APC1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: APC1_SCHPO
• UniProt AC: Q9URV2
• Protein Name: Anaphase-promoting complex subunit 1
• Gene Name: cut4
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1458
• 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. Mutations to this protein prevent the exit from mitosis..
• Protein Sequence: MLELKTNVIQDPELKDSLDLQENDRVEIIGDAVHYIVNDHLNRVFNYTVDQQKIHAALITTFASGKKAIVVILDDIGYVYYVGDNNNDSYIINVPFSTESAWSSPSGLYLQRHRSSDENLNTDLPHIFCLNDPLDELTLIKFDGKKILSLFDSIVYVVGEIVVTHNKKEKKLSFWRSRFIDPESDQSIKSSRNRRRESSFSREKNPDLTRSDSIHYTANTRLSEKFEEQGLAYSTIFSHIESFPITGSTSFDSILGNGVLVITTLVKELEKGYMMLFRLVRDRSPYFLDSLQLHAINLSAIKSKHLQKIVVLSSKGKVSLESPMSPSLPIEGTFRSFRVHGATLYLEDTDGVQRYISLDNRASNSLVKWCLSVIRYVLPLREYEIFYTGHLYALFAFKLSHDEAFISSILACFTFFSRDKVHVEPIEDCNEAYSLSSKFHFKKEILIASQLSSHLDYSTFKNYLMPLAITLHFISEELRLDSVVKPRKDQLVALLLQITTWLKWPRYCEYYNFDIAETFLSIPLSIQVDVEEPVGPTSILQWIIECLRSQSTVPFYGLESYGLPHSCSTMFPQTLSLMQLLDCLLNPNMTLQNLVEEMVRLGISRKRCERYPFGILCIIFTVLEIAAEEYSPNWESEELRLVNRLDVDSFLHPKTPKWVFNKQDQEVKEIKALTSTVTDSTLVDTQSFHPYKVVTDMIFREDRRLAEVNKLLNYSSQITIMTEHFDVDLSSVPMQQKVAQCICVRTLSVPIGAGMLTYGSKNPLPTEKVTPRLFNFTLHLHPGTLIIQPNKEFVTQELTEWPEFNVGVALGLSISKFSKEINTSWIMFNRPETLTAYHAGFLFGLGLNGHLKALATWHSFIYLTSKHDTTSIGLLLGLASSYLGSMDAKVTKLLSVHISALLPVGSNELNISPLTQTAGILGIGLLFHDSCHRRMSEVTMEEILASNESELKNEGYKLAAGFSLGLINLGRGSNLPGMSDLKLVSRLQVGISSQATFQSLEAGSPGAIMALTMIYMKTNDLEVAKKIDIPKSRYLLDFYRPDLILLRVAGKNLIMWDEVKADYEWVKYQIPDIMLSQFDLQEKKVLSSDDLLLYNVLAGICFSLGLRFAGTGNPKAKEILINFLDSFIRLCHLPAKTHDERVTAVTVIRCTQIVALSSSCVMAGYCDLDVLRRLRVLHGRMEPVNYGAQMATHMALGILSLGGGRYSLSRSNLAIAALLISFYPQFPRTTQDNRAHLQAARNLWALAVEERCIIPRNQDTKQPCIVPLNVVQKSGAVQKLEAPILLPPYDSISSVSTLGDKYWNLKIDLDNNSDYRELLRESQTLTLMPYDRTSSKEEPLNLFPKLKDTSSPLWNLVKTSRLFQSSNSPLNVASLQESNNKTSLGVKLLLSMDFDNLTRDRLLSLQILLQFFESCWTGVLLNKFHSRQYLFLSRDLVEDLSLRVWEYVYSHNHNEESV

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
211	Phosphorylation	KNPDLTRSDSIHYTA CCCCCCHHCCEEEEC	30.40	29996109
213	Phosphorylation	PDLTRSDSIHYTANT CCCCHHCCEEEECCC	16.71	29996109

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

Oops, there are no upstream regulatory protein records of APC1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of APC1_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of APC1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STI1_SCHPO	sti1	genetic	8918880
PDE1_SCHPO	cgs2	genetic	8918880
MAD2_SCHPO	mad2	genetic	9461438
SLP1_SCHPO	slp1	genetic	9461438
RPN12_SCHPO	rpn12	genetic	16904908
APC3_SCHPO	nuc2	physical	8918880
CUT9_SCHPO	cut9	physical	8918880
CUT9_SCHPO	cut9	physical	10526233
APC4_SCHPO	cut20	physical	10526233
APC3_SCHPO	nuc2	physical	10526233
KAPR_SCHPO	cgs1	genetic	8918880
CLR6_SCHPO	clr6	genetic	18354085
APC8_SCHPO	cut23	genetic	18354085
UBP8_SCHPO	ubp8	genetic	24948786
SGF11_SCHPO	sgf11	genetic	24948786
SUS1_SCHPO	sus1	genetic	24948786

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.