PTMA_HUMAN
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 03-AUG-2022, entry version 201.
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="http://atlasgeneticsoncology.org/Genes/PTMAID44094ch2q37.html";
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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; 149.
DR CORUM; P06454; -.
DR DIP; DIP-40743N; -.
DR IntAct; P06454; 35.
DR MINT; P06454; -.
DR STRING; 9606.ENSP00000344547; -.
DR GlyGen; P06454; 1 site, 1 O-linked glycan (1 site).
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; P06454; -.
DR PeptideAtlas; P06454; -.
DR PRIDE; P06454; -.
DR ProteomicsDB; 51903; -. [P06454-1]
DR ProteomicsDB; 51904; -. [P06454-2]
DR TopDownProteomics; P06454-1; -. [P06454-1]
DR TopDownProteomics; P06454-2; -. [P06454-2]
DR Antibodypedia; 11847; 346 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 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 OrthoDB; 1520399at2759; -.
DR TreeFam; TF350357; -.
DR PathwayCommons; P06454; -.
DR SignaLink; P06454; -.
DR SIGNOR; P06454; -.
DR BioGRID-ORCS; 5757; 270 hits in 1048 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 97 other tissues.
DR ExpressionAtlas; P06454; baseline and differential.
DR Genevisible; P06454; HS.
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; IBA:GO_Central.
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 GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc.
DR DisProt; DP01677; -.
DR InterPro; IPR004931; Pro/parathymosin.
DR PANTHER; PTHR22745; PTHR22745; 1.
DR Pfam; PF03247; Prothymosin; 1.
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
