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P53_CAVPO
ID   P53_CAVPO               Reviewed;         391 AA.
AC   Q9WUR6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Cellular tumor antigen p53;
DE   AltName: Full=Tumor suppressor p53;
GN   Name=TP53;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   PubMed=10331945; DOI=10.1006/geno.1999.5794;
RA   D'erchia A.M., Pesole G., Tullo A., Saccone C., Sbisa E.;
RT   "Guinea pig p53 mRNA: identification of new elements in coding and
RT   untranslated regions and their functional and evolutionary implications.";
RL   Genomics 58:50-64(1999).
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 E4F1. Interacts with YWHAZ; the interaction enhances TP53
CC       transcriptional activity. Phosphorylation of YWHAZ inhibits this
CC       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
CC       arrest. Interacts with ANKRD2. Interacts with RFFL and RNF34; involved
CC       in p53/TP53 ubiquitination. Interacts with MTA1 and COP1. Interacts
CC       with CCAR2 (via N-terminus). Interacts with MORC3. Interacts (via C-
CC       terminus) with POU4F2 (via C-terminus). Interacts (via oligomerization
CC       region) with NOP53; the interaction is direct and may prevent the MDM2-
CC       mediated proteasomal degradation of TP53. Interacts with AFG1L;
CC       mediates mitochondrial translocation of TP53. Interacts with UBD.
CC       Interacts with TAF6. Interacts with C10orf90/FATS; the interaction
CC       inhibits binding of TP53 and MDM2 (By similarity). Interacts with
CC       NUPR1; interaction is stress-dependent. Forms a complex with EP300 and
CC       NUPR1; this complex binds CDKN1A promoter leading to transcriptional
CC       induction of CDKN1A (By similarity). Interacts with PRMT5 in response
CC       to DNA damage; the interaction is TTC5/STRAP dependent (By similarity).
CC       Interacts with PPP1R13L (via SH3 domain and ANK repeats); the
CC       interaction inhibits pro-apoptotic activity of p53/TP53 (By
CC       similarity). Interacts with PPP1R13B/ASPP1 and TP53BP2/ASPP2; the
CC       interactions promotes pro-apoptotic activity (By similarity). When
CC       phosphorylated at Ser-15, interacts with DDX3X and gamma-tubulin (By
CC       similarity). Interacts with KAT7/HBO1; leading to inhibit histone
CC       acetyltransferase activity of KAT7/HBO1 (By similarity). Interacts (via
CC       N-terminus) with E3 ubiquitin-protein ligase MUL1; the interaction
CC       results in ubiquitination of cytoplasmic TP53 at Lys-24 and subsequent
CC       proteasomal degradation (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}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:P04637}.
CC       Note=Interaction with BANP promotes nuclear localization. Recruited
CC       into PML bodies together with CHEK2. Translocates to mitochondria upon
CC       oxidative stress. Translocates to mitochondria in response to mitomycin
CC       C treatment (By similarity). {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 on Ser-390 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/TP53, particularly in the nucleus, thus inducing
CC       the transactivation of p53/TP53 target genes. Phosphorylated by DYRK2
CC       at Ser-46 in response to genotoxic stress. Phosphorylated at Ser-313
CC       and Ser-390 by CDK2 in response to DNA-damage (By similarity).
CC       Phosphorylation at Ser-15 is required for interaction with DDX3X and
CC       gamma-tubulin (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P04637}.
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 at Lys-289 and Lys-290, which leads to proteasomal degradation.
CC       Deubiquitinated by USP10, leading to stabilize it. Ubiquitinated by
CC       TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation.
CC       Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7,
CC       leading to stabilize it. Ubiquitinated by COP1, which leads to
CC       proteasomal degradation (By similarity). Ubiquitination and subsequent
CC       proteasomal degradation is negatively regulated by CCAR2 (By
CC       similarity). Polyubiquitinated by C10orf90/FATS, polyubiquitination is
CC       'Lys-48'-linkage independent and non-proteolytic, leading to TP53
CC       stabilization (By similarity). {ECO:0000250|UniProtKB:P02340,
CC       ECO:0000250|UniProtKB:P04637}.
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 by PRMT5; methylation is increased after
CC       DNA damage and might possibly affect TP53 target gene specificity (By
CC       similarity). Polyubiquitinated by MUL1 at Lys-24 which leads to
CC       proteasomal degradation (By similarity).
CC       {ECO:0000250|UniProtKB:P04637}.
CC   -!- PTM: Sumoylated with SUMO1. Sumoylated at Lys-384 by UBC9 (By
CC       similarity). {ECO:0000250}.
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}.
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DR   EMBL; AJ009673; CAB43196.1; -; mRNA.
DR   RefSeq; NP_001166211.1; NM_001172740.1.
DR   AlphaFoldDB; Q9WUR6; -.
DR   SMR; Q9WUR6; -.
DR   STRING; 10141.ENSCPOP00000012841; -.
DR   Ensembl; ENSCPOT00000014394; ENSCPOP00000012841; ENSCPOG00000014252.
DR   GeneID; 100379269; -.
DR   KEGG; cpoc:100379269; -.
DR   CTD; 7157; -.
DR   eggNOG; ENOG502QVY3; Eukaryota.
DR   GeneTree; ENSGT00950000183153; -.
DR   HOGENOM; CLU_019621_0_0_1; -.
DR   InParanoid; Q9WUR6; -.
DR   OMA; FHKKGEP; -.
DR   OrthoDB; 257530at2759; -.
DR   TreeFam; TF106101; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000014252; Expressed in zone of skin and 13 other tissues.
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; Cytoskeleton; DNA-binding; Endoplasmic reticulum;
KW   Isopeptide bond; Metal-binding; Methylation; Mitochondrion; Necrosis;
KW   Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc.
FT   CHAIN           1..391
FT                   /note="Cellular tumor antigen p53"
FT                   /id="PRO_0000185696"
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          53..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..108
FT                   /note="Interaction with WWOX"
FT                   /evidence="ECO:0000250"
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          284..320
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          347..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        303..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..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         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        24
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
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        290
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;  43288 MW;  321D40702383573E CRC64;
     MEEPHSDLSI EPPLSQETFS DLWKLLPENN VLSDSLSPPM DHLLLSPEEV ASWLGENPDG
     DGHVSAAPVS EAPTSAGPAL VAPAPATSWP LSSSVPSHKP YRGSYGFEVH FLKSGTAKSV
     TCTYSPGLNK LFCQLAKTCP VQVWVESPPP PGTRVRALAI YKKSQHMTEV VRRCPHHERC
     SDSDGLAPPQ HLIRVEGNLH AEYVDDRTTF RHSVVVPYEP PEVGSDCTTI HYNYMCNSSC
     MGGMNRRPIL TIITLEDSSG KLLGRDSFEV RVCACPGRDR RTEEENFRKK GGLCPEPTPG
     NIKRALPTST SSSPQPKKKP LDAEYFTLKI RGRKNFEILR EINEALEFKD AQTEKEPGES
     RPHSSYPKSK KGQSTSCHKK LMFKREGLDS D
 
 
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