CC106_HUMAN - dbPTM
CC106_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CC106_HUMAN
UniProt AC Q9BWC9
Protein Name Coiled-coil domain-containing protein 106
Gene Name CCDC106
Organism Homo sapiens (Human).
Sequence Length 280
Subcellular Localization Nucleus . Colocalizes with p53/TP53.
Protein Description Promotes the degradation of p53/TP53 protein and inhibits its transactivity..
Protein Sequence MNDRSSRRRTMKDDETFEISIPFDEAPHLDPQIFYSLSPSRRNFEEPPEAASSALALMNSVKTQLHMALERNSWLQKRIEDLEEERDFLRCQLDKFISSARMEAEDHCRMKPGPRRMEGDSRGGAGGEASDPESAASSLSGASEEGSASERRRQKQKGGASRRRFGKPKARERQRVKDADGVLCRYKKILGTFQKLKSMSRAFEHHRVDRNTVALTTPIAELLIVAPEKLAEVGEFDPSKERLLEYSRRCFLALDDETLKKVQALKKSKLLLPITYRFKR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
5Phosphorylation---MNDRSSRRRTMK
---CCCHHHCCCCCC
30.9324260401
20PhosphorylationDDETFEISIPFDEAP
CCCCEEEEEECCCCC
19.6027732954
35PhosphorylationHLDPQIFYSLSPSRR
CCCHHHHHHCCCCCC
15.4426074081
36PhosphorylationLDPQIFYSLSPSRRN
CCHHHHHHCCCCCCC
16.1826074081
38PhosphorylationPQIFYSLSPSRRNFE
HHHHHHCCCCCCCCC
18.1925849741
40PhosphorylationIFYSLSPSRRNFEEP
HHHHCCCCCCCCCCC
40.2626074081
121PhosphorylationPRRMEGDSRGGAGGE
CCCCCCCCCCCCCCC
43.6222210691
130PhosphorylationGGAGGEASDPESAAS
CCCCCCCCCHHHHHH
49.7728348404
134PhosphorylationGEASDPESAASSLSG
CCCCCHHHHHHHHCC
34.2330108239
137PhosphorylationSDPESAASSLSGASE
CCHHHHHHHHCCCCC
31.3730108239
138PhosphorylationDPESAASSLSGASEE
CHHHHHHHHCCCCCC
23.1030108239
140PhosphorylationESAASSLSGASEEGS
HHHHHHHCCCCCCCC
33.9730108239
147PhosphorylationSGASEEGSASERRRQ
CCCCCCCCHHHHHHH
31.72-
149PhosphorylationASEEGSASERRRQKQ
CCCCCCHHHHHHHHH
33.0822210691
161PhosphorylationQKQKGGASRRRFGKP
HHHHCCHHHHHCCCC
29.60-
163MethylationQKGGASRRRFGKPKA
HHCCHHHHHCCCCCH
35.47-
192PhosphorylationRYKKILGTFQKLKSM
HHHHHHHHHHHHHHH
21.3224719451
195UbiquitinationKILGTFQKLKSMSRA
HHHHHHHHHHHHHHH
54.41-
198PhosphorylationGTFQKLKSMSRAFEH
HHHHHHHHHHHHHHH
32.21-
200PhosphorylationFQKLKSMSRAFEHHR
HHHHHHHHHHHHHCC
27.7824719451
212PhosphorylationHHRVDRNTVALTTPI
HCCCCCCCCEECCCH
14.19-
216PhosphorylationDRNTVALTTPIAELL
CCCCCEECCCHHHHH
22.31-
217PhosphorylationRNTVALTTPIAELLI
CCCCEECCCHHHHHH
17.34-
240UbiquitinationVGEFDPSKERLLEYS
HCCCCCCHHHHHHHH
52.8429967540
269UbiquitinationVQALKKSKLLLPITY
HHHHHHHCCCCEEEE
52.62-
269SumoylationVQALKKSKLLLPITY
HHHHHHHCCCCEEEE
52.62-
269SumoylationVQALKKSKLLLPITY
HHHHHHHCCCCEEEE
52.62-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
130SPhosphorylationKinaseCK2BP67870
PSP
147SPhosphorylationKinaseCK2BP67870
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CC106_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 CC106_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATF4_HUMANATF4physical
16169070
CSN6_HUMANCOPS6physical
16169070
KAT5_HUMANKAT5physical
16169070
LRIF1_HUMANLRIF1physical
16169070
UT14A_HUMANUTP14Aphysical
16169070
SETB1_HUMANSETDB1physical
16169070
P53_HUMANTP53physical
16169070
ERG28_HUMANC14orf1physical
16169070
RBM48_HUMANRBM48physical
16169070
DPYL1_HUMANCRMP1physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
A4_HUMANAPPphysical
21832049
FAM9B_HUMANFAM9Bphysical
25416956
TE2IP_HUMANTERF2IPphysical
26186194
NFM_HUMANNEFMphysical
26186194
TERF2_HUMANTERF2physical
26186194
KCC1A_HUMANCAMK1physical
26186194
TERF2_HUMANTERF2physical
28514442
TE2IP_HUMANTERF2IPphysical
28514442
KCC1A_HUMANCAMK1physical
28514442
NFM_HUMANNEFMphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CC106_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP