H4_RAT
ID H4_RAT Reviewed; 103 AA.
AC P62804; P02304; P02305; Q5BM23; Q7M0E8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Histone H4;
DE Contains:
DE RecName: Full=Osteogenic growth peptide;
DE Short=OGP;
GN Name=H4c2; Synonyms=Hist1h4b, Hist4;
GN and
GN Name=Hist1h4m;
GN and
GN Name=H4f16; Synonyms=H4ft, Hist4h4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=3691674; DOI=10.1016/0014-4827(87)90293-x;
RA Grimes S., Weisz-Carrington P., Daum H. III, Smith J., Green L., Wright K.,
RA Stein G., Stein J.;
RT "A rat histone H4 gene closely associated with the testis-specific H1t
RT gene.";
RL Exp. Cell Res. 173:534-545(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=2920170; DOI=10.1016/0167-4781(89)90032-8;
RA Wolfe S.A., Anderson J.V., Grimes S.R., Stein G.S., Stein J.S.;
RT "Comparison of the structural organization and expression of germinal and
RT somatic rat histone H4 genes.";
RL Biochim. Biophys. Acta 1007:140-150(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1706721; DOI=10.1016/s0021-9258(18)38164-x;
RA Wolfe S.A., Grimes S.R.;
RT "Protein-DNA interactions within the rat histone H4t promoter.";
RL J. Biol. Chem. 266:6637-6643(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Spleen;
RX PubMed=16042990; DOI=10.1016/j.peptides.2005.03.013;
RA Poirier R., Lemaire I., Dumont M., Leduc N., Le H.T., Lemaire S.;
RT "Correlation between the expression of the histone H4 mRNA variant H4-v.1
RT and the levels of histone H4-(86-100) and H4-(89-102) (OGP) in various rat
RT tissues and alveolar macrophages.";
RL Peptides 26:1503-1511(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [6]
RP PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2 AND LYS-17, AND METHYLATION
RP AT LYS-21.
RX PubMed=5171427; DOI=10.1016/s0300-9084(71)80165-7;
RA Sautiere P., Tyrou D., Moschetto Y., Biserte G.;
RT "Primary structure of glycine-rich and arginine-rich histone isolated from
RT chloroleukemic tumor of the rat.";
RL Biochimie 53:479-483(1971).
RN [7]
RP PROTEIN SEQUENCE OF 5-14 AND 19-32.
RC TISSUE=Liver;
RX PubMed=7932740; DOI=10.1006/jmbi.1994.1629;
RA Baneres J.L., Essalouh L., Jariel-Encontre I., Mesnier D., Garrod S.,
RA Parello J.;
RT "Evidence indicating proximity in the nucleosome between the histone H4 N
RT termini and the globular domain of histone H1.";
RL J. Mol. Biol. 243:48-59(1994).
RN [8]
RP PROTEIN SEQUENCE OF 61-78, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 90-103, AND SUBCELLULAR LOCATION.
RX PubMed=1582415; DOI=10.1002/j.1460-2075.1992.tb05238.x;
RA Bab I., Gazit D., Chorev M., Muhlrad A., Shteyer A., Greenberg Z.,
RA Namdar M., Kahn A.;
RT "Histone H4-related osteogenic growth peptide (OGP): a novel circulating
RT stimulator of osteoblastic activity.";
RL EMBO J. 11:1867-1873(1992).
RN [10]
RP ALTERNATIVE INITIATION.
RX PubMed=10318873; DOI=10.1074/jbc.274.20.14474;
RA Bab I., Smith E., Gavish H., Attar-Namdar M., Chorev M., Chen Y.C.,
RA Muhlrad A., Birnbaum M.J., Stein G., Frenkel B.;
RT "Biosynthesis of osteogenic growth peptide via alternative translational
RT initiation at AUG85 of histone H4 mRNA.";
RL J. Biol. Chem. 274:14474-14481(1999).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19343714; DOI=10.1002/pmic.200800558;
RA Pramod K.S., Bharat K., Sanjay G.;
RT "Mass spectrometry-compatible silver staining of histones resolved on
RT acetic acid-urea-Triton PAGE.";
RL Proteomics 9:2589-2592(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-81 AND TYR-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: [Histone H4]: Core component of nucleosome. Nucleosomes wrap
CC and compact DNA into chromatin, limiting DNA accessibility to the
CC cellular machineries which require DNA as a template. Histones thereby
CC play a central role in transcription regulation, DNA repair, DNA
CC replication and chromosomal stability. DNA accessibility is regulated
CC via a complex set of post-translational modifications of histones, also
CC called histone code, and nucleosome remodeling.
CC -!- FUNCTION: [Osteogenic growth peptide]: Stimulates osteogenesis and
CC hematopoiesis. {ECO:0000269|PubMed:1582415}.
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 DNA
CC (By similarity). Found in a co-chaperone complex with DNJC9, MCM2 and
CC histone H3.3-H4 dimers (By similarity). Within the complex, interacts
CC with DNJC9 (via C-terminus); the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P62805, ECO:0000250|UniProtKB:P62806}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1582415}. Chromosome
CC {ECO:0000269|PubMed:1582415}.
CC -!- SUBCELLULAR LOCATION: [Osteogenic growth peptide]: Secreted
CC {ECO:0000269|PubMed:1582415}. Note=Osteogenic growth peptide is
CC secreted by a mechanism independent from a hydrophobic signal sequence.
CC The mature peptide may be imported into secretory lysosomes by an
CC ABCA1-related protein. {ECO:0000269|PubMed:1582415}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Histone H4;
CC IsoId=P62804-1; Sequence=Displayed;
CC Name=OGP precursor;
CC IsoId=P62804-2; Sequence=VSP_018804;
CC -!- TISSUE SPECIFICITY: OGP is found in serum. A potentially OGP-specific
CC transcript is highly expressed in spleen with lower levels in lung,
CC liver, thymus, spinal chord, pituitary gland, adrenal gland, bone
CC marrow and lymph nodes as well as very low levels in kidney, heart and
CC brain. {ECO:0000269|PubMed:16042990}.
CC -!- PTM: Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac)
CC and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in
CC heterochromatin. {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.
CC {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and
CC H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac)
CC and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric
CC dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a
CC crucial role in the germ-cell lineage (By similarity).
CC {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1,
CC H4K20me2, H4K20me3). Monomethylation is performed by KMT5A/SET8.
CC Trimethylation is performed by KMT5B and KMT5C and induces gene
CC silencing. Monomethylated at Lys-13 (H4K12me1) by N6AMT1; H4K12me1
CC modification is present at the promoters of numerous genes encoding
CC cell cycle regulators. {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation
CC increases the association of H3.3-H4 with the histone chaperone HIRA,
CC thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome
CC assembly of H3.1-H4 (By similarity). {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to
CC ultraviolet irradiation. This may weaken the interaction between
CC histones and DNA and facilitate DNA accessibility to repair proteins.
CC Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA
CC damage. The exact role of H4K91ub1 in DNA damage response is still
CC unclear but it may function as a licensing signal for additional
CC histone H4 post-translational modifications such as H4 Lys-21
CC methylation (H4K20me) (By similarity). {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Sumoylated, which is associated with transcriptional repression.
CC {ECO:0000250|UniProtKB:P62805}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Butyrylation of histones marks active promoters and competes with
CC histone acetylation. {ECO:0000250|UniProtKB:P62806}.
CC -!- PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by
CC promoting dissociation of the H2A-H2B dimers from nucleosomes.
CC {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Ufmylated; monofmylated by UFL1 at Lys-32 (H4K31Ufm1) in response
CC to DNA damage. {ECO:0000250|UniProtKB:P62805}.
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:P62805}.
CC -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
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DR EMBL; M27433; AAA60735.1; -; Genomic_DNA.
DR EMBL; X13554; CAA31906.1; -; Genomic_DNA.
DR EMBL; M28409; AAA41306.1; -; Genomic_DNA.
DR EMBL; AY936209; AAX28930.1; -; mRNA.
DR EMBL; BC100619; AAI00620.1; -; mRNA.
DR PIR; A91265; HSRT4.
DR PIR; S53749; S53749.
DR RefSeq; NP_001116941.1; NM_001123469.1. [P62804-1]
DR RefSeq; NP_001258150.1; NM_001271221.1. [P62804-1]
DR RefSeq; NP_073177.1; NM_022686.2. [P62804-1]
DR RefSeq; XP_003749904.3; XM_003749856.4. [P62804-1]
DR RefSeq; XP_008761668.1; XM_008763446.1. [P62804-1]
DR RefSeq; XP_008761670.1; XM_008763448.2. [P62804-1]
DR RefSeq; XP_008769992.1; XM_008771770.2. [P62804-1]
DR RefSeq; XP_008772221.1; XM_008773999.1. [P62804-1]
DR RefSeq; XP_578415.4; XM_578415.6. [P62804-1]
DR AlphaFoldDB; P62804; -.
DR SMR; P62804; -.
DR BioGRID; 1200084; 1.
DR BioGRID; 249165; 6.
DR BioGRID; 253434; 2.
DR BioGRID; 254947; 2.
DR BioGRID; 595036; 2.
DR IntAct; P62804; 4.
DR MINT; P62804; -.
DR STRING; 10116.ENSRNOP00000039602; -.
DR iPTMnet; P62804; -.
DR PhosphoSitePlus; P62804; -.
DR SwissPalm; P62804; -.
DR jPOST; P62804; -.
DR PaxDb; P62804; -.
DR PRIDE; P62804; -.
DR ABCD; P62804; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000040210; ENSRNOP00000039602; ENSRNOG00000032224. [P62804-1]
DR Ensembl; ENSRNOT00000080490; ENSRNOP00000071163; ENSRNOG00000054017. [P62804-1]
DR Ensembl; ENSRNOT00000088408; ENSRNOP00000074659; ENSRNOG00000063552. [P62804-1]
DR Ensembl; ENSRNOT00000105806; ENSRNOP00000093704; ENSRNOG00000065263. [P62804-1]
DR Ensembl; ENSRNOT00000106060; ENSRNOP00000091116; ENSRNOG00000065263. [P62804-1]
DR Ensembl; ENSRNOT00000107328; ENSRNOP00000087795; ENSRNOG00000070513. [P62804-1]
DR Ensembl; ENSRNOT00000112120; ENSRNOP00000079614; ENSRNOG00000066473. [P62804-1]
DR Ensembl; ENSRNOT00000112947; ENSRNOP00000091037; ENSRNOG00000064025. [P62804-1]
DR Ensembl; ENSRNOT00000114507; ENSRNOP00000080829; ENSRNOG00000070706. [P62804-1]
DR Ensembl; ENSRNOT00000115294; ENSRNOP00000087751; ENSRNOG00000067648. [P62804-1]
DR Ensembl; ENSRNOT00000117583; ENSRNOP00000080971; ENSRNOG00000065263. [P62804-1]
DR Ensembl; ENSRNOT00000120238; ENSRNOP00000091524; ENSRNOG00000066473. [P62804-1]
DR GeneID; 291152; -.
DR GeneID; 295277; -.
DR GeneID; 364723; -.
DR GeneID; 64627; -.
DR KEGG; rno:291152; -.
DR KEGG; rno:295277; -.
DR KEGG; rno:364723; -.
DR KEGG; rno:64627; -.
DR UCSC; RGD:620814; rat. [P62804-1]
DR CTD; 291152; -.
DR CTD; 295277; -.
DR CTD; 364723; -.
DR CTD; 64627; -.
DR RGD; 620814; Hist1h4b.
DR eggNOG; KOG3467; Eukaryota.
DR GeneTree; ENSGT01030000234703; -.
DR GeneTree; ENSGT01050000244867; -.
DR HOGENOM; CLU_109117_2_3_1; -.
DR InParanoid; P62804; -.
DR OMA; QKEHING; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; P62804; -.
DR Reactome; R-RNO-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-RNO-110331; Cleavage of the damaged purine.
DR Reactome; R-RNO-171306; Packaging Of Telomere Ends.
DR Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-RNO-212300; PRC2 methylates histones and DNA.
DR Reactome; R-RNO-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-RNO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-RNO-3214841; PKMTs methylate histone lysines.
DR Reactome; R-RNO-3214842; HDMs demethylate histones.
DR Reactome; R-RNO-3214847; HATs acetylate histones.
DR Reactome; R-RNO-3214858; RMTs methylate histone arginines.
DR Reactome; R-RNO-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-RNO-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-RNO-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-RNO-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-RNO-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
DR Reactome; R-RNO-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR Reactome; R-RNO-9670095; Inhibition of DNA recombination at telomere.
DR PRO; PR:P62804; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000032224; Expressed in pancreas and 15 other tissues.
DR Genevisible; P62804; RN.
DR GO; GO:0043505; C:CENP-A containing nucleosome; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000228; C:nuclear chromosome; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISO:RGD.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:RGD.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISO:RGD.
DR GO; GO:0006334; P:nucleosome assembly; ISO:RGD.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR CDD; cd00076; H4; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR001951; Histone_H4.
DR InterPro; IPR019809; Histone_H4_CS.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR Pfam; PF15511; CENP-T_C; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00047; HISTONE_H4; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Chromosome; Citrullination;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW DNA-binding; Hydroxylation; Isopeptide bond; Methylation; Nucleosome core;
KW Nucleus; Osteogenesis; Phosphoprotein; Reference proteome; Secreted;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5171427"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158355"
FT PEPTIDE 90..103
FT /note="Osteogenic growth peptide"
FT /id="PRO_0000225591"
FT DNA_BIND 17..21
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:5171427"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 4
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 4
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 4
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 4
FT /note="Symmetric dimethylarginine; by PRMT5 and PRMT7;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 6
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 9
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 13
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 17
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:5171427"
FT MOD_RES 17
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 17
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 17
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 17
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 21
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 21
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:5171427"
FT MOD_RES 21
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:5171427"
FT MOD_RES 32
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 45
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 45
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 45
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 52
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 60
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 60
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 80
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 80
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 80
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 80
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 89
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 92
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in UFM1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform OGP precursor)"
FT /evidence="ECO:0000305"
FT /id="VSP_018804"
SQ SEQUENCE 103 AA; 11367 MW; A9E5DFD3F8B97598 CRC64;
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG
