ID   ANC2_MOUSE              Reviewed;         837 AA.
AC   Q8BZQ7; Q3TCK5; Q8R2Q1;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Anaphase-promoting complex subunit 2;
DE            Short=APC2;
DE   AltName: Full=Cyclosome subunit 2;
GN   Name=Anapc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Epididymis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH NEUROD2.
RX   PubMed=19900895; DOI=10.1126/science.1177087;
RA   Yang Y., Kim A.H., Yamada T., Wu B., Bilimoria P.M., Ikeuchi Y.,
RA   de la Iglesia N., Shen J., Bonni A.;
RT   "A Cdc20-APC ubiquitin signaling pathway regulates presynaptic
RT   differentiation.";
RL   Science 326:575-578(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549 AND SER-712, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Together with the RING-H2 protein ANAPC11, constitutes the
CC       catalytic component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC       progression through mitosis and the G1 phase of the cell cycle. The
CC       APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation of
CC       'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC       formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. The
CC       CDC20-APC/C complex positively regulates the formation of synaptic
CC       vesicle clustering at active zone to the presynaptic membrane in
CC       postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 drives
CC       presynaptic differentiation. {ECO:0000250|UniProtKB:Q9UJX6,
CC       ECO:0000269|PubMed:19900895}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC       subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC       ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC       ANAPC16 that assemble into a complex of at least 19 chains with a
CC       combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC       and FBXO5 (By similarity). In the context of the APC/C complex,
CC       directly interacts with UBE2C and UBE2S (By similarity). Interacts (via
CC       cullin domain) with ANAPC11 and with UBCH10 (By similarity). Interacts
CC       with NEUROD2 (PubMed:19900895). Interacts with FBXO43; the interaction
CC       is direct. {ECO:0000250|UniProtKB:Q9UJX6, ECO:0000269|PubMed:19900895}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00330}.
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DR   EMBL; AK033784; BAC28472.1; -; mRNA.
DR   EMBL; AK170676; BAE41951.1; -; mRNA.
DR   EMBL; AL732309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC027351; AAH27351.1; -; mRNA.
DR   EMBL; BC137583; AAI37584.1; -; mRNA.
DR   CCDS; CCDS15761.1; -.
DR   RefSeq; NP_780509.2; NM_175300.4.
DR   AlphaFoldDB; Q8BZQ7; -.
DR   SMR; Q8BZQ7; -.
DR   BioGRID; 221196; 51.
DR   CORUM; Q8BZQ7; -.
DR   IntAct; Q8BZQ7; 37.
DR   MINT; Q8BZQ7; -.
DR   STRING; 10090.ENSMUSP00000028341; -.
DR   iPTMnet; Q8BZQ7; -.
DR   PhosphoSitePlus; Q8BZQ7; -.
DR   EPD; Q8BZQ7; -.
DR   jPOST; Q8BZQ7; -.
DR   MaxQB; Q8BZQ7; -.
DR   PaxDb; 10090-ENSMUSP00000028341; -.
DR   ProteomicsDB; 296407; -.
DR   Pumba; Q8BZQ7; -.
DR   Antibodypedia; 4358; 343 antibodies from 32 providers.
DR   DNASU; 99152; -.
DR   Ensembl; ENSMUST00000028341.11; ENSMUSP00000028341.5; ENSMUSG00000026965.13.
DR   GeneID; 99152; -.
DR   KEGG; mmu:99152; -.
DR   UCSC; uc008ird.2; mouse.
DR   AGR; MGI:2139135; -.
DR   CTD; 29882; -.
DR   MGI; MGI:2139135; Anapc2.
DR   VEuPathDB; HostDB:ENSMUSG00000026965; -.
DR   eggNOG; KOG2165; Eukaryota.
DR   GeneTree; ENSGT00390000016127; -.
DR   HOGENOM; CLU_007149_2_0_1; -.
DR   InParanoid; Q8BZQ7; -.
DR   OMA; FMYETFA; -.
DR   OrthoDB; 2786196at2759; -.
DR   PhylomeDB; Q8BZQ7; -.
DR   TreeFam; TF105442; -.
DR   Reactome; R-MMU-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-MMU-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-MMU-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-MMU-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR   Reactome; R-MMU-176412; Phosphorylation of the APC/C.
DR   Reactome; R-MMU-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 99152; 23 hits in 80 CRISPR screens.
DR   ChiTaRS; Anapc2; mouse.
DR   PRO; PR:Q8BZQ7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8BZQ7; Protein.
DR   Bgee; ENSMUSG00000026965; Expressed in internal carotid artery and 273 other cell types or tissues.
DR   ExpressionAtlas; Q8BZQ7; baseline and differential.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR   GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR   GO; GO:0090129; P:positive regulation of synapse maturation; IDA:UniProtKB.
DR   GO; GO:0031915; P:positive regulation of synaptic plasticity; IDA:UniProtKB.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.20.1310.10; Cullin Repeats; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR044554; APC2-like.
DR   InterPro; IPR014786; APC2_C.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45957; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR   PANTHER; PTHR45957:SF1; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF08672; ANAPC2; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   SMART; SM01013; APC2; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SUPFAM; SSF75632; Cullin homology domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
DR   Genevisible; Q8BZQ7; MM.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Differentiation; Mitosis; Neurogenesis;
KW   Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..837
FT                   /note="Anaphase-promoting complex subunit 2"
FT                   /id="PRO_0000119812"
FT   REGION          478..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..498
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX6"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX6"
FT   MOD_RES         485
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX6"
FT   MOD_RES         549
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         712
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         825
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   CONFLICT        680
FT                   /note="V -> L (in Ref. 1; BAC28472)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   837 AA;  95307 MW;  02E62B928C0E20B3 CRC64;
     MEAEGVAVAA AAAAAAAAAT IIASDDCDSR PGQELLVAWN TVSTGLVPPA ALGLASSRTS
     GAVPPKEEEL RAAVEVLRGH GLHSVLEEWF VEVLQNDLQG NIATEFWNAI ALRENSVDEP
     QCLGLLLDAF GLLESRLDPY LHSLELLEKW TRLGLLMGAG AQGLREKVHT MLRGVLFFST
     PRTFQEMVQR LYGRFLRVYM QSKRKGEGGT DPELEGELDS RYARRRYYRL LQSPLCAGCG
     SDKQQCWCRQ ALEQFNQLSQ VLHRLSLLER VCAEAVTTTL HQVTRERMED RCRGEYERSF
     LREFHKWIER VVGWLGKVFL QDNPTRPTSP EAGNTLRRWR CHVQRFFYRI YATLRIEELF
     SIIRDFPDSR PAIEDLKYCL ERTDQRQQLL VSLKVALETR LLHPGVNTCD IITLYISAIK
     ALRVLDPSMV ILEVACEPIR RYLRTREDTV RQIVAGLTGD SDGTGDLAVE LSKTDPACLE
     TGQDSEDDSG EPEDWVPDPV DADPVKSSSK RRSSDIISLL VSIYGSKDLF INEYRSLLAD
     RLLHQFSFSP EREIRNVELL KLRFGEAPMH FCEVMLKDMA DSRRINANIR EEDEKRPVEE
     QPPFGVYAVI LSSEFWPPFK DEKLEVPEDI RAALDVYCKK YEKLKAMRTL SWKHTLGLVT
     MDVELADRTL SVAVTPVQAV VLLYFQNQAS WTLEELSKVV KMPVALLRRR MSVWLQQGVL
     REEPPGTFSV IEEERPQDRD NMVLIDSDDE SDSGMASQAD QKEEELLLFW AYIQAMLTNL
     ESLSLERIYS MLRMFVMTGP ALAEIDLQEL QGYLQKKVRD QQLIYSAGVY RLPKNSN
//