APC4_YEAST - dbPTM
APC4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APC4_YEAST
UniProt AC Q04601
Protein Name Anaphase-promoting complex subunit 4
Gene Name APC4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 652
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication..
Protein Sequence MSSPINDYFIDYNPLFPIFATRIAKGLAIYRVSDHARLAVIPIRNINLVANYDWDTTTGKFLSIFFKDGTIRIHDIFKDGRLVSFLRIPSTKISKGIWDRIPLRYEPNNRDFACNIIDDLPKLIRFVKDSKRINIVPYTQPNSLWRGPDEDDLDSNEKLDVHVVFNEGNDKITVFFNGDYAVFLSVDNIENENSLKSIIKVQDGFYQCFYEDGTVQTLNLGPLLQSKSSVNLLNYIMVIKELIGYMLTHLEFINRELATPYLDFVKRLCDEAYGYGKLKSELEALFLLGEISCDLEDWLCNSVGEKNFKRWKYLGCEAYQKTVQILTLIFVPACERIIIYVEKLRAILQAFSIQNKLSYTSDLTAVEVLLKSSQKLLTMTLNSIIGLGRDETLFEKFFIWFNDRLHEALDEDYKLKFQFEDDLYFGYDLLSYFDRILSKKGTEPSSIIDVKLYRDLINSMSDMEKDIAQSNVNSHIQQHILVDLKTDVFAQKYPSSQINLLDAIKLPKHNYIVYLIQVTKHNSAQEPFSEENKKKLYIGTLKDENLGIISKESSVKIPALFKSYRLSSTRFVPNRVHSLLRDIGLSDSNYHSSHVTDYRGENYENEEDDGTIAIPAYIRENRENDDFIACTAKVSVDGRSASLVFPKEKQNV
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
3Phosphorylation-----MSSPINDYFI
-----CCCCCCCCCC
28.6228889911
8PhosphorylationMSSPINDYFIDYNPL
CCCCCCCCCCCCCCC
9.6528889911
12PhosphorylationINDYFIDYNPLFPIF
CCCCCCCCCCCHHHH
17.5428889911
21PhosphorylationPLFPIFATRIAKGLA
CCHHHHHHHHHHCCE
16.3228889911
92AcetylationFLRIPSTKISKGIWD
EEEECCCCCCCCCHH
49.6924489116
442PhosphorylationRILSKKGTEPSSIID
HHHHCCCCCCCCCCC
54.3127214570
523PhosphorylationIQVTKHNSAQEPFSE
EEECCCCCCCCCCCH
30.9230377154
568PhosphorylationFKSYRLSSTRFVPNR
HCEECCCCCCCCCHH
28.3519779198
569PhosphorylationKSYRLSSTRFVPNRV
CEECCCCCCCCCHHH
25.4219779198
640PhosphorylationKVSVDGRSASLVFPK
EEEECCCEEEEECCH
27.9527017623

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

Oops, there are no upstream regulatory protein records of APC4_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APC4_YEAST !!

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

Oops, there are no SNP-PTM records of APC4_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC16_YEASTCDC16physical
15060174
SWM1_YEASTSWM1physical
15060174
APC2_YEASTAPC2physical
15060174
APC1_YEASTAPC1physical
15060174
APC4_YEASTAPC4physical
15060174
CDC27_YEASTCDC27physical
15060174
APC5_YEASTAPC5physical
15060174
CDC23_YEASTCDC23physical
15060174
MND2_YEASTMND2physical
15060174
APC9_YEASTAPC9physical
15060174
APC10_YEASTDOC1physical
15060174
APC11_YEASTAPC11physical
15060174
CDC26_YEASTCDC26physical
15060174
SWM1_YEASTSWM1physical
12477395
MND2_YEASTMND2physical
12477395
APC1_YEASTAPC1physical
12477395
APC2_YEASTAPC2physical
12477395
CDC27_YEASTCDC27physical
12477395
APC4_YEASTAPC4physical
12477395
APC5_YEASTAPC5physical
12477395
CDC16_YEASTCDC16physical
12477395
CDC23_YEASTCDC23physical
12477395
APC9_YEASTAPC9physical
12477395
APC10_YEASTDOC1physical
12477395
APC11_YEASTAPC11physical
12477395
CDC26_YEASTCDC26physical
12477395
CDC27_YEASTCDC27physical
9469814
APC9_YEASTAPC9physical
9469814
APC10_YEASTDOC1physical
9469814
CDC23_YEASTCDC23physical
16554755
APC9_YEASTAPC9physical
16554755
ECM13_YEASTECM13physical
17634282
KAR4_YEASTKAR4physical
17634282
SNF1_YEASTSNF1physical
17634282
AAKG_YEASTSNF4physical
17634282
FZF1_YEASTFZF1physical
17634282
CDC23_YEASTCDC23physical
17634282
DUS3_YEASTDUS3physical
17634282
YM17_YEASTERG29physical
17634282
APC5_YEASTAPC5physical
17634282
RLF2_YEASTRLF2physical
17634282
APC1_YEASTAPC1physical
21186364
APC2_YEASTAPC2physical
21186364
CDC16_YEASTCDC16physical
21186364
CDC27_YEASTCDC27physical
21186364
APC5_YEASTAPC5physical
21186364
CDC23_YEASTCDC23physical
21186364
MND2_YEASTMND2physical
21186364
APC9_YEASTAPC9physical
21186364
APC10_YEASTDOC1physical
21186364
APC11_YEASTAPC11physical
21186364
APC5_YEASTAPC5physical
21307936

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APC4_YEAST

loading...

Related Literatures of Post-Translational Modification

TOP