CDC26_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CDC26_HUMAN
• UniProt AC: Q8NHZ8
• Protein Name: Anaphase-promoting complex subunit CDC26
• Gene Name: CDC26
• Organism: Homo sapiens (Human).
• Sequence Length: 85
• Subcellular Localization: Nucleus.
• Protein Description: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex..
• Protein Sequence: MLRRKPTRLELKLDDIEEFENIRKDLETRKKQKEDVEVVGGSDGEGAIGLSSDPKSREQMINDRIGYKPQPKPNNRSSQFGSLEF

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
7	Phosphorylation	-MLRRKPTRLELKLD -CCCCCCCCEEEEHH	51.42	26074081
42	Phosphorylation	DVEVVGGSDGEGAIG CCEECCCCCCCCCCC	36.19	19664994
51	Phosphorylation	GEGAIGLSSDPKSRE CCCCCCCCCCHHHHH	27.73	22167270
52	Phosphorylation	EGAIGLSSDPKSREQ CCCCCCCCCHHHHHH	64.08	22167270
56	Phosphorylation	GLSSDPKSREQMIND CCCCCHHHHHHHHHH	46.57	25159151
67	Phosphorylation	MINDRIGYKPQPKPN HHHHCCCCCCCCCCC	19.68	23312004
68	Acetylation	INDRIGYKPQPKPNN HHHCCCCCCCCCCCC	31.78	23749302
77	Phosphorylation	QPKPNNRSSQFGSLE CCCCCCCCCCCCCCC	30.52	25159151
78	Phosphorylation	PKPNNRSSQFGSLEF CCCCCCCCCCCCCCC	26.71	17525332
82	Phosphorylation	NRSSQFGSLEF---- CCCCCCCCCCC----	26.47	17525332

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
7	T	Phosphorylation	Kinase	LATS1	O95835	PSP
7	T	Phosphorylation	Kinase	LATS2	Q9NRM7	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CDC26_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 CDC26_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDC16_HUMAN	CDC16	physical	19668213
APC7_HUMAN	ANAPC7	physical	26344197
CDC16_HUMAN	CDC16	physical	21516116
CDC16_HUMAN	CDC16	physical	25723520
CDC20_HUMAN	CDC20	physical	25723520
MD2L1_HUMAN	MAD2L1	physical	25723520
CDC27_HUMAN	CDC27	physical	25723520
FZR1_HUMAN	FZR1	physical	25723520

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

Phosphorylation

"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-78 AND SER-82, AND MASSSPECTROMETRY.
PubMed: 17525332

"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-42, 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-42, AND MASSSPECTROMETRY.
PubMed: 18669648