TYB4_HUMAN
ID TYB4_HUMAN Reviewed; 44 AA.
AC P62328; P01253; P01254; Q546P5; Q63576; Q9UE55;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Thymosin beta-4 {ECO:0000303|PubMed:3500230};
DE Short=T beta-4;
DE AltName: Full=Fx {ECO:0000303|PubMed:1999398};
DE Contains:
DE RecName: Full=Hemoregulatory peptide AcSDKP {ECO:0000305};
DE AltName: Full=Ac-Ser-Asp-Lys-Pro {ECO:0000303|PubMed:7694679};
DE AltName: Full=N-acetyl-SDKP;
DE Short=AcSDKP {ECO:0000303|PubMed:7694679};
DE AltName: Full=Seraspenide {ECO:0000303|PubMed:7694679};
GN Name=TMSB4X; Synonyms=TB4X, THYB4, TMSB4;
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], INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=3500230;
RA Gondo H., Kudo J., White J.W., Barr C., Selvanayagam P., Saunders G.F.;
RT "Differential expression of the human thymosin-beta 4 gene in lymphocytes,
RT macrophages, and granulocytes.";
RL J. Immunol. 139:3840-3848(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16010977; DOI=10.1007/s11010-005-7642-4;
RA Yang S.P., Lee H.J., Su Y.;
RT "Molecular cloning and structural characterization of the functional human
RT thymosin beta4 gene.";
RL Mol. Cell. Biochem. 272:97-105(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-44, FUNCTION, INTERACTION WITH ACTIN, CLEAVAGE OF
RP INITIATOR METHIONINE, AND ACETYLATION AT SER-2.
RX PubMed=1999398; DOI=10.1016/s0021-9258(20)64278-8;
RA Safer D., Elzinga M., Nachmias V.T.;
RT "Thymosin beta 4 and Fx, an actin-sequestering peptide, are
RT indistinguishable.";
RL J. Biol. Chem. 266:4029-4032(1991).
RN [5]
RP PROTEIN SEQUENCE OF 2-44, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP ACETYLATION AT SER-2.
RC TISSUE=Tear;
RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
RA Suarez T., Elortza F.;
RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed
RT by in silico and in vitro analyses for antimicrobial peptide
RT identification.";
RL J. Proteome Res. 14:2649-2658(2015).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-44, AND INDUCTION.
RX PubMed=6548414; DOI=10.1016/0092-8674(84)90270-8;
RA Friedman R.L., Manly S.P., McMahon M., Kerr I.M., Stark G.R.;
RT "Transcriptional and posttranscriptional regulation of interferon-induced
RT gene expression in human cells.";
RL Cell 38:745-755(1984).
RN [7]
RP DEGRADATION (HEMOREGULATORY PEPTIDE ACSDKP).
RX PubMed=8257427; DOI=10.1042/bj2960373;
RA Rieger K.J., Saez-Servent N., Papet M.P., Wdzieczak-Bakala J., Morgat J.L.,
RA Thierry J., Voelter W., Lenfant M.;
RT "Involvement of human plasma angiotensin I-converting enzyme in the
RT degradation of the haemoregulatory peptide N-acetyl-seryl-aspartyl-lysyl-
RT proline.";
RL Biochem. J. 296:373-378(1993).
RN [8]
RP FUNCTION (HEMOREGULATORY PEPTIDE ACSDKP).
RX PubMed=7694679;
RA Bonnet D., Lemoine F.M., Pontvert-Delucq S., Baillou C., Najman A.,
RA Guigon M.;
RT "Direct and reversible inhibitory effect of the tetrapeptide acetyl-N-Ser-
RT Asp-Lys-Pro (Seraspenide) on the growth of human CD34+ subpopulations in
RT response to growth factors.";
RL Blood 82:3307-3314(1993).
RN [9]
RP DEGRADATION (HEMOREGULATORY PEPTIDE ACSDKP).
RX PubMed=7876104; DOI=10.1074/jbc.270.8.3656;
RA Rousseau A., Michaud A., Chauvet M.T., Lenfant M., Corvol P.;
RT "The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and
RT specific substrate of the N-terminal active site of human angiotensin-
RT converting enzyme.";
RL J. Biol. Chem. 270:3656-3661(1995).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-12; LYS-26; LYS-32 AND
RP LYS-39, AND IDENTIFICATION BY MASS 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 [12]
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].
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 [13]
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 [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=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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-23; SER-31 AND THR-34,
RP AND 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12, 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 [18]
RP STRUCTURE BY NMR OF WILD-TYPE AND OF MUTANTS LYS-12; SER-16 AND LEU-18 IN
RP COMPLEX WITH ACTIN, AND FUNCTION.
RX PubMed=10848969; DOI=10.1046/j.1432-1327.2000.01380.x;
RA Simenel C., Van Troys M., Vandekerckhove J., Ampe C., Delepierre M.;
RT "Structural requirements for thymosin beta4 in its contact with actin. An
RT NMR-analysis of thymosin beta4 mutants in solution and correlation with
RT their biological activity.";
RL Eur. J. Biochem. 267:3530-3538(2000).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-44 IN COMPLEX WITH ACTA1; GSN
RP AND COBL, AND SUBUNIT.
RX PubMed=23009842; DOI=10.1016/j.bpj.2012.07.030;
RA Durer Z.A., Kudryashov D.S., Sawaya M.R., Altenbach C., Hubbell W.,
RA Reisler E.;
RT "Structural states and dynamics of the D-loop in actin.";
RL Biophys. J. 103:930-939(2012).
CC -!- FUNCTION: Plays an important role in the organization of the
CC cytoskeleton (PubMed:1999398, PubMed:10848969). Binds to and sequesters
CC actin monomers (G actin) and therefore inhibits actin polymerization
CC (PubMed:1999398, PubMed:10848969). {ECO:0000269|PubMed:10848969,
CC ECO:0000269|PubMed:1999398}.
CC -!- FUNCTION: [Hemoregulatory peptide AcSDKP]: Potent inhibitor of bone
CC marrow derived stem cell differentiation (PubMed:7694679). Acts by
CC inhibits the entry of hematopoietic pluripotent stem cells into the S-
CC phase (By similarity). {ECO:0000250|UniProtKB:P62326,
CC ECO:0000269|PubMed:7694679}.
CC -!- SUBUNIT: Identified in a complex composed of ACTA1, COBL, GSN AND
CC TMSB4X (PubMed:23009842). Interacts with SERPINB1 (By similarity).
CC {ECO:0000250|UniProtKB:P62326, ECO:0000269|PubMed:23009842}.
CC -!- INTERACTION:
CC P62328; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-712598, EBI-357530;
CC P62328; P05067: APP; NbExp=3; IntAct=EBI-712598, EBI-77613;
CC P62328; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-712598, EBI-3866319;
CC P62328; Q13643: FHL3; NbExp=3; IntAct=EBI-712598, EBI-741101;
CC P62328; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-712598, EBI-5916454;
CC P62328; O75031: HSF2BP; NbExp=3; IntAct=EBI-712598, EBI-7116203;
CC P62328; Q15323: KRT31; NbExp=3; IntAct=EBI-712598, EBI-948001;
CC P62328; O76011: KRT34; NbExp=3; IntAct=EBI-712598, EBI-1047093;
CC P62328; O76013-2: KRT36; NbExp=3; IntAct=EBI-712598, EBI-11958506;
CC P62328; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-712598, EBI-10261141;
CC P62328; P40692: MLH1; NbExp=16; IntAct=EBI-712598, EBI-744248;
CC P62328; Q8TAS1-2: UHMK1; NbExp=3; IntAct=EBI-712598, EBI-12157345;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:1999398}.
CC -!- TISSUE SPECIFICITY: Expressed in several hemopoietic cell lines and
CC lymphoid malignant cells. Decreased levels in myeloma cells.
CC {ECO:0000269|PubMed:3500230}.
CC -!- INDUCTION: By alpha interferons. Decreased levels in THP-1 cells after
CC treatment with recombinant interferon-lambda.
CC {ECO:0000269|PubMed:3500230, ECO:0000269|PubMed:6548414}.
CC -!- PTM: [Hemoregulatory peptide AcSDKP]: AcSDKP is inactivated by ACE,
CC which removes the dipeptide Lys-Pro from its C-terminus.
CC {ECO:0000269|PubMed:7876104, ECO:0000269|PubMed:8257427}.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR EMBL; M17733; AAA36745.1; -; mRNA.
DR EMBL; AJ295158; CAC43317.1; -; Genomic_DNA.
DR EMBL; BT007090; AAP35753.1; -; mRNA.
DR EMBL; X02493; CAA26323.1; -; mRNA.
DR CCDS; CCDS35202.1; -.
DR PIR; I56000; A38682.
DR RefSeq; NP_066932.1; NM_021109.3.
DR PDB; 3TU5; X-ray; 3.00 A; B=21-44.
DR PDB; 4PL7; X-ray; 2.30 A; A/B=2-44.
DR PDB; 4PL8; X-ray; 2.00 A; H=2-44.
DR PDBsum; 3TU5; -.
DR PDBsum; 4PL7; -.
DR PDBsum; 4PL8; -.
DR AlphaFoldDB; P62328; -.
DR BMRB; P62328; -.
DR SMR; P62328; -.
DR BioGRID; 112969; 41.
DR IntAct; P62328; 44.
DR MINT; P62328; -.
DR STRING; 9606.ENSP00000370010; -.
DR MoonDB; P62328; Curated.
DR MoonProt; P62328; -.
DR iPTMnet; P62328; -.
DR PhosphoSitePlus; P62328; -.
DR BioMuta; TMSB4X; -.
DR DMDM; 78103211; -.
DR DOSAC-COBS-2DPAGE; P62328; -.
DR EPD; P62328; -.
DR jPOST; P62328; -.
DR MassIVE; P62328; -.
DR MaxQB; P62328; -.
DR PaxDb; P62328; -.
DR PeptideAtlas; P62328; -.
DR PRIDE; P62328; -.
DR ProteomicsDB; 57395; -.
DR TopDownProteomics; P62328; -.
DR Antibodypedia; 8508; 279 antibodies from 28 providers.
DR DNASU; 7114; -.
DR Ensembl; ENST00000380633.1; ENSP00000370007.1; ENSG00000205542.11.
DR Ensembl; ENST00000380635.5; ENSP00000370009.1; ENSG00000205542.11.
DR Ensembl; ENST00000380636.1; ENSP00000370010.1; ENSG00000205542.11.
DR Ensembl; ENST00000451311.7; ENSP00000414376.2; ENSG00000205542.11.
DR GeneID; 7114; -.
DR KEGG; hsa:7114; -.
DR MANE-Select; ENST00000451311.7; ENSP00000414376.2; NM_021109.4; NP_066932.1.
DR UCSC; uc004cvf.4; human.
DR CTD; 7114; -.
DR DisGeNET; 7114; -.
DR GeneCards; TMSB4X; -.
DR HGNC; HGNC:11881; TMSB4X.
DR HPA; ENSG00000205542; Low tissue specificity.
DR MIM; 300159; gene.
DR neXtProt; NX_P62328; -.
DR OpenTargets; ENSG00000205542; -.
DR PharmGKB; PA36581; -.
DR VEuPathDB; HostDB:ENSG00000205542; -.
DR eggNOG; KOG4794; Eukaryota.
DR GeneTree; ENSGT00940000154433; -.
DR HOGENOM; CLU_208046_0_0_1; -.
DR InParanoid; P62328; -.
DR OrthoDB; 1632292at2759; -.
DR PhylomeDB; P62328; -.
DR PathwayCommons; P62328; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; P62328; -.
DR BioGRID-ORCS; 7114; 8 hits in 636 CRISPR screens.
DR ChiTaRS; TMSB4X; human.
DR GeneWiki; Thymosin_beta-4; -.
DR GenomeRNAi; 7114; -.
DR Pharos; P62328; Tbio.
DR PRO; PR:P62328; -.
DR Proteomes; UP000005640; Chromosome X.
DR Bgee; ENSG00000205542; Expressed in monocyte and 94 other tissues.
DR ExpressionAtlas; P62328; baseline and differential.
DR Genevisible; P62328; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0003785; F:actin monomer binding; IDA:CAFA.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IMP:CAFA.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; IDA:UniProtKB.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IDA:CAFA.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:CAFA.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:CAFA.
DR GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IDA:CAFA.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IDA:CAFA.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:CAFA.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IDA:CAFA.
DR GO; GO:1905273; P:positive regulation of proton-transporting ATP synthase activity, rotational mechanism; IDA:CAFA.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:CAFA.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IGI:CAFA.
DR GO; GO:0042989; P:sequestering of actin monomers; IDA:CAFA.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:CAFA.
DR DisProt; DP00357; -.
DR Gene3D; 1.20.5.520; -; 1.
DR InterPro; IPR001152; Beta-thymosin.
DR InterPro; IPR038386; Beta-thymosin_sf.
DR PANTHER; PTHR12021; PTHR12021; 1.
DR Pfam; PF01290; Thymosin; 1.
DR PIRSF; PIRSF001828; Thymosin_beta; 1.
DR SMART; SM00152; THY; 1.
DR PROSITE; PS00500; THYMOSIN_B4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1999398,
FT ECO:0000269|PubMed:25946035, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895"
FT CHAIN 2..44
FT /note="Thymosin beta-4"
FT /evidence="ECO:0000269|PubMed:25946035"
FT /id="PRO_0000045920"
FT PEPTIDE 2..5
FT /note="Hemoregulatory peptide AcSDKP"
FT /evidence="ECO:0000305|PubMed:7694679"
FT /id="PRO_0000034295"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:1999398,
FT ECO:0000269|PubMed:25946035, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 12
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 26
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 32
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 12
FT /note="K->P: Very weak actin binding; no inhibition of
FT actin polymerization."
FT MUTAGEN 16
FT /note="S->A: Binds actin 2.5-fold less than wild-type;
FT little change in inhibition of actin polymerization."
FT MUTAGEN 16
FT /note="S->AS: Very weak actin binding; no inhibition of
FT actin polymerization."
FT MUTAGEN 18
FT /note="L->A,P: Very weak actin binding; no inhibition of
FT actin polymerization."
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:4PL8"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4PL8"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:4PL7"
SQ SEQUENCE 44 AA; 5053 MW; 440C6158482DAAD0 CRC64;
MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES
