APC7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: APC7_HUMAN
• UniProt AC: Q9UJX3
• Protein Name: Anaphase-promoting complex subunit 7
• Gene Name: ANAPC7
• Organism: Homo sapiens (Human).
• Sequence Length: 599
• 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: MDPGDAAILESSLRILYRLFESVLPPLPAALQSRMNVIDHVRDMAAAGLHSNVRLLSSLLLTMSNNNPELFSPPQKYQLLVYHADSLFHDKEYRNAVSKYTMALQQKKALSKTSKVRPSTGNSASTPQSQCLPSEIEVKYKMAECYTMLKQDKDAIAILDGIPSRQRTPKINMMLANLYKKAGQERPSVTSYKEVLRQCPLALDAILGLLSLSVKGAEVASMTMNVIQTVPNLDWLSVWIKAYAFVHTGDNSRAISTICSLEKKSLLRDNVDLLGSLADLYFRAGDNKNSVLKFEQAQMLDPYLIKGMDVYGYLLAREGRLEDVENLGCRLFNISDQHAEPWVVSGCHSFYSKRYSRALYLGAKAIQLNSNSVQALLLKGAALRNMGRVQEAIIHFREAIRLAPCRLDCYEGLIECYLASNSIREAMVMANNVYKTLGANAQTLTLLATVCLEDPVTQEKAKTLLDKALTQRPDYIKAVVKKAELLSREQKYEDGIALLRNALANQSDCVLHRILGDFLVAVNEYQEAMDQYSIALSLDPNDQKSLEGMQKMEKEESPTDATQEEDVDDMEGSGEEGDLEGSDSEAAQWADQEQWFGMQ

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
17	Phosphorylation	ESSLRILYRLFESVL HHHHHHHHHHHHHCC	11.69	14657031
23	Phosphorylation	LYRLFESVLPPLPAA HHHHHHHCCCCCCHH	7.97	14657031
30	Phosphorylation	VLPPLPAALQSRMNV CCCCCCHHHHHHCHH	12.28	14657031
51	Phosphorylation	MAAAGLHSNVRLLSS HHHCCCHHHHHHHHH	41.90	14657031
57	Phosphorylation	HSNVRLLSSLLLTMS HHHHHHHHHHHHHCC	24.43	14657031
58	Phosphorylation	SNVRLLSSLLLTMSN HHHHHHHHHHHHCCC	24.01	-
62	Phosphorylation	LLSSLLLTMSNNNPE HHHHHHHHCCCCCHH	20.65	-
64	Phosphorylation	SSLLLTMSNNNPELF HHHHHHCCCCCHHHC	31.04	14657031
77	Phosphorylation	LFSPPQKYQLLVYHA HCCCCHHEEEEEEEH	10.11	25884760
91	Phosphorylation	ADSLFHDKEYRNAVS HHHHCCCHHHHHHHH	48.34	22067460
91	Ubiquitination	ADSLFHDKEYRNAVS HHHHCCCHHHHHHHH	48.34	-
91	Acetylation	ADSLFHDKEYRNAVS HHHHCCCHHHHHHHH	48.34	26051181
92	Phosphorylation	DSLFHDKEYRNAVSK HHHCCCHHHHHHHHH	56.64	22067460
98	Phosphorylation	KEYRNAVSKYTMALQ HHHHHHHHHHHHHHH	19.96	28348404
99 (in isoform 2)	Ubiquitination	-	37.83	-
99	Ubiquitination	EYRNAVSKYTMALQQ HHHHHHHHHHHHHHH	37.83	21906983
100	Phosphorylation	YRNAVSKYTMALQQK HHHHHHHHHHHHHHH	8.34	20049867
101	Phosphorylation	RNAVSKYTMALQQKK HHHHHHHHHHHHHHH	10.33	28348404
107	Ubiquitination	YTMALQQKKALSKTS HHHHHHHHHHHHCCC	27.36	-
107	2-Hydroxyisobutyrylation	YTMALQQKKALSKTS HHHHHHHHHHHHCCC	27.36	-
107	Malonylation	YTMALQQKKALSKTS HHHHHHHHHHHHCCC	27.36	26320211
107	Acetylation	YTMALQQKKALSKTS HHHHHHHHHHHHCCC	27.36	25953088
111	Phosphorylation	LQQKKALSKTSKVRP HHHHHHHHCCCCCCC	38.45	30631047
115	Ubiquitination	KALSKTSKVRPSTGN HHHHCCCCCCCCCCC	47.71	-
119	Phosphorylation	KTSKVRPSTGNSAST CCCCCCCCCCCCCCC	38.08	25159151
120	Phosphorylation	TSKVRPSTGNSASTP CCCCCCCCCCCCCCC	42.96	29978859
123	Phosphorylation	VRPSTGNSASTPQSQ CCCCCCCCCCCCHHH	25.58	25159151
125	Phosphorylation	PSTGNSASTPQSQCL CCCCCCCCCCHHHCC	40.20	25159151
126	Phosphorylation	STGNSASTPQSQCLP CCCCCCCCCHHHCCC	25.68	25159151
129	Phosphorylation	NSASTPQSQCLPSEI CCCCCCHHHCCCCHH	24.86	29978859
131	Glutathionylation	ASTPQSQCLPSEIEV CCCCHHHCCCCHHHH	7.95	22555962
134	Phosphorylation	PQSQCLPSEIEVKYK CHHHCCCCHHHHHHH	37.95	29396449
139	Acetylation	LPSEIEVKYKMAECY CCCHHHHHHHHHHHH	26.77	26051181
139	Ubiquitination	LPSEIEVKYKMAECY CCCHHHHHHHHHHHH	26.77	-
153	Ubiquitination	YTMLKQDKDAIAILD HHHHHHCHHHHHHCC	46.71	21906983
181	Ubiquitination	MLANLYKKAGQERPS HHHHHHHHHCCCCCC	44.16	-
188	Phosphorylation	KAGQERPSVTSYKEV HHCCCCCCCCCHHHH	44.22	21406692
190	Phosphorylation	GQERPSVTSYKEVLR CCCCCCCCCHHHHHH	30.58	21406692
191	Phosphorylation	QERPSVTSYKEVLRQ CCCCCCCCHHHHHHH	31.86	21406692
192	Phosphorylation	ERPSVTSYKEVLRQC CCCCCCCHHHHHHHC	11.21	21406692
193	Ubiquitination	RPSVTSYKEVLRQCP CCCCCCHHHHHHHCH	40.91	21906983
211	Phosphorylation	DAILGLLSLSVKGAE HHHHHHHHHHCCCHH	24.52	24719451
263	Malonylation	STICSLEKKSLLRDN HHHHHHHHHHHHCCC	53.61	26320211
263	Ubiquitination	STICSLEKKSLLRDN HHHHHHHHHHHHCCC	53.61	19608861
263	Acetylation	STICSLEKKSLLRDN HHHHHHHHHHHHCCC	53.61	23954790
264	Ubiquitination	TICSLEKKSLLRDNV HHHHHHHHHHHCCCH	36.64	-
265	Phosphorylation	ICSLEKKSLLRDNVD HHHHHHHHHHCCCHH	43.64	24719451
288	Ubiquitination	YFRAGDNKNSVLKFE HHCCCCCCCCEEEHH	56.17	21906983
288 (in isoform 2)	Ubiquitination	-	56.17	-
293 (in isoform 2)	Ubiquitination	-	44.70	-
293	Ubiquitination	DNKNSVLKFEQAQML CCCCCEEEHHHHHCC	44.70	21906983
306	Ubiquitination	MLDPYLIKGMDVYGY CCCHHHHCCCCHHHH	45.66	-
311	Phosphorylation	LIKGMDVYGYLLARE HHCCCCHHHHHHHHC	8.86	-
313	Phosphorylation	KGMDVYGYLLAREGR CCCCHHHHHHHHCCC	4.85	-
353	Acetylation	GCHSFYSKRYSRALY CCCHHHCHHHHHHHH	43.93	26051181
353	Ubiquitination	GCHSFYSKRYSRALY CCCHHHCHHHHHHHH	43.93	-
360	Phosphorylation	KRYSRALYLGAKAIQ HHHHHHHHHHCCEEE	11.34	28152594
364	Ubiquitination	RALYLGAKAIQLNSN HHHHHHCCEEECCCH	44.20	-
364 (in isoform 2)	Ubiquitination	-	44.20	-
364	Acetylation	RALYLGAKAIQLNSN HHHHHHCCEEECCCH	44.20	26051181
379	Acetylation	SVQALLLKGAALRNM HHHHHHHHHHHHHHC	46.61	23236377
379 (in isoform 2)	Ubiquitination	-	46.61	-
379	Ubiquitination	SVQALLLKGAALRNM HHHHHHHHHHHHHHC	46.61	21906983
420	Phosphorylation	LIECYLASNSIREAM HHHHHHHCCCHHHHH	28.63	-
422	Phosphorylation	ECYLASNSIREAMVM HHHHHCCCHHHHHHH	22.11	-
434	Phosphorylation	MVMANNVYKTLGANA HHHHHHHHHHCCCCH	10.61	23917254
460	Ubiquitination	EDPVTQEKAKTLLDK CCCCCHHHHHHHHHH	45.42	-
462	Ubiquitination	PVTQEKAKTLLDKAL CCCHHHHHHHHHHHH	51.26	-
467	Malonylation	KAKTLLDKALTQRPD HHHHHHHHHHHCCCH	45.31	32601280
467	Ubiquitination	KAKTLLDKALTQRPD HHHHHHHHHHHCCCH	45.31	21906983
467	Acetylation	KAKTLLDKALTQRPD HHHHHHHHHHHCCCH	45.31	23749302
467 (in isoform 2)	Ubiquitination	-	45.31	-
475	Phosphorylation	ALTQRPDYIKAVVKK HHHCCCHHHHHHHHH	13.65	-
477	Ubiquitination	TQRPDYIKAVVKKAE HCCCHHHHHHHHHHH	28.97	21906983
477 (in isoform 2)	Ubiquitination	-	28.97	-
482	Ubiquitination	YIKAVVKKAELLSRE HHHHHHHHHHHHCCH	35.17	-
487	Phosphorylation	VKKAELLSREQKYED HHHHHHHCCHHHHHH	46.53	24719451
491	Ubiquitination	ELLSREQKYEDGIAL HHHCCHHHHHHHHHH	45.94	21906983
509	Glutathionylation	ALANQSDCVLHRILG HHCCCCHHHHHHHHH	4.20	22555962
551	Ubiquitination	KSLEGMQKMEKEESP HHHHHHHHHHHCCCC	39.88	-
557	Phosphorylation	QKMEKEESPTDATQE HHHHHCCCCCCCCCH	33.90	26074081
559	Phosphorylation	MEKEESPTDATQEED HHHCCCCCCCCCHHH	47.77	26074081

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
17	S	Phosphorylation	Kinase	PLK1	P53350	PhosphoELM
23	S	Phosphorylation	Kinase	PLK1	P53350	PhosphoELM
30	S	Phosphorylation	Kinase	PLK1	P53350	PhosphoELM
51	S	Phosphorylation	Kinase	PLK1	P53350	PSP
57	S	Phosphorylation	Kinase	PLK1	P53350	PSP
64	S	Phosphorylation	Kinase	PLK1	P53350	PSP
86	S	Phosphorylation	Kinase	AURKA	O14965	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of APC7_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 APC7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EP300_HUMAN	EP300	physical	16319895
CBP_HUMAN	CREBBP	physical	16319895
APC7_HUMAN	ANAPC7	physical	19091741
MDC1_HUMAN	MDC1	physical	19826003
CDC20_HUMAN	CDC20	physical	19826003
CDC27_HUMAN	CDC27	physical	22939629
CDC16_HUMAN	CDC16	physical	22939629
TRI33_HUMAN	TRIM33	physical	23160376
CDC27_HUMAN	CDC27	physical	23160376
APC5_HUMAN	ANAPC5	physical	23160376
BUB1B_HUMAN	BUB1B	physical	23160376
E2F1_HUMAN	E2F1	physical	25368385
APC16_HUMAN	ANAPC16	physical	25490258
CDC27_HUMAN	CDC27	physical	25490258
NP1L4_HUMAN	NAP1L4	physical	26344197
CDC16_HUMAN	CDC16	physical	27173435
CDC27_HUMAN	CDC27	physical	27173435
CDC23_HUMAN	CDC23	physical	27173435

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.