CCD97_HUMAN - dbPTM
CCD97_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCD97_HUMAN
UniProt AC Q96F63
Protein Name Coiled-coil domain-containing protein 97
Gene Name CCDC97
Organism Homo sapiens (Human).
Sequence Length 343
Subcellular Localization
Protein Description
Protein Sequence MEAVATATAAKEPDKGCIEPGPGHWGELSRTPVPSKPQDKVEAAEATPVALDSDTSGAENAAVSAMLHAVAASRLPVCSQQQGEPDLTEHEKVAILAQLYHEKPLVFLERFRTGLREEHLACFGHVRGDHRADFYCAEVARQGTARPRTLRTRLRNRRYAALRELIQGGEYFSDEQMRFRAPLLYEQYIGQYLTQEELSARTPTHQPPKPGSPGRPACPLSNLLLQSYEERELQQRLLQQQEEEEACLEEEEEEEDSDEEDQRSGKDSEAWVPDSEERLILREEFTSRMHQRFLDGKDGDFDYSTVDDNPDFDNLDIVARDEEERYFDEEEPEDAPSPELDGD
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
1Acetylation-------MEAVATAT
-------CCCCCHHH		7.2319413330
11AcetylationVATATAAKEPDKGCI
CCHHHCCCCCCCCCC		68.2826051181
15AcetylationTAAKEPDKGCIEPGP
HCCCCCCCCCCCCCC		67.4126051181
27UbiquitinationPGPGHWGELSRTPVP
CCCCCCHHCCCCCCC		38.0829967540
29PhosphorylationPGHWGELSRTPVPSK
CCCCHHCCCCCCCCC		29.7925159151
31PhosphorylationHWGELSRTPVPSKPQ
CCHHCCCCCCCCCCH		25.8430576142
35PhosphorylationLSRTPVPSKPQDKVE
CCCCCCCCCCHHHCH		58.1427251275
36UbiquitinationSRTPVPSKPQDKVEA
CCCCCCCCCHHHCHH		40.4029967540
47PhosphorylationKVEAAEATPVALDSD
HCHHHHCCCEEECCC		15.1420068231
53PhosphorylationATPVALDSDTSGAEN
CCCEEECCCCCCHHH		43.5728348404
55PhosphorylationPVALDSDTSGAENAA
CEEECCCCCCHHHHH		32.7728348404
56PhosphorylationVALDSDTSGAENAAV
EEECCCCCCHHHHHH		40.7828348404
92UbiquitinationPDLTEHEKVAILAQL
CCCCHHHHHHHHHHH		38.5829967540
127MethylationLACFGHVRGDHRADF
HHHHCCCCCCCCHHC		38.86-
135PhosphorylationGDHRADFYCAEVARQ
CCCCHHCHHHHHHHC		7.4129978859
147PhosphorylationARQGTARPRTLRTRL
HHCCCCCCCHHHHHH		31.0132142685
149PhosphorylationQGTARPRTLRTRLRN
CCCCCCCHHHHHHHC		24.23-
159PhosphorylationTRLRNRRYAALRELI
HHHHCHHHHHHHHHH		7.93-
178MethylationYFSDEQMRFRAPLLY
CCCHHHHHHCHHHHH		20.00-
185PhosphorylationRFRAPLLYEQYIGQY
HHCHHHHHHHHHHHH		14.52-
188PhosphorylationAPLLYEQYIGQYLTQ
HHHHHHHHHHHHCCH		8.62-
192PhosphorylationYEQYIGQYLTQEELS
HHHHHHHHCCHHHHH		13.4033259812
194PhosphorylationQYIGQYLTQEELSAR
HHHHHHCCHHHHHCC		29.06-
199PhosphorylationYLTQEELSARTPTHQ
HCCHHHHHCCCCCCC		20.9826074081
201UbiquitinationTQEELSARTPTHQPP
CHHHHHCCCCCCCCC		37.5533845483
202PhosphorylationQEELSARTPTHQPPK
HHHHHCCCCCCCCCC		32.0523401153
204PhosphorylationELSARTPTHQPPKPG
HHHCCCCCCCCCCCC		32.3123927012
212PhosphorylationHQPPKPGSPGRPACP
CCCCCCCCCCCCCCH		32.4823927012
221PhosphorylationGRPACPLSNLLLQSY
CCCCCHHHHHHHHHH		15.5823927012
227PhosphorylationLSNLLLQSYEERELQ
HHHHHHHHHHHHHHH		34.1923927012
228PhosphorylationSNLLLQSYEERELQQ
HHHHHHHHHHHHHHH		14.6223927012
232UbiquitinationLQSYEERELQQRLLQ
HHHHHHHHHHHHHHH		54.9629967540
257PhosphorylationEEEEEEDSDEEDQRS
HHHHHCCCCHHHHHC		50.6419664994
264PhosphorylationSDEEDQRSGKDSEAW
CCHHHHHCCCCCCCC		44.5630278072
266UbiquitinationEEDQRSGKDSEAWVP
HHHHHCCCCCCCCCC		60.3733845483
268PhosphorylationDQRSGKDSEAWVPDS
HHHCCCCCCCCCCCH		32.4723663014
272PhosphorylationGKDSEAWVPDSEERL
CCCCCCCCCCHHHHH		4.9432142685
275PhosphorylationSEAWVPDSEERLILR
CCCCCCCHHHHHHHH		34.9725159151
297UbiquitinationHQRFLDGKDGDFDYS
HHHHHCCCCCCCCCC		59.2029967540
303PhosphorylationGKDGDFDYSTVDDNP
CCCCCCCCCCCCCCC		13.2627642862
304PhosphorylationKDGDFDYSTVDDNPD
CCCCCCCCCCCCCCC		24.6521712546
305PhosphorylationDGDFDYSTVDDNPDF
CCCCCCCCCCCCCCC		23.0221712546
320UbiquitinationDNLDIVARDEEERYF
CCCCEEECCHHHHHC		40.7627667366
326PhosphorylationARDEEERYFDEEEPE
ECCHHHHHCCCCCCC		20.7528176443
337PhosphorylationEEPEDAPSPELDGD-
CCCCCCCCCCCCCC-		32.5025159151
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 CCD97_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCD97_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 CCD97_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SF3B3_HUMANSF3B3physical
26344197
SF3B5_HUMANSF3B5physical
26344197
PAXI1_HUMANPAXIP1physical
28514442
TTC33_HUMANTTC33physical
28514442
SF3A2_HUMANSF3A2physical
28514442
SF3A3_HUMANSF3A3physical
28514442
SF3A1_HUMANSF3A1physical
28514442
SF3B1_HUMANSF3B1physical
28514442
CIZ1_HUMANCIZ1physical
28514442
ATF1_HUMANATF1physical
28514442
SF3B4_HUMANSF3B4physical
28514442
U2AFM_HUMANZRSR2physical
28514442
PI51A_HUMANPIP5K1Aphysical
28514442
SF3B3_HUMANSF3B3physical
28514442
SF3B2_HUMANSF3B2physical
28514442
SF3B6_HUMANSF3B6physical
28514442
JUN_HUMANJUNphysical
28514442
SF3B5_HUMANSF3B5physical
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 CCD97_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-257, AND MASS SPECTROMETRY.
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-337, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-257, AND MASS SPECTROMETRY.
"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-257; SER-275 ANDSER-337, AND MASS SPECTROMETRY.
"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-337, AND MASSSPECTROMETRY.

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