ID PTTG2_HUMAN Reviewed; 202 AA. AC Q9NZH5; O95355; Q6NTC9; Q9UNJ6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 16-NOV-2011, sequence version 2. DT 16-MAR-2016, entry version 90. DE RecName: Full=Securin-2; DE AltName: Full=Pituitary tumor-transforming gene 2 protein; GN Name=PTTG2; 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 [GENOMIC DNA] (ISOFORM 2), TISSUE SPECIFICITY, AND RP VARIANT PRO-44. RX PubMed=10084610; DOI=10.1210/jc.84.3.1149; RA Prezant T.R., Kadioglu P., Melmed S.; RT "An intronless homolog of human proto-oncogene hPTTG is expressed in RT pituitary tumors: evidence for hPTTG family."; RL J. Clin. Endocrinol. Metab. 84:1149-1152(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP VARIANT PRO-44. RX PubMed=10806349; DOI=10.1016/S0378-1119(00)00096-2; RA Chen L., Puri R., Lefkowitz E.J., Kakar S.S.; RT "Identification of the human pituitary tumor transforming gene (hPTTG) RT family: molecular structure, expression, and chromosomal RT localization."; RL Gene 248:41-50(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT PRO-44. RC TISSUE=Pituitary adenoma; RA Mu Y.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NZH5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NZH5-2; Sequence=VSP_031444; CC -!- TISSUE SPECIFICITY: Expressed at low levels in the pituitary, CC liver, spleen, prostate, testis, ovary, small intestine and colon. CC Also expressed in various pituitary, testicular, liver and ovarian CC tumors. {ECO:0000269|PubMed:10084610, CC ECO:0000269|PubMed:10806349}. CC -!- DOMAIN: The N-terminal destruction box (D-box) acts as a CC recognition signal for degradation via the ubiquitin-proteasome CC pathway. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the securin family. {ECO:0000305}. 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; AF116538; AAD41262.2; -; Genomic_DNA. DR EMBL; AF200719; AAF72579.1; -; Genomic_DNA. DR EMBL; AF095288; AAC64410.1; -; mRNA. DR EMBL; AC021106; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069114; AAH69114.1; -; mRNA. DR EMBL; BC069400; AAH69400.1; -; mRNA. DR CCDS; CCDS54755.1; -. [Q9NZH5-2] DR RefSeq; NP_006598.2; NM_006607.2. [Q9NZH5-2] DR UniGene; Hs.668806; -. DR BioGrid; 115967; 1. DR STRING; 9606.ENSP00000424261; -. DR iPTMnet; Q9NZH5; -. DR PhosphoSite; Q9NZH5; -. DR BioMuta; PTTG2; -. DR DMDM; 357529040; -. DR EPD; Q9NZH5; -. DR PaxDb; Q9NZH5; -. DR PRIDE; Q9NZH5; -. DR Ensembl; ENST00000504686; ENSP00000424261; ENSG00000250254. [Q9NZH5-2] DR GeneID; 10744; -. DR KEGG; hsa:10744; -. DR UCSC; uc011bye.3; human. [Q9NZH5-1] DR CTD; 10744; -. DR GeneCards; PTTG2; -. DR HGNC; HGNC:9691; PTTG2. DR HPA; HPA008890; -. DR HPA; HPA045034; -. DR MIM; 604231; gene. DR neXtProt; NX_Q9NZH5; -. DR PharmGKB; PA34035; -. DR GeneTree; ENSGT00390000009693; -. DR HOVERGEN; HBG053264; -. DR InParanoid; Q9NZH5; -. DR KO; K06635; -. DR OrthoDB; EOG7MPRH0; -. DR TreeFam; TF330797; -. DR GenomeRNAi; 10744; -. DR NextBio; 40797; -. DR PRO; PR:Q9NZH5; -. DR Proteomes; UP000005640; Chromosome 4. DR CleanEx; HS_PTTG2; -. DR Genevisible; Q9NZH5; HS. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0030414; F:peptidase inhibitor activity; IBA:GO_Central. DR GO; GO:0051276; P:chromosome organization; IEA:InterPro. DR GO; GO:0045143; P:homologous chromosome segregation; IBA:GO_Central. DR GO; GO:2000816; P:negative regulation of mitotic sister chromatid separation; IBA:GO_Central. DR GO; GO:0010466; P:negative regulation of peptidase activity; IBA:GOC. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR InterPro; IPR018008; Securin_separation-inh_met. DR InterPro; IPR006940; Securin_separation_inhibitor. DR PANTHER; PTHR10418; PTHR10418; 1. DR Pfam; PF04856; Securin; 1. PE 2: Evidence at transcript level; KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm; KW Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; KW Reference proteome; SH3-binding. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O95997}. FT CHAIN 2 202 Securin-2. FT /FTId=PRO_0000319106. FT MOTIF 61 64 D-box. {ECO:0000250}. FT MOTIF 163 173 SH3-binding. {ECO:0000250}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000250|UniProtKB:O95997}. FT MOD_RES 165 165 Phosphoserine. FT {ECO:0000250|UniProtKB:O95997}. FT VAR_SEQ 179 202 LQSPSSILSTLDVELPAVCYDIDI -> FAVSFKHSVDPGC FT (in isoform 2). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.3}. FT /FTId=VSP_031444. FT VARIANT 44 44 R -> P (in dbSNP:rs6811863). FT {ECO:0000269|PubMed:10084610, FT ECO:0000269|PubMed:10806349, FT ECO:0000269|Ref.3}. FT /FTId=VAR_038956. SQ SEQUENCE 202 AA; 22302 MW; 3CBE738EC7817263 CRC64; MATLIYVDKE IGEPGTRVAA KDVLKLESRP SIKALDGISQ VLTRRFGKTY DAPSALPKAT RKALGTVNRA TEKSVKTNGP RKQKQPSFSA KKMTEKTVKT KSSVPASDDA YPEIEKFFPF NLLDFESFDL PEERQIAHLP LSGVPLMILD EEGELEKLFQ LGPPSPVKMP SPPWECNLLQ SPSSILSTLD VELPAVCYDI DI //