RS3_CANLF
ID RS3_CANLF Reviewed; 243 AA.
AC E2RH47;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=40S ribosomal protein S3;
DE EC=4.2.99.18 {ECO:0000250|UniProtKB:P23396};
GN Name=RPS3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.70 ANGSTROMS).
RX PubMed=18400176; DOI=10.1016/j.str.2008.01.007;
RA Chandramouli P., Topf M., Menetret J.F., Eswar N., Cannone J.J.,
RA Gutell R.R., Sali A., Akey C.W.;
RT "Structure of the mammalian 80S ribosome at 8.7 A resolution.";
RL Structure 16:535-548(2008).
CC -!- FUNCTION: Involved in translation as a component of the 40S small
CC ribosomal subunit. Has endonuclease activity and plays a role in repair
CC of damaged DNA. Cleaves phosphodiester bonds of DNAs containing altered
CC bases with broad specificity and cleaves supercoiled DNA more
CC efficiently than relaxed DNA. Displays high binding affinity for 7,8-
CC dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive
CC oxygen species (ROS). Has also been shown to bind with similar affinity
CC to intact and damaged DNA. Stimulates the N-glycosylase activity of the
CC base excision protein OGG1. Enhances the uracil excision activity of
CC UNG1. Also stimulates the cleavage of the phosphodiester backbone by
CC APEX1. When located in the mitochondrion, reduces cellular ROS levels
CC and mitochondrial DNA damage. Has also been shown to negatively
CC regulate DNA repair in cells exposed to hydrogen peroxide. Plays a role
CC in regulating transcription as part of the NF-kappa-B p65-p50 complex
CC where it binds to the RELA/p65 subunit, enhances binding of the complex
CC to DNA and promotes transcription of target genes. Represses its own
CC translation by binding to its cognate mRNA. Binds to and protects
CC TP53/p53 from MDM2-mediated ubiquitination. Involved in spindle
CC formation and chromosome movement during mitosis by regulating
CC microtubule polymerization. Involved in induction of apoptosis through
CC its role in activation of CASP8. Induces neuronal apoptosis by
CC interacting with the E2F1 transcription factor and acting
CC synergistically with it to up-regulate pro-apoptotic proteins
CC BCL2L11/BIM and HRK/Dp5. Interacts with TRADD following exposure to UV
CC radiation and induces apoptosis by caspase-dependent JNK activation.
CC {ECO:0000250|UniProtKB:P23396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18;
CC Evidence={ECO:0000250|UniProtKB:P23396};
CC -!- SUBUNIT: Component of the 40S small ribosomal subunit. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.
CC Interacts with HNRPD. Interacts with PRMT1; the interaction methylates
CC RPS3. Interacts with SUMO1; the interaction sumoylates RPS3. Interacts
CC with UBC9. Interacts with CDK1; the interaction phosphorylates RPS3.
CC Interacts with PRKCD; the interaction phosphorylates RPS3. Interacts
CC with PKB/AKT; the interaction phosphorylates RPS3. Interacts with E2F1;
CC the interaction occurs in the absence of nerve growth factor and
CC increases transcription of pro-apoptotic proteins BCL2L11/BIM and
CC HRK/Dp5. Interacts with the base excision repair proteins APEX1 and
CC OGG1; interaction with OGG1 increases OGG1 N-glycosylase activity.
CC Interacts with UNG; the interaction increases the uracil excision
CC activity of UNG1. Interacts with HSP90; the interaction prevents the
CC ubiquitination and proteasome-dependent degradation of RPS3 and is
CC suppressed by increased ROS levels. Interacts with TOM70; the
CC interaction promotes translocation of RPS3 to the mitochondrion.
CC Interacts (via N-terminus) with RELA (via N-terminus); the interaction
CC enhances the DNA-binding activity of the NF-kappa-B p65-p50 complex.
CC Interacts with NFKBIA; the interaction is direct and may bridge the
CC interaction between RPS3 and RELA. Interacts with IKKB; the interaction
CC phosphorylates RPS3 and enhances its translocation to the nucleus.
CC Interacts (via KH domain) with MDM2 and TP53. Interacts with TRADD.
CC Interacts with CRY1. {ECO:0000250|UniProtKB:P23396,
CC ECO:0000250|UniProtKB:P62908}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23396}. Nucleus
CC {ECO:0000250|UniProtKB:P23396}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P23396}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P23396}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P23396}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P23396}. Note=In normal cells, located mainly in
CC the cytoplasm with small amounts in the nucleus but translocates to the
CC nucleus in cells undergoing apoptosis. Nuclear translocation is induced
CC by DNA damaging agents such as hydrogen peroxide. Accumulates in the
CC mitochondrion in response to increased ROS levels. Localizes to the
CC spindle during mitosis. Localized in cytoplasmic mRNP granules
CC containing untranslated mRNAs. {ECO:0000250|UniProtKB:P23396,
CC ECO:0000250|UniProtKB:P62908}.
CC -!- PTM: Methylation by PRMT1 is required for import into the nucleolus and
CC for ribosome assembly. {ECO:0000250|UniProtKB:P23396}.
CC -!- PTM: Sumoylation by SUMO1 enhances protein stability through increased
CC resistance to proteolysis. Sumoylation occurs at one or more of the
CC three consensus sites, Lys-18, Lys-214 and Lys-230.
CC {ECO:0000250|UniProtKB:P23396}.
CC -!- PTM: Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase.
CC Phosphorylation by PRKCD occurs on a non-ribosomal-associated form
CC which results in translocation of RPS3 to the nucleus and enhances its
CC endonuclease activity. Phosphorylated on Ser-209 by IKKB in response to
CC activation of the NF-kappa-B p65-p50 complex which enhances the
CC association of RPS3 with importin-alpha and mediates the nuclear
CC translocation of RPS3. Phosphorylation by MAPK is required for
CC translocation to the nucleus following exposure of cells to DNA
CC damaging agents such as hydrogen peroxide. Phosphorylation by PKB/AKT
CC mediates RPS3 nuclear translocation, enhances RPS3 endonuclease
CC activity and suppresses RPS3-induced neuronal apoptosis.
CC {ECO:0000250|UniProtKB:P23396}.
CC -!- PTM: Ubiquitinated. This is prevented by interaction with HSP90 which
CC stabilizes the protein. Monoubiquitinated at Lys-214 by ZNF598 when a
CC ribosome has stalled during translation of poly(A) sequences, leading
CC to preclude synthesis of a long poly-lysine tail and initiate the
CC ribosome quality control (RQC) pathway to degrade the potentially
CC detrimental aberrant nascent polypeptide.
CC {ECO:0000250|UniProtKB:P23396}.
CC -!- PTM: Ufmylated by UFL1. {ECO:0000250|UniProtKB:P62908}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000305}.
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DR RefSeq; NP_001300706.1; NM_001313777.1.
DR PDB; 4V5Z; EM; 8.70 A; c=1-243.
DR PDBsum; 4V5Z; -.
DR AlphaFoldDB; E2RH47; -.
DR BMRB; E2RH47; -.
DR SMR; E2RH47; -.
DR STRING; 9615.ENSCAFP00000008052; -.
DR PaxDb; E2RH47; -.
DR PRIDE; E2RH47; -.
DR Ensembl; ENSCAFT00030033380; ENSCAFP00030029127; ENSCAFG00030018057.
DR Ensembl; ENSCAFT00040031863; ENSCAFP00040027712; ENSCAFG00040017211.
DR Ensembl; ENSCAFT00845021062; ENSCAFP00845016559; ENSCAFG00845011844.
DR GeneID; 476804; -.
DR KEGG; cfa:476804; -.
DR CTD; 6188; -.
DR VEuPathDB; HostDB:ENSCAFG00845011844; -.
DR eggNOG; KOG3181; Eukaryota.
DR GeneTree; ENSGT00390000008610; -.
DR HOGENOM; CLU_058591_2_1_1; -.
DR InParanoid; E2RH47; -.
DR OMA; YIKKCGE; -.
DR OrthoDB; 1135751at2759; -.
DR TreeFam; TF300901; -.
DR Reactome; R-CFA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-CFA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-CFA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-CFA-72649; Translation initiation complex formation.
DR Reactome; R-CFA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-CFA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-CFA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-CFA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-CFA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-CFA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; E2RH47; -.
DR Proteomes; UP000002254; Chromosome 21.
DR Bgee; ENSCAFG00000005402; Expressed in lymph node and 49 other tissues.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0071159; C:NF-kappaB complex; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:Ensembl.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0032357; F:oxidized purine DNA binding; IEA:Ensembl.
DR GO; GO:0032358; F:oxidized pyrimidine DNA binding; IEA:Ensembl.
DR GO; GO:0051018; F:protein kinase A binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:Ensembl.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0097100; F:supercoiled DNA binding; IEA:Ensembl.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045738; P:negative regulation of DNA repair; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:1905053; P:positive regulation of base-excision repair; IEA:Ensembl.
DR GO; GO:2001272; P:positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IEA:Ensembl.
DR GO; GO:1902546; P:positive regulation of DNA N-glycosylase activity; IEA:Ensembl.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IEA:Ensembl.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IEA:Ensembl.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0061481; P:response to TNF agonist; IEA:Ensembl.
DR GO; GO:0051225; P:spindle assembly; IEA:Ensembl.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.1140.32; -; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR001351; Ribosomal_S3_C.
DR InterPro; IPR036419; Ribosomal_S3_C_sf.
DR InterPro; IPR018280; Ribosomal_S3_CS.
DR InterPro; IPR005703; Ribosomal_S3_euk/arc.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR SUPFAM; SSF54821; SSF54821; 1.
DR TIGRFAMs; TIGR01008; uS3_euk_arch; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; DNA damage; DNA repair; DNA-binding; Isopeptide bond; Lyase;
KW Membrane; Methylation; Mitochondrion; Mitochondrion inner membrane;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; Transcription; Transcription regulation;
KW Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CHAIN 2..243
FT /note="40S ribosomal protein S3"
FT /id="PRO_0000405584"
FT DOMAIN 21..92
FT /note="KH type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00118"
FT REGION 200..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 6
FT /note="Phosphoserine; by PKC/PRKCD"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 42
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 64
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 65
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 67
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 70
FT /note="Phosphothreonine; by PKB"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 132
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62908"
FT MOD_RES 209
FT /note="Phosphoserine; by IKKB"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 221
FT /note="Phosphothreonine; by CDK1 and PKC/PRKCD"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P23396"
SQ SEQUENCE 243 AA; 26674 MW; 6B9BB34FDEE04AAF CRC64;
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG
EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA QAESLRYKLL GGLAVRRACY
GVLRFIMESG AKGCEVVVSG KLRGQRAKSM KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG
VLGIKVKIML PWDPSGKIGP KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV
PTA
