ID PTMA_HUMAN Reviewed; 111 AA. AC P06454; Q15249; Q15592; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 210. DE RecName: Full=Prothymosin alpha; DE Contains: DE RecName: Full=Prothymosin alpha, N-terminally processed; DE Contains: DE RecName: Full=Thymosin alpha-1; GN Name=PTMA; Synonyms=TMSA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3467312; DOI=10.1073/pnas.83.24.9403; RA Eschenfeldt W.H., Berger S.L.; RT "The human prothymosin alpha gene is polymorphic and induced upon growth RT stimulation: evidence using a cloned cDNA."; RL Proc. Natl. Acad. Sci. U.S.A. 83:9403-9407(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=3466166; DOI=10.1073/pnas.83.23.8926; RA Goodall G.J., Dominguez F., Horecker B.L.; RT "Molecular cloning of cDNA for human prothymosin alpha."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8926-8928(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND PARTIAL PROTEIN RP SEQUENCE. RX PubMed=2708378; DOI=10.1016/s0021-9258(18)83269-0; RA Eschenfeldt W.H., Manrow R.E., Krug M.S., Berger S.L.; RT "Isolation and partial sequencing of the human prothymosin alpha gene RT family. Evidence against export of the gene products."; RL J. Biol. Chem. 264:7546-7555(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=2785990; DOI=10.1016/s0021-9258(18)81807-5; RA Gomez-Marquez J., Segade F., Dosil M., Pichel J.G., Bustelo X.R., RA Freire M.; RT "The expression of prothymosin alpha gene in T lymphocytes and leukemic RT lymphoid cells is tied to lymphocyte proliferation."; RL J. Biol. Chem. 264:8451-8454(1989). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Fetal thymus; RA Li Z., Fan Q., Huang W., An L.; RT "A novel prothymosin alpha cDNA from thymus."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Cervix, Lung, PNS, Skin, and Testis; 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15. RX PubMed=7916742; DOI=10.1007/bf00202480; RA Szabo P., Panneerselvam C., Clinton M., Frangou-Lazaridis M., Weksler D., RA Whittington E., Macera M.J., Grzeschik K.H., Selvakumar A., Horecker B.L.; RT "Prothymosin alpha gene in humans: organization of its promoter region and RT localization to chromosome 2."; RL Hum. Genet. 90:629-634(1993). RN [8] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=3532956; DOI=10.1016/0003-9861(86)90717-4; RA Pan L.X., Haritos A.A., Wideman J., Komiyama T., Chang M., Stein S., RA Salvin S.B., Horecker B.L.; RT "Human prothymosin alpha: amino acid sequence and immunologic properties."; RL Arch. Biochem. Biophys. 250:197-201(1986). RN [9] RP PHOSPHORYLATION AT SER-2, AND ACETYLATION AT SER-2. RX PubMed=8485135; DOI=10.1021/bi00068a015; RA Sburlati A.R., De La Rosa A., Batey D.W., Kurys G.L., Manrow R.E., RA Pannell L.K., Martin B.M., Sheeley D.M., Berger S.L.; RT "Phosphorylation of human and bovine prothymosin alpha in vivo."; RL Biochemistry 32:4587-4596(1993). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP INTERACTION WITH NUPR1. RX PubMed=16478804; DOI=10.1073/pnas.0508955103; RA Malicet C., Giroux V., Vasseur S., Dagorn J.C., Neira J.L., Iovanna J.L.; RT "Regulation of apoptosis by the p8/prothymosin alpha complex."; RL Proc. Natl. Acad. Sci. U.S.A. 103:2671-2676(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-102, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-15, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND SER-2, PHOSPHORYLATION RP [LARGE SCALE ANALYSIS] AT SER-2 AND SER-9, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] 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., Buerckstuemmer T., RA 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 [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2 AND SER-10, 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., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-10, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [25] RP STRUCTURE BY NMR OF 2-29, AND ACETYLATION AT SER-2. RX PubMed=22115779; DOI=10.1016/j.bbrc.2011.11.041; RA Elizondo-Riojas M.A., Chamow S.M., Tuthill C.W., Gorenstein D.G., RA Volk D.E.; RT "NMR structure of human thymosin alpha-1."; RL Biochem. Biophys. Res. Commun. 416:356-361(2011). CC -!- FUNCTION: Prothymosin alpha may mediate immune function by conferring CC resistance to certain opportunistic infections. CC -!- SUBUNIT: Interacts with NUPR1; regulates apoptotic process. CC {ECO:0000269|PubMed:16478804}. CC -!- INTERACTION: CC P06454; O60356: NUPR1; NbExp=7; IntAct=EBI-2682091, EBI-3908808; CC P06454; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-2682091, EBI-750109; CC P06454-2; P22607: FGFR3; NbExp=3; IntAct=EBI-10194874, EBI-348399; CC P06454-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-10194874, EBI-8285963; CC P06454-2; Q14145: KEAP1; NbExp=6; IntAct=EBI-10194874, EBI-751001; CC P06454-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10194874, EBI-741480; CC P06454-2; Q9Y649; NbExp=3; IntAct=EBI-10194874, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P06454-1; Sequence=Displayed; CC Name=2; CC IsoId=P06454-2; Sequence=VSP_011508; CC -!- PTM: Covalently linked to a small RNA of about 20 nucleotides. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the pro/parathymosin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44094/PTMA"; 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; M14630; AAA61182.1; -; mRNA. DR EMBL; M14483; AAA61183.1; -; mRNA. DR EMBL; M67480; AAA63240.1; -; Genomic_DNA. DR EMBL; J04797; AAA63240.1; JOINED; Genomic_DNA. DR EMBL; M67480; AAA63239.1; -; Genomic_DNA. DR EMBL; J04797; AAA63239.1; JOINED; Genomic_DNA. DR EMBL; M26708; AAA60213.1; -; mRNA. DR EMBL; AF348514; AAK30146.1; -; mRNA. DR EMBL; BC051265; AAH51265.1; -; mRNA. DR EMBL; BC066905; AAH66905.1; -; mRNA. DR EMBL; BC070480; AAH70480.1; -; mRNA. DR EMBL; BC071647; AAH71647.1; -; mRNA. DR EMBL; BC071879; AAH71879.1; -; mRNA. DR EMBL; S56449; AAD13882.1; -; Genomic_DNA. DR CCDS; CCDS42833.1; -. [P06454-1] DR CCDS; CCDS46541.1; -. [P06454-2] DR PIR; A42004; TNHUA. DR PIR; C33356; C33356. DR RefSeq; NP_001092755.1; NM_001099285.1. [P06454-1] DR RefSeq; NP_002814.3; NM_002823.4. [P06454-2] DR PDB; 2L9I; NMR; -; A=2-29. DR PDB; 2MNQ; NMR; -; A=2-29. DR PDBsum; 2L9I; -. DR PDBsum; 2MNQ; -. DR AlphaFoldDB; P06454; -. DR BMRB; P06454; -. DR SMR; P06454; -. DR BioGRID; 111724; 176. DR CORUM; P06454; -. DR DIP; DIP-40743N; -. DR IntAct; P06454; 37. DR MINT; P06454; -. DR STRING; 9606.ENSP00000344547; -. DR GlyGen; P06454; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P06454; -. DR PhosphoSitePlus; P06454; -. DR SwissPalm; P06454; -. DR BioMuta; PTMA; -. DR EPD; P06454; -. DR jPOST; P06454; -. DR MassIVE; P06454; -. DR MaxQB; P06454; -. DR PaxDb; 9606-ENSP00000344547; -. DR PeptideAtlas; P06454; -. DR ProteomicsDB; 51903; -. [P06454-1] DR ProteomicsDB; 51904; -. [P06454-2] DR Pumba; P06454; -. DR TopDownProteomics; P06454-1; -. [P06454-1] DR TopDownProteomics; P06454-2; -. [P06454-2] DR Antibodypedia; 11847; 395 antibodies from 34 providers. DR DNASU; 5757; -. DR Ensembl; ENST00000341369.11; ENSP00000344547.7; ENSG00000187514.17. [P06454-1] DR Ensembl; ENST00000409115.8; ENSP00000386819.3; ENSG00000187514.17. [P06454-2] DR GeneID; 5757; -. DR KEGG; hsa:5757; -. DR MANE-Select; ENST00000409115.8; ENSP00000386819.3; NM_002823.5; NP_002814.3. [P06454-2] DR UCSC; uc002vsc.5; human. [P06454-1] DR AGR; HGNC:9623; -. DR CTD; 5757; -. DR DisGeNET; 5757; -. DR GeneCards; PTMA; -. DR HGNC; HGNC:9623; PTMA. DR HPA; ENSG00000187514; Low tissue specificity. DR MIM; 188390; gene. DR neXtProt; NX_P06454; -. DR OpenTargets; ENSG00000187514; -. DR PharmGKB; PA33966; -. DR VEuPathDB; HostDB:ENSG00000187514; -. DR eggNOG; ENOG502S55T; Eukaryota. DR GeneTree; ENSGT00940000155762; -. DR HOGENOM; CLU_136539_0_1_1; -. DR InParanoid; P06454; -. DR OMA; CILGMYP; -. DR TreeFam; TF350357; -. DR PathwayCommons; P06454; -. DR SignaLink; P06454; -. DR SIGNOR; P06454; -. DR BioGRID-ORCS; 5757; 277 hits in 1106 CRISPR screens. DR ChiTaRS; PTMA; human. DR GeneWiki; Thymosin_%CE%B11; -. DR GenomeRNAi; 5757; -. DR Pharos; P06454; Tbio. DR PRO; PR:P06454; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P06454; Protein. DR Bgee; ENSG00000187514; Expressed in calcaneal tendon and 99 other cell types or tissues. DR ExpressionAtlas; P06454; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:CAFA. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:CAFA. DR GO; GO:0042393; F:histone binding; IPI:DisProt. DR GO; GO:0043167; F:ion binding; EXP:DisProt. DR GO; GO:0006351; P:DNA-templated transcription; TAS:ProtInc. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR DisProt; DP01677; -. DR IDEAL; IID00699; -. DR InterPro; IPR004931; Pro/parathymosin. DR PANTHER; PTHR22745; PROTHYMOSIN ALPHA; 1. DR PANTHER; PTHR22745:SF0; PROTHYMOSIN ALPHA; 1. DR Pfam; PF03247; Prothymosin; 1. DR Genevisible; P06454; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..111 FT /note="Prothymosin alpha" FT /id="PRO_0000423255" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|PubMed:22115779, FT ECO:0000269|PubMed:8485135, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..111 FT /note="Prothymosin alpha, N-terminally processed" FT /id="PRO_0000299250" FT PEPTIDE 2..29 FT /note="Thymosin alpha-1" FT /id="PRO_0000029865" FT REGION 1..111 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 12..29 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 43..82 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 83..111 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 2 FT /note="N-acetylserine; in Prothymosin alpha, N-terminally FT processed" FT /evidence="ECO:0000269|PubMed:22115779, FT ECO:0000269|PubMed:8485135, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:8485135, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 8 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P01252" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 13 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P01252" FT MOD_RES 14 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P01252" FT MOD_RES 15 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 15 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26350" FT MOD_RES 102 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 103 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26350" FT MOD_RES 107 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 103 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 40 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:2785990, ECO:0000303|PubMed:3466166, FT ECO:0000303|Ref.5" FT /id="VSP_011508" FT HELIX 3..6 FT /evidence="ECO:0007829|PDB:2L9I" FT HELIX 9..28 FT /evidence="ECO:0007829|PDB:2L9I" SQ SEQUENCE 111 AA; 12203 MW; 910BBF9D8D14B8E7 CRC64; MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAE NEENGEQEAD NEVDEEEEEG GEEEEEEEEG DGEEEDGDED EEAESATGKR AAEDDEDDDV DTKKQKTDED D //