APC2_YEAST - dbPTM
APC2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APC2_YEAST
UniProt AC Q12440
Protein Name Anaphase-promoting complex subunit 2
Gene Name APC2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 853
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 MSFQITPTRDLKVITDELQTLSSYIFHTNIVDDLNSLLTWMSPNDAKSNHQLRPPSLRIKNIIKVLFPNNATTSPYSMINTSQANNSIVNEGNTNKELQLQLFSTLKEFYIFQVRYHFFLHFNNINYLKDIQRWENYYEFPLRYVPIFDVNVNDWALELNSLRHYLLNRNIKFKNNLRTRLDKLIMDDDFDLADNLIQWLKSANGSLSSTELIVNALYSKINKFCEDNMSRVWNKRFMIMETFNKFINQYWSQFSKLVGCPEDDHELTTTVFNCFESNFLRIRTNEIFDICVLAYPDSKVTLLELRKIMKDFKDYTNIVTTFLSDFKKYILNPSVTTVDALLRYVKTIKAFLVLDPTGRCLHSITTFVKPYFQERKHLVNVLLYAMLDLPEEELKEKINFNVDMKALLSLVDTLHDSDINQDTNITKRDKNKKSPFLWNLKVKGKRELNKDLPIRHAMLYEHILNYYIAWVPEPNDMIPGNIKSSYIKTNLFEVLLDLFESREFFISEFRNLLTDRLFTLKFYTLDEKWTRCLKLIREKIVKFTETSHSNYITNGILGLLETTAPAADADQSNLNSIDVMLWDIKCSEELCRKMHEVAGLDPIIFPKFISLLYWKYNCDTQGSNDLAFHLPIDLERELQKYSDIYSQLKPGRKLQLCKDKGKVEIQLAFKDGRKLVLDVSLEQCSVINQFDSPNDEPICLSLEQLSESLNIAPPRLTHLLDFWIQKGVLLKENGTYSVIEHSEMDFDQAQKTAPMEIENSNYELHNDSEIERKYELTLQRSLPFIEGMLTNLGAMKLHKIHSFLKITVPKDWGYNRITLQQLEGYLNTLADEGRLKYIANGSYEIVKNGHKNS
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
76PhosphorylationNNATTSPYSMINTSQ
CCCCCCCCCCCCHHH		15.6128889911
316PhosphorylationMKDFKDYTNIVTTFL
HHHHCHHHHHHHHHH		28.7121551504
320PhosphorylationKDYTNIVTTFLSDFK
CHHHHHHHHHHHHHH		14.1821551504
321PhosphorylationDYTNIVTTFLSDFKK
HHHHHHHHHHHHHHH		16.2221551504
324PhosphorylationNIVTTFLSDFKKYIL
HHHHHHHHHHHHHCC		36.4921551504
409PhosphorylationVDMKALLSLVDTLHD
CCHHHHHHHHHHHCC		27.4829688323
413PhosphorylationALLSLVDTLHDSDIN
HHHHHHHHHCCCCCC		20.6529688323
417PhosphorylationLVDTLHDSDINQDTN
HHHHHCCCCCCCCCC		29.6429688323
423PhosphorylationDSDINQDTNITKRDK
CCCCCCCCCCCCCCC		20.8229688323
426PhosphorylationINQDTNITKRDKNKK
CCCCCCCCCCCCCCC		23.3029688323
434PhosphorylationKRDKNKKSPFLWNLK
CCCCCCCCCCCEEEE		23.6121551504
837PhosphorylationADEGRLKYIANGSYE
HCCCCEEEEECCCEE		15.1723749301
842PhosphorylationLKYIANGSYEIVKNG
EEEEECCCEEECCCC		21.2823749301
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 APC2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APC2_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 APC2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APC1_YEASTAPC1physical
11805826
CDC16_YEASTCDC16physical
11805826
CDC23_YEASTCDC23physical
11805826
CDC27_YEASTCDC27physical
11805826
CDC23_YEASTCDC23physical
9430641
CDC16_YEASTCDC16physical
9469815
CDC27_YEASTCDC27physical
9469815
CDC23_YEASTCDC23physical
9469815
CDC16_YEASTCDC16physical
15060174
SWM1_YEASTSWM1physical
15060174
APC1_YEASTAPC1physical
15060174
APC2_YEASTAPC2physical
15060174
CDC27_YEASTCDC27physical
15060174
APC5_YEASTAPC5physical
15060174
APC4_YEASTAPC4physical
15060174
CDC23_YEASTCDC23physical
15060174
MND2_YEASTMND2physical
15060174
APC9_YEASTAPC9physical
15060174
APC10_YEASTDOC1physical
15060174
APC11_YEASTAPC11physical
15060174
CDC26_YEASTCDC26physical
15060174
CDC27_YEASTCDC27physical
9469814
APC1_YEASTAPC1physical
9469814
APC9_YEASTAPC9physical
9469814
APC10_YEASTDOC1physical
9469814
APC5_YEASTAPC5physical
9469814
APC4_YEASTAPC4physical
9469814
CG22_YEASTCLB2genetic
9430641
SECU_YEASTPDS1genetic
9430641
APC4_YEASTAPC4physical
16554755
CDC23_YEASTCDC23physical
16554755
APC1_YEASTAPC1physical
16554755
APC1_YEASTAPC1physical
16429126
CDC16_YEASTCDC16physical
16429126
CDC23_YEASTCDC23physical
16429126
CDC27_YEASTCDC27physical
16429126
CDC16_YEASTCDC16physical
15797379
APC4_YEASTAPC4physical
15797379
CDC23_YEASTCDC23physical
15797379
MND2_YEASTMND2physical
15797379
APC10_YEASTDOC1physical
15797379
APC11_YEASTAPC11physical
15797379
HSP7F_YEASTSSE1genetic
22908312
APC11_YEASTAPC11physical
24225956
UBC3_YEASTCDC34genetic
27708008
LCB2_YEASTLCB2genetic
27708008
CAB5_YEASTCAB5genetic
27708008
SYF1_YEASTSYF1genetic
27708008
RMRP_YEASTSNM1genetic
27708008
PSB3_YEASTPUP3genetic
27708008
PRP43_YEASTPRP43genetic
27708008
PRP18_YEASTPRP18genetic
27708008
YHS2_YEASTCIA2genetic
27708008
ARP4_YEASTARP4genetic
27708008
ARP3_YEASTARP3genetic
27708008
UTP15_YEASTUTP15genetic
27708008
COPZ_YEASTRET3genetic
27708008
PGTB2_YEASTBET2genetic
27708008
LSM1_YEASTLSM1genetic
27708008
BRE5_YEASTBRE5genetic
27708008
ISW2_YEASTISW2genetic
27708008
DPOA2_YEASTPOL12genetic
27708008
CDC27_YEASTCDC27genetic
27708008
ORC2_YEASTORC2genetic
27708008
RSC6_YEASTRSC6genetic
27708008
CDC48_YEASTCDC48genetic
27708008
RPN5_YEASTRPN5genetic
27708008
YRB1_YEASTYRB1genetic
27708008
APC4_YEASTAPC4genetic
27708008
CDC37_YEASTCDC37genetic
27708008
SPC19_YEASTSPC19genetic
27708008
CAK1_YEASTCAK1genetic
27708008
RPN11_YEASTRPN11genetic
27708008
ECO1_YEASTECO1genetic
27708008
CDC14_YEASTCDC14genetic
27708008
CDC26_YEASTCDC26genetic
27708008
RSC8_YEASTRSC8genetic
27708008
RPN12_YEASTRPN12genetic
27708008
RNA15_YEASTRNA15genetic
27708008
PRS8_YEASTRPT6genetic
27708008
HSF_YEASTHSF1genetic
27708008
NU145_YEASTNUP145genetic
27708008
CDC20_YEASTCDC20genetic
27708008
OKP1_YEASTOKP1genetic
27708008
RPN1_YEASTRPN1genetic
27708008
BRL1_YEASTBRL1genetic
27708008
CDC23_YEASTCDC23genetic
27708008
SMC3_YEASTSMC3genetic
27708008
HACD_YEASTPHS1genetic
27708008
CDC6_YEASTCDC6genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
CDC16_YEASTCDC16genetic
27708008
PRI2_YEASTPRI2genetic
27708008
ASK1_YEASTASK1genetic
27708008
PRS7_YEASTRPT1genetic
27708008
RSC4_YEASTRSC4genetic
27708008
ARP9_YEASTARP9genetic
27708008
DCP2_YEASTDCP2genetic
27708008
MVD1_YEASTMVD1genetic
27708008
RFC4_YEASTRFC4genetic
27708008
XRN2_YEASTRAT1genetic
27708008
APC5_YEASTAPC5genetic
27708008
PRS10_YEASTRPT4genetic
27708008
ARP7_YEASTARP7genetic
27708008
RPN7_YEASTRPN7genetic
27708008
BUR1_YEASTSGV1genetic
27708008
ORC4_YEASTORC4genetic
27708008
MUM2_YEASTMUM2genetic
27708008
UBC4_YEASTUBC4genetic
27708008
SGF29_YEASTSGF29genetic
27708008
SIN3_YEASTSIN3genetic
27708008
SLK19_YEASTSLK19genetic
27708008
RDL1_YEASTRDL1genetic
27708008
PDE2_YEASTPDE2genetic
27708008
RAD1_YEASTRAD1genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
HSP7F_YEASTSSE1genetic
27708008
YP150_YEASTYPL150Wgenetic
27708008
YP084_YEASTYPR084Wgenetic
27708008
HDA3_YEASTHDA3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APC2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76, AND MASSSPECTROMETRY.

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