ID NPM_RAT Reviewed; 292 AA. AC P13084; Q63698; Q64269; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 27-MAR-2024, entry version 191. DE RecName: Full=Nucleophosmin; DE Short=NPM; DE AltName: Full=Nucleolar phosphoprotein B23; DE AltName: Full=Nucleolar protein NO38; DE AltName: Full=Numatrin; GN Name=Npm1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B23.1 AND B23.2), AND PARTIAL PROTEIN RP SEQUENCE. RX PubMed=3417636; DOI=10.1016/s0021-9258(18)37633-6; RA Chang J.-H., Dumbar T.S., Olson M.O.J.; RT "cDNA and deduced primary structure of rat protein B23, a nucleolar protein RT containing highly conserved sequences."; RL J. Biol. Chem. 263:12824-12827(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM B23.2). RX PubMed=2745414; DOI=10.1016/s0021-9258(18)80126-0; RA Chang J.-H., Olson M.O.J.; RT "A single gene codes for two forms of rat nucleolar protein B23 mRNA."; RL J. Biol. Chem. 264:11732-11737(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS B23.1 AND B23.2). RX PubMed=2211699; DOI=10.1016/s0021-9258(17)44742-9; RA Chang J.-H., Olson M.O.J.; RT "Structure of the gene for rat nucleolar protein B23."; RL J. Biol. Chem. 265:18227-18233(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B23.1). RC TISSUE=Pituitary, and Thymus; 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 [5] RP PROTEIN SEQUENCE OF 55-101; 238-246 AND 266-271, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus; RA Lubec G., Chen W.-Q.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP INTERACTION WITH CEBPA. RX PubMed=20075868; DOI=10.1038/emboj.2009.404; RA Muller C., Bremer A., Schreiber S., Eichwald S., Calkhoven C.F.; RT "Nucleolar retention of a translational C/EBPalpha isoform stimulates rDNA RT transcription and cell size."; RL EMBO J. 29:897-909(2010). CC -!- FUNCTION: Involved in diverse cellular processes such as ribosome CC biogenesis, centrosome duplication, protein chaperoning, histone CC assembly, cell proliferation, and regulation of tumor suppressors CC p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear CC export. Associated with nucleolar ribonucleoprotein structures and bind CC single-stranded nucleic acids. Acts as a chaperonin for the core CC histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on CC apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 CC endonuclease activity on AP single-stranded RNA. May exert a control of CC APEX1 endonuclease activity within nucleoli devoted to repair AP on CC rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, CC regulates centrosome duplication. Regulates centriole duplication: CC phosphorylation by PLK2 is able to trigger centriole replication. CC Negatively regulates the activation of EIF2AK2/PKR and suppresses CC apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. CC Antagonizes the inhibitory effect of ATF5 on cell proliferation and CC relieves ATF5-induced G2/M blockade. In complex with MYC enhances the CC transcription of MYC target genes (By similarity). May act as CC chaperonin or cotransporter in the nucleolar localization of CC transcription termination factor TTF1 (By similarity). CC {ECO:0000250|UniProtKB:P06748, ECO:0000250|UniProtKB:Q61937}. CC -!- SUBUNIT: Decamer formed by two pentameric rings associated in a head- CC to-head fashion (By similarity). Disulfide-linked dimers under certain CC conditions (By similarity). The SWAP complex consists of NPM1, NCL, CC PARP1 and SWAP70 (By similarity). Interacts with NSUN2 and SENP3. CC Interacts with the methylated form of RPS10. Interacts (via N-terminal CC domain) with APEX1; the interaction is RNA-dependent and decreases in CC hydrogen peroxide-damaged cells. Interacts with NEK2. Interacts with CC ROCK2 and BRCA2. Interacts with RPGR. Interacts with CENPW. Interacts CC with EIF2AK2/PKR. Interacts with CEBPA (isoform 4) (PubMed:20075868). CC Interacts with DDX31; this interaction prevents interaction between CC NPM1 and HDM2. Interacts with MYC; competitive with NOP53. Interacts CC with NOP53; the interaction is direct and competitive with MYC (By CC similarity). Interacts with LRRC34 (By similarity). Interacts with CC RRP1B. Interacts with NPM3. Interacts with ALKBH2 (By similarity). CC Interacts with TTF1 (via C-terminal region) (By similarity). CC {ECO:0000250|UniProtKB:P06748, ECO:0000250|UniProtKB:Q61937}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P06748}. Nucleus, nucleoplasm CC {ECO:0000250|UniProtKB:P06748}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000250|UniProtKB:P06748}. CC Note=Generally nucleolar, but is translocated to the nucleoplasm in CC case of serum starvation or treatment with anticancer drugs. Can CC shuttle between cytoplasm and nucleus. Co-localizes with the methylated CC form of RPS10 in the granular component (GC) region of the nucleolus. CC Colocalized with nucleolin and APEX1 in nucleoli. NEK2 is required for CC its localization to the centrosome during mitosis. CC {ECO:0000250|UniProtKB:P06748}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B23.1; CC IsoId=P13084-1; Sequence=Displayed; CC Name=B23.2; CC IsoId=P13084-2; Sequence=VSP_003617; CC -!- PTM: Acetylated at C-terminal lysine residues, thereby increasing CC affinity to histones. {ECO:0000250|UniProtKB:P06748}. CC -!- PTM: ADP-ribosylated. {ECO:0000250|UniProtKB:P06748}. CC -!- PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4 CC by PLK2 in S phase is required for centriole duplication and is CC sufficient to trigger centriole replication. Phosphorylation at Ser-4 CC by PLK1 takes place during mitosis. Phosphorylated by CDK2 at Ser-125 CC and Thr-198. Phosphorylation at Thr-198 may trigger initiation of CC centrosome duplication. Phosphorylated by CDK1 at Thr-198, Thr-217, CC Thr-232 and Thr-235 during cell mitosis. When these four sites are CC phosphorated, RNA-binding activity seem to be abolished. May be CC phosphorylated at Ser-70 by NEK2. The Thr-198 phosphorylated form has CC higher affinity for ROCK2 (By similarity). CC {ECO:0000250|UniProtKB:P06748}. CC -!- PTM: Sumoylated by ARF. {ECO:0000250|UniProtKB:P06748}. CC -!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:P06748}. CC -!- PTM: May be ubiquitinated. Ubiquitination leads to proteasomal CC degradation. Deubiquitinated by USP36 (By similarity). CC {ECO:0000250|UniProtKB:P06748}. CC -!- SIMILARITY: Belongs to the nucleoplasmin 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; J03969; AAA40796.1; -; mRNA. DR EMBL; M37039; AAA41730.1; -; Genomic_DNA. DR EMBL; M37035; AAA41730.1; JOINED; Genomic_DNA. DR EMBL; M37036; AAA41730.1; JOINED; Genomic_DNA. DR EMBL; M37037; AAA41730.1; JOINED; Genomic_DNA. DR EMBL; M37038; AAA41730.1; JOINED; Genomic_DNA. DR EMBL; M37041; AAA41731.1; -; Genomic_DNA. DR EMBL; M37035; AAA41731.1; JOINED; Genomic_DNA. DR EMBL; M37036; AAA41731.1; JOINED; Genomic_DNA. DR EMBL; M37037; AAA41731.1; JOINED; Genomic_DNA. DR EMBL; M37038; AAA41731.1; JOINED; Genomic_DNA. DR EMBL; M37040; AAA41731.1; JOINED; Genomic_DNA. DR EMBL; M25062; AAA40795.1; -; Genomic_DNA. DR EMBL; J04943; AAA40794.1; -; mRNA. DR EMBL; J04944; AAA40793.1; -; Genomic_DNA. DR EMBL; BC060579; AAH60579.1; -; mRNA. DR EMBL; BC088088; AAH88088.1; -; mRNA. DR PIR; A28939; A28939. DR PIR; A36089; A36089. DR PIR; B36089; A34168. DR RefSeq; NP_037124.1; NM_012992.4. [P13084-1] DR AlphaFoldDB; P13084; -. DR BMRB; P13084; -. DR SMR; P13084; -. DR BioGRID; 247531; 7. DR IntAct; P13084; 5. DR MINT; P13084; -. DR STRING; 10116.ENSRNOP00000006591; -. DR iPTMnet; P13084; -. DR PhosphoSitePlus; P13084; -. DR SwissPalm; P13084; -. DR jPOST; P13084; -. DR PaxDb; 10116-ENSRNOP00000006591; -. DR GeneID; 25498; -. DR KEGG; rno:25498; -. DR UCSC; RGD:3192; rat. [P13084-1] DR AGR; RGD:3192; -. DR CTD; 4869; -. DR RGD; 3192; Npm1. DR VEuPathDB; HostDB:ENSRNOG00000004616; -. DR eggNOG; KOG0488; Eukaryota. DR HOGENOM; CLU_058838_0_0_1; -. DR InParanoid; P13084; -. DR OrthoDB; 5360624at2759; -. DR PhylomeDB; P13084; -. DR TreeFam; TF327704; -. DR Reactome; R-RNO-3899300; SUMOylation of transcription cofactors. DR Reactome; R-RNO-606279; Deposition of new CENPA-containing nucleosomes at the centromere. DR Reactome; R-RNO-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain. DR Reactome; R-RNO-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation. DR Reactome; R-RNO-9833482; PKR-mediated signaling. DR PRO; PR:P13084; -. DR Proteomes; UP000002494; Chromosome 10. DR Bgee; ENSRNOG00000004616; Expressed in thymus and 19 other cell types or tissues. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0001652; C:granular component; ISO:RGD. DR GO; GO:0015934; C:large ribosomal subunit; ISO:RGD. DR GO; GO:0016363; C:nuclear matrix; IDA:RGD. DR GO; GO:0016607; C:nuclear speck; ISO:RGD. DR GO; GO:0005730; C:nucleolus; ISO:RGD. DR GO; GO:0005654; C:nucleoplasm; IDA:RGD. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:RGD. DR GO; GO:0032993; C:protein-DNA complex; ISO:RGD. DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD. DR GO; GO:0015935; C:small ribosomal subunit; ISO:RGD. DR GO; GO:0031616; C:spindle pole centrosome; ISO:RGD. DR GO; GO:0005524; F:ATP binding; IMP:RGD. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:RGD. DR GO; GO:0003677; F:DNA binding; IDA:RGD. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD. DR GO; GO:0019899; F:enzyme binding; IDA:RGD. DR GO; GO:0042393; F:histone binding; ISO:RGD. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0140693; F:molecular condensate scaffold activity; ISO:RGD. DR GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB. DR GO; GO:0002039; F:p53 binding; IPI:RGD. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IPI:RGD. DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD. DR GO; GO:0043422; F:protein kinase B binding; IDA:RGD. DR GO; GO:0019901; F:protein kinase binding; ISO:RGD. DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB. DR GO; GO:0043023; F:ribosomal large subunit binding; ISO:RGD. DR GO; GO:0043024; F:ribosomal small subunit binding; ISO:RGD. DR GO; GO:0003723; F:RNA binding; ISO:RGD. DR GO; GO:0019843; F:rRNA binding; ISO:RGD. DR GO; GO:0030957; F:Tat protein binding; ISO:RGD. DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD. DR GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB. DR GO; GO:0003300; P:cardiac muscle hypertrophy; IEP:RGD. DR GO; GO:0006884; P:cell volume homeostasis; ISO:RGD. DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD. DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:RGD. DR GO; GO:0034644; P:cellular response to UV; ISO:RGD. DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB. DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central. DR GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IDA:RGD. DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB. DR GO; GO:0097421; P:liver regeneration; IEP:RGD. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:RGD. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0010826; P:negative regulation of centrosome duplication; ISO:RGD. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:RGD. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD. DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISO:RGD. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD. DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; ISS:UniProtKB. DR GO; GO:0006913; P:nucleocytoplasmic transport; ISO:RGD. DR GO; GO:0006334; P:nucleosome assembly; ISO:RGD. DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0031328; P:positive regulation of cellular biosynthetic process; ISO:RGD. DR GO; GO:0010825; P:positive regulation of centrosome duplication; ISO:RGD. DR GO; GO:0051054; P:positive regulation of DNA metabolic process; IDA:RGD. DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:RGD. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; ISO:RGD. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB. DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:RGD. DR GO; GO:0031648; P:protein destabilization; ISO:RGD. DR GO; GO:0008104; P:protein localization; ISO:RGD. DR GO; GO:0050821; P:protein stabilization; ISO:RGD. DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD. DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD. DR GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB. DR GO; GO:0010824; P:regulation of centrosome duplication; ISO:RGD. DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; ISO:RGD. DR GO; GO:0060735; P:regulation of eIF2 alpha phosphorylation by dsRNA; ISS:UniProtKB. DR GO; GO:0032071; P:regulation of endodeoxyribonuclease activity; ISS:UniProtKB. DR GO; GO:0060699; P:regulation of endoribonuclease activity; ISS:UniProtKB. DR GO; GO:1902629; P:regulation of mRNA stability involved in cellular response to UV; ISO:RGD. DR GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:RGD. DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD. DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:RGD. DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; ISO:RGD. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISO:RGD. DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; ISO:RGD. DR GO; GO:0006407; P:rRNA export from nucleus; ISO:RGD. DR GO; GO:0009303; P:rRNA transcription; IMP:RGD. DR Gene3D; 1.10.10.2100; -; 1. DR Gene3D; 2.60.120.340; Nucleoplasmin core domain; 1. DR InterPro; IPR032569; NPM1_C. DR InterPro; IPR004301; Nucleoplasmin. DR InterPro; IPR024057; Nucleoplasmin_core_dom. DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf. DR PANTHER; PTHR22747:SF28; NUCLEOPHOSMIN; 1. DR PANTHER; PTHR22747; NUCLEOPLASMIN; 1. DR Pfam; PF16276; NPM1-C; 1. DR Pfam; PF03066; Nucleoplasmin; 1. DR SUPFAM; SSF69203; Nucleoplasmin-like core domain; 1. DR World-2DPAGE; 0004:P13084; -. DR Genevisible; P13084; RN. PE 1: Evidence at protein level; KW Acetylation; ADP-ribosylation; Alternative splicing; Chaperone; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Disulfide bond; DNA-binding; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; KW Ubl conjugation. FT CHAIN 1..292 FT /note="Nucleophosmin" FT /id="PRO_0000219483" FT REGION 1..185 FT /note="Required for interaction with SENP3" FT /evidence="ECO:0000250" FT REGION 1..117 FT /note="Necessary for interaction with APEX1" FT /evidence="ECO:0000250" FT REGION 138..248 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 241..292 FT /note="Required for nucleolar localization" FT /evidence="ECO:0000250" FT MOTIF 152..157 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 190..196 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 160..185 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 200..216 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 217..234 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 55 FT /note="Interaction between pentamers" FT /evidence="ECO:0000250" FT SITE 80 FT /note="Interaction between pentamers" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 4 FT /note="Phosphoserine; by PLK1 and PLK2" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 32 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 43 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 67 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q61937" FT MOD_RES 70 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 75 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 95 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 125 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 139 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 150 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 154 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 198 FT /note="Phosphothreonine; by CDK1 and CDK2" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 206 FT /note="ADP-ribosylserine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 211 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 217 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000250" FT MOD_RES 225 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 227 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 228 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 232 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 235 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 240 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 248 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 255 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 258 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 265 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 265 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q61937" FT MOD_RES 271 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 277 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT MOD_RES 290 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 27 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 141 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 150 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 214 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 228 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250" FT CROSSLNK 246 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 246 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 248 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 255 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 255 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 261 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250" FT CROSSLNK 261 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 265 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 265 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT CROSSLNK 271 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P06748" FT VAR_SEQ 256..292 FT /note="GGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL -> AH (in FT isoform B23.2)" FT /evidence="ECO:0000303|PubMed:2745414, FT ECO:0000303|PubMed:3417636" FT /id="VSP_003617" SQ SEQUENCE 292 AA; 32560 MW; 1372A474F9ED2457 CRC64; MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE EDAESEDEDE EDVKLLGMSG KRSAPGGGNK VPQKKVKLDE DDDEDDEDDE DDEDDDDDDF DEEETEEKVP VKKSVRDTPA KNAQKSNQNG KDLKPSTPRS KGQESFKKQE KTPKTPKGPS SVEDIKAKMQ ASIEKGGSLP KVEAKFINYV KNCFRMTDQE AIQDLWQWRK SL //