BIP_RAT
ID BIP_RAT Reviewed; 654 AA.
AC P06761;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000250|UniProtKB:P11021};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=78 kDa glucose-regulated protein {ECO:0000250|UniProtKB:P11021};
DE Short=GRP-78 {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=Binding-immunoglobulin protein {ECO:0000250|UniProtKB:P11021};
DE Short=BiP {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=Heat shock protein 70 family protein 5 {ECO:0000250|UniProtKB:P11021};
DE Short=HSP70 family protein 5 {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=Heat shock protein family A member 5 {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=Immunoglobulin heavy chain-binding protein {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=Steroidogenesis-activator polypeptide {ECO:0000303|PubMed:3563495};
DE Flags: Precursor;
GN Name=Hspa5 {ECO:0000312|RGD:2843};
GN Synonyms=Grp78 {ECO:0000250|UniProtKB:P11021};
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].
RX PubMed=3087629; DOI=10.1016/0092-8674(86)90746-4;
RA Munro S., Pelham H.R.B.;
RT "An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated
RT protein and immunoglobulin heavy chain binding protein.";
RL Cell 46:291-300(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RX PubMed=3468506; DOI=10.1073/pnas.84.3.680;
RA Chang S.C., Wooden S.K., Nakaki T., Kim Y.K., Lin A.Y., Kung L.,
RA Attenello J.W., Lee A.S.;
RT "Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its
RT regulatory sequences and the effect of protein glycosylation on its
RT expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:680-684(1987).
RN [4]
RP PROTEIN SEQUENCE OF 50-60; 165-181; 307-324; 475-492 AND 533-540, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 626-654.
RX PubMed=3563495; DOI=10.1126/science.3563495;
RA Pedersen R.C., Brownie A.C.;
RT "Steroidogenesis-activator polypeptide isolated from a rat Leydig cell
RT tumor.";
RL Science 236:188-190(1987).
RN [6]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [7]
RP INTERACTION WITH TMEM132A.
RC STRAIN=Sprague-Dawley;
RX PubMed=12514190; DOI=10.1074/jbc.m212083200;
RA Oh-hashi K., Naruse Y., Amaya F., Shimosato G., Tanaka M.;
RT "Cloning and characterization of a novel GRP78-binding protein in the rat
RT brain.";
RL J. Biol. Chem. 278:10531-10537(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; THR-648 AND SER-649, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Endoplasmic reticulum chaperone that plays a key role in
CC protein folding and quality control in the endoplasmic reticulum lumen
CC (By similarity). Involved in the correct folding of proteins and
CC degradation of misfolded proteins via its interaction with
CC DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from
CC its substrate (By similarity). Acts as a key repressor of the
CC ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed
CC endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region
CC of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby
CC inactivating ERN1/IRE1. Accumulation of misfolded protein in the
CC endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1,
CC allowing homodimerization and subsequent activation of ERN1/IRE1 (By
CC similarity). Plays an auxiliary role in post-translational transport of
CC small presecretory proteins across endoplasmic reticulum (ER). May
CC function as an allosteric modulator for SEC61 channel-forming
CC translocon complex, likely cooperating with SEC62 to enable the
CC productive insertion of these precursors into SEC61 channel. Appears to
CC specifically regulate translocation of precursors having inhibitory
CC residues in their mature region that weaken channel gating. May also
CC play a role in apoptosis and cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P11021,
CC ECO:0000250|UniProtKB:P20029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:G3I8R9};
CC -!- ACTIVITY REGULATION: The chaperone activity is regulated by ATP-induced
CC allosteric coupling of the nucleotide-binding (NBD) and substrate-
CC binding (SBD) domains (By similarity). In the ADP-bound and nucleotide-
CC free (apo) states, the two domains have little interaction (By
CC similarity). In contrast, in the ATP-bound state the two domains are
CC tightly coupled, which results in drastically accelerated kinetics in
CC both binding and release of polypeptide substrates (By similarity). J
CC domain-containing co-chaperones (DNAJB9/ERdj4 or DNAJC10/ERdj5)
CC stimulate the ATPase activity and are required for efficient substrate
CC recognition by HSPA5/BiP. Homooligomerization inactivates participating
CC HSPA5/BiP protomers and probably act as reservoirs to store HSPA5/BiP
CC molecules when they are not needed by the cell (By similarity).
CC {ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P11021}.
CC -!- SUBUNIT: Monomer and homooligomer; homooligomerization via the
CC interdomain linker inactivates the chaperone activity and acts as a
CC storage of HSPA5/BiP molecules (By similarity). Interacts with DNAJC1
CC (via J domain) (By similarity). Component of an EIF2 complex at least
CC composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and
CC HSPA5 (By similarity). Part of a large chaperone multiprotein complex
CC comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB,
CC SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at very low
CC levels, CALR nor CANX (PubMed:12475965). Interacts with TMEM132A and
CC TRIM21 (PubMed:12514190). May form a complex with ERLEC1, OS9, SEL1L
CC and SYVN1 (By similarity). Interacts with DNAJC10 (By similarity).
CC Interacts with DNAJB9/ERdj4; leading to recruit HSPA5/BiP to ERN1/IRE1
CC (By similarity). Interacts with ERN1/IRE1; interaction takes place
CC following interaction with DNAJB9/ERdj4 and leads to inactivate
CC ERN1/IRE1 (By similarity). Interacts with MX1 (By similarity).
CC Interacts with METTL23 (By similarity). Interacts with CEMIP; the
CC interaction induces calcium leakage from the endoplasmic reticulum and
CC cell migration (By similarity). Interacts with PCSK4 form; the
CC interaction takes place in the endoplasmic reticulum (By similarity).
CC Interacts with CIPC (By similarity). Interacts with CCDC88B (via C-
CC terminus); the interaction opposes ERN1-mediated JNK activation,
CC protecting against apoptosis (By similarity). Interacts with INPP5K;
CC necessary for INPP5K localization at the endoplasmic reticulum (By
CC similarity). Interacts with MANF; the interaction is direct (By
CC similarity). Interacts with LOXL2; leading to activate the ERN1/IRE1-
CC XBP1 pathway of the unfolded protein response (By similarity).
CC Interacts with CLU under stressed condition; interaction increases CLU
CC protein stability; facilitates its retrotranslocation and
CC redistribution to the mitochondria; cooperatively suppress stress-
CC induced apoptosis by stabilizing mitochondrial membrane integrity (By
CC similarity). Interacts with CCDC47 (By similarity). Interacts with CLN3
CC (By similarity). Interacts with KIAA1324; may regulate the function of
CC HSPA5 in apoptosis and cell proliferation. Interacts with CASP7 (By
CC similarity). Interacts with ILDR2; the interaction stabilizes ILDR2
CC expression (By similarity). {ECO:0000250|UniProtKB:G3I8R9,
CC ECO:0000250|UniProtKB:P11021, ECO:0000250|UniProtKB:P20029,
CC ECO:0000269|PubMed:12475965, ECO:0000269|PubMed:12514190}.
CC -!- INTERACTION:
CC P06761; Q9R0C9: Sigmar1; NbExp=3; IntAct=EBI-916036, EBI-1557826;
CC P06761; P06882: Tg; NbExp=6; IntAct=EBI-916036, EBI-1549657;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P11021}. Melanosome
CC {ECO:0000250|UniProtKB:P11021}. Cytoplasm
CC {ECO:0000250|UniProtKB:P20029}. Cell surface. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV (By
CC similarity). Localizes to the cell surface in epithelial cells; high
CC levels of free iron promotes cell surface localization (By similarity).
CC {ECO:0000250|UniProtKB:P11021}.
CC -!- DOMAIN: The interdomain linker regulates the chaperone activity by
CC mediating the formation of homooligomers. Homooligomers are formed by
CC engagement of the interdomain linker of one HSPA5/BiP molecule as a
CC typical substrate of an adjacent HSPA5/BiP molecule. HSPA5/BiP
CC oligomerization inactivates participating HSPA5/BiP protomers.
CC HSPA5/BiP oligomers probably act as reservoirs to store HSPA5/BiP
CC molecules when they are not needed by the cell. When the levels of
CC unfolded proteins rise, cells can rapidly break up these oligomers to
CC make active monomers. {ECO:0000250|UniProtKB:G3I8R9}.
CC -!- PTM: In unstressed cells, AMPylation at Thr-518 by FICD inactivates the
CC chaperome activity: AMPylated form is locked in a relatively inert
CC state and only weakly stimulated by J domain-containing proteins. In
CC response to endoplasmic reticulum stress, de-AMPylation by the same
CC protein, FICD, restores the chaperone activity.
CC {ECO:0000250|UniProtKB:G3I8R9}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; M14050; AAA40817.1; -; mRNA.
DR EMBL; BC062017; AAH62017.1; -; mRNA.
DR EMBL; M14866; AAA41277.1; -; Genomic_DNA.
DR PIR; A23948; HHRTGB.
DR RefSeq; NP_037215.1; NM_013083.2.
DR AlphaFoldDB; P06761; -.
DR SMR; P06761; -.
DR BioGRID; 247646; 13.
DR CORUM; P06761; -.
DR IntAct; P06761; 21.
DR MINT; P06761; -.
DR STRING; 10116.ENSRNOP00000025064; -.
DR CarbonylDB; P06761; -.
DR iPTMnet; P06761; -.
DR PhosphoSitePlus; P06761; -.
DR SwissPalm; P06761; -.
DR jPOST; P06761; -.
DR PaxDb; P06761; -.
DR PRIDE; P06761; -.
DR GeneID; 25617; -.
DR KEGG; rno:25617; -.
DR UCSC; RGD:2843; rat.
DR CTD; 3309; -.
DR RGD; 2843; Hspa5.
DR VEuPathDB; HostDB:ENSRNOG00000018294; -.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P06761; -.
DR OMA; AYTKNQD; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P06761; -.
DR TreeFam; TF105044; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:P06761; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000018294; Expressed in ovary and 20 other tissues.
DR Genevisible; P06761; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IPI:RGD.
DR GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
DR GO; GO:0071277; P:cellular response to calcium ion; IEP:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEP:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR GO; GO:0071353; P:cellular response to interleukin-4; ISO:RGD.
DR GO; GO:0071287; P:cellular response to manganese ion; IEP:ParkinsonsUK-UCL.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; ISO:RGD.
DR GO; GO:0021589; P:cerebellum structural organization; ISO:RGD.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD.
DR GO; GO:0006983; P:ER overload response; ISO:RGD.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; ISO:RGD.
DR GO; GO:0001554; P:luteolysis; IEP:RGD.
DR GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IEP:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; ISS:UniProtKB.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:MGI.
DR GO; GO:1904313; P:response to methamphetamine hydrochloride; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0097501; P:stress response to metal ion; IEP:RGD.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Hydrolase; Isopeptide bond; Methylation; Nitration;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Signal;
KW Ubl conjugation.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..654
FT /note="Endoplasmic reticulum chaperone BiP"
FT /id="PRO_0000013569"
FT REGION 1..80
FT /note="Required for interaction with KIAA1324"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 125..280
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 409..419
FT /note="Interdomain linker"
FT /evidence="ECO:0000250|UniProtKB:G3I8R9"
FT REGION 420..500
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 631..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 651..654
FT /note="Prevents secretion from ER"
FT BINDING 36..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 227..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 293..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 364..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 160
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 271
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 353
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 447
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 492
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 518
FT /note="O-AMP-threonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:G3I8R9"
FT MOD_RES 518
FT /note="Phosphothreonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOD_RES 585
FT /note="N6,N6,N6-trimethyllysine; by METTL21A; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 585
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOD_RES 585
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOD_RES 591
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOD_RES 643
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 648
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT CONFLICT 29
FT /note="T -> M (in Ref. 3; AAA41277)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="S -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="K -> KK (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 654 AA; 72347 MW; 9D686C6484150108 CRC64;
MKFTVVAAAL LLLCAVRAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV EIIANDQGNR
ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG RTWNDPSVQQ DIKFLPFKVV
EKKTKPYIQV DIGGGQTKTF APEEISAMVL TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ
RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG
VFEVVATNGD THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS
SQHQARIEIE SFFEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD LKKSDIDEIV
LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV QAGVLSGDQD TGDLVLLDVC
PLTLGIETVG GVMTKLIPRN TVVPTKKSQI FSTASDNQPT VTIKVYEGER PLTKDNHLLG
TFDLTGIPPA PRGVPQIEVT FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER
MVNDAEKFAE EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSPED KETMEKAVEE
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSGGP PPTGEEDTSE KDEL
