APC10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: APC10_HUMAN
• UniProt AC: Q9UM13
• Protein Name: Anaphase-promoting complex subunit 10
• Gene Name: ANAPC10
• Organism: Homo sapiens (Human).
• Sequence Length: 185
• 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..
• Protein Sequence: MTTPNKTPPGADPKQLERTGTVREIGSQAVWSLSSCKPGFGVDQLRDDNLETYWQSDGSQPHLVNIQFRRKTTVKTLCIYADYKSDESYTPSKISVRVGNNFHNLQEIRQLELVEPSGWIHVPLTDNHKKPTRTFMIQIAVLANHQNGRDTHMRQIKIYTPVEESSIGKFPRCTTIDFMMYRSIR

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
2	Phosphorylation	------MTTPNKTPP ------CCCCCCCCC	51.46	22199227
2	Acetylation	------MTTPNKTPP ------CCCCCCCCC	51.46	22814378
3	Phosphorylation	-----MTTPNKTPPG -----CCCCCCCCCC	24.46	25850435
6	Ubiquitination	--MTTPNKTPPGADP --CCCCCCCCCCCCH	64.71	21906983
7	Phosphorylation	-MTTPNKTPPGADPK -CCCCCCCCCCCCHH	41.16	22199227
14	Ubiquitination	TPPGADPKQLERTGT CCCCCCHHHHCCCEE	68.97	22817900
17	Ubiquitination	GADPKQLERTGTVRE CCCHHHHCCCEEEEE	45.78	21890473
25	Ubiquitination	RTGTVREIGSQAVWS CCEEEEEEHHHHEEE	4.51	21890473
40	Ubiquitination	LSSCKPGFGVDQLRD CCCCCCCCCCHHHCC	13.46	21890473
44	Ubiquitination	KPGFGVDQLRDDNLE CCCCCCHHHCCCCCC	35.67	21890473
48	Ubiquitination	GVDQLRDDNLETYWQ CCHHHCCCCCCEEEE	56.00	21890473
52	Ubiquitination	LRDDNLETYWQSDGS HCCCCCCEEEECCCC	32.97	21890473
71	Acetylation	VNIQFRRKTTVKTLC EEEEEECCCEEEEEE	44.27	20167786
72	Phosphorylation	NIQFRRKTTVKTLCI EEEEECCCEEEEEEE	34.70	26074081
73	Phosphorylation	IQFRRKTTVKTLCIY EEEECCCEEEEEEEE	24.04	26074081
76	Phosphorylation	RRKTTVKTLCIYADY ECCCEEEEEEEEEEC	23.64	26074081
80	Phosphorylation	TVKTLCIYADYKSDE EEEEEEEEEECCCCC	7.76	22817900
82	Acetylation	KTLCIYADYKSDESY EEEEEEEECCCCCCC	34.13	-
83	Phosphorylation	TLCIYADYKSDESYT EEEEEEECCCCCCCC	12.29	22817900
88	Phosphorylation	ADYKSDESYTPSKIS EECCCCCCCCCCEEE	39.02	30631047
89	Phosphorylation	DYKSDESYTPSKISV ECCCCCCCCCCEEEE	22.18	27461979
90	Phosphorylation	YKSDESYTPSKISVR CCCCCCCCCCEEEEE	30.30	30576142
92	Phosphorylation	SDESYTPSKISVRVG CCCCCCCCEEEEEEC	34.52	30631047
93	Ubiquitination	DESYTPSKISVRVGN CCCCCCCEEEEEECC	39.96	21906983
104	Ubiquitination	RVGNNFHNLQEIRQL EECCCCCCHHHEEEE	39.00	22817900
127	Ubiquitination	IHVPLTDNHKKPTRT EEEECCCCCCCCCEE	43.58	22817900
131	Ubiquitination	LTDNHKKPTRTFMIQ CCCCCCCCCEEEEEE	31.73	22817900
160	Phosphorylation	MRQIKIYTPVEESSI EEEEEEECCCCHHCC	25.08	-
165	Phosphorylation	IYTPVEESSIGKFPR EECCCCHHCCCCCCC	17.47	24719451
169	Ubiquitination	VEESSIGKFPRCTTI CCHHCCCCCCCCCEE	50.99	22817900
169	Acetylation	VEESSIGKFPRCTTI CCHHCCCCCCCCCEE	50.99	19608861
175	Phosphorylation	GKFPRCTTIDFMMYR CCCCCCCEEEEEEEE	23.36	-
180	Acetylation	CTTIDFMMYRSIR-- CCEEEEEEEECCC--	2.25	19608861
180	Ubiquitination	CTTIDFMMYRSIR-- CCEEEEEEEECCC--	2.25	21890473
181	Phosphorylation	TTIDFMMYRSIR--- CEEEEEEEECCC---	6.88	-
203	Ubiquitination	------------------------- -------------------------		21890473
207	Ubiquitination	----------------------------- -----------------------------		21890473

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

Oops, there are no upstream regulatory protein records of APC10_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of APC10_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 APC10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD2_HUMAN	SMAD2	physical	15144564
SMAD3_HUMAN	SMAD3	physical	15144564
CDC27_HUMAN	CDC27	physical	10498862
CDC16_HUMAN	CDC16	physical	10498862
CDC23_HUMAN	CDC23	physical	22939629
CDC16_HUMAN	CDC16	physical	22939629
APC1_HUMAN	ANAPC1	physical	22939629
CDC27_HUMAN	CDC27	physical	22939629
APC4_HUMAN	ANAPC4	physical	22939629
APC7_HUMAN	ANAPC7	physical	22939629
ANC2_HUMAN	ANAPC2	physical	26344197
APC7_HUMAN	ANAPC7	physical	26344197
CDC26_HUMAN	CDC26	physical	26344197
NP1L4_HUMAN	NAP1L4	physical	26344197
TAF3_HUMAN	TAF3	physical	26344197
UTP15_HUMAN	UTP15	physical	26344197
NUP98_HUMAN	NUP98	physical	27097363
HXD13_HUMAN	HOXD13	physical	27097363
LNP1_HUMAN	LNP1	physical	27097363
HHEX_HUMAN	HHEX	physical	27097363

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-169, AND MASS SPECTROMETRY.
PubMed: 19608861