ID H2A2A_HUMAN Reviewed; 130 AA. AC Q6FI13; B2R5F0; P20670; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 03-APR-2013, entry version 100. DE RecName: Full=Histone H2A type 2-A; DE AltName: Full=Histone H2A.2; DE AltName: Full=Histone H2A/o; GN Name=HIST2H2AA3; Synonyms=H2AFO, HIST2H2AA; GN and GN Name=HIST2H2AA4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8179821; DOI=10.1089/dna.1994.13.161; RA Mannironi C., Orr A., Hatch C., Pilch D., Ivanova V., Bonner W.; RT "The relative expression of human histone H2A genes is similar in RT different types of proliferating cells."; RL DNA Cell Biol. 13:161-170(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PHOSPHORYLATION AT THR-121. RX PubMed=15078818; DOI=10.1101/gad.1184604; RA Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., RA Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.; RT "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during RT mitosis in the early Drosophila embryo."; RL Genes Dev. 18:877-888(2004). RN [9] RP PHOSPHORYLATION AT SER-2, AND MUTAGENESIS OF SER-2. RX PubMed=15010469; DOI=10.1074/jbc.M400099200; RA Zhang Y., Griffin K., Mondal N., Parvin J.D.; RT "Phosphorylation of histone H2A inhibits transcription on chromatin RT templates."; RL J. Biol. Chem. 279:21866-21872(2004). RN [10] RP UBIQUITINATION AT LYS-120. RX PubMed=15386022; DOI=10.1038/nature02985; RA Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., RA Jones R.S., Zhang Y.; RT "Role of histone H2A ubiquitination in Polycomb silencing."; RL Nature 431:873-878(2004). RN [11] RP ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, AND MASS SPECTROMETRY. RX PubMed=15823041; DOI=10.1021/bi047505c; RA Hagiwara T., Hidaka Y., Yamada M.; RT "Deimination of histone H2A and H4 at arginine 3 in HL-60 RT granulocytes."; RL Biochemistry 44:5827-5834(2005). RN [12] RP UBIQUITINATION AT LYS-120. RX PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002; RA Cao R., Tsukada Y., Zhang Y.; RT "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene RT silencing."; RL Mol. Cell 20:845-854(2005). RN [13] RP UBIQUITINATION AT LYS-120. RX PubMed=16702407; DOI=10.1101/gad.373706; RA Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M., RA de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B., RA Neefjes J., Hoeijmakers J.H.J., Vermeulen W., Dantuma N.P.; RT "DNA damage triggers nucleotide excision repair-dependent RT monoubiquitylation of histone H2A."; RL Genes Dev. 20:1343-1352(2006). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT LYS-6, AND RP PHOSPHORYLATION AT SER-2. RX PubMed=16319397; DOI=10.1074/mcp.M500288-MCP200; RA Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.; RT "Characterization of histones H2A and H2B variants and their post- RT translational modifications by mass spectrometry."; RL Mol. Cell. Proteomics 5:541-552(2006). RN [15] RP MASS SPECTROMETRY, ACETYLATION AT SER-2 AND LYS-6, AND UBIQUITINATION RP AT LYS-120. RX PubMed=16457589; DOI=10.1021/pr050269n; RA Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.; RT "Precise characterization of human histones in the H2A gene family by RT top down mass spectrometry."; RL J. Proteome Res. 5:248-253(2006). RN [16] RP UBIQUITINATION. RX PubMed=18001824; DOI=10.1016/j.cell.2007.09.040; RA Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J., RA Lukas C., Lukas J.; RT "RNF8 ubiquitylates histones at DNA double-strand breaks and promotes RT assembly of repair proteins."; RL Cell 131:887-900(2007). RN [17] RP UBIQUITINATION. RX PubMed=18001825; DOI=10.1016/j.cell.2007.09.041; RA Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.; RT "RNF8 transduces the DNA-damage signal via histone ubiquitylation and RT checkpoint protein assembly."; RL Cell 131:901-914(2007). RN [18] RP UBIQUITINATION. RX PubMed=19203578; DOI=10.1016/j.cell.2008.12.042; RA Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K., RA Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M., RA Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L., RA Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R., RA Durocher D.; RT "The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling RT cascade at sites of DNA damage."; RL Cell 136:420-434(2009). RN [19] RP UBIQUITINATION. RX PubMed=19203579; DOI=10.1016/j.cell.2008.12.041; RA Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H., RA Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J., RA Lukas J., Lukas C.; RT "RNF168 binds and amplifies ubiquitin conjugates on damaged RT chromosomes to allow accumulation of repair proteins."; RL Cell 136:435-446(2009). RN [20] RP CROTONYLATION AT LYS-37; LYS-119; LYS-120 AND LYS-126. 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., RA Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.; RT "Identification of 67 histone marks and histone lysine crotonylation RT as a new type of histone modification."; RL Cell 146:1016-1028(2011). RN [21] RP UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168. RX PubMed=22980979; DOI=10.1016/j.cell.2012.08.005; RA Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E., RA Vermeulen W., Marteijn J.A., Sixma T.K.; RT "RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage RT signaling."; RL Cell 150:1182-1195(2012). RN [22] RP UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168. RX PubMed=22713238; DOI=10.4161/cc.20919; RA Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L.; RT "A novel ubiquitin mark at the N-terminal tail of histone H2As RT targeted by RNF168 ubiquitin ligase."; RL Cell Cycle 11:2538-2544(2012). CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and CC compact DNA into chromatin, limiting DNA accessibility to the CC cellular machineries which require DNA as a template. Histones CC thereby play a central role in transcription regulation, DNA CC repair, DNA replication and chromosomal stability. DNA CC accessibility is regulated via a complex set of post-translational CC modifications of histones, also called histone code, and CC nucleosome remodeling. CC -!- SUBUNIT: The nucleosome is a histone octamer containing two CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps CC approximately 147 bp of DNA. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- PTM: The chromatin-associated form is phosphorylated on Thr-121 CC during mitosis (Probable). CC -!- PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. CC -!- PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1 and CC RNF2/RING2 complex gives a specific tag for epigenetic CC transcriptional repression and participates in X chromosome CC inactivation of female mammals. It is involved in the initiation CC of both imprinted and random X inactivation. Ubiquitinated H2A is CC enriched in inactive X chromosome chromatin. Ubiquitination of H2A CC functions downstream of methylation of 'Lys-27' of histone H3 CC (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by CC ultraviolet and may be involved in DNA repair. Following DNA CC double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' CC linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 CC ligases RNF8 and RNF168, leading to the recruitment of repair CC proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys- CC 16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage CC is initiated by RNF168 that mediates monoubiquitination at these 2 CC sites, and 'Lys-63'-linked ubiquitin are then conjugated to CC monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin CC chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys- CC 63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct CC events. CC -!- PTM: Phosphorylation on Ser-2 is enhanced during mitosis. CC Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses CC transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by CC RPS6KA5/MSK1. CC -!- PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex CC may play a crucial role in the germ-cell lineage (By similarity). CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ CC cells and marks testis-specific genes in post-meiotic cells, CC including X-linked genes that escape sex chromosome inactivation CC in haploid cells. Crotonylation marks active promoters and CC enhancers and confers resistance to transcriptional repressors. It CC is also associated with post-meiotically activated genes on CC autosomes. CC -!- MASS SPECTROMETRY: Mass=13997.9; Method=Electrospray; Range=2-130; CC Note=Monoisotopic with N-acetylserine; Source=PubMed:16457589; CC -!- SIMILARITY: Belongs to the histone H2A family. 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; L19779; AAC24465.1; -; mRNA. DR EMBL; AY131971; AAN59957.1; -; Genomic_DNA. DR EMBL; AK312163; BAG35097.1; -; mRNA. DR EMBL; CR536525; CAG38762.1; -; mRNA. DR EMBL; CR541872; CAG46670.1; -; mRNA. DR EMBL; AL591493; CAI12562.1; -; Genomic_DNA. DR EMBL; AL591493; CAI12565.1; -; Genomic_DNA. DR EMBL; CH878687; EAW50859.1; -; Genomic_DNA. DR EMBL; BC096705; AAH96705.1; -; mRNA. DR EMBL; BC096739; AAH96739.1; -; mRNA. DR EMBL; BC098171; AAH98171.1; -; mRNA. DR IPI; IPI00216457; -. DR PIR; S06742; S06742. DR RefSeq; NP_001035807.1; NM_001040874.1. DR RefSeq; NP_003507.1; NM_003516.2. DR UniGene; Hs.530461; -. DR UniGene; Hs.741531; -. DR ProteinModelPortal; Q6FI13; -. DR SMR; Q6FI13; 14-119. DR DIP; DIP-33167N; -. DR IntAct; Q6FI13; 17. DR STRING; 9606.ENSP00000358155; -. DR PhosphoSite; Q6FI13; -. DR PaxDb; Q6FI13; -. DR PRIDE; Q6FI13; -. DR DNASU; 723790; -. DR DNASU; 8337; -. DR Ensembl; ENST00000369159; ENSP00000358155; ENSG00000203812. DR Ensembl; ENST00000369161; ENSP00000358158; ENSG00000183558. DR Ensembl; ENST00000580456; ENSP00000464221; ENSG00000266225. DR GeneID; 723790; -. DR GeneID; 8337; -. DR KEGG; hsa:723790; -. DR KEGG; hsa:8337; -. DR UCSC; uc001esw.3; human. DR CTD; 723790; -. DR CTD; 8337; -. DR GeneCards; GC01M149813; -. DR GeneCards; GC01P149822; -. DR HGNC; HGNC:4736; HIST2H2AA3. DR HGNC; HGNC:29668; HIST2H2AA4. DR MIM; 142720; gene. DR neXtProt; NX_Q6FI13; -. DR PharmGKB; PA29113; -. DR eggNOG; COG5262; -. DR HOGENOM; HOG000234652; -. DR HOVERGEN; HBG009342; -. DR InParanoid; Q6FI13; -. DR KO; K11251; -. DR OMA; TAHPLEV; -. DR OrthoDB; EOG4TXBTD; -. DR PhylomeDB; Q6FI13; -. DR Reactome; REACT_111183; Meiosis. DR Reactome; REACT_115566; Cell Cycle. DR Reactome; REACT_116125; Disease. DR NextBio; 31220; -. DR Bgee; Q6FI13; -. DR CleanEx; HS_HIST2H2AA3; -. DR CleanEx; HS_HIST2H2AA4; -. DR Genevestigator; Q6FI13; -. DR GermOnline; ENSG00000183558; Homo sapiens. DR GermOnline; ENSG00000203812; Homo sapiens. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro. DR Gene3D; 1.10.20.10; -; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR002119; Histone_H2A. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00620; HISTONEH2A. DR SMART; SM00414; H2A; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00046; HISTONE_H2A; 1. PE 1: Evidence at protein level; KW Acetylation; Chromosome; Citrullination; Complete proteome; KW DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 1 Removed. FT CHAIN 2 130 Histone H2A type 2-A. FT /FTId=PRO_0000055232. FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 2 2 Phosphoserine; by RPS6KA5. FT MOD_RES 4 4 Citrulline; alternate. FT MOD_RES 6 6 N6-acetyllysine. FT MOD_RES 37 37 N6-crotonyl-L-lysine. FT MOD_RES 119 119 N6-crotonyl-L-lysine. FT MOD_RES 120 120 N6-crotonyl-L-lysine; alternate. FT MOD_RES 121 121 Phosphothreonine (Probable). FT MOD_RES 126 126 N6-crotonyl-L-lysine. FT CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin); FT alternate. FT MUTAGEN 2 2 S->A: Blocks the inhibition of FT transcription by RPS6KA5/MSK1. SQ SEQUENCE 130 AA; 14095 MW; 53AEDC6CE3FE8317 CRC64; MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK TESHHKAKGK //