Q61781
Gene name |
Krt14 (Krt1-14) |
Protein name |
Keratin, type I cytoskeletal 14 |
Names |
Cytokeratin-14, CK-14, Keratin-14, K14 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:16664 |
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 Q61781
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q61781-F1 | Predicted | AlphaFoldDB |
24 variants for Q61781
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389211523 | 21 | G>D | No | EVA | |
| rs27088292 | 30 | I>V | No | EVA | |
| rs259755485 | 44 | G>S | No | EVA | |
| rs585163618 | 94 | G>A | No | EVA | |
| rs583000238 | 100 | F>L | No | EVA | |
| rs580428319 | 104 | L>F | No | EVA | |
| rs240520818 | 110 | G>S | No | EVA | |
| rs260947805 | 147 | T>S | No | EVA | |
| rs3389200225 | 164 | E>V | No | EVA | |
| rs3389211540 | 223 | D>A | No | EVA | |
| rs3389196313 | 229 | R>S | No | EVA | |
| rs3389136712 | 230 | V>M | No | EVA | |
| rs3389163838 | 233 | E>G | No | EVA | |
| rs3402297532 | 239 | A>V | No | EVA | |
| rs3389200230 | 247 | S>N | No | EVA | |
| rs3389189510 | 254 | Y>N | No | EVA | |
| rs3389196344 | 313 | F>I | No | EVA | |
| rs3389200247 | 327 | S>C | No | EVA | |
| rs3389163857 | 343 | T>S | No | EVA | |
| rs3389205490 | 375 | Q>P | No | EVA | |
| rs3389210549 | 388 | E>V | No | EVA | |
| rs3389211474 | 396 | E>K | No | EVA | |
| rs3389136713 | 430 | A>V | No | EVA | |
| rs3389200266 | 442 | Q>* | No | EVA |
No associated diseases with Q61781
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| basal part of cell | The region of a cell situated near the base. For example, in a polarized epithelial cell, the basal surface rests on the basal lamina that separates the epithelium from other tissue. |
| cell periphery | The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures. |
| cornified envelope | A type of plasma membrane that has been modified through addition of distinct intracellular and extracellular components, including ceramide, found in cornifying epithelial cells (corneocytes). |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
| intermediate filament | A cytoskeletal structure that forms a distinct elongated structure, characteristically 10 nm in diameter, that occurs in the cytoplasm of eukaryotic cells. Intermediate filaments form a fibrous system, composed of chemically heterogeneous subunits and involved in mechanically integrating the various components of the cytoplasmic space. Intermediate filaments may be divided into five chemically distinct classes: Type I, acidic keratins; Type II, basic keratins; Type III, including desmin, vimentin and others; Type IV, neurofilaments and related filaments; and Type V, lamins. |
| keratin filament | A filament composed of acidic and basic keratins (types I and II), typically expressed in epithelial cells. The keratins are the most diverse classes of IF proteins, with a large number of keratin isoforms being expressed. Each type of epithelium always expresses a characteristic combination of type I and type II keratins. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| keratin filament binding | Binding to a keratin filament, an intermediate filament composed of acidic and basic keratins (types I and II), typically expressed in epithelial cells. |
| structural molecule activity | The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| aging | A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700). |
| epithelial cell differentiation | The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium. |
| hair cycle | The cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair; one of the collection or mass of filaments growing from the skin of an animal, and forming a covering for a part of the head or for any part or the whole of the body. |
| intermediate filament bundle assembly | The formation of the bundles of intermediate filaments. Intermediate filament-associated proteins (IFAPs) cross-link intermediate filaments with one another, forming a bundle or a network, and with other cell structures, including the plasma membrane. The organization of intermediate filaments and their supportive function in various cells types depends in large part on their linkage to other cell structures via IFAPs. |
| intermediate filament organization | Control of the spatial distribution of intermediate filaments; includes organizing filaments into meshworks, bundles, or other structures, as by cross-linking. |
| keratinocyte differentiation | The process in which a relatively unspecialized cell acquires specialized features of a keratinocyte. |
| stem cell differentiation | The process in which a relatively unspecialized cell acquires specialized features of a stem cell. A stem cell is a cell that retains the ability to divide and proliferate throughout life to provide progenitor cells that can differentiate into specialized cells. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P02533 | KRT14 | Keratin, type I cytoskeletal 14 | Homo sapiens (Human) | PR |
| P19001 | Krt19 | Keratin, type I cytoskeletal 19 | Mus musculus (Mouse) | PR |
| Q9D312 | Krt20 | Keratin, type I cytoskeletal 20 | Mus musculus (Mouse) | PR |
| Q9QWL7 | Krt17 | Keratin, type I cytoskeletal 17 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATCSRQFTS | SSSMKGSCGI | GGGSSRMSSI | LAGGSCRAPS | TYGGMSVTSS | RFSSGGACGI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GGGYGGSFSS | SSFGGGLGSG | FGGRFDGFGG | GFGGGLGGGF | GGGLGGGLGG | GIGDGLLVGS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EKVTMQNLND | RLATYLDKVR | ALEEANTELE | VKIRDWYQRQ | RPTEIKDYSP | YFKTIEDLKS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KILAATVDNA | NVLLQIDNAR | LAADDFRTKF | ETEQSLRMSV | EADINGLRRV | LDELTLARAD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LEMQIESLKE | ELAYLKKNHE | EEMASMRGQV | GGDVNVEMDA | APGVDLSRIL | NEMRDQYEKM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AEKNRKDAEE | WFFSKTEELN | REVATNSELV | QSGKSEISEL | RRTMQNLEIE | LQSQLSMKAS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LENNLEETKG | RYCMQLAQIQ | EMIGSVEEQL | AQLRCEMEQQ | NQEYKILLDV | KTRLEQEIAT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YRRLLEGEDA | HLSSSQFSSS | SQFSSGSQSS | RDVTSTNRQI | RTKVMDVHDG | KVVSTHEQVL |
| RTKN |