UniProt ID | CIRBP_HUMAN | |
---|---|---|
UniProt AC | Q14011 | |
Protein Name | Cold-inducible RNA-binding protein | |
Gene Name | CIRBP | |
Organism | Homo sapiens (Human). | |
Sequence Length | 172 | |
Subcellular Localization | Nucleus, nucleoplasm . Cytoplasm . Translocates from the nucleus to the cytoplasm after exposure to UV radiation. Translocates from the nucleus to the cytoplasm into stress granules upon various cytoplasmic stresses, such as osmotic and heat shocks. | |
Protein Description | Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Acts as a translational activator. Seems to play an essential role in cold-induced suppression of cell proliferation. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a translational repressor (By similarity). Promotes assembly of stress granules (SGs), when overexpressed.. | |
Protein Sequence | MASDEGKLFVGGLSFDTNEQSLEQVFSKYGQISEVVVVKDRETQRSRGFGFVTFENIDDAKDAMMAMNGKSVDGRQIRVDQAGKSSDNRSRGYRGGSAGGRGFFRGGRGRGRGFSRGGGDRGYGGNRFESRSGGYGGSRDYYSSRSQSGGYSDRSSGGSYRDSYDSYATHNE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
14 | Phosphorylation | KLFVGGLSFDTNEQS CEEECCEECCCCHHH | 25.09 | 27732954 | |
17 | Phosphorylation | VGGLSFDTNEQSLEQ ECCEECCCCHHHHHH | 38.35 | 27732954 | |
21 | Phosphorylation | SFDTNEQSLEQVFSK ECCCCHHHHHHHHHH | 27.91 | 27732954 | |
27 | Phosphorylation | QSLEQVFSKYGQISE HHHHHHHHHHCCEEE | 26.55 | 28122231 | |
29 | Phosphorylation | LEQVFSKYGQISEVV HHHHHHHHCCEEEEE | 17.05 | 28152594 | |
31 | Ubiquitination | QVFSKYGQISEVVVV HHHHHHCCEEEEEEE | 32.70 | - | |
33 | Phosphorylation | FSKYGQISEVVVVKD HHHHCCEEEEEEEEC | 19.22 | 28152594 | |
43 | Phosphorylation | VVVKDRETQRSRGFG EEEECCCCCHHCCEE | 30.12 | - | |
47 | Methylation | DRETQRSRGFGFVTF CCCCCHHCCEEEEEE | 46.80 | - | |
70 | Acetylation | AMMAMNGKSVDGRQI HHHHHCCEECCCCEE | 42.15 | - | |
70 | Acetylation | AMMAMNGKSVDGRQI HHHHHCCEECCCCEE | 42.15 | 26051181 | |
71 | Phosphorylation | MMAMNGKSVDGRQIR HHHHCCEECCCCEEE | 27.17 | 20068231 | |
84 | Ubiquitination | IRVDQAGKSSDNRSR EEEECCCCCCCCCCC | 50.21 | 21906983 | |
94 | Methylation | DNRSRGYRGGSAGGR CCCCCCCCCCCCCCC | 45.91 | - | |
94 | Dimethylation | DNRSRGYRGGSAGGR CCCCCCCCCCCCCCC | 45.91 | - | |
101 | Methylation | RGGSAGGRGFFRGGR CCCCCCCCCCCCCCC | 37.52 | - | |
101 | Dimethylation | RGGSAGGRGFFRGGR CCCCCCCCCCCCCCC | 37.52 | - | |
105 | Methylation | AGGRGFFRGGRGRGR CCCCCCCCCCCCCCC | 44.38 | - | |
105 | Dimethylation | AGGRGFFRGGRGRGR CCCCCCCCCCCCCCC | 44.38 | - | |
110 (in isoform 3) | Phosphorylation | - | 30.21 | 21815630 | |
116 | Methylation | GRGRGFSRGGGDRGY CCCCCCCCCCCCCCC | 45.58 | - | |
121 | Methylation | FSRGGGDRGYGGNRF CCCCCCCCCCCCCCC | 43.43 | - | |
123 | Phosphorylation | RGGGDRGYGGNRFES CCCCCCCCCCCCCCC | 23.82 | - | |
127 | Methylation | DRGYGGNRFESRSGG CCCCCCCCCCCCCCC | 39.73 | - | |
129 (in isoform 2) | Phosphorylation | - | 41.84 | 21815630 | |
130 | Phosphorylation | YGGNRFESRSGGYGG CCCCCCCCCCCCCCC | 29.09 | 24670416 | |
131 | Methylation | GGNRFESRSGGYGGS CCCCCCCCCCCCCCC | 31.93 | - | |
132 | Phosphorylation | GNRFESRSGGYGGSR CCCCCCCCCCCCCCC | 45.94 | 21945579 | |
135 | Phosphorylation | FESRSGGYGGSRDYY CCCCCCCCCCCCCCC | 23.10 | 21945579 | |
138 | Phosphorylation | RSGGYGGSRDYYSSR CCCCCCCCCCCCCCC | 20.02 | 21945579 | |
139 | Methylation | SGGYGGSRDYYSSRS CCCCCCCCCCCCCCC | 38.94 | - | |
141 | Phosphorylation | GYGGSRDYYSSRSQS CCCCCCCCCCCCCCC | 12.25 | 21945579 | |
142 | Phosphorylation | YGGSRDYYSSRSQSG CCCCCCCCCCCCCCC | 12.40 | 21945579 | |
143 | Phosphorylation | GGSRDYYSSRSQSGG CCCCCCCCCCCCCCC | 17.04 | 21945579 | |
144 | Phosphorylation | GSRDYYSSRSQSGGY CCCCCCCCCCCCCCC | 21.60 | 21945579 | |
145 | Methylation | SRDYYSSRSQSGGYS CCCCCCCCCCCCCCC | 32.54 | - | |
146 | Phosphorylation | RDYYSSRSQSGGYSD CCCCCCCCCCCCCCC | 30.55 | 22617229 | |
148 | Phosphorylation | YYSSRSQSGGYSDRS CCCCCCCCCCCCCCC | 35.12 | 22617229 | |
151 | Phosphorylation | SRSQSGGYSDRSSGG CCCCCCCCCCCCCCC | 15.78 | 28450419 | |
152 | Phosphorylation | RSQSGGYSDRSSGGS CCCCCCCCCCCCCCC | 29.80 | 28450419 | |
154 | Methylation | QSGGYSDRSSGGSYR CCCCCCCCCCCCCCC | 27.12 | - | |
155 | Phosphorylation | SGGYSDRSSGGSYRD CCCCCCCCCCCCCCC | 38.02 | 23401153 | |
156 | Phosphorylation | GGYSDRSSGGSYRDS CCCCCCCCCCCCCCC | 48.33 | 21712546 | |
159 | Phosphorylation | SDRSSGGSYRDSYDS CCCCCCCCCCCCCCC | 22.11 | 23401153 | |
160 | Phosphorylation | DRSSGGSYRDSYDSY CCCCCCCCCCCCCCC | 23.01 | 30177828 | |
163 | Phosphorylation | SGGSYRDSYDSYATH CCCCCCCCCCCCCCC | 23.11 | 22617229 | |
164 | Phosphorylation | GGSYRDSYDSYATHN CCCCCCCCCCCCCCC | 17.13 | 30177828 | |
166 | Phosphorylation | SYRDSYDSYATHNE- CCCCCCCCCCCCCC- | 14.40 | 23898821 | |
167 | Phosphorylation | YRDSYDSYATHNE-- CCCCCCCCCCCCC-- | 16.78 | 27273156 | |
169 | Phosphorylation | DSYDSYATHNE---- CCCCCCCCCCC---- | 19.59 | 28152594 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CIRBP_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CIRBP_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CIRBP_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...