RPB1_CRIGR
ID RPB1_CRIGR Reviewed; 1970 AA.
AC P11414; Q76M93;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB1;
DE Short=RNA polymerase II subunit B1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase II subunit A;
DE AltName: Full=DNA-directed RNA polymerase III largest subunit;
GN Name=POLR2A;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-1006.
RX PubMed=9272869; DOI=10.1016/s0378-1119(97)00204-7;
RA Sugaya K., Sasanuma S., Nohata J., Kimura T., Hongo E., Higashi T.,
RA Morimyo M., Tsuji H., Mita K.;
RT "Cloning and sequencing for the largest subunit of Chinese hamster RNA
RT polymerase II gene: identification of a mutation related to abnormal
RT induction of sister chromatid exchanges.";
RL Gene 194:267-272(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND VARIANT ASP-315.
RX PubMed=11674999; DOI=10.1016/s0378-1119(01)00615-1;
RA Sugaya K., Sasanuma S., Cook P.R., Mita K.;
RT "A mutation in the largest (catalytic) subunit of RNA polymerase II and its
RT relation to the arrest of the cell cycle in G(1) phase.";
RL Gene 274:77-81(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1466-1970.
RX PubMed=3122024; DOI=10.1128/mcb.8.1.321-329.1988;
RA Allison L.A., Wong J.K.-C., Fitzpatrick V.D., Moyle M., Ingles C.J.;
RT "The C-terminal domain of the largest subunit of RNA polymerase II of
RT Saccharomyces cerevisiae, Drosophila melanogaster, and mammals: a conserved
RT structure with an essential function.";
RL Mol. Cell. Biol. 8:321-329(1988).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic component of RNA polymerase II which synthesizes
CC mRNA precursors and many functional non-coding RNAs. Forms the
CC polymerase active center together with the second largest subunit. Pol
CC II is the central component of the basal RNA polymerase II
CC transcription machinery. It is composed of mobile elements that move
CC relative to each other. RPB1 is part of the core element with the
CC central large cleft, the clamp element that moves to open and close the
CC cleft and the jaws that are thought to grab the incoming DNA template.
CC At the start of transcription, a single-stranded DNA template strand of
CC the promoter is positioned within the central active site cleft of Pol
CC II. A bridging helix emanates from RPB1 and crosses the cleft near the
CC catalytic site and is thought to promote translocation of Pol II by
CC acting as a ratchet that moves the RNA-DNA hybrid through the active
CC site by switching from straight to bent conformations at each step of
CC nucleotide addition. During transcription elongation, Pol II moves on
CC the template as the transcript elongates. Elongation is influenced by
CC the phosphorylation status of the C-terminal domain (CTD) of Pol II
CC largest subunit (RPB1), which serves as a platform for assembly of
CC factors that regulate transcription initiation, elongation, termination
CC and mRNA processing (By similarity). Regulation of gene expression
CC levels depends on the balance between methylation and acetylation
CC levels of tha CTD-lysines (By similarity). Initiation or early
CC elongation steps of transcription of growth-factors-induced immediate
CC early genes are regulated by the acetylation status of the CTD (By
CC similarity). Methylation and dimethylation have a repressive effect on
CC target genes expression (By similarity). {ECO:0000250|UniProtKB:P08775,
CC ECO:0000250|UniProtKB:P24928}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6;
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. Component of a complex which is at least composed of
CC HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA
CC polymerase II, SUPT5H, and NCL/nucleolin. The large PER complex
CC involved in the repression of transcriptional termination is composed
CC of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active).
CC Interacts (via the C-terminal domain (CTD)) with U2AF2; recruits PRPF19
CC and the Prp19 complex to the pre-mRNA and may couple transcription to
CC pre-mRNA splicing. Interacts (via the C-terminal domain (CTD)) with
CC SMN1/SMN2; recruits SMN1/SMN2 to RNA Pol II elongation complexes.
CC Interacts via the phosphorylated C-terminal domain with WDR82 and with
CC SETD1A and SETD1B only in the presence of WDR82. When phosphorylated at
CC 'Ser-5', interacts with MEN1; the unphosphorylated form, or
CC phosphorylated at 'Ser-2' does not interact. When phosphorylated at
CC 'Ser-2', interacts with SUPT6H (via SH2 domain). Interacts with RECQL5
CC and TCEA1; binding of RECQL5 prevents TCEA1 binding. The phosphorylated
CC C-terminal domain interacts with FNBP3 and SYNCRIP. Interacts with
CC ATF7IP. Interacts with DDX5. Interacts with WWP2. Interacts with SETX.
CC Interacts (phosphorylated) with PIH1D1. Interacts (via the C-terminal
CC domain (CTD)) with TDRD3. Interacts with PRMT5. Interacts with XRN2.
CC Interacts with SAFB/SAFB1. Interacts with CCNL1. Interacts with CCNL2,
CC MYO1C, PAF1 and SFRS19. Interacts (via C-terminus) with CMTR1, CTDSP1
CC and SCAF8. Interacts (via the C-terminal domain (CTD)) with CCNT2 (By
CC similarity). Interacts with FUS (By similarity). Interacts with MCM3AP
CC (By similarity). Interacts with kinase SRPK2; the interaction occurs
CC during the co-transcriptional formation of inappropriate R-loops (By
CC similarity). {ECO:0000250|UniProtKB:P08775,
CC ECO:0000250|UniProtKB:P24928}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11674999}. Cytoplasm
CC {ECO:0000250|UniProtKB:P24928}. Chromosome
CC {ECO:0000250|UniProtKB:P24928}. Note=Hypophosphorylated form is mainly
CC found in the cytoplasm, while the hyperphosphorylated and active form
CC is nuclear (By similarity). Co-localizes with kinase SRPK2 and helicase
CC DDX23 at chromatin loci where unscheduled R-loops form (By similarity).
CC {ECO:0000250|UniProtKB:P24928}.
CC -!- DOMAIN: The C-terminal domain (CTD) serves as a platform for assembly
CC of factors that regulate transcription initiation, elongation,
CC termination and mRNA processing. {ECO:0000305}.
CC -!- PTM: The tandem heptapeptide repeats in the C-terminal domain (CTD) can
CC be highly phosphorylated. The phosphorylation activates Pol II.
CC Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the
CC heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7
CC phosphorylation of POLR2A associated with DNA promotes transcription
CC initiation by triggering dissociation from DNA. Phosphorylation also
CC takes place at 'Ser-7' of the heptapeptide repeat, which is required
CC for efficient transcription of snRNA genes and processing of the
CC transcripts. The phosphorylation state is believed to result from the
CC balanced action of site-specific CTD kinases and phosphatases, and a
CC 'CTD code' that specifies the position of Pol II within the
CC transcription cycle has been proposed. Dephosphorylated by the protein
CC phosphatase CTDSP1. {ECO:0000250|UniProtKB:P24928}.
CC -!- PTM: Among tandem heptapeptide repeats of the C-terminal domain (CTD)
CC some do not match the Y-S-P-T-S-P-S consensus, the seventh serine
CC residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-
CC consensus heptapeptide repeats can be alternatively acetylated,
CC methylated and dimethylated. EP300 is one of the enzyme able to
CC acetylate 'Lys-7'. Acetylation at 'Lys-7' of non-consensus heptapeptide
CC repeats is associated with 'Ser-2' phosphorylation and active
CC transcription. Regulates initiation or early elongation steps of
CC transcription specially for inducible genes.
CC {ECO:0000250|UniProtKB:P24928}.
CC -!- PTM: Methylated at Arg-1810 prior to transcription initiation when the
CC CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808
CC preventing this methylation. Symmetrically or asymmetrically
CC dimethylated at Arg-1810 by PRMT5 and CARM1 respectively. Symmetric or
CC asymmetric dimethylation modulates interactions with CTD-binding
CC proteins like SMN1/SMN2 and TDRD3. SMN1/SMN2 interacts preferentially
CC with the symmetrically dimethylated form while TDRD3 interacts with the
CC asymmetric form. Through the recruitment of SMN1/SMN2, symmetric
CC dimethylation is required for resolving RNA-DNA hybrids created by RNA
CC polymerase II, that form R-loop in transcription terminal regions, an
CC important step in proper transcription termination. CTD dimethylation
CC may also facilitate the expression of select RNAs. Among tandem
CC heptapeptide repeats of the C-terminal domain (CTD) some do not match
CC the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being
CC replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide
CC repeats can be alternatively acetylated, methylated, dimethylated and
CC trimethylated. Methylation occurs in the earliest transcription stages
CC and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
CC Dimethylation and trimehtylation at 'Lys-7' of non-consensus
CC heptapeptide repeats are exclusively associated with phosphorylated
CC CTD. {ECO:0000250|UniProtKB:P08775, ECO:0000250|UniProtKB:P24928}.
CC -!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation (By
CC similarity). Following UV treatment, the elongating form of RNA
CC polymerase II (RNA pol IIo) is ubiquitinated on UV damage sites without
CC leading to degradation: ubiquitination is facilitated by KIAA1530/UVSSA
CC and promotes RNA pol IIo backtracking to allow access to the nucleotide
CC excision repair machinery (By similarity).
CC {ECO:0000250|UniProtKB:P08775, ECO:0000250|UniProtKB:P24928}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; D87294; BAA22377.1; -; mRNA.
DR EMBL; AB052229; BAB60684.1; -; mRNA.
DR EMBL; M19538; AAA37008.1; -; Genomic_DNA.
DR PIR; A27677; A27677.
DR RefSeq; NP_001230931.1; NM_001244002.1.
DR PDB; 7B0Y; EM; 3.60 A; A=1-1970.
DR PDB; 7OKX; EM; 3.30 A; A=1-1970.
DR PDB; 7OKY; EM; 4.14 A; A=1-1970.
DR PDB; 7OO3; EM; 2.80 A; A=1-1970.
DR PDB; 7OOB; EM; 2.70 A; A=1-1970.
DR PDB; 7OOP; EM; 2.90 A; A=1-1970.
DR PDB; 7OPC; EM; 3.00 A; A=1-1970.
DR PDB; 7OPD; EM; 3.00 A; A=1-1970.
DR PDBsum; 7B0Y; -.
DR PDBsum; 7OKX; -.
DR PDBsum; 7OKY; -.
DR PDBsum; 7OO3; -.
DR PDBsum; 7OOB; -.
DR PDBsum; 7OOP; -.
DR PDBsum; 7OPC; -.
DR PDBsum; 7OPD; -.
DR AlphaFoldDB; P11414; -.
DR SMR; P11414; -.
DR STRING; 10029.XP_007625199.1; -.
DR GeneID; 100689016; -.
DR KEGG; cge:100689016; -.
DR CTD; 5430; -.
DR eggNOG; KOG0260; Eukaryota.
DR OrthoDB; 591636at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 36.
DR SMART; SM00663; RPOLA_N; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 43.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Cytoplasm; DNA-binding;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding; Methylation;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Repeat; Transcription;
KW Transferase; Ubl conjugation; Zinc.
FT CHAIN 1..1970
FT /note="DNA-directed RNA polymerase II subunit RPB1"
FT /id="PRO_0000073938"
FT REPEAT 1593..1599
FT /note="1"
FT REPEAT 1615..1621
FT /note="2"
FT REPEAT 1622..1628
FT /note="3"
FT REPEAT 1629..1635
FT /note="4"
FT REPEAT 1636..1642
FT /note="5"
FT REPEAT 1643..1649
FT /note="6"
FT REPEAT 1650..1656
FT /note="7"
FT REPEAT 1657..1663
FT /note="8"
FT REPEAT 1664..1670
FT /note="9"
FT REPEAT 1671..1677
FT /note="10"
FT REPEAT 1678..1684
FT /note="11"
FT REPEAT 1685..1691
FT /note="12"
FT REPEAT 1692..1698
FT /note="13"
FT REPEAT 1699..1705
FT /note="14"
FT REPEAT 1706..1712
FT /note="15"
FT REPEAT 1713..1719
FT /note="16"
FT REPEAT 1720..1726
FT /note="17"
FT REPEAT 1727..1733
FT /note="18"
FT REPEAT 1734..1740
FT /note="19"
FT REPEAT 1741..1747
FT /note="20"
FT REPEAT 1748..1754
FT /note="21"
FT REPEAT 1755..1761
FT /note="22"
FT REPEAT 1762..1768
FT /note="23"
FT REPEAT 1769..1775
FT /note="24"
FT REPEAT 1776..1782
FT /note="25"
FT REPEAT 1783..1789
FT /note="26"
FT REPEAT 1790..1796
FT /note="27"
FT REPEAT 1797..1803
FT /note="28"
FT REPEAT 1804..1810
FT /note="29"
FT REPEAT 1811..1817
FT /note="30"
FT REPEAT 1818..1824
FT /note="31"
FT REPEAT 1825..1831
FT /note="32"
FT REPEAT 1832..1838
FT /note="33"
FT REPEAT 1839..1845
FT /note="34"
FT REPEAT 1846..1852
FT /note="35"
FT REPEAT 1853..1859
FT /note="36"
FT REPEAT 1860..1866
FT /note="37"
FT REPEAT 1867..1873
FT /note="38"
FT REPEAT 1874..1880
FT /note="39"
FT REPEAT 1881..1887
FT /note="40"
FT REPEAT 1888..1894
FT /note="41"
FT REPEAT 1895..1901
FT /note="42"
FT REPEAT 1902..1908
FT /note="43"
FT REPEAT 1909..1915
FT /note="44"
FT REPEAT 1916..1922
FT /note="45"
FT REPEAT 1923..1929
FT /note="46"
FT REPEAT 1930..1936
FT /note="47"
FT REPEAT 1940..1946
FT /note="48"
FT REPEAT 1947..1953
FT /note="49"
FT REPEAT 1954..1960
FT /note="50; approximate"
FT REGION 833..845
FT /note="Bridging helix"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT REGION 1546..1970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1960
FT /note="C-terminal domain (CTD); 50 X 7 AA approximate
FT tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SNTRKEVG]"
FT COMPBIAS 1565..1584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with RPB2"
FT /evidence="ECO:0000250"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with RPB2"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1603
FT /note="Omega-N-methylated arginine; by CARM1; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1810
FT /note="Asymmetric dimethylarginine; alternate; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1810
FT /note="Symmetric dimethylarginine; alternate; by PRMT5"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1838
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08775"
FT MOD_RES 1838
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08775"
FT MOD_RES 1840
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1843
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1847
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08775"
FT MOD_RES 1849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1854
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1859
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1859
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1860
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1863
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1866
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1866
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1866
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1866
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1867
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1868
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1870
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1873
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1873
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08775"
FT MOD_RES 1873
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1874
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1877
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1881
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1885
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1887
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08775"
FT MOD_RES 1887
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1887
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1894
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08775"
FT MOD_RES 1896
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1899
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1908
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08775"
FT MOD_RES 1909
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1912
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1915
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1916
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1917
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1919
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1920
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1922
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08775"
FT MOD_RES 1922
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1922
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1923
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1926
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1929
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1930
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1931
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1933
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1934
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1936
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08775"
FT MOD_RES 1936
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1936
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT VARIANT 315
FT /note="A -> D"
FT /evidence="ECO:0000269|PubMed:11674999"
FT VARIANT 1006
FT /note="P -> S (related to abnormal induction of sister
FT chromatid exchanges)"
FT /evidence="ECO:0000269|PubMed:9272869"
FT CONFLICT 1498..1536
FT /note="PTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVG -> R (in
FT Ref. 3; AAA37008)"
FT /evidence="ECO:0000305"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 275..295
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 300..318
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 355..369
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 382..387
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 399..408
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 469..484
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 500..504
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 509..518
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 521..524
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 528..531
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 539..548
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 557..564
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 578..583
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 588..595
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 611..615
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 634..637
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 642..645
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 652..659
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 662..683
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 689..692
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 696..721
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 733..759
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 765..771
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 778..785
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 802..804
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 817..821
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 827..829
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 833..868
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 886..890
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 891..893
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 898..900
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 902..905
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 909..911
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 913..920
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 927..933
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 936..944
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 946..969
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 976..981
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 983..993
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1006..1019
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1028..1037
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1039..1048
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1053..1056
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1062..1079
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1087..1096
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1098..1100
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1121..1128
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1139..1143
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1146..1149
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1151..1161
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1166..1169
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1170..1177
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1185..1187
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1190..1197
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1207..1216
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1218..1223
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1228..1238
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1240..1242
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1243..1247
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1252..1254
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1256..1262
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1281..1295
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1297..1300
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1307..1310
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 1315..1317
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1318..1322
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1328..1331
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1335..1340
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1343..1347
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 1354..1356
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1358..1360
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1362..1368
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1371..1387
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 1388..1390
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1395..1404
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 1405..1407
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1408..1410
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1416..1419
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1422..1424
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1426..1432
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1435..1445
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1454..1459
FT /evidence="ECO:0007829|PDB:7OOB"
FT HELIX 1467..1469
FT /evidence="ECO:0007829|PDB:7OOB"
FT STRAND 1470..1475
FT /evidence="ECO:0007829|PDB:7OOB"
FT TURN 1477..1479
FT /evidence="ECO:0007829|PDB:7OOB"
SQ SEQUENCE 1970 AA; 217206 MW; 6876FC25692A657E CRC64;
MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP
RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL VKTMKVLRCV CFFCSKLLVD
SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG KNICEGGEEM DNKFGVEQPE GDEDLTKEKG
HGGCGRYQPR IRRSGLELYA EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP
RYARPEWMIV TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA
HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV RGNLMGKRVD
FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID RLQELVRRGN SQYPGAKYII
RDNGDRIDLR FHPKPSDLHL QTGYKVERHM CDGDIVIFNR QPTLHKMSMM GHRVRILPWS
TFRLNLSVTT PYNADFDGDE MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD
TLTAVRKFTK RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI
NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG SLVHISYLEM
GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ DIQNTIKKAK QDVIEVIEKA
HNNELEPTPG NTLRQTFENQ VNRILNDARD KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN
ISQVIAVVGQ QNVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA
MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES
VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN ELEREFERMR
EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL PSDLHPIKVV EGVKELSKKL
VIVNGDDPLS RQAQENATLL FNIHLRSTLC SRRMAEEFRL SGEAFDWLLG EIESKFNQAI
AHPGEMVGAL AAQSLGEPAT QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT
VFLLGQSARD AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP
DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD NAEKLVLRIR
IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG IEQISKVYMH LPQTDNKKKI
IITEDGEFKA LQEWILETDG VSLMRVLSEK DVDPVRTTSN DIVEIFTVLG IEAVRKALER
ELYHVISFDG SYVNYRHLAL LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM
EAAAHGESDP MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG
MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA ASDASGFSPG
YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY EPRSPGGYTP QSPSYSPTSP
SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP
TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS
YSPTSPNYSP TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT
SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPTSPKYT PTSPSYSPSS PEYTPTSPKY
SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP VYTPTSPKYS PTSPTYSPTS
PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT SPTYSLTSPA ISPDDSDEEN
