P53_MARMO
ID P53_MARMO Reviewed; 391 AA.
AC O36006;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=TP53;
OS Marmota monax (Woodchuck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Marmota.
OX NCBI_TaxID=9995;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9233767; DOI=10.1038/sj.onc.1201203;
RA Feitelson M.A., Ranganathan P.N., Clayton M.M., Zhang S.M.;
RT "Partial characterization of the woodchuck tumor suppressor, p53, and its
RT interaction with woodchuck hepatitis virus X antigen in
RT hepatocarcinogenesis.";
RL Oncogene 15:327-336(1997).
CC -!- FUNCTION: Acts as a tumor suppressor in many tumor types; induces
CC growth arrest or apoptosis depending on the physiological circumstances
CC and cell type. Involved in cell cycle regulation as a trans-activator
CC that acts to negatively regulate cell division by controlling a set of
CC genes required for this process. One of the activated genes is an
CC inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be
CC mediated either by stimulation of BAX and FAS antigen expression, or by
CC repression of Bcl-2 expression. Its pro-apoptotic activity is activated
CC via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By
CC similarity). However, this activity is inhibited when the interaction
CC with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By
CC similarity). In cooperation with mitochondrial PPIF is involved in
CC activating oxidative stress-induced necrosis; the function is largely
CC independent of transcription. Prevents CDK7 kinase activity when
CC associated to CAK complex in response to DNA damage, thus stopping cell
CC cycle progression. Induces the transcription of long intergenic non-
CC coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21
CC participates in TP53-dependent transcriptional repression leading to
CC apoptosis and seems to have an effect on cell-cycle regulation.
CC Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated
CC transcriptional activation of PER2. {ECO:0000250|UniProtKB:P02340,
CC ECO:0000250|UniProtKB:P04637}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Forms homodimers and homotetramers (By similarity). Binds DNA
CC as a homotetramer. Interacts with AXIN1. Probably part of a complex
CC consisting of TP53, HIPK2 and AXIN1. Interacts with histone
CC acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and
CC recruits them to promoters. Interacts (via C-terminus) with TAF1; when
CC TAF1 is part of the TFIID complex. Interacts with ING4; this
CC interaction may be indirect. Found in a complex with CABLES1 and TP73.
CC Interacts with HIPK1, HIPK2, and TP53INP1. Interacts with WWOX.
CC Interacts with USP7 and SYVN1. Interacts with HSP90AB1. Interacts with
CC CHD8; leading to recruit histone H1 and prevent transactivation
CC activity. Interacts with ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1,
CC UHRF2 and E4F. Interacts with YWHAZ; the interaction enhances TP53
CC transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits
CC this interaction. Interacts (via DNA-binding domain) with MAML1 (via N-
CC terminus). Interacts with MKRN1. Interacts with PML (via C-terminus).
CC Interacts with MDM2; leading to ubiquitination and proteasomal
CC degradation of TP53. Directly interacts with FBXO42; leading to
CC ubiquitination and degradation of TP53. Interacts (phosphorylated at
CC Ser-15 by ATM) with the phosphatase PP2A-PPP2R5C holoenzyme; regulates
CC stress-induced TP53-dependent inhibition of cell proliferation.
CC Interacts with PPP2R2A. Interacts with AURKA, DAXX, BRD7 and TRIM24.
CC Interacts (when monomethylated at Lys-380) with L3MBTL1. Interacts with
CC GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to
CC DNA damage. Interacts with CDK5 in neurons. Interacts with AURKB,
CC SETD2, UHRF2 and NOC2L. Interacts (via N-terminus) with PTK2/FAK1; this
CC promotes ubiquitination by MDM2. Interacts with PTK2B/PYK2; this
CC promotes ubiquitination by MDM2. Interacts with PRKCG. Interacts with
CC PPIF; the association implicates preferentially tetrameric TP53, is
CC induced by oxidative stress and is impaired by cyclosporin A (CsA).
CC Interacts with SNAI1; the interaction induces SNAI1 degradation via
CC MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion.
CC Interacts with KAT6A. Interacts with UBC9. Interacts with ZNF385B; the
CC interaction is direct. Interacts (via DNA-binding domain) with ZNF385A;
CC the interaction is direct and enhances p53/TP53 transactivation
CC functions on cell-cycle arrest target genes, resulting in growth arrest
CC (By similarity). Interacts with ANKRD2. Interacts with RFFL and RNF34;
CC involved in p53/TP53 ubiquitination. Interacts with MTA1 and COP1.
CC Interacts with CCAR2 (via N-terminus). Interacts with MORC3. Interacts
CC (via C-terminus) with POU4F2 (via C-terminus). Interacts (via
CC oligomerization region) with NOP53; the interaction is direct and may
CC prevent the MDM2-mediated proteasomal degradation of TP53. Interacts
CC with AFG1L; mediates mitochondrial translocation of TP53. Interacts
CC with UBD (By similarity). Interacts with TAF6 (By similarity).
CC Interacts with C10orf90/FATS; the interaction inhibits binding of TP53
CC and MDM2 (By similarity). Interacts with NUPR1; interaction is stress-
CC dependent. Forms a complex with EP300 and NUPR1; this complex binds
CC CDKN1A promoter leading to transcriptional induction of CDKN1A (By
CC similarity). Interacts with PRMT5 in response to DNA damage; the
CC interaction is TTC5/STRAP dependent (By similarity). Interacts with
CC PPP1R13L (via SH3 domain and ANK repeats); the interaction inhibits
CC pro-apoptotic activity of p53/TP53 (By similarity). Interacts with
CC PPP1R13B/ASPP1 and TP53BP2/ASPP2; the interactions promotes pro-
CC apoptotic activity (By similarity). Interacts with S100A4; this
CC interaction promotes TP53 degradation (By similarity). Interacts with
CC TTC5/STRAP; the interaction may result in increased mitochondrial-
CC dependent apoptosis (By similarity). Interacts with NQO1; this
CC interaction is NADH-dependent, stabilizes TP53 in response to oxidative
CC stress and protects it from ubiquitin-independent degradation by the
CC 20S proteasome. {ECO:0000250|UniProtKB:P02340,
CC ECO:0000250|UniProtKB:P04637, ECO:0000250|UniProtKB:P10361}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus
CC {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP promotes
CC nuclear localization. Recruited into PML bodies together with CHEK2.
CC Translocates to mitochondria upon oxidative stress. Translocates to
CC mitochondria in response to mitomycin C treatment (By similarity).
CC {ECO:0000250|UniProtKB:P04637}.
CC -!- DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the SETD7
CC methyltransferase. {ECO:0000250}.
CC -!- PTM: Phosphorylation on Ser residues mediates transcriptional
CC activation. Phosphorylation at Ser-9 by HIPK4 increases repression
CC activity on BIRC5 promoter (By similarity). Phosphorylated on Thr-18 by
CC VRK1, which may prevent the interaction with MDM2. Phosphorylated on
CC Ser-20 by CHEK2 in response to DNA damage, which prevents
CC ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to
CC reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis.
CC Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to DNA
CC damage. Phosphorylated by HIPK1. Phosphorylated on Ser-46 by HIPK2 upon
CC UV irradiation. Phosphorylation on Ser-46 is required for acetylation
CC by CREBBP. Phosphorylated by CK2 following UV but not gamma
CC irradiation. Stabilized by CDK5-mediated phosphorylation in response to
CC genotoxic and oxidative stresses at Ser-15, Ser-33 and Ser-46, leading
CC to accumulation of p53, particularly in the nucleus, thus inducing the
CC transactivation of p53/TP53 target genes. Phosphorylated by DYRK2 at
CC Ser-46 in response to genotoxic stress. Phosphorylated at Ser-313 and
CC Ser-390 by CDK2 in response to DNA-damage (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Monomethylated at Lys-370 by SETD7, leading to stabilization and
CC increased transcriptional activation. Monomethylated at Lys-368 by
CC SMYD2, leading to decreased DNA-binding activity and subsequent
CC transcriptional regulation activity. Lys-370 monomethylation prevents
CC interaction with SMYD2 and subsequent monomethylation at Lys-368.
CC Dimethylated at Lys-371 by EHMT1 and EHMT2. Monomethylated at Lys-380
CC by KMT5A, promoting interaction with L3MBTL1 and leading to repress
CC transcriptional activity. Demethylation of dimethylated Lys-368 by
CC KDM1A prevents interaction with TP53BP1 and represses TP53-mediated
CC transcriptional activation (By similarity). Monomethylated at Arg-331
CC and dimethylated at Arg-333 and Arg-335 by PRMT5; methylation is
CC increased after DNA damage and might possibly affect TP53 target gene
CC specificity (By similarity). {ECO:0000250|UniProtKB:P04637}.
CC -!- PTM: Sumoylated with SUMO1. Sumoylated at Lys-384 by UBC9 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal
CC degradation. Ubiquitinated by RFWD3, which works in cooperation with
CC MDM2 and may catalyze the formation of short polyubiquitin chains on
CC p53/TP53 that are not targeted to the proteasome. Ubiquitinated by
CC MKRN1, which leads to proteasomal degradation. Deubiquitinated by
CC USP10, leading to stabilize it. Ubiquitinated by TRIM24, RFFL, RNF34
CC and RNF125, which leads to proteasomal degradation. Ubiquitination by
CC TOPORS induces degradation. Deubiquitination by USP7, leading to
CC stabilize it. Ubiquitinated by COP1, which leads to proteasomal
CC degradation (By similarity). Ubiquitination and subsequent proteasomal
CC degradation is negatively regulated by CCAR2 (By similarity).
CC Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-
CC linkage independent and non-proteolytic, leading to TP53 stabilization
CC (By similarity). {ECO:0000250|UniProtKB:P02340,
CC ECO:0000250|UniProtKB:P04637}.
CC -!- PTM: Acetylation of Lys-380 by CREBBP enhances transcriptional
CC activity. Acetylation of Lys-380 by EP300. Deacetylation of Lys-380 by
CC SIRT1 impairs its ability to induce proapoptotic program and modulate
CC cell senescence. Deacetylation by SIRT2 impairs its ability to induce
CC transcription activation in a AKT-dependent manner. Acetylation at Lys-
CC 379 increases stability. Deacetylation at Lys-379 by SIRT6 decreases
CC its stability, thereby regulating cell senescence.
CC {ECO:0000250|UniProtKB:P04637}.
CC -!- DISEASE: Note=p53 is found in increased amounts in a wide variety of
CC transformed cells. p53 is frequently mutated or inactivated in many
CC types of cancer.
CC -!- SIMILARITY: Belongs to the p53 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; AJ001022; CAA04478.1; -; mRNA.
DR AlphaFoldDB; O36006; -.
DR SMR; O36006; -.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0048512; P:circadian behavior; ISS:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR CDD; cd08367; P53; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR InterPro; IPR011615; p53_DNA-bd.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR010991; p53_tetrameristn.
DR InterPro; IPR013872; p53_transactivation_domain.
DR InterPro; IPR002117; p53_tumour_suppressor.
DR PANTHER; PTHR11447; PTHR11447; 1.
DR Pfam; PF00870; P53; 1.
DR Pfam; PF08563; P53_TAD; 1.
DR Pfam; PF07710; P53_tetramer; 1.
DR PRINTS; PR00386; P53SUPPRESSR.
DR SUPFAM; SSF47719; SSF47719; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS00348; P53; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Apoptosis; Biological rhythms; Cell cycle;
KW Cytoplasm; DNA-binding; Endoplasmic reticulum; Isopeptide bond;
KW Metal-binding; Methylation; Mitochondrion; Necrosis; Nucleus;
KW Phosphoprotein; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation; Zinc.
FT CHAIN 1..391
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185707"
FT DNA_BIND 100..290
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT REGION 1..318
FT /note="Interaction with CCAR2"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT REGION 1..44
FT /note="Transcription activation (acidic)"
FT REGION 64..108
FT /note="Interaction with WWOX"
FT /evidence="ECO:0000250"
FT REGION 65..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..368
FT /note="Interaction with HIPK1"
FT /evidence="ECO:0000250"
FT REGION 98..298
FT /note="Required for interaction with ZNF385A"
FT /evidence="ECO:0000250"
FT REGION 111..234
FT /note="Required for interaction with FBXO42"
FT /evidence="ECO:0000250"
FT REGION 114..290
FT /note="Interaction with AXIN1"
FT /evidence="ECO:0000250"
FT REGION 254..292
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000250"
FT REGION 271..278
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 281..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..358
FT /note="Interaction with HIPK2"
FT /evidence="ECO:0000250"
FT REGION 323..354
FT /note="Oligomerization"
FT REGION 348..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..361
FT /note="Interaction with USP7"
FT /evidence="ECO:0000250"
FT REGION 366..385
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 303..319
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 337..348
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 368..370
FT /note="[KR]-[STA]-K motif"
FT COMPBIAS 281..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT SITE 118
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 9
FT /note="Phosphoserine; by HIPK4"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 15
FT /note="Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 18
FT /note="Phosphothreonine; by CK1, VRK1 and VRK2"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 20
FT /note="Phosphoserine; by CHEK2, CK1 and PLK3"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 33
FT /note="Phosphoserine; by CDK5 and CDK7"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 37
FT /note="Phosphoserine; by MAPKAPK5"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 46
FT /note="Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 118
FT /note="N6-acetyllysine; by KAT6A"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 181
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 267
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 282
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 303
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 313
FT /note="Phosphoserine; by AURKA, CDK1 and CDK2"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02340"
FT MOD_RES 331
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 333
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 335
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 368
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 368
FT /note="N6-methyllysine; by SMYD2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 370
FT /note="N6-methyllysine; by SETD7"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 371
FT /note="N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 371
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 379
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 380
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 380
FT /note="N6-acetyllysine; by KAT6A; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 380
FT /note="N6-methyllysine; by KMT5A; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT MOD_RES 390
FT /note="Phosphoserine; by CK2, CDK2 and NUAK1"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 289
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04637"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 391 AA; 43468 MW; E1DE5DB84BA40182 CRC64;
MEEAQSDLSI EPPLSQETFS DLWNLLPENN VLSPVLSPPM DDLLLSSEDV ENWFDKGPDE
ALQMSAAPAP KAPTPAASTL AAPSPATSWP LSSSVPSQNT YPGVYGFRLG FLHSGTAKSV
TCTYSPSLNK LFCQLAKTCP VQLWVDSTPP PGTRVRAMAI YKKSQHMTEV VRRCPHHERC
SDSDGLAPPQ HLIRVEGNLR AEYLDDRNTF RHSVVVPYEP PEVGSECTTI HYNYMCNSSC
MGGMNRRPIL TIITLEGSSG NLLGRNSFEV RVCACPGRDR RTEEENFRKR GEPCPEPPPR
STKRALPNGT SSSPQPKKKP LDGEYFTLKI RGRARFEMFQ ELNEALELKD AQAEKEPGES
RPHPSYLKSK KGQSTSRHKK IIFKREGPDS D
