CC130_HUMAN - dbPTM
CC130_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CC130_HUMAN
UniProt AC P13994
Protein Name Coiled-coil domain-containing protein 130
Gene Name CCDC130
Organism Homo sapiens (Human).
Sequence Length 396
Subcellular Localization
Protein Description
Protein Sequence MGERKGVNKYYPPDFNPEKHGSLNRYHNSHPLRERARKLSQGILIIRFEMPYNIWCDGCKNHIGMGVRYNAEKKKVGNYYTTPIYRFRMKCHLCVNYIEMQTDPANCDYVIVSGAQRKEERWDMADNEQVLTTEHEKKQKLETDAMFRLEHGEADRSTLKKALPTLSHIQEAQSAWKDDFALNSMLRRRFREKKKAIQEEEERDQALQAKASLTIPLVPETEDDRKLAALLKFHTLDSYEDKQKLKRTEIISRSWFPSAPGSASSSKVSGVLKKLAQSRRTALATSPITVGDLGIVRRRSRDVPESPQHAADTPKSGEPRVPEEAAQDRPMSPGDCPPETTETPKCSSPRGQEGSRQDKPLSPAGSSQEAADTPDTRHPCSLGSSLVADYSDSESE
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
19UbiquitinationPPDFNPEKHGSLNRY
CCCCCHHHCCCCCCC		55.30-
40PhosphorylationRERARKLSQGILIIR
HHHHHHHCCCEEEEE		29.4222617229
138UbiquitinationLTTEHEKKQKLETDA
CCHHHHHHHHCCCCH		50.08-
161UbiquitinationADRSTLKKALPTLSH
CCHHHHHHHHHHHHH		59.26-
184PhosphorylationKDDFALNSMLRRRFR
CCHHHHHHHHHHHHH		21.7528555341
210UbiquitinationRDQALQAKASLTIPL
HHHHHHHHHCCCCCC		26.08-
221PhosphorylationTIPLVPETEDDRKLA
CCCCCCCCCCHHHHH		38.35-
226UbiquitinationPETEDDRKLAALLKF
CCCCCHHHHHHHHHH		49.85-
235PhosphorylationAALLKFHTLDSYEDK
HHHHHHHCCCCHHHH		35.0829083192
238PhosphorylationLKFHTLDSYEDKQKL
HHHHCCCCHHHHHHH		33.2723312004
239PhosphorylationKFHTLDSYEDKQKLK
HHHCCCCHHHHHHHC		28.0127251275
242UbiquitinationTLDSYEDKQKLKRTE
CCCCHHHHHHHCCCE		37.07-
254PhosphorylationRTEIISRSWFPSAPG
CCEEECHHCCCCCCC		26.69-
262PhosphorylationWFPSAPGSASSSKVS
CCCCCCCCCCHHHHH		24.7428555341
281PhosphorylationKLAQSRRTALATSPI
HHHHHHHHHHHCCCC		25.5530108239
285PhosphorylationSRRTALATSPITVGD
HHHHHHHCCCCCHHH		35.5729255136
286PhosphorylationRRTALATSPITVGDL
HHHHHHCCCCCHHHH		14.5429255136
289PhosphorylationALATSPITVGDLGIV
HHHCCCCCHHHHHHH		23.0929255136
300PhosphorylationLGIVRRRSRDVPESP
HHHHCCCCCCCCCCC		30.9028348404
306PhosphorylationRSRDVPESPQHAADT
CCCCCCCCCCCCCCC		24.6430266825
313PhosphorylationSPQHAADTPKSGEPR
CCCCCCCCCCCCCCC		28.0830108239
316PhosphorylationHAADTPKSGEPRVPE
CCCCCCCCCCCCCCH		49.9822210691
332PhosphorylationAAQDRPMSPGDCPPE
HHCCCCCCCCCCCCC		28.5423401153
340PhosphorylationPGDCPPETTETPKCS
CCCCCCCCCCCCCCC		35.3923927012
341PhosphorylationGDCPPETTETPKCSS
CCCCCCCCCCCCCCC		35.8823927012
343PhosphorylationCPPETTETPKCSSPR
CCCCCCCCCCCCCCC		26.4223927012
347PhosphorylationTTETPKCSSPRGQEG
CCCCCCCCCCCCCCC		49.8828102081
348PhosphorylationTETPKCSSPRGQEGS
CCCCCCCCCCCCCCC		28.2522210691
355PhosphorylationSPRGQEGSRQDKPLS
CCCCCCCCCCCCCCC		26.4728102081
362PhosphorylationSRQDKPLSPAGSSQE
CCCCCCCCCCCCCCC		22.6423401153
366PhosphorylationKPLSPAGSSQEAADT
CCCCCCCCCCCCCCC		30.8430266825
367PhosphorylationPLSPAGSSQEAADTP
CCCCCCCCCCCCCCC		30.9930266825
373PhosphorylationSSQEAADTPDTRHPC
CCCCCCCCCCCCCCC		20.5223403867
391PhosphorylationSSLVADYSDSESE--
HHHEECCCCCCCC--		34.9024501219
393PhosphorylationLVADYSDSESE----
HEECCCCCCCC----		36.7624501219
395PhosphorylationADYSDSESE------
ECCCCCCCC------		53.1924501219
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

Oops, there are no upstream regulatory protein records of CC130_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CC130_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 CC130_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1A1_HUMANEEF1A1physical
16169070
ZBT16_HUMANZBTB16physical
16169070
PLAK_HUMANJUPphysical
22365833
ZN572_HUMANZNF572physical
25416956
ZZEF1_HUMANZZEF1physical
26186194
UBR1_HUMANUBR1physical
26186194
HECD3_HUMANHECTD3physical
26186194
2ABD_HUMANPPP2R2Dphysical
26186194
KDM8_HUMANKDM8physical
26186194
SPS1_HUMANSEPHS1physical
26186194
RIOX2_HUMANMINAphysical
26186194
KDM8_HUMANKDM8physical
28514442
ZZEF1_HUMANZZEF1physical
28514442
HECD3_HUMANHECTD3physical
28514442
UBR1_HUMANUBR1physical
28514442
2ABD_HUMANPPP2R2Dphysical
28514442
RCCD1_HUMANRCCD1physical
28514442
UBR2_HUMANUBR2physical
28514442
Drug and Disease Associations
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.
Regulatory Network of CC130_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-393 ANDSER-395, AND MASS SPECTROMETRY.

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