ID ANC2_HUMAN STANDARD; PRT; 822 AA. AC Q9UJX6; Q96DG5; Q96GG4; Q9P2E1; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Anaphase promoting complex subunit 2 (APC2) (Cyclosome subunit 2). GN Name=ANAPC2; Synonyms=APC2, KIAA1406; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND SUBUNIT. RX MEDLINE=98136241; PubMed=9469815; DOI=10.1126/science.279.5354.1219; RA Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.; RT "Identification of a cullin homology region in a subunit of the RT anaphase-promoting complex."; RL Science 279:1219-1222(1998). RN [2] RP NUCLEOTIDE SEQUENCE OF 252-822 (ISOFORM 1). RC TISSUE=Brain; RX MEDLINE=20181126; PubMed=10718198; RA Nagase T., Kikuno R., Ishikawa K.-I., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. RT The complete sequences of 150 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 243-822 (ISOFORM 2). RC TISSUE=Brain, Cervix, and Ovary; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [4] RP FUNCTION, AND INTERACTIONS WITH ANAPC11 AND UBCH10. RX MEDLINE=21602823; PubMed=11739784; RA Tang Z., Li B., Bharadwaj R., Zhu H., Oezkan E., Hakala K., RA Deisenhofer J., Yu H.; RT "APC2 cullin protein and APC11 RING protein comprise the minimal RT ubiquitin ligase module of the anaphase-promoting complex."; RL Mol. Biol. Cell 12:3839-3851(2001). CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome CC (APC/C), a cell cycle-regulated ubiquitin ligase that controls CC progression through mitosis and the G1 phase of the cell cycle. CC -!- PATHWAY: Ubiquitin conjugation; third step. CC -!- SUBUNIT: The APC/C is composed of at least 11 subunits. Interacts CC through the cullin domain with ANAPC11 and with UBCH10. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UJX6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UJX6-2; Sequence=VSP_008463; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the cullin family. CC -!- CAUTION: Ref.3 (AAH09487) sequence differs from that shown due to CC a wrong choice of frame. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF191337; AAF05751.1; -. DR EMBL; AB037827; BAA92644.1; -. DR EMBL; BC032503; AAH32503.1; -. DR EMBL; BC001579; AAH01579.1; -. DR EMBL; BC009487; AAH09487.2; ALT_SEQ. DR Ensembl; ENSG00000176248; Homo sapiens. DR Genew; HGNC:19989; ANAPC2. DR MIM; 606946; -. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; TAS. DR GO; GO:0008054; P:cyclin catabolism; TAS. DR GO; GO:0000079; P:regulation of cyclin dependent protein kina...; TAS. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolism; TAS. DR InterPro; IPR001373; Cullin. DR InterPro; IPR009058; Wing_hlx_DNA_bnd. DR SMART; SM00182; CULLIN; 1. DR PROSITE; PS01256; CULLIN_1; FALSE_NEG. DR PROSITE; PS50069; CULLIN_2; 1. KW Alternative splicing; Cell cycle; Cell division; Mitosis; KW Ubl conjugation pathway. FT VARSPLIC 350 352 Missing (in isoform 2). FT /FTId=VSP_008463. SQ SEQUENCE 822 AA; 93828 MW; 94A2B1D015805573 CRC64; MAAAVVVAEG DSDSRPGQEL LVAWNTVSTG LVPPAALGLV SSRTSGAVPP KEEELRAAVE VLRGHGLHSV LEEWFVEVLQ NDLQANISPE FWNAISQCEN SADEPQCLLL LLDAFGLLES RLDPYLRSLE LLEKWTRLGL LMGTGAQGLR EEVHTMLRGV LFFSTPRTFQ EMIQRLYGCF LRVYMQSKRK GEGGTDPELE GELDSRYARR RYYRLLQSPL CAGCSSDKQQ CWCRQALEQF HQLSQVLHRL SLLERVSAEA VTTTLHQVTR ERMEDRCRGE YERSFLREFH KWIERVVGWL GKVFLQDGPA RPASPEAGNT LRRWRCHVQR FFYRIYASLR IEELFSIVRD FPDSRPAIED LKYCLERTDQ RQQLLVSLKA ALETRLLHPG VNTCDIITLY ISAIKALRVL DPSMVILEVA CEPIRRYLRT REDTVRQIVA GLTGDSDGTG DLAVELSKTD PASLETGQDS EDDSGEPEDW VPDPVDADPG KSSSKRRSSD IISLLVSIYG SKDLFINEYR SLLADRLLHQ FSFSPEREIR NVELLKLRFG EAPMHFCEVM LKDMADSRRI NANIREEDEK RPAEEQPPFG VYAVILSSEF WPPFKDEKLE VPEDIRAALE AYCKKYEQLK AMRTLSWKHT LGLVTMDVEL ADRTLSVAVT PVQAVILLYF QDQASWTLEE LSKAVKMPVA LLRRRMSVWL QQGVLREEPP GTFSVIEEER PQDRDNMVLI DSDDESDSGM ASQADQKEEE LLLFWTYIQA MLTNLESLSL DRIYNMLRMF VVTGPALAEI DLQELQGYLQ KKVRDQQLVY SAGVYRLPKN CS //