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UBC_RAT
ID   UBC_RAT                 Reviewed;         810 AA.
AC   Q63429; Q3ZBA1;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Polyubiquitin-C;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=Ubiquitin-related;
DE   Flags: Precursor;
GN   Name=Ubc;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Brain cortex, and Hippocampus;
RX   PubMed=8018730; DOI=10.1016/0167-4781(94)90020-5;
RA   Hayashi T., Noga M., Matsuda M.;
RT   "Nucleotide sequence and expression of the rat polyubiquitin mRNA.";
RL   Biochim. Biophys. Acta 1218:232-234(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 381-810.
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-76.
RC   STRAIN=Wistar; TISSUE=Duodenum;
RX   PubMed=8031840; DOI=10.1016/0304-4165(94)90135-x;
RA   Hubbard M.J., Carne A.;
RT   "Differential feeding-related regulation of ubiquitin and calbindin9kDa in
RT   rat duodenum.";
RL   Biochim. Biophys. Acta 1200:191-196(1994).
RN   [4]
RP   PROTEIN SEQUENCE OF 30-42 AND 55-72, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Diao W., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: [Ubiquitin]: Exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is conjugated
CC       to target proteins via an isopeptide bond either as a monomer
CC       (monoubiquitin), a polymer linked via different Lys residues of the
CC       ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC       initiator Met of the ubiquitin (linear polyubiquitin chains).
CC       Polyubiquitin chains, when attached to a target protein, have different
CC       functions depending on the Lys residue of the ubiquitin that is linked:
CC       Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC       in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC       cycle regulation; Lys-29-linked is involved in proteotoxic stress
CC       response and cell cycle; Lys-33-linked is involved in kinase
CC       modification; Lys-48-linked is involved in protein degradation via the
CC       proteasome; Lys-63-linked is involved in endocytosis, DNA-damage
CC       responses as well as in signaling processes leading to activation of
CC       the transcription factor NF-kappa-B. Linear polymer chains formed via
CC       attachment by the initiator Met lead to cell signaling. Ubiquitin is
CC       usually conjugated to Lys residues of target proteins, however, in rare
CC       cases, conjugation to Cys or Ser residues has been observed. When
CC       polyubiquitin is free (unanchored-polyubiquitin), it also has distinct
CC       roles, such as in activation of protein kinases, and in signaling (By
CC       similarity). {ECO:0000250|UniProtKB:P0CG48}.
CC   -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P0CG48}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P0CG48}.
CC   -!- PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.
CC       Phosphorylated ubiquitin specifically binds and activates parkin
CC       (PRKN), triggering mitophagy. Phosphorylation does not affect E1-
CC       mediated E2 charging of ubiquitin but affects discharging of E2 enzymes
CC       to form polyubiquitin chains. It also affects deubiquitination by
CC       deubiquitinase enzymes such as USP30. {ECO:0000250|UniProtKB:P0CG48}.
CC   -!- PTM: [Ubiquitin]: Mono-ADP-ribosylated at the C-terminus by PARP9, a
CC       component of the PPAR9-DTX3L complex. ADP-ribosylation requires
CC       processing by E1 and E2 enzymes and prevents ubiquitin conjugation to
CC       substrates such as histones. {ECO:0000250|UniProtKB:P0CG48}.
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. Uba52 and
CC       Rps27a genes code for a single copy of ubiquitin fused to the ribosomal
CC       proteins L40 and S27a, respectively. UBB and UBC genes code for a
CC       polyubiquitin precursor with exact head to tail repeats, the number of
CC       repeats differ between species and strains.
CC   -!- MISCELLANEOUS: For the sake of clarity sequence features are annotated
CC       only for the first chain, and are not repeated for each of the
CC       following chains.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR   EMBL; D17296; BAA04129.1; -; mRNA.
DR   EMBL; BC103477; AAI03478.1; -; mRNA.
DR   PIR; S45359; S45359.
DR   RefSeq; NP_059010.1; NM_017314.1.
DR   PDB; 5L9U; EM; 6.40 A; S=1-78.
DR   PDBsum; 5L9U; -.
DR   AlphaFoldDB; Q63429; -.
DR   SMR; Q63429; -.
DR   BioGRID; 248372; 819.
DR   IntAct; Q63429; 2.
DR   MINT; Q63429; -.
DR   STRING; 10116.ENSRNOP00000043934; -.
DR   iPTMnet; Q63429; -.
DR   PhosphoSitePlus; Q63429; -.
DR   jPOST; Q63429; -.
DR   PaxDb; Q63429; -.
DR   PRIDE; Q63429; -.
DR   GeneID; 50522; -.
DR   KEGG; rno:50522; -.
DR   UCSC; RGD:621244; rat.
DR   CTD; 7316; -.
DR   RGD; 621244; Ubc.
DR   eggNOG; KOG0001; Eukaryota.
DR   InParanoid; Q63429; -.
DR   OrthoDB; 1536766at2759; -.
DR   PhylomeDB; Q63429; -.
DR   Reactome; R-RNO-110312; Translesion synthesis by REV1.
DR   Reactome; R-RNO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-RNO-110320; Translesion Synthesis by POLH.
DR   Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-RNO-1253288; Downregulation of ERBB4 signaling.
DR   Reactome; R-RNO-1295596; Spry regulation of FGF signaling.
DR   Reactome; R-RNO-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR   Reactome; R-RNO-168638; NOD1/2 Signaling Pathway.
DR   Reactome; R-RNO-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-RNO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-RNO-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-RNO-182971; EGFR downregulation.
DR   Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-RNO-201681; TCF dependent signaling in response to WNT.
DR   Reactome; R-RNO-202424; Downstream TCR signaling.
DR   Reactome; R-RNO-205043; NRIF signals cell death from the nucleus.
DR   Reactome; R-RNO-209543; p75NTR recruits signalling complexes.
DR   Reactome; R-RNO-209560; NF-kB is activated and signals survival.
DR   Reactome; R-RNO-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; R-RNO-2173788; Downregulation of TGF-beta receptor signaling.
DR   Reactome; R-RNO-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR   Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-RNO-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-RNO-2559585; Oncogene Induced Senescence.
DR   Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR   Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-RNO-3134975; Regulation of innate immune responses to cytosolic DNA.
DR   Reactome; R-RNO-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR   Reactome; R-RNO-450302; activated TAK1 mediates p38 MAPK activation.
DR   Reactome; R-RNO-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR   Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-RNO-4641257; Degradation of AXIN.
DR   Reactome; R-RNO-4641258; Degradation of DVL.
DR   Reactome; R-RNO-4641263; Regulation of FZD by ubiquitination.
DR   Reactome; R-RNO-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   Reactome; R-RNO-5357905; Regulation of TNFR1 signaling.
DR   Reactome; R-RNO-5357956; TNFR1-induced NFkappaB signaling pathway.
DR   Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-RNO-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-RNO-5632684; Hedgehog 'on' state.
DR   Reactome; R-RNO-5654726; Negative regulation of FGFR1 signaling.
DR   Reactome; R-RNO-5654727; Negative regulation of FGFR2 signaling.
DR   Reactome; R-RNO-5654732; Negative regulation of FGFR3 signaling.
DR   Reactome; R-RNO-5654733; Negative regulation of FGFR4 signaling.
DR   Reactome; R-RNO-5655862; Translesion synthesis by POLK.
DR   Reactome; R-RNO-5656121; Translesion synthesis by POLI.
DR   Reactome; R-RNO-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-RNO-5675482; Regulation of necroptotic cell death.
DR   Reactome; R-RNO-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-RNO-5685942; HDR through Homologous Recombination (HRR).
DR   Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-RNO-5689603; UCH proteinases.
DR   Reactome; R-RNO-5689877; Josephin domain DUBs.
DR   Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR   Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-RNO-5689901; Metalloprotease DUBs.
DR   Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-RNO-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-RNO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR   Reactome; R-RNO-5696400; Dual Incision in GG-NER.
DR   Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-RNO-6782135; Dual incision in TC-NER.
DR   Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-RNO-6783310; Fanconi Anemia Pathway.
DR   Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-RNO-6804760; Regulation of TP53 Activity through Methylation.
DR   Reactome; R-RNO-6807004; Negative regulation of MET activity.
DR   Reactome; R-RNO-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR   Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR   Reactome; R-RNO-69481; G2/M Checkpoints.
DR   Reactome; R-RNO-69541; Stabilization of p53.
DR   Reactome; R-RNO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-RNO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-RNO-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR   Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8863795; Downregulation of ERBB2 signaling.
DR   Reactome; R-RNO-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-RNO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-RNO-8948747; Regulation of PTEN localization.
DR   Reactome; R-RNO-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   Reactome; R-RNO-901032; ER Quality Control Compartment (ERQC).
DR   Reactome; R-RNO-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR   Reactome; R-RNO-9020702; Interleukin-1 signaling.
DR   Reactome; R-RNO-9033241; Peroxisomal protein import.
DR   Reactome; R-RNO-912631; Regulation of signaling by CBL.
DR   Reactome; R-RNO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-RNO-917937; Iron uptake and transport.
DR   Reactome; R-RNO-937039; IRAK1 recruits IKK complex.
DR   Reactome; R-RNO-937042; IRAK2 mediated activation of TAK1 complex.
DR   Reactome; R-RNO-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR   Reactome; R-RNO-9645460; Alpha-protein kinase 1 signaling pathway.
DR   Reactome; R-RNO-9646399; Aggrephagy.
DR   Reactome; R-RNO-9648002; RAS processing.
DR   Reactome; R-RNO-9664873; Pexophagy.
DR   Reactome; R-RNO-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR   Reactome; R-RNO-9706369; Negative regulation of FLT3.
DR   Reactome; R-RNO-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR   Reactome; R-RNO-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR   Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-RNO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q63429; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0002020; F:protease binding; ISO:RGD.
DR   GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:RGD.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   Pfam; PF00240; ubiquitin; 10.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 10.
DR   SUPFAM; SSF54236; SSF54236; 10.
DR   PROSITE; PS00299; UBIQUITIN_1; 10.
DR   PROSITE; PS50053; UBIQUITIN_2; 10.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_5000139688"
FT   CHAIN           77..152
FT                   /note="Ubiquitin"
FT                   /id="PRO_5000139689"
FT   CHAIN           153..228
FT                   /note="Ubiquitin"
FT                   /id="PRO_5000139690"
FT   CHAIN           229..304
FT                   /note="Ubiquitin"
FT                   /id="PRO_5000139691"
FT   CHAIN           305..380
FT                   /note="Ubiquitin"
FT                   /id="PRO_5000139692"
FT   CHAIN           381..456
FT                   /note="Ubiquitin"
FT                   /id="PRO_5000139693"
FT   CHAIN           457..532
FT                   /note="Ubiquitin"
FT                   /id="PRO_5000139694"
FT   CHAIN           533..608
FT                   /note="Ubiquitin"
FT                   /id="PRO_5000139695"
FT   CHAIN           609..684
FT                   /note="Ubiquitin"
FT                   /id="PRO_5000139696"
FT   CHAIN           685..760
FT                   /note="Ubiquitin"
FT                   /id="PRO_5000139697"
FT   CHAIN           761..810
FT                   /note="Ubiquitin-related"
FT                   /id="PRO_5000139698"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          77..152
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          153..228
FT                   /note="Ubiquitin-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          229..304
FT                   /note="Ubiquitin-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          305..380
FT                   /note="Ubiquitin-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          381..456
FT                   /note="Ubiquitin-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          457..532
FT                   /note="Ubiquitin-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          533..608
FT                   /note="Ubiquitin-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          609..684
FT                   /note="Ubiquitin-like 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          685..760
FT                   /note="Ubiquitin-like 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   SITE            130
FT                   /note="Interacts with activating enzyme"
FT                   /evidence="ECO:0000250"
FT   SITE            144
FT                   /note="Essential for function"
FT                   /evidence="ECO:0000250"
FT   SITE            148
FT                   /note="Interacts with activating enzyme"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         65
FT                   /note="Phosphoserine; by PINK1"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG48"
FT   MOD_RES         76
FT                   /note="ADP-ribosylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG48"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG48"
FT   CROSSLNK        6
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG48"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG48"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG48"
FT   CROSSLNK        29
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG48"
FT   CROSSLNK        33
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG48"
FT   CROSSLNK        48
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG48"
FT   CROSSLNK        63
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG48"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CONFLICT        776
FT                   /note="E -> D (in Ref. 2; AAI03478)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   810 AA;  91087 MW;  4D4ADB697ADA3315 CRC64;
     MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA
     KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
     ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
     LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
     SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ
     QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
     NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL
     TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH
     LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED
     GRTLSDYNIQ KESTLHLVLR LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI
     PPDQQRLIFA GKQLEDGRTL SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS
     VNTKKVKQED TRTFLTTVSR KSPSCACSWV
 
 
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