GenomeNet

Database: UniProt
Entry: P04911
LinkDB: P04911
Original site: P04911 
ID   H2A1_YEAST              Reviewed;         132 AA.
AC   P04911; D6VSK7;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   07-APR-2021, entry version 214.
DE   RecName: Full=Histone H2A.1;
GN   Name=HTA1; Synonyms=H2A1, SPT11; OrderedLocusNames=YDR225W;
GN   ORFNames=YD9934.10;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7041122; DOI=10.1073/pnas.79.5.1484;
RA   Choe J., Kolodrubetz D., Grunstein M.;
RT   "The two yeast histone H2A genes encode similar protein subtypes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:1484-1487(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7885847; DOI=10.1093/nar/23.3.507;
RA   Davies C.J., Hutchison C.A. III;
RT   "Insertion site specificity of the transposon Tn3.";
RL   Nucleic Acids Res. 23:507-514(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-132.
RX   PubMed=2848829;
RA   Konrad M.;
RT   "Analysis and in vivo disruption of the gene coding for adenylate kinase
RT   (ADK1) in the yeast Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 263:19468-19474(1988).
RN   [6]
RP   LACK OF UBIQUITINATION, AND MUTAGENESIS OF 120-LYS-LYS-121.
RX   PubMed=2201907; DOI=10.1128/mcb.10.9.4905;
RA   Swerdlow P.S., Schuster T., Finley D.;
RT   "A conserved sequence in histone H2A which is a ubiquitination site in
RT   higher eucaryotes is not required for growth in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 10:4905-4911(1990).
RN   [7]
RP   ACETYLATION AT LYS-5 AND LYS-8.
RX   PubMed=10082517; DOI=10.1128/mcb.19.4.2515;
RA   Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.;
RT   "Esa1p is an essential histone acetyltransferase required for cell cycle
RT   progression.";
RL   Mol. Cell. Biol. 19:2515-2526(1999).
RN   [8]
RP   FUNCTION, MUTAGENESIS OF SER-129, AND PHOSPHORYLATION AT SER-129.
RX   PubMed=11140636; DOI=10.1038/35050000;
RA   Downs J.A., Lowndes N.F., Jackson S.P.;
RT   "A role for Saccharomyces cerevisiae histone H2A in DNA repair.";
RL   Nature 408:1001-1004(2000).
RN   [9]
RP   LACK OF UBIQUITINATION, AND MUTAGENESIS OF 120-LYS-LYS-121; LYS-124 AND
RP   LYS-127.
RX   PubMed=10642555; DOI=10.1126/science.287.5452.501;
RA   Robzyk K., Recht J., Osley M.A.;
RT   "Rad6-dependent ubiquitination of histone H2B in yeast.";
RL   Science 287:501-504(2000).
RN   [10]
RP   ACETYLATION AT LYS-8.
RX   PubMed=11545749; DOI=10.1016/s1097-2765(01)00301-x;
RA   Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.;
RT   "Highly specific antibodies determine histone acetylation site usage in
RT   yeast heterochromatin and euchromatin.";
RL   Mol. Cell 8:473-479(2001).
RN   [11]
RP   ACETYLATION AT SER-2.
RX   PubMed=12915400; DOI=10.1074/jbc.c300355200;
RA   Song O.-K., Wang X., Waterborg J.H., Sternglanz R.;
RT   "An Nalpha-acetyltransferase responsible for acetylation of the N-terminal
RT   residues of histones H4 and H2A.";
RL   J. Biol. Chem. 278:38109-38112(2003).
RN   [12]
RP   FUNCTION, AND PHOSPHORYLATION.
RX   PubMed=15458641; DOI=10.1016/j.cub.2004.09.047;
RA   Shroff R., Arbel-Eden A., Pilch D.R., Ira G., Bonner W.M., Petrini J.H.J.,
RA   Haber J.E., Lichten M.;
RT   "Distribution and dynamics of chromatin modification induced by a defined
RT   DNA double-strand break.";
RL   Curr. Biol. 14:1703-1711(2004).
RN   [13]
RP   INTERACTION WITH ARP4.
RX   PubMed=15610740; DOI=10.1016/j.molcel.2004.12.003;
RA   Downs J.A., Allard S., Jobin-Robitaille O., Javaheri A., Auger A.,
RA   Bouchard N., Kron S.J., Jackson S.P., Cote J.;
RT   "Binding of chromatin-modifying activities to phosphorylated histone H2A at
RT   DNA damage sites.";
RL   Mol. Cell 16:979-990(2004).
RN   [14]
RP   FUNCTION, AND PHOSPHORYLATION.
RX   PubMed=15610741; DOI=10.1016/j.molcel.2004.11.027;
RA   Uenal E., Arbel-Eden A., Sattler U., Shroff R., Lichten M., Haber J.E.,
RA   Koshland D.;
RT   "DNA damage response pathway uses histone modification to assemble a
RT   double-strand break-specific cohesin domain.";
RL   Mol. Cell 16:991-1002(2004).
RN   [15]
RP   MUTAGENESIS OF SER-122.
RX   PubMed=15781691; DOI=10.1534/genetics.104.038570;
RA   Harvey A.C., Jackson S.P., Downs J.A.;
RT   "Saccharomyces cerevisiae histone H2A Ser122 facilitates DNA repair.";
RL   Genetics 170:543-553(2005).
RN   [16]
RP   SUMOYLATION AT LYS-127.
RX   PubMed=16598039; DOI=10.1101/gad.1404206;
RA   Nathan D., Ingvarsdottir K., Sterner D.E., Bylebyl G.R., Dokmanovic M.,
RA   Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S., Meluh P.B.,
RA   Johnson E.S., Berger S.L.;
RT   "Histone sumoylation is a negative regulator in Saccharomyces cerevisiae
RT   and shows dynamic interplay with positive-acting histone modifications.";
RL   Genes Dev. 20:966-976(2006).
RN   [17]
RP   FUNCTION, AND DEPHOSPHORYLATION.
RX   PubMed=16299494; DOI=10.1038/nature04384;
RA   Keogh M.-C., Kim J.-A., Downey M., Fillingham J., Chowdhury D.,
RA   Harrison J.C., Onishi M., Datta N., Galicia S., Emili A., Lieberman J.,
RA   Shen X., Buratowski S., Haber J.E., Durocher D., Greenblatt J.F.,
RA   Krogan N.J.;
RT   "A phosphatase complex that dephosphorylates gamma-H2AX regulates DNA
RT   damage checkpoint recovery.";
RL   Nature 439:497-501(2006).
RN   [18]
RP   SUCCINYLATION AT LYS-14 AND LYS-22, AND MALONYLATION AT LYS-120.
RX   PubMed=22389435; DOI=10.1074/mcp.m111.015875;
RA   Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT   "Lysine succinylation and lysine malonylation in histones.";
RL   Mol. Cell. Proteomics 11:100-107(2012).
RN   [19]
RP   METHYLATION AT GLN-106.
RX   PubMed=24352239; DOI=10.1038/nature12819;
RA   Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J.,
RA   Nielsen M.L., Kouzarides T.;
RT   "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
RT   modification.";
RL   Nature 505:564-568(2014).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
RX   PubMed=11566884; DOI=10.1093/emboj/20.18.5207;
RA   White C.L., Suto R.K., Luger K.;
RT   "Structure of the yeast nucleosome core particle reveals fundamental
RT   changes in internucleosome interactions.";
RL   EMBO J. 20:5207-5218(2001).
CC   -!- FUNCTION: Core component of nucleosome which plays a central role in
CC       DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA
CC       into chromatin, limiting DNA accessibility to the cellular machineries
CC       which require DNA as a template. Histones thereby play a central role
CC       in transcription regulation, DNA repair, DNA replication and
CC       chromosomal stability. DNA accessibility is regulated via a complex set
CC       of post-translational modifications of histones, also called histone
CC       code, and nucleosome remodeling. {ECO:0000269|PubMed:11140636,
CC       ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15610741,
CC       ECO:0000269|PubMed:16299494}.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC       each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC       two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC       DNA.
CC   -!- INTERACTION:
CC       P04911; P25293: NAP1; NbExp=3; IntAct=EBI-8072, EBI-11850;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC       from the PI3/PI4-kinase family.
CC   -!- PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA
CC       double-strand breaks (DSBs) generated by exogenous genotoxic agents and
CC       by stalled replication forks. Phosphorylation is dependent on the DNA
CC       damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side
CC       of a detected DSB site and may mark the surrounding chromatin for
CC       recruitment of proteins required for DNA damage signaling and repair.
CC       Gamma-H2A interacts with ARP4, a shared component of the NuA4 histone
CC       acetyltransferase complex and the INO80 and SWR1 chromatin remodeling
CC       complexes, and serves to recruit first NuA4, mediating histone H4
CC       acetylation, and subsequently the INO80/SWR1 complexes, facilitating
CC       DNA resection, to DSB sites. Gamma-H2A is required for sequestering
CC       cohesin around the break site, which is important for efficient post-
CC       replicative double-strand break repair by homologous recombination,
CC       holding the damaged chromatid close to its undamaged sister template.
CC       Gamma-H2A is removed from the DNA prior to the strand invasion-primer
CC       extension step of the repair process and subsequently dephosphorylated
CC       by PPH3, a component of the histone H2A phosphatase complex (HTP-C).
CC       Dephosphorylation is necessary for efficient recovery from the DNA
CC       damage checkpoint. {ECO:0000269|PubMed:11140636,
CC       ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15610741}.
CC   -!- PTM: N-acetylated by NAT4.
CC   -!- PTM: Acetylated by ESA1, a component of the NuA4 histone
CC       acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac.
CC   -!- PTM: Glutamine methylation at Gln-106 (H2AQ105me) by NOP1 is
CC       specifically dedicated to polymerase I. It is present at 35S ribosomal
CC       DNA locus and impairs binding of the FACT complex (PubMed:24352239).
CC       {ECO:0000269|PubMed:24352239}.
CC   -!- PTM: Sumoylated to from H2AK126su. May lead to transcriptional
CC       repression. {ECO:0000269|PubMed:16598039}.
CC   -!- MISCELLANEOUS: In contrast to vertebrates and insects, its C-terminus
CC       is not monoubiquitinated.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC   -!- CAUTION: To ensure consistency between histone entries, we follow the
CC       'Brno' nomenclature for histone modifications, with positions referring
CC       to those used in the literature for the 'closest' model organism. Due
CC       to slight variations in histone sequences between organisms and to the
CC       presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC       actual positions of modified amino acids in the sequence generally
CC       differ. In this entry the following conventions are used: H2AK4ac =
CC       acetylated Lys-5; H2AK7ac = acetylated Lys-8; H2AK126su = sumoylated
CC       Lys-127; H2AS128ph = phosphorylated Ser-129. {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; V01304; CAA24611.1; -; Genomic_DNA.
DR   EMBL; U13239; AAC33142.1; -; Genomic_DNA.
DR   EMBL; Z48612; CAA88505.1; -; Genomic_DNA.
DR   EMBL; M18455; AAA66318.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12067.1; -; Genomic_DNA.
DR   PIR; S05813; HSBYA1.
DR   RefSeq; NP_010511.3; NM_001180533.3.
DR   PDB; 1ID3; X-ray; 3.10 A; C/G=2-132.
DR   PDB; 3T7K; X-ray; 2.03 A; C/D=125-132.
DR   PDB; 4WNN; X-ray; 1.80 A; A/C/E/G=1-132.
DR   PDB; 5BT1; X-ray; 2.62 A; C=1-132.
DR   PDB; 6GEJ; EM; 3.60 A; E/F=1-132.
DR   PDB; 6GEN; EM; 3.60 A; E/F=1-132.
DR   PDB; 6QLD; EM; 4.15 A; g=17-121, i=17-118.
DR   PDBsum; 1ID3; -.
DR   PDBsum; 3T7K; -.
DR   PDBsum; 4WNN; -.
DR   PDBsum; 5BT1; -.
DR   PDBsum; 6GEJ; -.
DR   PDBsum; 6GEN; -.
DR   PDBsum; 6QLD; -.
DR   SMR; P04911; -.
DR   BioGRID; 32277; 636.
DR   ComplexPortal; CPX-1612; Nucleosome, variant HTA1-HTB1.
DR   ComplexPortal; CPX-2566; Nucleosome, variant HTA1-HTB2.
DR   DIP; DIP-419N; -.
DR   ELM; P04911; -.
DR   IntAct; P04911; 54.
DR   MINT; P04911; -.
DR   STRING; 4932.YDR225W; -.
DR   iPTMnet; P04911; -.
DR   MaxQB; P04911; -.
DR   PaxDb; P04911; -.
DR   PRIDE; P04911; -.
DR   EnsemblFungi; YDR225W_mRNA; YDR225W; YDR225W.
DR   GeneID; 851811; -.
DR   KEGG; sce:YDR225W; -.
DR   SGD; S000002633; HTA1.
DR   VEuPathDB; FungiDB:YDR225W; -.
DR   eggNOG; KOG1756; Eukaryota.
DR   GeneTree; ENSGT01020000230360; -.
DR   HOGENOM; CLU_062828_3_0_1; -.
DR   InParanoid; P04911; -.
DR   OMA; KANSGRD; -.
DR   Reactome; R-SCE-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR   Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR   Reactome; R-SCE-427359; SIRT1 negatively regulates rRNA expression.
DR   Reactome; R-SCE-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR   EvolutionaryTrace; P04911; -.
DR   PRO; PR:P04911; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P04911; protein.
DR   GO; GO:0000786; C:nucleosome; TAS:SGD.
DR   GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; TAS:SGD.
DR   GO; GO:0006342; P:chromatin silencing; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IMP:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
DR   CDD; cd00074; H2A; 1.
DR   Gene3D; 1.10.20.10; -; 1.
DR   IDEAL; IID50063; -.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   InterPro; IPR032458; Histone_H2A_CS.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding;
KW   Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12915400"
FT   CHAIN           2..132
FT                   /note="Histone H2A.1"
FT                   /id="PRO_0000055326"
FT   MOTIF           129..130
FT                   /note="[ST]-Q motif"
FT   SITE            120
FT                   /note="Not ubiquitinated"
FT                   /evidence="ECO:0000269|PubMed:10642555,
FT                   ECO:0000269|PubMed:2201907"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:12915400"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:10082517"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:10082517,
FT                   ECO:0000269|PubMed:11545749"
FT   MOD_RES         14
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:22389435"
FT   MOD_RES         22
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:22389435"
FT   MOD_RES         106
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000269|PubMed:24352239"
FT   MOD_RES         120
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:22389435"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:11140636"
FT   CROSSLNK        127
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   MUTAGEN         120..121
FT                   /note="KK->RR: No effect. No effect; when associated with
FT                   R-124 and R-127."
FT                   /evidence="ECO:0000269|PubMed:10642555,
FT                   ECO:0000269|PubMed:2201907"
FT   MUTAGEN         122
FT                   /note="S->A,E: Causes hypersensitivity to DNA-damage-
FT                   inducing agents and impairs sporulation."
FT                   /evidence="ECO:0000269|PubMed:15781691"
FT   MUTAGEN         124
FT                   /note="K->R: No effect; when associated with R-120; R-121
FT                   and R-127."
FT                   /evidence="ECO:0000269|PubMed:10642555"
FT   MUTAGEN         127
FT                   /note="K->R: No effect; when associated with R-120; R-121
FT                   and R-124."
FT                   /evidence="ECO:0000269|PubMed:10642555"
FT   MUTAGEN         129
FT                   /note="S->A: Causes hypersensitivity to DNA-damage-inducing
FT                   agents."
FT                   /evidence="ECO:0000269|PubMed:11140636"
FT   MUTAGEN         129
FT                   /note="S->E,T: No effect."
FT                   /evidence="ECO:0000269|PubMed:11140636"
FT   HELIX           19..23
FT                   /evidence="ECO:0007744|PDB:4WNN"
FT   HELIX           29..38
FT                   /evidence="ECO:0007744|PDB:4WNN"
FT   STRAND          41..45
FT                   /evidence="ECO:0007744|PDB:4WNN"
FT   HELIX           48..74
FT                   /evidence="ECO:0007744|PDB:4WNN"
FT   STRAND          78..80
FT                   /evidence="ECO:0007744|PDB:4WNN"
FT   HELIX           82..90
FT                   /evidence="ECO:0007744|PDB:4WNN"
FT   HELIX           93..99
FT                   /evidence="ECO:0007744|PDB:4WNN"
FT   STRAND          102..104
FT                   /evidence="ECO:0007744|PDB:1ID3"
FT   HELIX           115..117
FT                   /evidence="ECO:0007744|PDB:1ID3"
SQ   SEQUENCE   132 AA;  13989 MW;  A908C94A0363D13F CRC64;
     MSGGKGGKAG SAAKASQSRS AKAGLTFPVG RVHRLLRRGN YAQRIGSGAP VYLTAVLEYL
     AAEILELAGN AARDNKKTRI IPRHLQLAIR NDDELNKLLG NVTIAQGGVL PNIHQNLLPK
     KSAKATKASQ EL
//
DBGET integrated database retrieval system