Q6P6Q2 (K2C5_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 66.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Keratin, type II cytoskeletal 5 Alternative name(s): Cytokeratin-5 Short name=CK-5 Keratin-5 Short name=K5 Type-II keratin Kb5 | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 576 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Subunit structure | Heterotetramer of two type I and two type II keratins. Keratin-5 associates with keratin-14. Interacts with TCHP By similarity. UniProtKB P13647 |
| Tissue specificity | Expressed in the epidermis (at protein level) and testis (within pachytene spermatocytes). Ref.1 |
| Miscellaneous | There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa). |
| Sequence similarities | Belongs to the intermediate filament family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Intermediate filament Keratin |
| Domain | Coiled coil |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | keratin filament Inferred from direct assay Ref.1. Source: RGD |
| Molecular_function | structural molecule activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 576 | 576 | Keratin, type II cytoskeletal 5 | PRO_0000063729 | |||||
Regions | |||||||||
| Region | 1 – 163 | 163 | Head | ||||||
| Region | 164 – 473 | 310 | Rod | ||||||
| Region | 164 – 199 | 36 | Coil 1A | ||||||
| Region | 200 – 218 | 19 | Linker 1 | ||||||
| Region | 219 – 311 | 93 | Coil 1B | ||||||
| Region | 312 – 334 | 23 | Linker 12 | ||||||
| Region | 335 – 473 | 139 | Coil 2 | ||||||
| Region | 474 – 576 | 103 | Tail | ||||||
| Compositional bias | 39 – 135 | 97 | Gly-rich | ||||||
| Compositional bias | 532 – 576 | 45 | Ser-rich | ||||||
Sites | |||||||||
| Site | 413 | 1 | Stutter | ||||||
Amino acid modifications | |||||||||
| Modified residue | 21 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 60 | 1 | Phosphoserine By similarity UniProtKB P48668 | ||||||
| Modified residue | 71 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 114 | 1 | G → R in AAQ20893. Ref.1 | ||||||
| Sequence conflict | 473 | 1 | E → Q in AAQ20893. Ref.1 | ||||||
| Sequence conflict | 508 | 1 | S → F in AAQ20893. Ref.1 | ||||||
| Sequence conflict | 528 | 1 | R → L in AAQ20893. Ref.1 | ||||||
| Sequence conflict | 562 | 1 | K → Q in AAQ20893. Ref.1 | ||||||
| Sequence conflict | 575 | 1 | K → N in AAQ20893. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Acroplaxome, an F-actin-keratin-containing plate, anchors the acrosome to the nucleus during shaping of the spermatid head." Kierszenbaum A.L., Rivkin E., Tres L.L. Mol. Biol. Cell 14:4628-4640(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: Sprague-Dawley. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY342389 mRNA. Translation: AAQ20893.1. BC062086 mRNA. Translation: AAH62086.1. |
| IPI | IPI00382153. |
| RefSeq | NP_899162.1. NM_183333.1. |
| UniGene | Rn.129725. Rn.195318. |
3D structure databases | |
| ProteinModelPortal | Q6P6Q2. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q6P6Q2. |
Proteomic databases | |
| PRIDE | Q6P6Q2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 369017. |
| KEGG | rno:369017. |
Organism-specific databases | |
| CTD | 3852. |
| RGD | 727894. Krt5. |
Phylogenomic databases | |
| HOVERGEN | HBG013015. |
| KO | K07605. |
Gene expression databases | |
| Genevestigator | Q6P6Q2. |
Family and domain databases | |
| InterPro | IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR003054. Keratin_II. [Graphical view] |
| PANTHER | PTHR23239. PTHR23239. 1 hit. PTHR23239:SF18. PTHR23239:SF18. 1 hit. |
| Pfam | PF00038. Filament. 1 hit. [Graphical view] |
| PRINTS | PR01276. TYPE2KERATIN. |
| PROSITE | PS00226. IF. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 692068. |
Entry information
| Entry name | K2C5_RAT | ||||||||
| Accession | Primary (citable) accession number: Q6P6Q2 Secondary accession number(s): Q7TN97 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
