CC120_HUMAN - dbPTM
CC120_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CC120_HUMAN
UniProt AC Q96HB5
Protein Name Coiled-coil domain-containing protein 120
Gene Name CCDC120
Organism Homo sapiens (Human).
Sequence Length 630
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm . Cell projection . Cell projection, growth cone . Endosome . Localizes to the subdistal appendages of mother centrioles and proximal ends of both centrioles in
Protein Description Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells. [PubMed: 28422092 Together with CCDC68, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly]
Protein Sequence MEVKGQLISSPTFNAPAALFGEAAPQVKSERLRGLLDRQRTLQEALSLKLQELRKVCLQEAELTGQLPPECPLEPGERPQLVRRRPPTARAYPPPHPNQAHHSLCPAEELALEALEREVSVQQQIAAAARRLALAPDLSTEQRRRRRQVQADALRRLHELEEQLRDVRARLGLPVLPLPQPLPLSTGSVITTQGVCLGMRLAQLSQEDVVLHSESSSLSESGASHDNEEPHGCFSLAERPSPPKAWDQLRAVSGGSPERRTPWKPPPSDLYGDLKSRRNSVASPTSPTRSLPRSASSFEGRSVPATPVLTRGAGPQLCKPEGLHSRQWSGSQDSQMGFPRADPASDRASLFVARTRRSNSSEALLVDRAAGGGAGSPPAPLAPSASGPPVCKSSEVLYERPQPTPAFSSRTAGPPDPPRAARPSSAAPASRGAPRLPPVCGDFLLDYSLDRGLPRSGGGTGWGELPPAAEVPGPLSRRDGLLTMLPGPPPVYAADSNSPLLRTKDPHTRATRTKPCGLPPEAAEGPEVHPNPLLWMPPPTRIPSAGERSGHKNLALEGLRDWYIRNSGLAAGPQRRPVLPSVGPPHPPFLHARCYEVGQALYGAPSQAPLPHSRSFTAPPVSGRYGGCFY
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
9PhosphorylationEVKGQLISSPTFNAP
CCCCEECCCCCCCCC		38.5729116813
10PhosphorylationVKGQLISSPTFNAPA
CCCEECCCCCCCCCH		22.4426657352
10 (in isoform 3)Phosphorylation-22.4424719451
12PhosphorylationGQLISSPTFNAPAAL
CEECCCCCCCCCHHH		31.3121815630
44PhosphorylationDRQRTLQEALSLKLQ
HHHHHHHHHHHHHHH		55.4832142685
45 (in isoform 4)Phosphorylation-6.8927251275
47PhosphorylationRTLQEALSLKLQELR
HHHHHHHHHHHHHHH		30.4224719451
88PhosphorylationLVRRRPPTARAYPPP
HHHCCCCCCCCCCCC		31.3020363803
244PhosphorylationAERPSPPKAWDQLRA
CCCCCCCCHHHHHHH		66.5533259812
253PhosphorylationWDQLRAVSGGSPERR
HHHHHHHCCCCCCCC		36.1330576142
256PhosphorylationLRAVSGGSPERRTPW
HHHHCCCCCCCCCCC		27.4125849741
256 (in isoform 3)Phosphorylation-27.4124719451
261PhosphorylationGGSPERRTPWKPPPS
CCCCCCCCCCCCCCH		39.4625159151
268PhosphorylationTPWKPPPSDLYGDLK
CCCCCCCHHHCCCHH		46.1229978859
271PhosphorylationKPPPSDLYGDLKSRR
CCCCHHHCCCHHHHC		17.3727259358
276PhosphorylationDLYGDLKSRRNSVAS
HHCCCHHHHCCCCCC		43.7123090842
280 (in isoform 3)Phosphorylation-19.7624719451
280PhosphorylationDLKSRRNSVASPTSP
CHHHHCCCCCCCCCC		19.7623927012
283PhosphorylationSRRNSVASPTSPTRS
HHCCCCCCCCCCCCC		26.9330266825
285 (in isoform 3)Phosphorylation-44.8624719451
285PhosphorylationRNSVASPTSPTRSLP
CCCCCCCCCCCCCCC		44.8630266825
286PhosphorylationNSVASPTSPTRSLPR
CCCCCCCCCCCCCCC		27.8830266825
286 (in isoform 3)Phosphorylation-27.8824719451
288PhosphorylationVASPTSPTRSLPRSA
CCCCCCCCCCCCCCH		32.4330266825
290PhosphorylationSPTSPTRSLPRSASS
CCCCCCCCCCCCHHH		45.2423403867
291PhosphorylationPTSPTRSLPRSASSF
CCCCCCCCCCCHHHC		3.5433259812
294PhosphorylationPTRSLPRSASSFEGR
CCCCCCCCHHHCCCC		30.4821712546
296PhosphorylationRSLPRSASSFEGRSV
CCCCCCHHHCCCCCC		36.4923090842
297PhosphorylationSLPRSASSFEGRSVP
CCCCCHHHCCCCCCC		27.3423090842
297 (in isoform 3)Phosphorylation-27.3424719451
302PhosphorylationASSFEGRSVPATPVL
HHHCCCCCCCCCCEE		43.2225159151
302 (in isoform 3)Phosphorylation-43.2224719451
306PhosphorylationEGRSVPATPVLTRGA
CCCCCCCCCEECCCC		14.0920873877
306 (in isoform 3)Phosphorylation-14.0924719451
310PhosphorylationVPATPVLTRGAGPQL
CCCCCEECCCCCCCC		27.5623090842
311MethylationPATPVLTRGAGPQLC
CCCCEECCCCCCCCC		28.89-
315 (in isoform 4)Phosphorylation-24.3627251275
318 (in isoform 4)Phosphorylation-6.1027251275
329 (in isoform 3)Phosphorylation-21.8924719451
329 (in isoform 4)Phosphorylation-21.8927251275
329PhosphorylationGLHSRQWSGSQDSQM
CCCCCCCCCCCCCCC		21.8920068231
331PhosphorylationHSRQWSGSQDSQMGF
CCCCCCCCCCCCCCC		25.8717525332
331 (in isoform 3)Phosphorylation-25.8724719451
334PhosphorylationQWSGSQDSQMGFPRA
CCCCCCCCCCCCCCC		17.9020068231
337 (in isoform 4)Phosphorylation-23.0527251275
341 (in isoform 4)Phosphorylation-27.6327251275
348PhosphorylationADPASDRASLFVART
CCCCHHHHHEEEEEC		18.6432142685
349PhosphorylationDPASDRASLFVARTR
CCCHHHHHEEEEECC		24.2028555341
355PhosphorylationASLFVARTRRSNSSE
HHEEEEECCCCCCCC		22.2423312004
358 (in isoform 3)Phosphorylation-37.4624719451
358PhosphorylationFVARTRRSNSSEALL
EEEECCCCCCCCEEE		37.4630266825
360PhosphorylationARTRRSNSSEALLVD
EECCCCCCCCEEEEE		30.7023401153
360 (in isoform 3)Phosphorylation-30.7024719451
361PhosphorylationRTRRSNSSEALLVDR
ECCCCCCCCEEEEEC		31.0130266825
364 (in isoform 4)Phosphorylation-4.1527251275
366 (in isoform 4)Phosphorylation-4.9427251275
376PhosphorylationAAGGGAGSPPAPLAP
CCCCCCCCCCCCCCC		27.4625159151
376 (in isoform 3)Phosphorylation-27.4624719451
384PhosphorylationPPAPLAPSASGPPVC
CCCCCCCCCCCCCCC		29.4726074081
386PhosphorylationAPLAPSASGPPVCKS
CCCCCCCCCCCCCCC		57.0526074081
393 (in isoform 3)Phosphorylation-26.9724719451
393 (in isoform 4)Phosphorylation-26.9727251275
393PhosphorylationSGPPVCKSSEVLYER
CCCCCCCCCHHEECC		26.9725849741
394PhosphorylationGPPVCKSSEVLYERP
CCCCCCCCHHEECCC		19.7421945579
395 (in isoform 4)Phosphorylation-43.5727251275
395PhosphorylationPPVCKSSEVLYERPQ
CCCCCCCHHEECCCC		43.5732142685
398PhosphorylationCKSSEVLYERPQPTP
CCCCHHEECCCCCCC		18.3121945579
404PhosphorylationLYERPQPTPAFSSRT
EECCCCCCCCCCCCC		23.2321945579
408PhosphorylationPQPTPAFSSRTAGPP
CCCCCCCCCCCCCCC		22.4821945579
409PhosphorylationQPTPAFSSRTAGPPD
CCCCCCCCCCCCCCC		27.4821945579
411 (in isoform 4)Phosphorylation-37.6027251275
424PhosphorylationPPRAARPSSAAPASR
CCCCCCCCCCCCHHC		27.3627794612
425PhosphorylationPRAARPSSAAPASRG
CCCCCCCCCCCHHCC		31.0018691976
428 (in isoform 4)Phosphorylation-30.4127251275
430PhosphorylationPSSAAPASRGAPRLP
CCCCCCHHCCCCCCC		30.1330576142
435MethylationPASRGAPRLPPVCGD
CHHCCCCCCCCCCCH		60.33-
483PhosphorylationSRRDGLLTMLPGPPP
CCCCCCEECCCCCCC		23.0027542207
492PhosphorylationLPGPPPVYAADSNSP
CCCCCCEEECCCCCC		11.2227542207
496PhosphorylationPPVYAADSNSPLLRT
CCEEECCCCCCCCCC		34.1830278072
498PhosphorylationVYAADSNSPLLRTKD
EEECCCCCCCCCCCC		22.3730278072
533 (in isoform 4)Phosphorylation-8.1027251275
602PhosphorylationYEVGQALYGAPSQAP
HHHHHHHHCCCCCCC		17.7921945579
614MethylationQAPLPHSRSFTAPPV
CCCCCCCCCCCCCCC		32.52-
615 (in isoform 3)Phosphorylation-29.9324719451
615PhosphorylationAPLPHSRSFTAPPVS
CCCCCCCCCCCCCCC		29.9326657352
617PhosphorylationLPHSRSFTAPPVSGR
CCCCCCCCCCCCCCC		39.2323312004
647 (in isoform 5)Phosphorylation--
650 (in isoform 4)Phosphorylation-27251275
659 (in isoform 3)Phosphorylation--
694 (in isoform 4)Phosphorylation--
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 CC120_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CC120_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 CC120_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDFI_HUMANMDFIphysical
19447967
K1C40_HUMANKRT40physical
25416956
CCD57_HUMANCCDC57physical
25416956
BRCA1_HUMANBRCA1physical
25184681
SDCG8_HUMANSDCCAG8physical
28514442
CYH1_HUMANCYTH1physical
28514442
CYH2_HUMANCYTH2physical
28514442
MEIS2_HUMANMEIS2physical
28514442
MORN2_HUMANMORN2physical
28514442
CYH3_HUMANCYTH3physical
28514442
AINX_HUMANINAphysical
28514442
PBX2_HUMANPBX2physical
28514442
PKNX1_HUMANPKNOX1physical
28514442
PKNX2_HUMANPKNOX2physical
28514442
MEIS1_HUMANMEIS1physical
28514442
PBX3_HUMANPBX3physical
28514442
KLHL8_HUMANKLHL8physical
28514442
CE170_HUMANCEP170physical
28514442
MK09_HUMANMAPK9physical
28514442
NFM_HUMANNEFMphysical
28514442
MOCS1_HUMANMOCS1physical
28514442
PBX1_HUMANPBX1physical
28514442
PLCG1_HUMANPLCG1physical
28514442
STXB4_HUMANSTXBP4physical
28514442
DCTN6_HUMANDCTN6physical
28514442
ARMC8_HUMANARMC8physical
28514442
GID4_HUMANGID4physical
28514442
DCTN5_HUMANDCTN5physical
28514442
MAEA_HUMANMAEAphysical
28514442
ZMY19_HUMANZMYND19physical
28514442
CRTAP_HUMANCRTAPphysical
28514442
MKLN1_HUMANMKLN1physical
28514442
RMD5A_HUMANRMND5Aphysical
28514442
FGFR2_HUMANFGFR2physical
28514442
CTU2_HUMANCTU2physical
28514442
RBP10_HUMANRANBP10physical
28514442
WDR26_HUMANWDR26physical
28514442
BCAT1_HUMANBCAT1physical
28514442
ARP10_HUMANACTR10physical
28514442
DCAM_HUMANAMD1physical
28514442
P4R3A_HUMANSMEK1physical
28514442
HAUS4_HUMANHAUS4physical
28514442
AIP_HUMANAIPphysical
28514442
NDUS1_HUMANNDUFS1physical
28514442
GID8_HUMANGID8physical
28514442
RCBT2_HUMANRCBTB2physical
28514442
RN138_HUMANRNF138physical
28514442
MTFR1_HUMANMTFR1physical
28514442
LIPA1_HUMANPPFIA1physical
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 CC120_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND MASSSPECTROMETRY.
"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-360, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, 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-331, AND MASSSPECTROMETRY.

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