HSF1_BOVIN
ID HSF1_BOVIN Reviewed; 525 AA.
AC Q08DJ8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Heat shock factor protein 1 {ECO:0000250|UniProtKB:Q00613};
DE Short=HSF 1;
DE AltName: Full=Heat shock transcription factor 1 {ECO:0000250|UniProtKB:Q00613};
DE Short=HSTF 1;
GN Name=HSF1 {ECO:0000250|UniProtKB:Q00613};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a stress-inducible and DNA-binding transcription
CC factor that plays a central role in the transcriptional activation of
CC the heat shock response (HSR), leading to the expression of a large
CC class of molecular chaperones heat shock proteins (HSPs) that protect
CC cells from cellular insults' damage. In unstressed cells, is present in
CC a HSP90-containing multichaperone complex that maintains it in a non-
CC DNA-binding inactivated monomeric form. Upon exposure to heat and other
CC stress stimuli, undergoes homotrimerization and activates HSP gene
CC transcription through binding to site-specific heat shock elements
CC (HSEs) present in the promoter regions of HSP genes. Upon heat shock
CC stress, forms a chromatin-associated complex with TTC5/STRAP and
CC p300/EP300 to stimulate HSR transcription, therefore increasing cell
CC survival. Activation is reversible, and during the attenuation and
CC recovery phase period of the HSR, returns to its unactivated form.
CC Binds to inverted 5'-NGAAN-3' pentamer DNA sequences. Binds to
CC chromatin at heat shock gene promoters. Also serves several other
CC functions independently of its transcriptional activity. Involved in
CC the repression of Ras-induced transcriptional activation of the c-fos
CC gene in heat-stressed cells. Positively regulates pre-mRNA 3'-end
CC processing and polyadenylation of HSP70 mRNA upon heat-stressed cells
CC in a symplekin (SYMPK)-dependent manner. Plays a role in nuclear export
CC of stress-induced HSP70 mRNA. Plays a role in the regulation of mitotic
CC progression. Also plays a role as a negative regulator of non-
CC homologous end joining (NHEJ) repair activity in a DNA damage-dependent
CC manner. Involved in stress-induced cancer cell proliferation in a IER5-
CC dependent manner. {ECO:0000250|UniProtKB:Q00613}.
CC -!- SUBUNIT: Monomer; cytoplasmic latent and transcriptionally inactive
CC monomeric form in unstressed cells. Homotrimer; in response to stress,
CC such as heat shock, homotrimerizes and translocates into the nucleus,
CC binds to heat shock element (HSE) sequences in promoter of heat shock
CC protein (HSP) genes and acquires transcriptional ability. Interacts
CC (via monomeric form) with FKBP4; this interaction occurs in unstressed
CC cells. Associates (via monomeric form) with HSP90 proteins in a
CC multichaperone complex in unnstressed cell; this association maintains
CC HSF1 in a non-DNA-binding and transcriptional inactive form by
CC preventing HSF1 homotrimerization. Homotrimeric transactivation
CC activity is modulated by protein-protein interactions and post-
CC translational modifications. Interacts with HSP90AA1; this interaction
CC is decreased in a IER5-dependent manner, promoting HSF1 accumulation in
CC the nucleus, homotrimerization and DNA-binding activities. Part (via
CC regulatory domain in the homotrimeric form) of a large heat shock-
CC induced HSP90-dependent multichaperone complex at least composed of
CC FKBP4, FKBP5, HSP90 proteins, PPID, PPP5C and PTGES3; this association
CC maintains the HSF1 homotrimeric DNA-bound form in a transcriptionally
CC inactive form. Interacts with BAG3 (via BAG domain); this interaction
CC occurs in normal and heat-shocked cells promoting nuclear shuttling of
CC HSF1 in a BAG3-dependent manner. Interacts (via homotrimeric and
CC hyperphosphorylated form) with FKBP4; this interaction occurs upon heat
CC shock in a HSP90-dependent multichaperone complex. Interacts (via
CC homotrimeric form preferentially) with EEF1A proteins. In heat shocked
CC cells, stress-denatured proteins compete with HSF1 homotrimeric DNA-
CC bound form for association of the HSP90-dependent multichaperone
CC complex, and hence alleviating repression of HSF1-mediated
CC transcriptional activity. Interacts (via homotrimeric form
CC preferentially) with DAXX; this interaction relieves homotrimeric HSF1
CC from repression of its transcriptional activity by HSP90-dependent
CC multichaperone complex upon heat shock. Interacts (via D domain and
CC preferentially with hyperphosphorylated form) with JNK1; this
CC interaction occurs under both normal growth conditions and immediately
CC upon heat shock. Interacts (via D domain and preferentially with
CC hyperphosphorylated form) with MAPK3; this interaction occurs upon heat
CC shock. Interacts with IER5 (via central region); this interaction
CC promotes PPP2CA-induced dephosphorylation on Ser-121, Ser-307, Ser-314
CC and Thr-324 and HSF1 transactivation activity. Found in a
CC ribonucleoprotein complex composed of the HSF1 homotrimeric form,
CC translation elongation factor eEF1A proteins and non-coding RNA heat
CC shock RNA-1 (HSR1); this complex occurs upon heat shock and stimulates
CC HSF1 DNA-binding activity. Interacts (via transactivation domain) with
CC HSPA1A/HSP70 and DNAJB1; these interactions result in the inhibition of
CC heat shock- and HSF1-induced transcriptional activity during the
CC attenuation and recovery phase from heat shock. Interacts (via Ser-303
CC and Ser-307 phosphorylated form) with YWHAE; this interaction promotes
CC HSF1 sequestration in the cytoplasm in an ERK-dependent manner. Found
CC in a complex with IER5 and PPP2CA. Interacts with TPR; this interaction
CC increases upon heat shock and stimulates export of HSP70 mRNA.
CC Interacts with SYMPK (via N-terminus) and CSTF2; these interactions
CC occur upon heat shock. Interacts (via transactivation domain) with
CC HSPA8. Interacts with EEF1D; this interaction occurs at heat shock
CC promoter element (HSE) sequences. Interacts with MAPKAPK2. Interacts
CC with PRKACA/PKA. Interacts (via transactivation domain) with GTF2A2.
CC Interacts (via transactivation domain) with GTF2B. Interacts (via
CC transactivation domain) with TBP. Interacts with CDK9, CCNT1 and EP300.
CC Interacts (via N-terminus) with XRCC5 (via N-terminus) and XRCC6 (via
CC N-terminus); these interactions are direct and prevent XRCC5/XRCC6
CC heterodimeric binding and non-homologous end joining (NHEJ) repair
CC activities induced by ionizing radiation (IR). Interacts with PLK1;
CC this interaction occurs during the early mitotic period, increases upon
CC heat shock but does not modulate neither HSF1 homotrimerization and
CC DNA-binding activities. Interacts with CDC20; this interaction occurs
CC in mitosis in a MAD2L1-dependent manner and prevents PLK1-stimulated
CC degradation of HSF1 by blocking the recruitment of the SCF(BTRC)
CC ubiquitin ligase complex. Interacts with MAD2L1; this interaction
CC occurs in mitosis. Interacts with BTRC; this interaction occurs during
CC mitosis, induces its ubiquitin-dependent degradation following
CC stimulus-dependent phosphorylation, a process inhibited by CDC20.
CC Interacts with HSP90AA1 and HSP90AB1. Forms a complex with TTC5/STRAP
CC and p300/EP300; these interactions augment chromatin-bound HSF1 and
CC p300/EP300 histone acetyltransferase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q00613}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00613}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q00613}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q00613}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00613}.
CC Note=The monomeric form is cytoplasmic in unstressed cells.
CC Predominantly nuclear protein in both unstressed and heat shocked
CC cells. Translocates in the nucleus upon heat shock. Nucleocytoplasmic
CC shuttling protein. Colocalizes with IER5 in the nucleus. Colocalizes
CC with BAG3 to the nucleus upon heat stress. Localizes in subnuclear
CC granules called nuclear stress bodies (nSBs) upon heat shock.
CC Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock. Colocalizes
CC with PRKACA/PKA in the nucleus and nSBs upon heat shock. Relocalizes
CC from the nucleus to the cytoplasm during the attenuation and recovery
CC phase period of the heat shock response. Translocates in the cytoplasm
CC in a YWHAE- and XPO1/CRM1-dependent manner. Together with histone H2AX,
CC redistributed in discrete nuclear DNA damage-induced foci after
CC ionizing radiation (IR). Colocalizes with calcium-responsive
CC transactivator SS18L1 at kinetochore region on the mitotic chromosomes.
CC Colocalizes with gamma tubulin at centrosome. Localizes at spindle pole
CC in metaphase. Colocalizes with PLK1 at spindle poles during
CC prometaphase. {ECO:0000250|UniProtKB:Q00613}.
CC -!- DOMAIN: In unstressed cells, spontaneous homotrimerization is
CC inhibited. Intramolecular interactions between the hydrophobic repeat
CC HR-A/B and HR-C regions are necessary to maintain HSF1 in the inactive,
CC monomeric conformation. Furthermore, intramolecular interactions
CC between the regulatory domain and the nonadjacent transactivation
CC domain prevents transcriptional activation, a process that is relieved
CC upon heat shock. The regulatory domain is necessary for full repression
CC of the transcriptional activation domain in unstressed cells through
CC its phosphorylation on Ser-303 and Ser-307. In heat stressed cells,
CC HSF1 homotrimerization occurs through formation of a three-stranded
CC coiled-coil structure generated by intermolecular interactions between
CC HR-A/B regions allowing DNA-binding activity. The D domain is necessary
CC for translocation to the nucleus, interaction with JNK1 and MAPK3 and
CC efficient JNK1- and MAPK3-dependent phosphorylation. The regulatory
CC domain confers heat shock inducibility on the transcriptional
CC transactivation domain. The regulatory domain is necessary for
CC transcriptional activation through its phosphorylation on Ser-230 upon
CC heat shock. 9aaTAD is a transactivation motif present in a large number
CC of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:Q00613}.
CC -!- PTM: Phosphorylated. Phosphorylated in unstressed cells; this
CC phosphorylation is constitutive and implicated in the repression of
CC HSF1 transcriptional activity. Phosphorylated on Ser-121 by MAPKAPK2;
CC this phosphorylation promotes interaction with HSP90 proteins and
CC inhibits HSF1 homotrimerization, DNA-binding and transactivation
CC activities. Phosphorylation on Ser-303 by GSK3B/GSK3-beta and on Ser-
CC 307 by MAPK3 within the regulatory domain is involved in the repression
CC of HSF1 transcriptional activity and occurs in a RAF1-dependent manner.
CC Phosphorylation on Ser-303 and Ser-307 increases HSF1 nuclear export in
CC a YWHAE- and XPO1/CRM1-dependent manner. Phosphorylation on Ser-307 is
CC a prerequisite for phosphorylation on Ser-303. According to, Ser-303 is
CC not phosphorylated in unstressed cells. Phosphorylated on Ser-415 by
CC PLK1; phosphorylation promotes nuclear translocation upon heat shock.
CC Hyperphosphorylated upon heat shock and during the attenuation and
CC recovery phase period of the heat shock response. Phosphorylated on
CC Thr-142; this phosphorylation increases HSF1 transactivation activity
CC upon heat shock. Phosphorylation on Ser-230 by CAMK2A; this
CC phosphorylation enhances HSF1 transactivation activity upon heat shock.
CC Phosphorylation on Ser-327 by MAPK12; this phosphorylation enhances
CC HSF1 nuclear translocation, homotrimerization and transactivation
CC activities upon heat shock. Phosphorylated on Ser-320 by PRKACA/PKA;
CC this phosphorylation promotes nuclear localization and transcriptional
CC activity upon heat shock. Phosphorylated on Ser-359 by MAPK8; this
CC phosphorylation occurs upon heat shock, induces HSF1 translocation into
CC nuclear stress bodies and negatively regulates transactivation
CC activity. Neither basal nor stress-inducible phosphorylation on Ser-
CC 230, Ser-292, Ser-303, Ser-307, Ser-314, Ser-319, Ser-320, Thr-324,
CC Ser-327, Ser-339, Ser-346, Ser-359 and Ser-364 within the regulatory
CC domain is involved in the regulation of HSF1 subcellular localization
CC or DNA-binding activity; however, it negatively regulates HSF1
CC transactivation activity. Phosphorylated by PLK1 in the early mitotic
CC period; this phosphorylation regulates HSF1 localization to the spindle
CC pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex
CC inducing HSF1 degradation, and hence mitotic progression.
CC Dephosphorylated on Ser-121, Ser-307, Ser-314, Thr-324 by phosphatase
CC PPP2CA in an IER5-dependent manner, leading to HSF1-mediated
CC transactivation activity. {ECO:0000250|UniProtKB:Q00613}.
CC -!- PTM: Sumoylated with SUMO1 and SUMO2 upon heat shock in a ERK2-
CC dependent manner. Sumoylated by SUMO1 on Lys-298; sumoylation occurs
CC upon heat shock and promotes its localization to nuclear stress bodies
CC and DNA-binding activity. Phosphorylation on Ser-303 and Ser-307 is
CC probably a prerequisite for sumoylation.
CC {ECO:0000250|UniProtKB:Q00613}.
CC -!- PTM: Acetylated on Lys-118; this acetylation is decreased in a IER5-
CC dependent manner. Acetylated on Lys-118, Lys-208 and Lys-298; these
CC acetylations occur in a EP300-dependent manner. Acetylated on Lys-80;
CC this acetylation inhibits DNA-binding activity upon heat shock.
CC Deacetylated on Lys-80 by SIRT1; this deacetylation increases DNA-
CC binding activity. {ECO:0000250|UniProtKB:Q00613}.
CC -!- PTM: Ubiquitinated by SCF(BTRC) and degraded following stimulus-
CC dependent phosphorylation by PLK1 in mitosis. Polyubiquitinated.
CC Undergoes proteasomal degradation upon heat shock and during the
CC attenuation and recovery phase period of the heat shock response.
CC {ECO:0000250|UniProtKB:Q00613}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC123711; AAI23712.1; -; mRNA.
DR RefSeq; NP_001070277.1; NM_001076809.1.
DR AlphaFoldDB; Q08DJ8; -.
DR BMRB; Q08DJ8; -.
DR SMR; Q08DJ8; -.
DR STRING; 9913.ENSBTAP00000027654; -.
DR iPTMnet; Q08DJ8; -.
DR PaxDb; Q08DJ8; -.
DR PRIDE; Q08DJ8; -.
DR Ensembl; ENSBTAT00000027654; ENSBTAP00000027654; ENSBTAG00000020751.
DR GeneID; 506235; -.
DR KEGG; bta:506235; -.
DR CTD; 3297; -.
DR VEuPathDB; HostDB:ENSBTAG00000020751; -.
DR VGNC; VGNC:29981; HSF1.
DR eggNOG; KOG0627; Eukaryota.
DR GeneTree; ENSGT00940000158421; -.
DR HOGENOM; CLU_038829_2_0_1; -.
DR InParanoid; Q08DJ8; -.
DR OrthoDB; 1154048at2759; -.
DR TreeFam; TF330401; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000020751; Expressed in choroid plexus and 103 other tissues.
DR ExpressionAtlas; Q08DJ8; baseline and differential.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0101031; C:chaperone complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0061770; F:translation elongation factor binding; ISS:UniProtKB.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISS:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; ISS:UniProtKB.
DR GO; GO:0072738; P:cellular response to diamide; ISS:UniProtKB.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:1903936; P:cellular response to sodium arsenite; ISS:UniProtKB.
DR GO; GO:0034620; P:cellular response to unfolded protein; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:1900034; P:regulation of cellular response to heat; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR010542; Vert_HSTF_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR Pfam; PF06546; Vert_HS_TF; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW DNA damage; DNA repair; DNA-binding; Isopeptide bond; Kinetochore;
KW mRNA processing; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..525
FT /note="Heat shock factor protein 1"
FT /id="PRO_0000260263"
FT REGION 15..120
FT /note="DNA-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 130..203
FT /note="Hydrophobic repeat HR-A/B"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 203..224
FT /note="D domain"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 221..310
FT /note="Regulatory domain"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 266..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..525
FT /note="Transactivation domain"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 380..405
FT /note="Hydrophobic repeat HR-C"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 495..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 408..416
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT COMPBIAS 320..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 91
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 121
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 142
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 208
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 230
FT /note="Phosphoserine; by CAMK2A"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 298
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 303
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 307
FT /note="Phosphoserine; by MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 320
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 327
FT /note="Phosphoserine; by MAPK12"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 359
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 415
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT MOD_RES 520
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
SQ SEQUENCE 525 AA; 56702 MW; 985CF9E968B0040B CRC64;
MDLPVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVLDQG QFAKEVLPKY
FKHSNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ HPCFLRGQEQ LLENIKRKVT
SVSTLRSEDI KIRQDSVTKL LTDVQLMKGK QESMDSKLLA MKHENEALWR EVASLRQKHA
QQQKVVNKLI QFLISLVQSN RILGVKRKIP LMLNDGGPAH PMPKYGRQYS LEHIHGPGPY
PAPSPAYSGS SLYSPDAVTS SGPIISDITE LAPGSPVASS GGSVDERPLS SSPLVRVKEE
PPSPPQSPRA EGASPGRPSS MVETPLSPTT LIDSILRESE PTPVASTTPL VDTGGRPPSP
LPASAPEKCL SVACLDKTEL SDHLDAMDSN LDNLQTMLTS HGFSVDTSTL LDLFSPSVTV
PDMSLPDLDS SLASIQELLS PQEPPRPLEA EKSSPDSGKQ LVHYTAQPLL LLDPGSVDVG
SSDLPVLFEL GEGSYFSEGD DYSDDPTISL LTGSEPPKAK DPTVS
