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H2B3A_MOUSE
ID   H2B3A_MOUSE             Reviewed;         126 AA.
AC   Q9D2U9;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=H2B.U histone 2 {ECO:0000312|MGI:MGI:1925553};
DE   AltName: Full=Histone H2B type 3-A;
GN   Name=H2bu2 {ECO:0000312|MGI:MGI:1925553};
GN   Synonyms=Hist3h2ba {ECO:0000303|PubMed:12408966};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12408966; DOI=10.1006/geno.2002.6850;
RA   Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT   "The human and mouse replication-dependent histone genes.";
RL   Genomics 80:487-498(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [4]
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-15.
RX   PubMed=15197225; DOI=10.1084/jem.20032247;
RA   Fernandez-Capetillo O., Allis C.D., Nussenzweig A.;
RT   "Phosphorylation of histone H2B at DNA double-strand breaks.";
RL   J. Exp. Med. 199:1671-1677(2004).
RN   [5]
RP   PHOSPHORYLATION AT SER-15.
RX   PubMed=16039583; DOI=10.1016/j.immuni.2005.05.007;
RA   Odegard V.H., Kim S.T., Anderson S.M., Shlomchik M.J., Schatz D.G.;
RT   "Histone modifications associated with somatic hypermutation.";
RL   Immunity 23:101-110(2005).
RN   [6]
RP   PHOSPHORYLATION AT SER-37.
RX   PubMed=20647423; DOI=10.1126/science.1191241;
RA   Bungard D., Fuerth B.J., Zeng P.Y., Faubert B., Maas N.L., Viollet B.,
RA   Carling D., Thompson C.B., Jones R.G., Berger S.L.;
RT   "Signaling kinase AMPK activates stress-promoted transcription via histone
RT   H2B phosphorylation.";
RL   Science 329:1201-1205(2010).
RN   [7]
RP   CROTONYLATION AT LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND LYS-35.
RX   PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA   Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA   Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J.,
RA   Ye Y., Khochbin S., Ren B., Zhao Y.;
RT   "Identification of 67 histone marks and histone lysine crotonylation as a
RT   new type of histone modification.";
RL   Cell 146:1016-1028(2011).
RN   [8]
RP   SUCCINYLATION AT LYS-121.
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   [9]
RP   HYDROXYBUTYRYLATION AT LYS-13; LYS-21; LYS-24; LYS-25; LYS-35; LYS-44;
RP   LYS-47; LYS-58; LYS-86; LYS-109; LYS-117 AND LYS-121.
RX   PubMed=24681537; DOI=10.1038/nchembio.1497;
RA   Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., Debernardi A.,
RA   Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., Allis C.D., Ren B.,
RA   Khochbin S., Zhao Y.;
RT   "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone
RT   mark.";
RL   Nat. Chem. Biol. 10:365-370(2014).
RN   [10]
RP   HYDROXYBUTYRYLATION AT LYS-12; LYS-21; LYS-35; LYS-109 AND LYS-117.
RX   PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
RA   Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
RA   Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
RA   Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
RA   White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
RT   "Metabolic regulation of gene expression by histone lysine beta-
RT   hydroxybutyrylation.";
RL   Mol. Cell 62:194-206(2016).
RN   [11]
RP   LACTYLATION AT LYS-12; LYS-16; LYS-17; LYS-21; LYS-86; LYS-109 AND LYS-117.
RX   PubMed=31645732; DOI=10.1038/s41586-019-1678-1;
RA   Zhang D., Tang Z., Huang H., Zhou G., Cui C., Weng Y., Liu W., Kim S.,
RA   Lee S., Perez-Neut M., Ding J., Czyz D., Hu R., Ye Z., He M., Zheng Y.G.,
RA   Shuman H.A., Dai L., Ren B., Roeder R.G., Becker L., Zhao Y.;
RT   "Metabolic regulation of gene expression by histone lactylation.";
RL   Nature 574:575-580(2019).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH THE NUCLEOSOME CORE
RP   PARTICLE.
RX   PubMed=16107708; DOI=10.1128/mcb.25.17.7616-7624.2005;
RA   Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., Pehrson J.R.,
RA   Khochbin S., Luger K.;
RT   "Structural characterization of the histone variant macroH2A.";
RL   Mol. Cell. Biol. 25:7616-7624(2005).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC       DNA into chromatin, limiting DNA accessibility to the cellular
CC       machineries which require DNA as a template. Histones thereby play a
CC       central role in transcription regulation, DNA repair, DNA replication
CC       and chromosomal stability. DNA accessibility is regulated via a complex
CC       set of post-translational modifications of histones, also called
CC       histone code, and nucleosome remodeling.
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. {ECO:0000269|PubMed:16107708}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15197225}. Chromosome
CC       {ECO:0000269|PubMed:15197225}.
CC   -!- PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is
CC       required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me)
CC       methylation and transcription activation at specific gene loci, such as
CC       HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121
CC       (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic
CC       transcriptional activation and is also prerequisite for histone H3
CC       'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with
CC       the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub
CC       also acts as a regulator of mRNA splicing: deubiquitination by USP49 is
CC       required for efficient cotranscriptional splicing of a large set of
CC       exons (By similarity). {ECO:0000250|UniProtKB:P33778}.
CC   -!- PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis;
CC       which facilitates apoptotic chromatin condensation. Also phosphorylated
CC       on Ser-15 in response to DNA double strand breaks (DSBs), and in
CC       correlation with somatic hypermutation and immunoglobulin class-switch
CC       recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response
CC       to stress promotes transcription. {ECO:0000269|PubMed:15197225,
CC       ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423}.
CC   -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC       marks testis-specific genes in post-meiotic cells, including X-linked
CC       genes that escape sex chromosome inactivation in haploid cells.
CC       Crotonylation marks active promoters and enhancers and confers
CC       resistance to transcriptional repressors. It is also associated with
CC       post-meiotically activated genes on autosomes.
CC       {ECO:0000269|PubMed:21925322}.
CC   -!- PTM: Hydroxybutyrylation of histones is induced by starvation.
CC       {ECO:0000269|PubMed:27105115}.
CC   -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC       directly derived from endogenous or exogenous lactate, leading to
CC       stimulates gene transcription. {ECO:0000250|UniProtKB:P33778}.
CC   -!- MISCELLANEOUS: The human orthologous protein seems not to exist.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   EMBL; AY158942; AAO06252.1; -; Genomic_DNA.
DR   EMBL; AK018765; BAB31395.1; -; mRNA.
DR   EMBL; BC051921; AAH51921.1; -; mRNA.
DR   CCDS; CCDS24754.1; -.
DR   RefSeq; NP_084358.1; NM_030082.4.
DR   PDB; 1U35; X-ray; 3.00 A; D/H=1-126.
DR   PDB; 2F8N; X-ray; 2.90 A; D=1-126.
DR   PDB; 5B1L; X-ray; 2.35 A; D/H=1-126.
DR   PDB; 5B1M; X-ray; 2.34 A; D/H=1-126.
DR   PDB; 5XM0; X-ray; 2.87 A; D/H=1-126.
DR   PDB; 5XM1; X-ray; 3.45 A; D/H=1-126.
DR   PDB; 7DBH; EM; 3.60 A; D/H=1-126.
DR   PDB; 7VBM; EM; 3.40 A; D/H=1-126.
DR   PDBsum; 1U35; -.
DR   PDBsum; 2F8N; -.
DR   PDBsum; 5B1L; -.
DR   PDBsum; 5B1M; -.
DR   PDBsum; 5XM0; -.
DR   PDBsum; 5XM1; -.
DR   PDBsum; 7DBH; -.
DR   PDBsum; 7VBM; -.
DR   AlphaFoldDB; Q9D2U9; -.
DR   SMR; Q9D2U9; -.
DR   BioGRID; 219314; 2.
DR   STRING; 10090.ENSMUSP00000076397; -.
DR   iPTMnet; Q9D2U9; -.
DR   PhosphoSitePlus; Q9D2U9; -.
DR   SwissPalm; Q9D2U9; -.
DR   EPD; Q9D2U9; -.
DR   jPOST; Q9D2U9; -.
DR   MaxQB; Q9D2U9; -.
DR   PaxDb; Q9D2U9; -.
DR   PeptideAtlas; Q9D2U9; -.
DR   PRIDE; Q9D2U9; -.
DR   ProteomicsDB; 270918; -.
DR   DNASU; 78303; -.
DR   Ensembl; ENSMUST00000078267; ENSMUSP00000076397; ENSMUSG00000056895.
DR   GeneID; 78303; -.
DR   KEGG; mmu:78303; -.
DR   UCSC; uc007jcr.2; mouse.
DR   CTD; 78303; -.
DR   MGI; MGI:1925553; H2bu2.
DR   VEuPathDB; HostDB:ENSMUSG00000056895; -.
DR   eggNOG; KOG1744; Eukaryota.
DR   GeneTree; ENSGT01050000244832; -.
DR   HOGENOM; CLU_075666_2_1_1; -.
DR   InParanoid; Q9D2U9; -.
DR   OMA; ARLECCT; -.
DR   OrthoDB; 1536672at2759; -.
DR   PhylomeDB; Q9D2U9; -.
DR   TreeFam; TF300212; -.
DR   BioGRID-ORCS; 78303; 8 hits in 70 CRISPR screens.
DR   EvolutionaryTrace; Q9D2U9; -.
DR   PRO; PR:Q9D2U9; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9D2U9; protein.
DR   Bgee; ENSMUSG00000056895; Expressed in medial ganglionic eminence and 161 other tissues.
DR   Genevisible; Q9D2U9; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000558; Histone_H2B.
DR   PANTHER; PTHR23428; PTHR23428; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00621; HISTONEH2B.
DR   SMART; SM00427; H2B; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00357; HISTONE_H2B; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chromosome; DNA-binding; Hydroxylation;
KW   Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P23527"
FT   CHAIN           2..126
FT                   /note="H2B.U histone 2"
FT                   /id="PRO_0000244837"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..35
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylproline"
FT                   /evidence="ECO:0000250|UniProtKB:P23527"
FT   MOD_RES         12
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:27105115"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62807"
FT   MOD_RES         12
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21925322"
FT   MOD_RES         12
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:31645732"
FT   MOD_RES         13
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         13
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         13
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21925322"
FT   MOD_RES         15
FT                   /note="Phosphoserine; by STK4/MST1"
FT                   /evidence="ECO:0000269|PubMed:15197225,
FT                   ECO:0000269|PubMed:16039583"
FT   MOD_RES         16
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         16
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21925322"
FT   MOD_RES         16
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:31645732"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         17
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21925322"
FT   MOD_RES         17
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         17
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:31645732"
FT   MOD_RES         21
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         21
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:27105115"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         21
FT                   /note="N6-butyryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         21
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21925322"
FT   MOD_RES         21
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:31645732"
FT   MOD_RES         24
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         24
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21925322"
FT   MOD_RES         24
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         25
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         35
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         35
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:27105115"
FT   MOD_RES         35
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21925322"
FT   MOD_RES         35
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         35
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         37
FT                   /note="Phosphoserine; by AMPK"
FT                   /evidence="ECO:0000269|PubMed:20647423"
FT   MOD_RES         44
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         44
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         44
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         47
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         47
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         47
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62807"
FT   MOD_RES         58
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62807"
FT   MOD_RES         58
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         80
FT                   /note="Dimethylated arginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A08"
FT   MOD_RES         86
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A08"
FT   MOD_RES         86
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         86
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A08"
FT   MOD_RES         86
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:31645732"
FT   MOD_RES         87
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A08"
FT   MOD_RES         93
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A08"
FT   MOD_RES         109
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         109
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:27105115"
FT   MOD_RES         109
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         109
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:31645732"
FT   MOD_RES         109
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62807"
FT   MOD_RES         116
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00729"
FT   MOD_RES         117
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         117
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:27105115"
FT   MOD_RES         117
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         117
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:31645732"
FT   MOD_RES         117
FT                   /note="N6-methylated lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00729"
FT   MOD_RES         117
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         121
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         121
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         121
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   MOD_RES         121
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:22389435"
FT   CROSSLNK        21
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5QNW6"
FT   CROSSLNK        35
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P33778"
FT   CROSSLNK        121
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62808"
FT   HELIX           39..49
FT                   /evidence="ECO:0007829|PDB:5B1M"
FT   HELIX           57..84
FT                   /evidence="ECO:0007829|PDB:5B1M"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:5B1M"
FT   HELIX           92..102
FT                   /evidence="ECO:0007829|PDB:5B1M"
FT   HELIX           106..123
FT                   /evidence="ECO:0007829|PDB:5B1M"
SQ   SEQUENCE   126 AA;  13994 MW;  DC1CF72D9457CC56 CRC64;
     MPEPSRSTPA PKKGSKKAIT KAQKKDGKKR KRGRKESYSI YVYKVLKQVH PDTGISSKAM
     GIMNSFVNDI FERIASEASR LAHYNKRSTI TSREVQTAVR LLLPGELAKH AVSEGTKAVT
     KYTSSK
 
 
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