UniProt ID | CCDC8_HUMAN | |
---|---|---|
UniProt AC | Q9H0W5 | |
Protein Name | Coiled-coil domain-containing protein 8 | |
Gene Name | CCDC8 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 538 | |
Subcellular Localization | Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . | |
Protein Description | Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. [PubMed: 24793695] | |
Protein Sequence | MLQIGEDVDYLLIPREVRLAGGVWRVISKPATKEAEFRERLTQFLEEEGRTLEDVARIMEKSTPHPPQPPKKPKEPRVRRRVQQMVTPPPRLVVGTYDSSNASDSEFSDFETSRDKSRQGPRRGKKVRKMPVSYLGSKFLGSDLESEDDEELVEAFLRRQEKQPSAPPARRRVNLPVPMFEDNLGPQLSKADRWREYVSQVSWGKLKRRVKGWAPRAGPGVGEARLASTAVESAGVSSAPEGTSPGDRLGNAGDVCVPQASPRRWRPKINWASFRRRRKEQTAPTGQGADIEADQGGEAADSQREEAIADQREGAAGNQRAGAPADQGAEAADNQREEAADNQRAGAPAEEGAEAADNQREEAADNQRAEAPADQRSQGTDNHREEAADNQRAEAPADQGSEVTDNQREEAVHDQRERAPAVQGADNQRAQARAGQRAEAAHNQRAGAPGIQEAEVSAAQGTTGTAPGARARKQVKTVRFQTPGRFSWFCKRRRAFWHTPRLPTLPKRVPRAGEARNLRVLRAEARAEAEQGEQEDQL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
62 | Phosphorylation | VARIMEKSTPHPPQP HHHHHHHCCCCCCCC | 33.59 | 21406692 | |
63 | Phosphorylation | ARIMEKSTPHPPQPP HHHHHHCCCCCCCCC | 36.36 | 21406692 | |
87 | Phosphorylation | RRVQQMVTPPPRLVV HHHHHHCCCCCEEEE | 25.41 | 23186163 | |
96 | Phosphorylation | PPRLVVGTYDSSNAS CCEEEEEEECCCCCC | 16.73 | 29978859 | |
97 | Phosphorylation | PRLVVGTYDSSNASD CEEEEEEECCCCCCC | 14.11 | 29978859 | |
99 | Phosphorylation | LVVGTYDSSNASDSE EEEEEECCCCCCCCC | 18.32 | 29978859 | |
100 | Phosphorylation | VVGTYDSSNASDSEF EEEEECCCCCCCCCC | 33.25 | 29978859 | |
103 | Phosphorylation | TYDSSNASDSEFSDF EECCCCCCCCCCCCC | 46.01 | 29978859 | |
105 | Phosphorylation | DSSNASDSEFSDFET CCCCCCCCCCCCCCC | 37.74 | 29978859 | |
108 | Phosphorylation | NASDSEFSDFETSRD CCCCCCCCCCCCCCC | 37.02 | 29978859 | |
112 | Phosphorylation | SEFSDFETSRDKSRQ CCCCCCCCCCCHHCC | 29.11 | 29978859 | |
113 | Phosphorylation | EFSDFETSRDKSRQG CCCCCCCCCCHHCCC | 31.14 | 29978859 | |
117 | Phosphorylation | FETSRDKSRQGPRRG CCCCCCHHCCCCCCC | 33.84 | 23401153 | |
134 | Phosphorylation | VRKMPVSYLGSKFLG CCCCCHHHHCHHHCC | 18.47 | 23532336 | |
137 | Phosphorylation | MPVSYLGSKFLGSDL CCHHHHCHHHCCCCC | 20.03 | 23532336 | |
142 | Phosphorylation | LGSKFLGSDLESEDD HCHHHCCCCCCCCCH | 40.96 | 22617229 | |
146 | Phosphorylation | FLGSDLESEDDEELV HCCCCCCCCCHHHHH | 54.33 | 22617229 | |
190 | Ubiquitination | NLGPQLSKADRWREY CCCCCCCHHHHHHHH | 64.00 | - | |
197 | Phosphorylation | KADRWREYVSQVSWG HHHHHHHHHHHHCHH | 9.23 | - | |
199 | Phosphorylation | DRWREYVSQVSWGKL HHHHHHHHHHCHHHH | 24.78 | 27251275 | |
202 | Phosphorylation | REYVSQVSWGKLKRR HHHHHHHCHHHHHHH | 23.60 | 29978859 | |
237 | Phosphorylation | AVESAGVSSAPEGTS HHHHCCCCCCCCCCC | 21.62 | 29978859 | |
238 | Phosphorylation | VESAGVSSAPEGTSP HHHCCCCCCCCCCCC | 45.49 | 29978859 | |
243 | Phosphorylation | VSSAPEGTSPGDRLG CCCCCCCCCCCCCCC | 30.04 | 24719451 | |
244 | Phosphorylation | SSAPEGTSPGDRLGN CCCCCCCCCCCCCCC | 37.43 | 29978859 | |
261 | Phosphorylation | DVCVPQASPRRWRPK CCCCCCCCCCCCCCC | 17.43 | 19664994 | |
273 | Phosphorylation | RPKINWASFRRRRKE CCCCCHHHHHHHHHH | 15.76 | 29978859 | |
302 | Phosphorylation | QGGEAADSQREEAIA CCCCCCHHHHHHHHH | 26.81 | 17525332 | |
320 | Methylation | EGAAGNQRAGAPADQ CHHHCCCCCCCCHHH | 38.70 | - | |
344 | Methylation | EEAADNQRAGAPAEE HHHHHHHCCCCCHHH | 41.04 | - | |
401 | Phosphorylation | EAPADQGSEVTDNQR CCCCCCCCCCCHHHH | 24.22 | 26471730 | |
445 | Methylation | AEAAHNQRAGAPGIQ HHHHHHHCCCCCCCC | 40.06 | - | |
465 | Phosphorylation | AAQGTTGTAPGARAR HCCCCCCCCCCHHHH | 27.82 | 24173317 | |
477 | Phosphorylation | RARKQVKTVRFQTPG HHHCCCEEEEECCCC | 20.32 | 22817900 | |
487 | Phosphorylation | FQTPGRFSWFCKRRR ECCCCCEEHHHCCCC | 20.20 | 29978859 | |
499 | Phosphorylation | RRRAFWHTPRLPTLP CCCHHCCCCCCCCCC | 10.74 | - |
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 CCDC8_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CCDC8_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 CCDC8_HUMAN !! |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
614205 | 3M syndrome 3 (3M3) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASSSPECTROMETRY. | |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND MASSSPECTROMETRY. |