ID UBE2C_HUMAN Reviewed; 179 AA. AC O00762; A6NP33; E1P5N7; G3XAB7; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 163. DE RecName: Full=Ubiquitin-conjugating enzyme E2 C; DE EC=2.3.2.23 {ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:20061386}; DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme C; DE EC=2.3.2.24 {ECO:0000269|PubMed:17588522}; DE AltName: Full=E2 ubiquitin-conjugating enzyme C; DE AltName: Full=UbcH10; DE AltName: Full=Ubiquitin carrier protein C; DE AltName: Full=Ubiquitin-protein ligase C; GN Name=UBE2C; Synonyms=UBCH10; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF CYS-114. RX PubMed=9122200; DOI=10.1073/pnas.94.6.2362; RA Townsley F.M., Aristarkhov A., Beck S., Hershko A., Ruderman J.V.; RT "Dominant-negative cyclin-selective ubiquitin carrier protein E2- RT C/UbcH10 blocks cells in metaphase."; RL Proc. Natl. Acad. Sci. U.S.A. 94:2362-2367(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC TISSUE=Lung adenocarcinoma, Lymph, Melanoma, Teratocarcinoma, and RC Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF CYS-114. RX PubMed=15558010; DOI=10.1038/nature03023; RA Rape M., Kirschner M.W.; RT "Autonomous regulation of the anaphase-promoting complex couples RT mitosis to S-phase entry."; RL Nature 432:588-595(2004). RN [7] RP CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING ENZYME. RX PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014; RA Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.; RT "E3-independent monoubiquitination of ubiquitin-binding proteins."; RL Mol. Cell 26:891-898(2007). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=18485873; DOI=10.1016/j.cell.2008.04.012; RA Jin L., Williamson A., Banerjee S., Philipp I., Rape M.; RT "Mechanism of ubiquitin-chain formation by the human anaphase- RT promoting complex."; RL Cell 133:653-665(2008). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP FUNCTION. RX PubMed=19820702; DOI=10.1038/ncb1983; RA Garnett M.J., Mansfeld J., Godwin C., Matsusaka T., Wu J., Russell P., RA Pines J., Venkitaraman A.R.; RT "UBE2S elongates ubiquitin chains on APC/C substrates to promote RT mitotic exit."; RL Nat. Cell Biol. 11:1363-1369(2009). RN [11] RP FUNCTION. RX PubMed=19822757; DOI=10.1073/pnas.0907887106; RA Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H., RA Rape M.; RT "Identification of a physiological E2 module for the human anaphase- RT promoting complex."; RL Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20061386; DOI=10.1074/jbc.M109.089003; RA David Y., Ziv T., Admon A., Navon A.; RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to RT preferred lysines."; RL J. Biol. Chem. 285:8595-8604(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS). RX PubMed=11927573; DOI=10.1074/jbc.M109398200; RA Lin Y., Hwang W.C., Basavappa R.; RT "Structural and functional analysis of the human mitotic-specific RT ubiquitin-conjugating enzyme, UbcH10."; RL J. Biol. Chem. 277:21913-21921(2002). CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its CC covalent attachment to other proteins. In vitro catalyzes 'Lys- CC 11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential CC factor of the anaphase promoting complex/cyclosome (APC/C), a cell CC cycle-regulated ubiquitin ligase that controls progression through CC mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains CC on APC/C substrates, leading to the degradation of APC/C CC substrates by the proteasome and promoting mitotic exit. CC {ECO:0000269|PubMed:15558010, ECO:0000269|PubMed:18485873, CC ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:19822757, CC ECO:0000269|PubMed:20061386}. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating CC enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine CC = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 CC ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE- CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133, CC ECO:0000269|PubMed:18485873, ECO:0000269|PubMed:20061386}. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin- CC activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor CC protein]-L-lysine. {ECO:0000269|PubMed:17588522}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388, CC ECO:0000269|PubMed:18485873}. CC -!- SUBUNIT: Component of the APC/C complex. CC {ECO:0000269|PubMed:19820702}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=O00762-1; Sequence=Displayed; CC Name=2; CC IsoId=O00762-2; Sequence=VSP_045647; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=O00762-3; Sequence=VSP_045648; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=O00762-4; Sequence=VSP_045649; CC Note=No experimental confirmation available.; CC -!- PTM: Autoubiquitinated by the APC/C complex, leading to its CC degradation by the proteasome. Its degradation plays a central CC role in APC/C regulation, allowing cyclin-A accumulation before S CC phase entry. APC/C substrates inhibit the autoubiquitination of CC UBE2C/UBCH10 but not its E2 function, hence APC/C remaining active CC until its substrates have been destroyed. CC {ECO:0000269|PubMed:15558010}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/UBE2CID44079ch20q13.html"; 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; U73379; AAB53362.1; -; mRNA. DR EMBL; BT007300; AAP35964.1; -; mRNA. DR EMBL; AL050348; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75804.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75805.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75806.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75807.1; -; Genomic_DNA. DR EMBL; BC007656; AAH07656.1; -; mRNA. DR EMBL; BC016292; AAH16292.1; -; mRNA. DR EMBL; BC050736; AAH50736.1; -; mRNA. DR EMBL; BI858659; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BM556795; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BU844974; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS13370.1; -. [O00762-1] DR CCDS; CCDS13371.1; -. [O00762-4] DR CCDS; CCDS13372.1; -. [O00762-3] DR CCDS; CCDS13374.1; -. [O00762-2] DR RefSeq; NP_001268670.1; NM_001281741.1. DR RefSeq; NP_001268671.1; NM_001281742.1. DR RefSeq; NP_008950.1; NM_007019.3. [O00762-1] DR RefSeq; NP_861515.1; NM_181799.2. [O00762-4] DR RefSeq; NP_861516.1; NM_181800.2. [O00762-3] DR RefSeq; NP_861517.1; NM_181801.3. [O00762-2] DR UniGene; Hs.93002; -. DR PDB; 1I7K; X-ray; 1.95 A; A/B=1-179. DR PDB; 4YII; X-ray; 1.80 A; U=27-179. DR PDBsum; 1I7K; -. DR PDBsum; 4YII; -. DR ProteinModelPortal; O00762; -. DR SMR; O00762; 29-173. DR BioGrid; 116249; 61. DR DIP; DIP-52725N; -. DR IntAct; O00762; 9. DR STRING; 9606.ENSP00000348838; -. DR PhosphoSite; O00762; -. DR MaxQB; O00762; -. DR PaxDb; O00762; -. DR PRIDE; O00762; -. DR DNASU; 11065; -. DR Ensembl; ENST00000335046; ENSP00000335674; ENSG00000175063. [O00762-4] DR Ensembl; ENST00000352551; ENSP00000333975; ENSG00000175063. [O00762-3] DR Ensembl; ENST00000356455; ENSP00000348838; ENSG00000175063. [O00762-1] DR Ensembl; ENST00000372568; ENSP00000361649; ENSG00000175063. [O00762-2] DR GeneID; 11065; -. DR KEGG; hsa:11065; -. DR UCSC; uc002xpl.3; human. DR UCSC; uc002xpm.3; human. [O00762-1] DR UCSC; uc002xpo.3; human. DR CTD; 11065; -. DR GeneCards; UBE2C; -. DR HGNC; HGNC:15937; UBE2C. DR HPA; CAB011464; -. DR HPA; CAB035990; -. DR HPA; HPA034569; -. DR HPA; HPA054975; -. DR MIM; 605574; gene. DR neXtProt; NX_O00762; -. DR PharmGKB; PA38057; -. DR eggNOG; KOG0421; Eukaryota. DR eggNOG; ENOG4111IGV; LUCA. DR GeneTree; ENSGT00760000119350; -. DR HOGENOM; HOG000233454; -. DR HOVERGEN; HBG063308; -. DR InParanoid; O00762; -. DR KO; K06688; -. DR OMA; AELWDKD; -. DR OrthoDB; EOG7M0NTH; -. DR PhylomeDB; O00762; -. DR TreeFam; TF101116; -. DR BRENDA; 2.3.2.B6; 2681. DR Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex. DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B. DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase. DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase. DR Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins. DR Reactome; R-HSA-176412; Phosphorylation of the APC/C. DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; O00762; -. DR UniPathway; UPA00143; -. DR ChiTaRS; UBE2C; human. DR EvolutionaryTrace; O00762; -. DR GeneWiki; UBE2C; -. DR GenomeRNAi; 11065; -. DR NextBio; 42051; -. DR PRO; PR:O00762; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; O00762; -. DR CleanEx; HS_UBE2C; -. DR ExpressionAtlas; O00762; baseline and differential. DR Genevisible; O00762; HS. DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0051488; P:activation of anaphase-promoting complex activity; TAS:UniProtKB. DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB. DR GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome. DR GO; GO:0007094; P:mitotic spindle assembly checkpoint; TAS:Reactome. DR GO; GO:0008054; P:negative regulation of cyclin-dependent protein serine/threonine kinase by cyclin degradation; IDA:UniProtKB. DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome. DR GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:UniProtKB. DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome. DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IBA:GO_Central. DR GO; GO:0051439; P:regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR Gene3D; 3.10.110.10; -; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR Pfam; PF00179; UQ_con; 1. DR SUPFAM; SSF54495; SSF54495; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Cell cycle; Cell division; Complete proteome; Mitosis; KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; KW Transferase; Ubl conjugation; Ubl conjugation pathway. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:21406692}. FT CHAIN 2 179 Ubiquitin-conjugating enzyme E2 C. FT /FTId=PRO_0000082560. FT ACT_SITE 114 114 Glycyl thioester intermediate. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 3 3 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT VAR_SEQ 1 39 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_045647. FT VAR_SEQ 44 72 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_045648. FT VAR_SEQ 73 140 VYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNI FT CLDILKEKWSALYDVRTILLSIQSLLG -> AVGSIRTSST FT VCLLSGPRETQDSSKPLVWGLGWDMRLLLELTLQLFLQMP FT (in isoform 4). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_045649. FT VARIANT 25 25 G -> D. FT /FTId=VAR_007694. FT MUTAGEN 114 114 C->S: Loss of function; inhibition of FT cyclin-B degradation. FT {ECO:0000269|PubMed:15558010, FT ECO:0000269|PubMed:9122200}. FT HELIX 30 45 {ECO:0000244|PDB:4YII}. FT STRAND 50 54 {ECO:0000244|PDB:4YII}. FT STRAND 61 68 {ECO:0000244|PDB:4YII}. FT STRAND 78 84 {ECO:0000244|PDB:4YII}. FT TURN 87 91 {ECO:0000244|PDB:4YII}. FT STRAND 95 100 {ECO:0000244|PDB:4YII}. FT STRAND 111 113 {ECO:0000244|PDB:4YII}. FT HELIX 116 118 {ECO:0000244|PDB:4YII}. FT TURN 119 121 {ECO:0000244|PDB:4YII}. FT HELIX 128 140 {ECO:0000244|PDB:4YII}. FT HELIX 150 155 {ECO:0000244|PDB:4YII}. FT HELIX 159 172 {ECO:0000244|PDB:4YII}. SQ SEQUENCE 179 AA; 19652 MW; 0B6F58A1F0665D9A CRC64; MASQNRDPAA TSVAAARKGA EPSGGAARGP VGKRLQQELM TLMMSGDKGI SAFPESDNLF KWVGTIHGAA GTVYEDLRYK LSLEFPSGYP YNAPTVKFLT PCYHPNVDTQ GNICLDILKE KWSALYDVRT ILLSIQSLLG EPNIDSPLNT HAAELWKNPT AFKKYLQETY SKQVTSQEP //