APC2/YLR127C Protein Information Help

Standard Name Apc2p 1, 2
Systematic Name Ylr127cp
Alias Rsi1p , Tid2p 3
ORF Classification Verified
Description Subunit of the Anaphase-Promoting Complex/Cyclosome (APC/C), which is a ubiquitin-protein ligase required for degradation of anaphase inhibitors, including mitotic cyclins, during the metaphase/anaphase transition; component of the catalytic core of the APC/C; has similarity to cullin Cdc53p (1, 4, 5)
Name Description Anaphase Promoting Complex 1
Experimental Data
Molecules/cell 432 6
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 853
Molecular Weight (Da) 99,977
Isoelectric Point (pI) 6.68

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Apc2p (InterPro)
Physical Interactions There are 102 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052EF8 | Q12440
MIPS: YLR127C
NCBI: 1256867 | 1297041 | 1360535 | 21466053 | 21466054 | 21466055 | 21466056 | 2204277 | 55976297 | 62467559 | 6323156 | 995689 | NP_013228.1 | NM_001182014.1
GenBank/EMBL/DDBJ: DAA09438.1 | AY899244 | U53877 | X89514 | X91258 | Z73299 | Z73300
Amino Acid Sequence (or in FASTA format)
 
       1  MSFQITPTRD LKVITDELQT LSSYIFHTNI VDDLNSLLTW MSPNDAKSNH
      51  QLRPPSLRIK NIIKVLFPNN ATTSPYSMIN TSQANNSIVN EGNTNKELQL
     101  QLFSTLKEFY IFQVRYHFFL HFNNINYLKD IQRWENYYEF PLRYVPIFDV
     151  NVNDWALELN SLRHYLLNRN IKFKNNLRTR LDKLIMDDDF DLADNLIQWL
     201  KSANGSLSST ELIVNALYSK INKFCEDNMS RVWNKRFMIM ETFNKFINQY
     251  WSQFSKLVGC PEDDHELTTT VFNCFESNFL RIRTNEIFDI CVLAYPDSKV
     301  TLLELRKIMK DFKDYTNIVT TFLSDFKKYI LNPSVTTVDA LLRYVKTIKA
     351  FLVLDPTGRC LHSITTFVKP YFQERKHLVN VLLYAMLDLP EEELKEKINF
     401  NVDMKALLSL VDTLHDSDIN QDTNITKRDK NKKSPFLWNL KVKGKRELNK
     451  DLPIRHAMLY EHILNYYIAW VPEPNDMIPG NIKSSYIKTN LFEVLLDLFE
     501  SREFFISEFR NLLTDRLFTL KFYTLDEKWT RCLKLIREKI VKFTETSHSN
     551  YITNGILGLL ETTAPAADAD QSNLNSIDVM LWDIKCSEEL CRKMHEVAGL
     601  DPIIFPKFIS LLYWKYNCDT QGSNDLAFHL PIDLERELQK YSDIYSQLKP
     651  GRKLQLCKDK GKVEIQLAFK DGRKLVLDVS LEQCSVINQF DSPNDEPICL
     701  SLEQLSESLN IAPPRLTHLL DFWIQKGVLL KENGTYSVIE HSEMDFDQAQ
     751  KTAPMEIENS NYELHNDSEI ERKYELTLQR SLPFIEGMLT NLGAMKLHKI
     801  HSFLKITVPK DWGYNRITLQ QLEGYLNTLA DEGRLKYIAN GSYEIVKNGH
     851  KNS*

external links for Apc2p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Candida (CGD) BioPIXIE MIPS YeastGFP
Candida (CandidaDB) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Apc2p
1) Zachariae W, et al.  (1998) Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins. Science 279(5354):1216-9
2) Yu H, et al.  (1998) Identification of a cullin homology region in a subunit of the anaphase-promoting complex. Science 279(5354):1219-22
3) Dresser ME, et al.  (1997) DMC1 functions in a Saccharomyces cerevisiae meiotic pathway that is largely independent of the RAD51 pathway. Genetics 147(2):533-44
4) Zachariae W and Nasmyth K  (1999) Whose end is destruction: cell division and the anaphase-promoting complex. Genes Dev 13(16):2039-58
5) Buschhorn BA, et al.  (2011) Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1. Nat Struct Mol Biol 18(1):6-13
6) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41