ID PTTG2_HUMAN Reviewed; 202 AA. AC Q9NZH5; O95355; Q6NTC9; Q9UNJ6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 30-NOV-2010, entry version 51. 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), AND TISSUE SPECIFICITY. RX MEDLINE=99182101; 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), AND TISSUE SPECIFICITY. RX MEDLINE=20267846; 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). RC TISSUE=Pituitary adenoma; RA Mu Y.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP ARG-44. 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). 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. CC -!- DOMAIN: The N-terminal destruction box (D-box) acts as a CC recognition signal for degradation via the ubiquitin-proteasome CC pathway (By similarity). CC -!- SIMILARITY: Belongs to the securin family. 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; BC069114; AAH69114.1; -; mRNA. DR EMBL; BC069400; AAH69400.1; -; mRNA. DR IPI; IPI00008631; -. DR IPI; IPI00021381; -. DR RefSeq; NP_006598.2; NM_006607.2. DR UniGene; Hs.668806; -. DR STRING; Q9NZH5; -. DR PhosphoSite; Q9NZH5; -. DR PRIDE; Q9NZH5; -. DR Ensembl; ENST00000352433; ENSP00000344936; ENSG00000164611. DR Ensembl; ENST00000393964; ENSP00000377536; ENSG00000164611. DR GeneID; 10744; -. DR KEGG; hsa:10744; -. DR UCSC; uc003gtc.1; human. DR CTD; 10744; -. DR GeneCards; GC04P037964; -. DR HGNC; HGNC:9691; PTTG2. DR HPA; CAB008373; -. DR MIM; 604231; gene. DR PharmGKB; PA34035; -. DR HOVERGEN; HBG053264; -. DR InParanoid; Q9NZH5; -. DR NextBio; 40797; -. DR ArrayExpress; Q9NZH5; -. DR Bgee; Q9NZH5; -. DR CleanEx; HS_PTTG2; -. DR Genevestigator; Q9NZH5; -. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW. DR GO; GO:0051276; P:chromosome organization; IEA:InterPro. DR GO; GO:0006259; P:DNA metabolic process; IEA:InterPro. DR InterPro; IPR018008; Securin_separation-inh_met. DR InterPro; IPR006940; Securin_separation_inhibitor. DR PANTHER; PTHR10418; Securin; 1. DR Pfam; PF04856; Securin; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Cytoplasm; Nucleus; KW Phosphoprotein; Polymorphism; Proto-oncogene; SH3-binding. FT CHAIN 1 202 Securin-2. FT /FTId=PRO_0000319106. FT MOTIF 61 64 D-box (By similarity). FT MOTIF 163 173 SH3-binding (By similarity). FT MOD_RES 165 165 Phosphoserine. FT VAR_SEQ 179 202 LQSPSSILSTLDVELPAVCYDIDI -> FAVSFKHSVDPGC FT (in isoform 2). FT /FTId=VSP_031444. FT VARIANT 44 44 P -> R (in dbSNP:rs6811863). FT /FTId=VAR_038956. SQ SEQUENCE 202 AA; 22243 MW; 20A246EEC4D74675 CRC64; MATLIYVDKE IGEPGTRVAA KDVLKLESRP SIKALDGISQ VLTPRFGKTY DAPSALPKAT RKALGTVNRA TEKSVKTNGP RKQKQPSFSA KKMTEKTVKT KSSVPASDDA YPEIEKFFPF NLLDFESFDL PEERQIAHLP LSGVPLMILD EEGELEKLFQ LGPPSPVKMP SPPWECNLLQ SPSSILSTLD VELPAVCYDI DI //