P46525 · CS120_WHEAT
- ProteinCold-shock protein CS120
- GeneCS120
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids391 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
May reduce intracellular freezing damage during winter by hydrogen-bonding to the lattice of the nascent ice crystals, thus modifying the structure and/or propagation of ice crystals.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Biological Process | cold acclimation | |
Biological Process | response to abscisic acid | |
Biological Process | response to water deprivation |
Names & Taxonomy
Protein names
- Recommended nameCold-shock protein CS120
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Pooideae > Triticodae > Triticeae > Triticinae > Triticum
Accessions
- Primary accessionP46525
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000100063 | 1-391 | Cold-shock protein CS120 | |||
Sequence: MENQAHIAGEKKGIMEKIKEKLPGGHGDHKETAGTHGHPGTATHGAPATGGAYGQQGHAGTTGTGLHGAHAGEKKGVMENIKDKLPGGHQDHQQTGGTYGQQGHTGTATHGTPATGGTYGQQGHTGTATHGTPATGGTYGEQGHTGVTGTGTHGTGEKKGVMENIKEKLPGGHGDHQQTGGTYGQQGHTGTATHGTPAGGGTYEQHGHTGMTGTGTHGTGEKKGVMENIKDKLPGGHGDHQQTGGTYGQQGHTGTATQGTPAGGGTYEQHGHTGMTGAGTHSTGEKKGVMENIKEKLPGGHSDHQQTGGAYGQQGHTGTATHGTPAGGGTYGQHGHAGVIGTETHGTTATGGTHGQHGHTGTTGTGTHGSDGIGEKKSLMDKIKDKLPGQH |
Proteomic databases
Expression
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 9-31 | 1-1 | ||||
Sequence: GEKKGIMEKIKEKLPGGHGDHKE | ||||||
Region | 9-391 | 6 X 23 AA approximate repeats | ||||
Sequence: GEKKGIMEKIKEKLPGGHGDHKETAGTHGHPGTATHGAPATGGAYGQQGHAGTTGTGLHGAHAGEKKGVMENIKDKLPGGHQDHQQTGGTYGQQGHTGTATHGTPATGGTYGQQGHTGTATHGTPATGGTYGEQGHTGVTGTGTHGTGEKKGVMENIKEKLPGGHGDHQQTGGTYGQQGHTGTATHGTPAGGGTYEQHGHTGMTGTGTHGTGEKKGVMENIKDKLPGGHGDHQQTGGTYGQQGHTGTATQGTPAGGGTYEQHGHTGMTGAGTHSTGEKKGVMENIKEKLPGGHSDHQQTGGAYGQQGHTGTATHGTPAGGGTYGQHGHAGVIGTETHGTTATGGTHGQHGHTGTTGTGTHGSDGIGEKKSLMDKIKDKLPGQH | ||||||
Compositional bias | 21-35 | Basic and acidic residues | ||||
Sequence: KLPGGHGDHKETAGT | ||||||
Region | 21-391 | Disordered | ||||
Sequence: KLPGGHGDHKETAGTHGHPGTATHGAPATGGAYGQQGHAGTTGTGLHGAHAGEKKGVMENIKDKLPGGHQDHQQTGGTYGQQGHTGTATHGTPATGGTYGQQGHTGTATHGTPATGGTYGEQGHTGVTGTGTHGTGEKKGVMENIKEKLPGGHGDHQQTGGTYGQQGHTGTATHGTPAGGGTYEQHGHTGMTGTGTHGTGEKKGVMENIKDKLPGGHGDHQQTGGTYGQQGHTGTATQGTPAGGGTYEQHGHTGMTGAGTHSTGEKKGVMENIKEKLPGGHSDHQQTGGAYGQQGHTGTATHGTPAGGGTYGQHGHAGVIGTETHGTTATGGTHGQHGHTGTTGTGTHGSDGIGEKKSLMDKIKDKLPGQH | ||||||
Repeat | 49-62 | 2-1 | ||||
Sequence: TGGAYGQQGHAGTT | ||||||
Region | 49-363 | 11 X 14 AA approximate repeats | ||||
Sequence: TGGAYGQQGHAGTTGTGLHGAHAGEKKGVMENIKDKLPGGHQDHQQTGGTYGQQGHTGTATHGTPATGGTYGQQGHTGTATHGTPATGGTYGEQGHTGVTGTGTHGTGEKKGVMENIKEKLPGGHGDHQQTGGTYGQQGHTGTATHGTPAGGGTYEQHGHTGMTGTGTHGTGEKKGVMENIKDKLPGGHGDHQQTGGTYGQQGHTGTATQGTPAGGGTYEQHGHTGMTGAGTHSTGEKKGVMENIKEKLPGGHSDHQQTGGAYGQQGHTGTATHGTPAGGGTYGQHGHAGVIGTETHGTTATGGTHGQHGHTGTT | ||||||
Compositional bias | 72-89 | Basic and acidic residues | ||||
Sequence: GEKKGVMENIKDKLPGGH | ||||||
Repeat | 72-94 | 1-2 | ||||
Sequence: GEKKGVMENIKDKLPGGHQDHQQ | ||||||
Compositional bias | 91-152 | Polar residues | ||||
Sequence: DHQQTGGTYGQQGHTGTATHGTPATGGTYGQQGHTGTATHGTPATGGTYGEQGHTGVTGTGT | ||||||
Repeat | 95-108 | 2-2 | ||||
Sequence: TGGTYGQQGHTGTA | ||||||
Repeat | 115-128 | 2-3 | ||||
Sequence: TGGTYGQQGHTGTA | ||||||
Repeat | 135-148 | 2-4 | ||||
Sequence: TGGTYGEQGHTGVT | ||||||
Repeat | 156-178 | 1-3 | ||||
Sequence: GEKKGVMENIKEKLPGGHGDHQQ | ||||||
Compositional bias | 159-173 | Basic and acidic residues | ||||
Sequence: KGVMENIKEKLPGGH | ||||||
Compositional bias | 178-198 | Polar residues | ||||
Sequence: QTGGTYGQQGHTGTATHGTPA | ||||||
Repeat | 179-192 | 2-5 | ||||
Sequence: TGGTYGQQGHTGTA | ||||||
Repeat | 199-212 | 2-6 | ||||
Sequence: GGGTYEQHGHTGMT | ||||||
Repeat | 220-242 | 1-4 | ||||
Sequence: GEKKGVMENIKDKLPGGHGDHQQ | ||||||
Compositional bias | 223-237 | Basic and acidic residues | ||||
Sequence: KGVMENIKDKLPGGH | ||||||
Compositional bias | 242-264 | Polar residues | ||||
Sequence: QTGGTYGQQGHTGTATQGTPAGG | ||||||
Repeat | 243-256 | 2-7 | ||||
Sequence: TGGTYGQQGHTGTA | ||||||
Repeat | 263-276 | 2-8 | ||||
Sequence: GGGTYEQHGHTGMT | ||||||
Repeat | 284-306 | 1-5 | ||||
Sequence: GEKKGVMENIKEKLPGGHSDHQQ | ||||||
Compositional bias | 287-301 | Basic and acidic residues | ||||
Sequence: KGVMENIKEKLPGGH | ||||||
Compositional bias | 306-326 | Polar residues | ||||
Sequence: QTGGAYGQQGHTGTATHGTPA | ||||||
Repeat | 307-320 | 2-9 | ||||
Sequence: TGGAYGQQGHTGTA | ||||||
Repeat | 327-340 | 2-10 | ||||
Sequence: GGGTYGQHGHAGVI | ||||||
Compositional bias | 343-369 | Polar residues | ||||
Sequence: ETHGTTATGGTHGQHGHTGTTGTGTHG | ||||||
Repeat | 350-363 | 2-11 | ||||
Sequence: TGGTHGQHGHTGTT | ||||||
Repeat | 374-391 | 1-6 | ||||
Sequence: GEKKSLMDKIKDKLPGQH | ||||||
Compositional bias | 374-391 | Basic and acidic residues | ||||
Sequence: GEKKSLMDKIKDKLPGQH |
Domain
Contains 6 A-type repeats and 11 B-type repeats similar to those found in maize, rice and barley dehydrin and rab proteins.
Sequence similarities
Belongs to the plant dehydrin family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length391
- Mass (Da)38,898
- Last updated2005-06-21 v2
- ChecksumE53CB63E80B1F43B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 21-35 | Basic and acidic residues | ||||
Sequence: KLPGGHGDHKETAGT | ||||||
Compositional bias | 72-89 | Basic and acidic residues | ||||
Sequence: GEKKGVMENIKDKLPGGH | ||||||
Compositional bias | 91-152 | Polar residues | ||||
Sequence: DHQQTGGTYGQQGHTGTATHGTPATGGTYGQQGHTGTATHGTPATGGTYGEQGHTGVTGTGT | ||||||
Compositional bias | 159-173 | Basic and acidic residues | ||||
Sequence: KGVMENIKEKLPGGH | ||||||
Compositional bias | 178-198 | Polar residues | ||||
Sequence: QTGGTYGQQGHTGTATHGTPA | ||||||
Compositional bias | 223-237 | Basic and acidic residues | ||||
Sequence: KGVMENIKDKLPGGH | ||||||
Compositional bias | 242-264 | Polar residues | ||||
Sequence: QTGGTYGQQGHTGTATQGTPAGG | ||||||
Compositional bias | 287-301 | Basic and acidic residues | ||||
Sequence: KGVMENIKEKLPGGH | ||||||
Compositional bias | 306-326 | Polar residues | ||||
Sequence: QTGGAYGQQGHTGTATHGTPA | ||||||
Compositional bias | 343-369 | Polar residues | ||||
Sequence: ETHGTTATGGTHGQHGHTGTTGTGTHG | ||||||
Compositional bias | 374-391 | Basic and acidic residues | ||||
Sequence: GEKKSLMDKIKDKLPGQH |
Keywords
- Technical term