P42932
PR
Gene name |
Cct8 (Cctq) |
Protein name |
T-complex protein 1 subunit theta |
Names |
TCP-1-theta, CCT-theta |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:12469 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P42932
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P42932-F1 | Predicted | AlphaFoldDB |
26 variants for P42932
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389424337 | 30 | Y>H | No | EVA | |
| rs1131782622 | 34 | Q>R | No | EVA | |
| rs3389423363 | 57 | I>N | No | EVA | |
| rs3389440440 | 58 | N>I | No | EVA | |
| rs230506727 | 108 | A>T | No | EVA | |
| rs3389413844 | 133 | E>* | No | EVA | |
| rs3389426993 | 141 | E>D | No | EVA | |
| rs3412994290 | 151 | A>V | No | EVA | |
| rs242741581 | 153 | N>S | No | EVA | |
| rs222603091 | 161 | S>T | No | EVA | |
| rs3389440441 | 182 | L>F | No | EVA | |
| rs3389430186 | 238 | K>* | No | EVA | |
| rs3389421978 | 264 | E>K | No | EVA | |
| rs223427272 | 300 | I>M | No | EVA | |
| rs3389393009 | 318 | K>* | No | EVA | |
| rs3389430165 | 323 | R>L | No | EVA | |
| rs3389413814 | 401 | V>G | No | EVA | |
| rs3389392968 | 405 | D>G | No | EVA | |
| rs233086257 | 426 | Y>F | No | EVA | |
| rs3389426214 | 430 | C>* | No | EVA | |
| rs3389426257 | 431 | P>S | No | EVA | |
| rs13473680 | 456 | S>F | No | EVA | |
| rs3389426240 | 459 | K>SDG* | No | EVA | |
| rs3389421947 | 462 | E>* | No | EVA | |
| rs3389421949 | 488 | A>D | No | EVA | |
| rs3389417707 | 546 | Q>H | No | EVA |
No associated diseases with P42932
3 regional properties for P42932
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Chaperonin TCP-1, conserved site | 44 - 56 | IPR002194-1 |
| conserved_site | Chaperonin TCP-1, conserved site | 65 - 81 | IPR002194-2 |
| conserved_site | Chaperonin TCP-1, conserved site | 93 - 101 | IPR002194-3 |
10 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell body | The portion of a cell bearing surface projections such as axons, dendrites, cilia, or flagella that includes the nucleus, but excludes all cell projections. |
| centrosome | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. |
| chaperonin-containing T-complex | A multisubunit ring-shaped complex that mediates protein folding in the cytosol without a cofactor. |
| cilium | A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| intermediate filament cytoskeleton | Cytoskeletal structure made from intermediate filaments, typically organized in the cytosol as an extended system that stretches from the nuclear envelope to the plasma membrane. Some intermediate filaments run parallel to the cell surface, while others traverse the cytosol; together they form an internal framework that helps support the shape and resilience of the cell. |
| microtubule | Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| zona pellucida receptor complex | A multisubunit complex comprising the chaperonin-containing T-complex and several other components involved in mediating sperm-oocyte Interaction. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process. |
| unfolded protein binding | Binding to an unfolded protein. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| binding of sperm to zona pellucida | The process in which the sperm binds to the zona pellucida glycoprotein layer of the egg. The process begins with the attachment of the sperm plasma membrane to the zona pellucida and includes attachment of the acrosome inner membrane to the zona pellucida after the acrosomal reaction takes place. |
| chaperone-mediated protein folding | The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone. |
| pore complex assembly | The aggregation, arrangement and bonding together of a set of components to form a pore complex. A pore complex is a small opening in a membrane that allows the passage of liquids and/or gases. |
| positive regulation of establishment of protein localization to telomere | Any process that activates or increases the frequency, rate or extent of establishment of protein localization to telomere. |
| positive regulation of telomere maintenance via telomerase | Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase. |
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| protein stabilization | Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation. |
| toxin transport | The directed movement of a toxin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALHVPKAPG | FAQMLKDGAK | HFSGLEEAVY | RNIQACKELA | QTTRTAYGPN | GMNKMVINRL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EKLFVTNDAA | TILRELEVQH | PAAKMIVMAS | HMQEQEVGDG | TNFVLVFAGA | LLELAEELLR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IGLSVSEVIS | GYEIACKKAH | EILPELVCCS | AKNLRDVDEV | SSLLRTSIMS | KQYGSETFLA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KLIAQACVSI | FPDSGNFNVD | NIRVCKILGS | GIYSSSVLHG | MVFKKETEGD | VTSVKDAKIA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VYSCPFDGMI | TETKGTVLIK | TAEELMNFSK | GEENLMDAQV | KAIAGTGANV | IVTGGKVADI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ALHYANKYNI | MLVRLNSKWD | LRRLCKTVGA | TALPKLTPPV | QEEMGHCDSV | YLSEVGDTQV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VVFKHEKEDG | AISTIVLRGS | TDNLMDDIER | AVDDGVNTFK | VLTRDKRLVP | GGGATEIELA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KQITSYGETC | PGLEQYAIKK | FAEAFEAIPR | ALAENSGVKA | NEVISKLYSV | HQEGNKNVGL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DIEAEVPAVK | DMLEASILDT | YLGKYWAIKL | ATNAAVTVLR | VDQIIMAKPA | GGPKPPSGKK |
| DWDDDQND |