CCD25_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CCD25_HUMAN
• UniProt AC: Q86WR0
• Protein Name: Coiled-coil domain-containing protein 25
• Gene Name: CCDC25
• Organism: Homo sapiens (Human).
• Sequence Length: 208
• Protein Sequence: MVFYFTSSSVNSSAYTIYMGKDKYENEDLIKHGWPEDIWFHVDKLSSAHVYLRLHKGENIEDIPKEVLMDCAHLVKANSIQGCKMNNVNVVYTPWSNLKKTADMDVGQIGFHRQKDVKIVTVEKKVNEILNRLEKTKVERFPDLAAEKECRDREERNEKKAQIQEMKKREKEEMKKKREMDELRSYSSLMKVENMSSNQDGNDSDEFM

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
4	Phosphorylation	----MVFYFTSSSVN ----CEEEEECCCCC	8.44	24211406
6	Phosphorylation	--MVFYFTSSSVNSS --CEEEEECCCCCCC	19.13	23401153
7	Phosphorylation	-MVFYFTSSSVNSSA -CEEEEECCCCCCCE	15.66	24211406
8	Phosphorylation	MVFYFTSSSVNSSAY CEEEEECCCCCCCEE	34.94	24211406
9	Phosphorylation	VFYFTSSSVNSSAYT EEEEECCCCCCCEEE	25.70	24211406
12	Phosphorylation	FTSSSVNSSAYTIYM EECCCCCCCEEEEEE	17.75	23401153
13	Phosphorylation	TSSSVNSSAYTIYMG ECCCCCCCEEEEEEC	21.79	23401153
15	Phosphorylation	SSVNSSAYTIYMGKD CCCCCCEEEEEECCC	8.80	24211406
16	Phosphorylation	SVNSSAYTIYMGKDK CCCCCEEEEEECCCC	12.83	23401153
18	Phosphorylation	NSSAYTIYMGKDKYE CCCEEEEEECCCCCC	7.63	24211406
23	Ubiquitination	TIYMGKDKYENEDLI EEEECCCCCCCCCHH	58.93	19608861
23	Acetylation	TIYMGKDKYENEDLI EEEECCCCCCCCCHH	58.93	19608861
32	Ubiquitination	ENEDLIKHGWPEDIW CCCCHHHCCCCHHEE	36.23	-
76	Ubiquitination	MDCAHLVKANSIQGC HHHHHHHHHHCCCCC	48.49	-
76	Acetylation	MDCAHLVKANSIQGC HHHHHHHHHHCCCCC	48.49	25953088
84	Acetylation	ANSIQGCKMNNVNVV HHCCCCCCCCCEEEE	52.03	25953088
99	Acetylation	YTPWSNLKKTADMDV EECHHHCCHHCCCCC	52.94	25953088
100	Ubiquitination	TPWSNLKKTADMDVG ECHHHCCHHCCCCCC	52.70	-
101	Phosphorylation	PWSNLKKTADMDVGQ CHHHCCHHCCCCCCC	26.71	28258704
124	Acetylation	VKIVTVEKKVNEILN EEEEEEHHHHHHHHH	58.65	25953088
124	2-Hydroxyisobutyrylation	VKIVTVEKKVNEILN EEEEEEHHHHHHHHH	58.65	-
125	Malonylation	KIVTVEKKVNEILNR EEEEEHHHHHHHHHH	36.47	26320211
167	2-Hydroxyisobutyrylation	KAQIQEMKKREKEEM HHHHHHHHHHHHHHH	48.18	-
185	Phosphorylation	REMDELRSYSSLMKV HHHHHHHHHHHHHHH	41.83	27251275
186	Phosphorylation	EMDELRSYSSLMKVE HHHHHHHHHHHHHHH	8.88	28796482
187	Phosphorylation	MDELRSYSSLMKVEN HHHHHHHHHHHHHHC	20.45	24275569
188	Phosphorylation	DELRSYSSLMKVENM HHHHHHHHHHHHHCC	25.01	28555341
195	Sulfoxidation	SLMKVENMSSNQDGN HHHHHHCCCCCCCCC	2.69	21406390
196	Phosphorylation	LMKVENMSSNQDGND HHHHHCCCCCCCCCC	37.41	28176443
197	Phosphorylation	MKVENMSSNQDGNDS HHHHCCCCCCCCCCC	27.95	28176443
204	Phosphorylation	SNQDGNDSDEFM--- CCCCCCCCCCCC---	42.94	26846344

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CCD25_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CCD25_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CCD25_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GMCL1_HUMAN	GMCL1	physical	25416956
PEPL1_HUMAN	NPEPL1	physical	26344197

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-204, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-204, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-204, AND MASSSPECTROMETRY.
PubMed: 18669648

"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-204, AND MASSSPECTROMETRY.
PubMed: 17081983