APC4_HUMAN - dbPTM
APC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APC4_HUMAN
UniProt AC Q9UJX5
Protein Name Anaphase-promoting complex subunit 4
Gene Name ANAPC4
Organism Homo sapiens (Human).
Sequence Length 808
Subcellular Localization
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 MLRFPTCFPSFRVVGEKQLPQEIIFLVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENTGKEVTCLAWRPDGKLLAFALADTKKIVLCDVEKPESLHSFSVEAPVSCMHWMEVTVESSVLTSFYNAEDESNLLLPKLPTLPKNYSNTSKIFSEENSDEIIKLLGDVRLNILVLGGSSGFIELYAYGMFKIARVTGIAGTCLALCLSSDLKSLSVVTEVSTNGASEVSYFQLETNLLYSFLPEVTRMARKFTHISALLQYINLSLTCMCEAWEEILMQMDSRLTKFVQEKNTTTSVQDEFMHLLLWGKASAELQTLLMNQLTVKGLKKLGQSIESSYSSIQKLVISHLQSGSESLLYHLSELKGMASWKQKYEPLGLDAAGIEEAITAVGSFILKANELLQVIDSSMKNFKAFFRWLYVAMLRMTEDHVLPELNKMTQKDITFVAEFLTEHFNEAPDLYNRKGKYFNVERVGQYLKDEDDDLVSPPNTEGNQWYDFLQNSSHLKESPLLFPYYPRKSLHFVKRRMENIIDQCLQKPADVIGKSMNQAICIPLYRDTRSEDSTRRLFKFPFLWNNKTSNLHYLLFTILEDSLYKMCILRRHTDISQSVSNGLIAIKFGSFTYATTEKVRRSIYSCLDAQFYDDETVTVVLKDTVGREGRDRLLVQLPLSLVYNSEDSAEYQFTGTYSTRLDEQCSAIPTRTMHFEKHWRLLESMKAQYVAGNGFRKVSCVLSSNLRHVRVFEMDIDDEWELDESSDEEEEASNKPVKIKEEVLSESEAENQQAGAAALAPEIVIKVEKLDPELDS
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
3Methylation-----MLRFPTCFPS
-----CCCCCCCCCC
33.91-
29PhosphorylationEIIFLVWSPKRDLIA
EEEEEEECCHHHHHH
17.0524719451
87PhosphorylationLAFALADTKKIVLCD
EEEEEECCCEEEEEE
28.7321406692
89UbiquitinationFALADTKKIVLCDVE
EEEECCCEEEEEECC
39.89-
147UbiquitinationPKLPTLPKNYSNTSK
CCCCCCCCCCCCHHH
72.18-
147UbiquitinationPKLPTLPKNYSNTSK
CCCCCCCCCCCCHHH
72.18-
154UbiquitinationKNYSNTSKIFSEENS
CCCCCHHHHCCCCCH
45.81-
154UbiquitinationKNYSNTSKIFSEENS
CCCCCHHHHCCCCCH
45.81-
199PhosphorylationMFKIARVTGIAGTCL
HHHHHHHHCCHHHHH
19.81-
204PhosphorylationRVTGIAGTCLALCLS
HHHCCHHHHHHHHHC
8.70-
211PhosphorylationTCLALCLSSDLKSLS
HHHHHHHCCCCCCCE
22.32-
212PhosphorylationCLALCLSSDLKSLSV
HHHHHHCCCCCCCEE
33.73-
256PhosphorylationTRMARKFTHISALLQ
HHHHHHHHHHHHHHH
22.7225072903
259PhosphorylationARKFTHISALLQYIN
HHHHHHHHHHHHHHH
12.7825072903
264PhosphorylationHISALLQYINLSLTC
HHHHHHHHHHHHHHH
7.5525072903
268PhosphorylationLLQYINLSLTCMCEA
HHHHHHHHHHHHHHH
19.6925072903
270PhosphorylationQYINLSLTCMCEAWE
HHHHHHHHHHHHHHH
8.5325072903
285PhosphorylationEILMQMDSRLTKFVQ
HHHHHCHHHHHHHHH
24.6925072903
332UbiquitinationLTVKGLKKLGQSIES
CHHHHHHHHHHHHHH
63.99-
332UbiquitinationLTVKGLKKLGQSIES
CHHHHHHHHHHHHHH
63.99-
336PhosphorylationGLKKLGQSIESSYSS
HHHHHHHHHHHCCHH
26.9030622161
339PhosphorylationKLGQSIESSYSSIQK
HHHHHHHHCCHHHHH
32.6730622161
340PhosphorylationLGQSIESSYSSIQKL
HHHHHHHCCHHHHHH
19.0830622161
341PhosphorylationGQSIESSYSSIQKLV
HHHHHHCCHHHHHHH
18.7330622161
342PhosphorylationQSIESSYSSIQKLVI
HHHHHCCHHHHHHHH
23.9430622161
343PhosphorylationSIESSYSSIQKLVIS
HHHHCCHHHHHHHHH
22.3230622161
371PhosphorylationSELKGMASWKQKYEP
HHHCCCHHHHHHCCC
26.3924719451
422PhosphorylationKAFFRWLYVAMLRMT
HHHHHHHHHHHHHHC
4.5329396449
429PhosphorylationYVAMLRMTEDHVLPE
HHHHHHHCCCCCHHH
31.6521406692
441PhosphorylationLPELNKMTQKDITFV
HHHHHHCCHHHHHHH
33.7927251275
446PhosphorylationKMTQKDITFVAEFLT
HCCHHHHHHHHHHHH
23.3827251275
468UbiquitinationDLYNRKGKYFNVERV
CHHHCCCCCCCHHHH
50.1021890473
468AcetylationDLYNRKGKYFNVERV
CHHHCCCCCCCHHHH
50.1025953088
468 (in isoform 1)Ubiquitination-50.1021890473
468 (in isoform 2)Ubiquitination-50.1021890473
469PhosphorylationLYNRKGKYFNVERVG
HHHCCCCCCCHHHHC
14.7322817900
469UbiquitinationLYNRKGKYFNVERVG
HHHCCCCCCCHHHHC
14.73-
478PhosphorylationNVERVGQYLKDEDDD
CHHHHCHHCCCCCCC
15.1322115753
488PhosphorylationDEDDDLVSPPNTEGN
CCCCCCCCCCCCCCC
41.7722199227
492PhosphorylationDLVSPPNTEGNQWYD
CCCCCCCCCCCHHHH
51.5522199227
498PhosphorylationNTEGNQWYDFLQNSS
CCCCCHHHHHHHCCC
6.2528796482
508UbiquitinationLQNSSHLKESPLLFP
HHCCCCCCCCCCCCC
51.20-
510PhosphorylationNSSHLKESPLLFPYY
CCCCCCCCCCCCCCC
21.1828674419
516PhosphorylationESPLLFPYYPRKSLH
CCCCCCCCCCHHHHH
20.83-
520UbiquitinationLFPYYPRKSLHFVKR
CCCCCCHHHHHHHHH
53.52-
521UbiquitinationFPYYPRKSLHFVKRR
CCCCCHHHHHHHHHH
28.49-
526UbiquitinationRKSLHFVKRRMENII
HHHHHHHHHHHHHHH
33.09-
543 (in isoform 2)Phosphorylation-7.2623090842
625PhosphorylationIKFGSFTYATTEKVR
EEECCEEEECCHHHH
10.43-
627PhosphorylationFGSFTYATTEKVRRS
ECCEEEECCHHHHHH
25.69-
628PhosphorylationGSFTYATTEKVRRSI
CCEEEECCHHHHHHH
26.15-
630AcetylationFTYATTEKVRRSIYS
EEEECCHHHHHHHHH
38.667695573
736PhosphorylationKVSCVLSSNLRHVRV
EEEEEEECCCCEEEE
35.4018452278
757PhosphorylationDEWELDESSDEEEEA
CCCCCCCCCCHHHHH
42.6324260401
758PhosphorylationEWELDESSDEEEEAS
CCCCCCCCCHHHHHH
47.1722496350
765PhosphorylationSDEEEEASNKPVKIK
CCHHHHHHCCCCCCH
48.9827732954
772SumoylationSNKPVKIKEEVLSES
HCCCCCCHHHHHCHH
41.95-
772SumoylationSNKPVKIKEEVLSES
HCCCCCCHHHHHCHH
41.9528112733
777PhosphorylationKIKEEVLSESEAENQ
CCHHHHHCHHHHHHH
44.2329255136
779PhosphorylationKEEVLSESEAENQQA
HHHHHCHHHHHHHHH
38.4429255136
798SumoylationLAPEIVIKVEKLDPE
HCCEEEEEEEECCCC
33.1928112733
798SumoylationLAPEIVIKVEKLDPE
HCCEEEEEEEECCCC
33.19-

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
779SPhosphorylationKinaseCDK1P06493
PSP
779SPhosphorylationKinasePLK1P53350
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APC4_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
468Ubiquitination465 (3)RQ;Lrs34811474
  • Intelligence (MTAG)
29326435

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APC15_HUMANANAPC15physical
21926987
CDC27_HUMANCDC27physical
21926987
CDC16_HUMANCDC16physical
21926987
APC7_HUMANANAPC7physical
21926987
APC11_HUMANANAPC11physical
21926987
CDC20_HUMANCDC20physical
21926987
BUB1B_HUMANBUB1Bphysical
21926987
BUB3_HUMANBUB3physical
21926987
MD2L1_HUMANMAD2L1physical
21926987
CDC27_HUMANCDC27physical
21336306
APC4_HUMANANAPC4physical
21336306
CDC20_HUMANCDC20physical
21336306
BUB1B_HUMANBUB1Bphysical
21336306
CCNA2_HUMANCCNA2physical
21336306
CCNB1_HUMANCCNB1physical
21336306
MD2L1_HUMANMAD2L1physical
21335556
CDC27_HUMANCDC27physical
21335556
CDC16_HUMANCDC16physical
21335556
CDC20_HUMANCDC20physical
21335556
CDC20_HUMANCDC20physical
18471975
CDC27_HUMANCDC27physical
18471975
APC5_HUMANANAPC5physical
22939629
CDC27_HUMANCDC27physical
22939629
CDC16_HUMANCDC16physical
22939629
CDC23_HUMANCDC23physical
22939629
APC7_HUMANANAPC7physical
22939629
TRI33_HUMANTRIM33physical
23160376
APC15_HUMANANAPC15physical
23160376
MD2L1_HUMANMAD2L1physical
23160376
BUB3_HUMANBUB3physical
23160376
BUB1B_HUMANBUB1Bphysical
23160376
CDC20_HUMANCDC20physical
23160376
APC1_HUMANANAPC1physical
23078409
APC10_HUMANANAPC10physical
23078409
APC11_HUMANANAPC11physical
23078409
APC13_HUMANANAPC13physical
23078409
APC15_HUMANANAPC15physical
23078409
APC16_HUMANANAPC16physical
23078409
ANC2_HUMANANAPC2physical
23078409
APC5_HUMANANAPC5physical
23078409
APC7_HUMANANAPC7physical
23078409
CDC16_HUMANCDC16physical
23078409
CDC20_HUMANCDC20physical
23078409
CDC23_HUMANCDC23physical
23078409
CDC26_HUMANCDC26physical
23078409
CDC27_HUMANCDC27physical
23078409
FZR1_HUMANFZR1physical
23078409
APC1_HUMANANAPC1physical
25043029
APC10_HUMANANAPC10physical
25043029
APC11_HUMANANAPC11physical
25043029
APC13_HUMANANAPC13physical
25043029
APC16_HUMANANAPC16physical
25043029
ANC2_HUMANANAPC2physical
25043029
APC5_HUMANANAPC5physical
25043029
APC7_HUMANANAPC7physical
25043029
CDC16_HUMANCDC16physical
25043029
CDC20_HUMANCDC20physical
25043029
CDC23_HUMANCDC23physical
25043029
CDC26_HUMANCDC26physical
25043029
CDC27_HUMANCDC27physical
25043029
FZR1_HUMANFZR1physical
25043029
DCPS_HUMANDCPSphysical
25043029
APC15_HUMANANAPC15physical
25043029
NEK2_HUMANNEK2physical
23288039
KI18A_HUMANKIF18Aphysical
23288039
APC7_HUMANANAPC7physical
23288039
APC1_HUMANANAPC1physical
24464857
CDC27_HUMANCDC27physical
24464857
APC4_HUMANANAPC4physical
24464857
BUB1B_HUMANBUB1Bphysical
24464857
CDC20_HUMANCDC20physical
24464857
BUB3_HUMANBUB3physical
24464857
ANC2_HUMANANAPC2physical
12956947
APC11_HUMANANAPC11physical
12956947
CDC16_HUMANCDC16physical
12956947
APC1_HUMANANAPC1physical
12956947
CDC27_HUMANCDC27physical
12956947
APC5_HUMANANAPC5physical
12956947
APC7_HUMANANAPC7physical
12956947
CDC23_HUMANCDC23physical
12956947
APC10_HUMANANAPC10physical
12956947
CDC27_HUMANCDC27physical
26083744
CDC23_HUMANCDC23physical
26083744
CDC16_HUMANCDC16physical
26083744
APC10_HUMANANAPC10physical
26083744
APC13_HUMANANAPC13physical
26083744
APC15_HUMANANAPC15physical
26083744
FBX5_HUMANFBXO5physical
26083744
ANC2_HUMANANAPC2physical
26083744
APC4_HUMANANAPC4physical
26083744
FZR1_HUMANFZR1physical
26083744
APC5_HUMANANAPC5physical
26083744
APC7_HUMANANAPC7physical
26083744
APC11_HUMANANAPC11physical
26083744
APC1_HUMANANAPC1physical
26083744
APC16_HUMANANAPC16physical
26083744
CDC26_HUMANCDC26physical
26083744
CDC27_HUMANCDC27physical
25490258
APC7_HUMANANAPC7physical
25490258
APC16_HUMANANAPC16physical
25490258
APC1_HUMANANAPC1physical
25490258
ANC2_HUMANANAPC2physical
25490258
APC5_HUMANANAPC5physical
25490258
CDC16_HUMANCDC16physical
25490258
CDC23_HUMANCDC23physical
25490258
APC10_HUMANANAPC10physical
25490258
APC11_HUMANANAPC11physical
25490258
CDC26_HUMANCDC26physical
25490258
APC13_HUMANANAPC13physical
25490258
APC15_HUMANANAPC15physical
25490258
APC10_HUMANANAPC10physical
26344197
APC16_HUMANANAPC16physical
26344197
ANC2_HUMANANAPC2physical
26344197
APC7_HUMANANAPC7physical
26344197
CDC23_HUMANCDC23physical
26344197
CDC26_HUMANCDC26physical
26344197
UBE2S_HUMANUBE2Sphysical
25306923
CDC27_HUMANCDC27physical
25750436
CCNB1_HUMANCCNB1physical
25750436
CDC20_HUMANCDC20physical
25750436
CCNA2_HUMANCCNA2physical
25750436
NEK2_HUMANNEK2physical
25750436
MD2L1_HUMANMAD2L1physical
25750436
APC10_HUMANANAPC10physical
25750436
FBX5_HUMANFBXO5physical
25750436
BUB1B_HUMANBUB1Bphysical
25750436
CDK1_HUMANCDK1physical
25750436
CDC16_HUMANCDC16physical
25723520
CDC26_HUMANCDC26physical
25723520
CDC27_HUMANCDC27physical
25723520
BUB3_HUMANBUB3physical
24151075
CDC20_HUMANCDC20physical
24151075
MD2L1_HUMANMAD2L1physical
24151075
BUB1B_HUMANBUB1Bphysical
24151075
CDC27_HUMANCDC27physical
25673878
CDC20_HUMANCDC20physical
25673878
MD2L1_HUMANMAD2L1physical
25673878
ANC2_HUMANANAPC2physical
25673878
NEK2_HUMANNEK2physical
25673878
FZR1_HUMANFZR1physical
25673878
CDC16_HUMANCDC16physical
25673878
BUB1B_HUMANBUB1Bphysical
25673878
BUB1B_HUMANBUB1Bphysical
26986935
APC7_HUMANANAPC7physical
26986935
CDC20_HUMANCDC20physical
26986935
MD2L1_HUMANMAD2L1physical
26986935
PSMD8_HUMANPSMD8physical
26986935
CDC20_HUMANCDC20physical
23007648
BUB1B_HUMANBUB1Bphysical
23007648
MD2L1_HUMANMAD2L1physical
23007648
CDC27_HUMANCDC27physical
23007648
BUB3_HUMANBUB3physical
23007648
CDC27_HUMANCDC27physical
26960431
NUP98_HUMANNUP98physical
27097363
HXD13_HUMANHOXD13physical
27097363
LNP1_HUMANLNP1physical
27097363
HHEX_HUMANHHEXphysical
27097363
CDC20_HUMANCDC20physical
27097363
BUB1B_HUMANBUB1Bphysical
27097363
BUB3_HUMANBUB3physical
27097363
MD2L1_HUMANMAD2L1physical
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.
Regulatory Network of APC4_HUMAN

loading...

Related Literatures of Post-Translational Modification
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-757 AND SER-758, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779, AND MASSSPECTROMETRY.
"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-777 AND SER-779, ANDMASS SPECTROMETRY.
"Mitotic regulation of the human anaphase-promoting complex byphosphorylation.";
Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,Peters J.-M.;
EMBO J. 22:6598-6609(2003).
Cited for: PHOSPHORYLATION AT TYR-469 AND SER-779.

TOP