UniProt ID | CDC42_HUMAN | |
---|---|---|
UniProt AC | P60953 | |
Protein Name | Cell division control protein 42 homolog | |
Gene Name | CDC42 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 191 | |
Subcellular Localization |
Cell membrane Lipid-anchor Cytoplasmic side . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Midbody . Localizes to spindle during prometaphase cells. Moves to the central spindle as cells |
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Protein Description | Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration. Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons. Facilitates filopodia formation upon DOCK11-activation (By similarity). Also plays a role in phagocytosis through organization of the F-actin cytoskeleton associated with forming phagocytic cups.. | |
Protein Sequence | MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL | |
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 |
---|---|---|---|---|---|
5 | Ubiquitination | ---MQTIKCVVVGDG ---CCEEEEEEECCC | 25.10 | - | |
6 | S-palmitoylation | --MQTIKCVVVGDGA --CCEEEEEEECCCC | 2.19 | 29575903 | |
30 | Phosphorylation | YTTNKFPSEYVPTVF EECCCCCHHHCCCEE | 44.70 | - | |
32 | O-AMP-tyrosine | TNKFPSEYVPTVFDN CCCCCHHHCCCEECC | 18.96 | - | |
32 | Phosphorylation | TNKFPSEYVPTVFDN CCCCCHHHCCCEECC | 18.96 | - | |
32 | O-linked_Glycosylation | TNKFPSEYVPTVFDN CCCCCHHHCCCEECC | 18.96 | 24141704 | |
32 | AMPylation | TNKFPSEYVPTVFDN CCCCCHHHCCCEECC | 18.96 | 19362538 | |
35 | O-AMP-threonine | FPSEYVPTVFDNYAV CCHHHCCCEECCEEE | 24.62 | - | |
35 | Phosphorylation | FPSEYVPTVFDNYAV CCHHHCCCEECCEEE | 24.62 | - | |
35 | O-linked_Glycosylation | FPSEYVPTVFDNYAV CCHHHCCCEECCEEE | 24.62 | 7775453 | |
35 | AMPylation | FPSEYVPTVFDNYAV CCHHHCCCEECCEEE | 24.62 | 19039103 | |
64 | Phosphorylation | DTAGQEDYDRLRPLS CCCCCCCHHHCCCCC | 11.38 | 20736484 | |
71 | Phosphorylation | YDRLRPLSYPQTDVF HHHCCCCCCCCCCEE | 37.13 | 18669648 | |
107 (in isoform 1) | Ubiquitination | - | 74.38 | 21890473 | |
107 (in isoform 2) | Ubiquitination | - | 74.38 | 21890473 | |
107 | Ubiquitination | EITHHCPKTPFLLVG CHHCCCCCCCEEEEE | 74.38 | - | |
128 | Acetylation | DDPSTIEKLAKNKQK CCHHHHHHHHHCCCC | 50.31 | 26051181 | |
128 (in isoform 1) | Ubiquitination | - | 50.31 | 21890473 | |
128 | Ubiquitination | DDPSTIEKLAKNKQK CCHHHHHHHHHCCCC | 50.31 | - | |
128 (in isoform 2) | Ubiquitination | - | 50.31 | 21890473 | |
133 (in isoform 1) | Ubiquitination | - | 60.02 | 21890473 | |
133 (in isoform 2) | Ubiquitination | - | 60.02 | 21890473 | |
133 | Ubiquitination | IEKLAKNKQKPITPE HHHHHHCCCCCCCHH | 60.02 | - | |
135 | Acetylation | KLAKNKQKPITPETA HHHHCCCCCCCHHHH | 39.74 | 19608861 | |
135 (in isoform 2) | Ubiquitination | - | 39.74 | 21890473 | |
135 | Ubiquitination | KLAKNKQKPITPETA HHHHCCCCCCCHHHH | 39.74 | - | |
135 (in isoform 1) | Ubiquitination | - | 39.74 | 21890473 | |
138 | Phosphorylation | KNKQKPITPETAEKL HCCCCCCCHHHHHHH | 24.49 | 28060719 | |
141 | Phosphorylation | QKPITPETAEKLARD CCCCCHHHHHHHHHH | 41.12 | 28985074 | |
144 (in isoform 2) | Ubiquitination | - | 45.01 | 21890473 | |
144 | Acetylation | ITPETAEKLARDLKA CCHHHHHHHHHHHHH | 45.01 | 23749302 | |
144 (in isoform 1) | Ubiquitination | - | 45.01 | 21890473 | |
144 | Ubiquitination | ITPETAEKLARDLKA CCHHHHHHHHHHHHH | 45.01 | - | |
153 (in isoform 2) | Ubiquitination | - | 48.73 | 21890473 | |
153 | Acetylation | ARDLKAVKYVECSAL HHHHHHCCEEECHHH | 48.73 | 25953088 | |
153 | Ubiquitination | ARDLKAVKYVECSAL HHHHHHCCEEECHHH | 48.73 | 22053931 | |
154 | Phosphorylation | RDLKAVKYVECSALT HHHHHCCEEECHHHC | 8.55 | 28152594 | |
157 | S-palmitoylation | KAVKYVECSALTQKG HHCCEEECHHHCHHH | 1.74 | 29575903 | |
161 | Phosphorylation | YVECSALTQKGLKNV EEECHHHCHHHHHHH | 28.14 | 25159151 | |
163 | Acetylation | ECSALTQKGLKNVFD ECHHHCHHHHHHHHC | 62.06 | 26051181 | |
163 (in isoform 2) | Ubiquitination | - | 62.06 | 21890473 | |
163 | Ubiquitination | ECSALTQKGLKNVFD ECHHHCHHHHHHHHC | 62.06 | 21890473 | |
166 | Ubiquitination | ALTQKGLKNVFDEAI HHCHHHHHHHHCHHH | 60.79 | 21906983 | |
166 (in isoform 2) | Ubiquitination | - | 60.79 | 21890473 | |
182 (in isoform 1) | Phosphorylation | - | 55.97 | - | |
183 | Ubiquitination | ALEPPEPKKSRRCVL HHCCCCCCCCCCEEE | 62.81 | 22053931 | |
183 (in isoform 2) | Ubiquitination | - | 62.81 | 21890473 | |
184 | Ubiquitination | LEPPEPKKSRRCVLL HCCCCCCCCCCEEEC | 60.97 | 22053931 | |
184 (in isoform 2) | Ubiquitination | - | 60.97 | 21890473 | |
188 | Geranylgeranylation | EPKKSRRCVLL---- CCCCCCCEEEC---- | 2.16 | 10676816 | |
188 | Methylation | EPKKSRRCVLL---- CCCCCCCEEEC---- | 2.16 | 10676816 | |
188 | Geranylgeranylation | EPKKSRRCVLL---- CCCCCCCEEEC---- | 2.16 | 10676816 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
35 | T | Glycosylation |
| 7777059 |
* 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 CDC42_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. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135 AND LYS-144, AND MASSSPECTROMETRY. |