| Tag | Content |
|---|
| CPLM ID | CPLM-014947 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Keratin, type I cytoskeletal 14 |
Protein Synonyms/Alias | Cytokeratin-14; CK-14; Keratin-14; K14; Type I keratin Ka14 |
Gene Name | Krt14 |
Gene Synonyms/Alias | Ka14; Krt1-14 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 174 | KDYSPYFKTIEDLKS | acetylation | [1] | | 370 | ENNLEETKGRYCMQL | acetylation | [1] | | 472 | VMDVHDGKVVSTHEQ | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro (By similarity). |
Sequence Annotation | REGION 1 121 Head.
REGION 122 429 Rod.
REGION 122 157 Coil 1A.
REGION 158 175 Linker 1.
REGION 176 267 Coil 1B.
REGION 268 290 Linker 12.
REGION 291 429 Coil 2.
REGION 430 485 Tail.
REGION 432 485 Interaction with Type I keratins and
DISULFID 374 374 Interchain (By similarity). |
Keyword | Coiled coil; Complete proteome; Cytoplasm; Disulfide bond; Intermediate filament; Keratin; Nucleus; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 485 AA |
Protein Sequence | MATCSRQFTS SSSMKGSCGI GGGSSRMSSV LAGGSCRAPS TYGGMSRFSS AGAYAVGSGY 60
GGGFSSSSFG GGFGGGIGGG IGGGLGGGIG GGFGGGIGGG FGGGIGSGFG GGLGDGLLVG 120
SEKVTMQNLN DRLATYLDKV RALEEANSDL EVKIRDWYQR QRPTEIKDYS PYFKTIEDLK 180
SKILAATVDN ANVLLQIDNA RLAADDFRTK FETEQSLRIN VESDINGLRR VLDELTLARA 240
DLEMQIESLK EELAYLKKNH EEEMASMRGQ VGGDVNVEMD AAPGVDLSRI LNEMRDQYEK 300
MAEKNRKDAE DWFFTKTEEL NREVATNSEL VQSGKSEISE LRRTMQNLEI ELQSQLSMKA 360
SLENNLEETK GRYCMQLAQI QEMIGSVEEQ LAQLRCEMEQ QNQEYKILLD VKTRLEQEIA 420
TYRRLLEGED AHLSSAQFSS SSQFSSGSQS SRDVTSTNRQ IRTKVMDVHD GKVVSTHEQV 480
LRTKN 485 |
Gene Ontology | GO:0071944; C:cell periphery; IEA:Compara. GO:0005737; C:cytoplasm; ISS:UniProtKB. GO:0045095; C:keratin filament; IDA:UniProtKB. GO:0005634; C:nucleus; ISS:UniProtKB. GO:0005198; F:structural molecule activity; IEA:InterPro. GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB. GO:0045110; P:intermediate filament bundle assembly; ISS:UniProtKB. GO:0010212; P:response to ionizing radiation; IEP:RGD. GO:0010043; P:response to zinc ion; IEP:RGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |