89 |
Q08043 |
0.63 |
CCT6A |
908 |
P40227 |
0.63 |
ENO3 |
2027 |
P13929 |
0.63 |
FLNA |
2316 |
P21333 |
0.63 |
FN1 |
2335 |
P02751 |
0.63 |
HSPA1A |
3303 |
P0DMV8 |
0.63 |
HSPA1B |
3304 |
P0DMV9 |
0.63 |
ITGB5 |
3693 |
P18084 |
0.63 |
LIMS1 |
3987 |
P48059 |
0.63 |
EXOSC10 |
5394 |
Q01780 |
0.63 |
RYR1 |
6261 |
P21817 |
0.63 |
SGCG |
6445 |
Q13326 |
0.63 |
MAST2 |
23139 |
Q6P0Q8 |
0.63 |
ANKRD28 |
23243 |
O15084 |
0.63 |
POMP |
51371 |
Q9Y244 |
0.63 |
PARD3 |
56288 |
Q8TEW0 |
0.63 |
SH3RF1 |
57630 |
Q7Z6J0 |
0.63 |
CLIP4 |
79745 |
Q8N3C7 |
0.63 |
ABLIM2 |
84448 |
Q6H8Q1 |
0.63 |
NEK9 |
91754 |
Q8TD19 |
0.63 |
AMOT |
154796 |
Q4VCS5 |
0.63 |
C1QTNF9 |
338872 |
P0C862 |
0.63 |
CRYAB |
1410 |
P02511 |
0.65 |
SRPK2 |
6733 |
P78362 |
0.70 |
NBR1 |
4077 |
Q14596 |
0.74 |
ANK1 |
286 |
P16157 |
0.78 |
OBSL1 |
23363 |
O75147 |
0.79 |
FHL1 |
2273 |
Q13642 |
0.82 |
VAV2 |
7410 |
P52735 |
0.82 |
CALM2 |
805 |
P62158 |
0.83 |
CALM3 |
808 |
P62158 |
0.83 |
CAPN3 |
825 |
P20807 |
0.85 |
ACTN1 |
87 |
P12814 |
0.90 |
ACTN2 |
88 |
P35609 |
0.90 |
NEB |
4703 |
P20929 |
0.90 |
TTN |
7273 |
Q8WZ42 |
0.90 |
TCAP |
8557 |
O15273 |
0.90 |
ANXA7 |
310 |
P20073 |
0.49 |
EWSR1 |
2130 |
Q01844 |
0.49 |
SRSF2 |
6427 |
Q01130 |
0.49 |
CPSF6 |
11052 |
Q16630 |
0.49 |
SPEN |
23013 |
Q96T58 |
0.49 |
MAPK1 |
5594 |
P28482 |
0.52 |
ACTA2 |
59 |
P62736 |
0.55 |
SUN2 |
25777 |
Q9UH99 |
0.56 |
ACTN4 |
81 |
O43707 |
0.63 |
ADRB2 |
154 |
P07550 |
0.63 |
ATP5D |
513 |
P30049 |
0.63 |
CHD4 |
1108 |
Q14839 |
0.63 |
DFFA |
1676 |
O00273 |
0.63 |
ENO1 |
2023 |
P06733 |
0.63 |
ESR1 |
2099 |
P03372 |
0.63 |
ESR2 |
2100 |
Q92731 |
0.63 |
HSPB2 |
3316 |
Q16082 |
0.63 |
IGHG1 |
3500 |
P01857 |
0.63 |
ABLIM1 |
3983 |
O14639 |
0.63 |
MCM2 |
4171 |
P49736 |
0.63 |
MYBPC2 |
4606 |
Q14324 |
0.63 |
MYBPH |
4608 |
Q13203 |
0.63 |
MYC |
4609 |
P01106 |
0.63 |
NEO1 |
4756 |
Q92859 |
0.63 |
NTRK1 |
4914 |
P04629 |
0.63 |
PYGM |
5837 |
P11217 |
0.63 |
RNF2 |
6045 |
Q99496 |
0.63 |
RPL12 |
6136 |
P30050 |
0.63 |
RPS6KA1 |
6195 |
Q15418 |
0.63 |
SP1 |
6667 |
P08047 |
0.63 |
TTC3 |
7267 |
P53804 |
0.63 |
UBE2I |
7329 |
P63279 |
0.63 |
SUMO1 |
7341 |
P63165 |
0.63 |
UGP2 |
7360 |
Q16851 |
0.63 |
VDAC1 |
7416 |
P21796 |
0.63 |
YWHAZ |
7534 |
P63104 |
0.63 |
SF1 |
7536 |
Q15637 |
0.63 |
GAN |
8139 |
Q9H2C0 |
0.63 |
DYSF |
8291 |
O75923 |
0.63 |
CUL4B |
8450 |
Q13620 |
0.63 |
CUL3 |
8452 |
Q13618 |
0.63 |
CUL2 |
8453 |
Q13617 |
0.63 |
ASH2L |
9070 |
Q9UBL3 |
0.63 |
MED26 |
9441 |
O95402 |
0.63 |
RAPGEF2 |
9693 |
Q9Y4G8 |
0.63 |
CEP57 |
9702 |
Q86XR8 |
0.63 |
CUL7 |
9820 |
Q14999 |
0.63 |
DNAJB6 |
10049 |
O75190 |
0.63 |
OPTN |
10133 |
Q96CV9 |
0.63 |
MCRS1 |
10445 |
Q96EZ8 |
0.63 |
YWHAQ |
10971 |
P27348 |
0.63 |
COPS5 |
10987 |
Q92905 |
0.63 |
FSTL1 |
11167 |
Q12841 |
0.63 |
GABARAP |
11337 |
O95166 |
0.63 |
MYCBP2 |
23077 |
O75592 |
0.63 |
TAB2 |
23118 |
Q9NYJ8 |
0.63 |
DNAJB5 |
25822 |
O75953 |
0.63 |
RNF167 |
26001 |
Q9H6Y7 |
0.63 |
PHGDH |
26227 |
O43175 |
0.63 |
ITGB1BP2 |
26548 |
Q9UKP3 |
0.63 |
SH3GLB1 |
51100 |
Q9Y371 |
0.63 |
DDX56 |
54606 |
Q9NY93 |
0.63 |
MED29 |
55588 |
Q9NX70 |
0.63 |
JPH1 |
56704 |
Q9HDC5 |
0.63 |
FNDC3B |
64778 |
Q53EP0 |
0.63 |
MAP1LC3B |
81631 |
Q9GZQ8 |
0.63 |
MED10 |
84246 |
Q9BTT4 |
0.63 |
MYPN |
84665 |
Q86TC9 |
0.63 |
TRIM55 |
84675 |
Q9BYV6 |
0.63 |
MED19 |
219541 |
A0JLT2 |
0.63 |
PKM |
5315 |
P14618 |
0.68 |
SYNM |
23336 |
O15061 |
0.68 |
SMURF2 |
64750 |
Q9HAU4 |
0.70 |
ALB |
213 |
P02768 |
0.72 |
ARRB1 |
408 |
P49407 |
0.72 |
DYRK2 |
8445 |
Q92630 |
0.72 |
CDK2 |
1017 |
P24941 |
0.73 |
NEDD8 |
4738 |
Q15843 |
0.73 |
MYBPC1 |
4604 |
Q00872 |
0.75 |
MYBPC3 |
4607 |
Q14896 |
0.75 |
MYOM1 |
8736 |
P52179 |
0.75 |
MYOM2 |
9172 |
P54296 |
0.75 |
ANKRD2 |
26287 |
Q9GZV1 |
0.75 |
PUF60 |
22827 |
Q9UHX1 |
0.76 |
ASF1B |
55723 |
Q9NVP2 |
0.76 |
ANKRD23 |
200539 |
Q86SG2 |
0.78 |
FHL2 |
2274 |
Q14192 |
0.88 |
ANKRD1 |
27063 |
Q15327 |
0.88 |
OBSCN |
84033 |
Q5VST9 |
0.90 |
TRIM63 |
84676 |
Q969Q1 |
0.90 |