LMNA_RAT
ID LMNA_RAT Reviewed; 665 AA.
AC P48679;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Prelamin-A/C;
DE Contains:
DE RecName: Full=Lamin-A/C;
DE Flags: Precursor;
GN Name=Lmna; Synonyms=Lmn1;
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=1426247; DOI=10.1016/0014-5793(92)80927-9;
RA Ozaki T., Sakiyama S.;
RT "Lamin A gene expression is specifically suppressed in v-src-transformed
RT cells.";
RL FEBS Lett. 312:165-168(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-663.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Jonnalagadda V.S., Parnaik V.K.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 124-132; 209-215; 320-328 AND 629-643.
RC TISSUE=Liver;
RX PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
RA Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
RA Watanabe Y., Furukawa K., Horigome T.;
RT "Proteome analysis of a rat liver nuclear insoluble protein fraction and
RT localization of a novel protein, ISP36, to compartments in the
RT interchromatin space.";
RL FEBS J. 272:4327-4338(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; THR-496; SER-500 AND
RP THR-510, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer
CC on the nucleoplasmic side of the inner nuclear membrane, which is
CC thought to provide a framework for the nuclear envelope and may also
CC interact with chromatin. Lamin A and C are present in equal amounts in
CC the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1
CC to the DNA double-strand breaks (DSBs) to prevent chromosome
CC translocation by immobilizing broken DNA ends (By similarity). Plays an
CC important role in nuclear assembly, chromatin organization, nuclear
CC membrane and telomere dynamics. Required for normal development of
CC peripheral nervous system and skeletal muscle and for muscle satellite
CC cell proliferation. Required for osteoblastogenesis and bone formation.
CC Also prevents fat infiltration of muscle and bone marrow, helping to
CC maintain the volume and strength of skeletal muscle and bone. Required
CC for cardiac homeostasis. {ECO:0000250|UniProtKB:P02545,
CC ECO:0000250|UniProtKB:P48678}.
CC -!- FUNCTION: Prelamin-A/C can accelerate smooth muscle cell senescence. It
CC acts to disrupt mitosis and induce DNA damage in vascular smooth muscle
CC cells (VSMCs), leading to mitotic failure, genomic instability, and
CC premature senescence (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer of lamin A and lamin C. Interacts with lamin-
CC associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin.
CC Interacts with SREBF1, SREBF2, SUN1, SUN2 and TMEM43. Interacts with
CC TMEM201. Proteolytically processed isoform A interacts with NARF.
CC Prelamin-A/C interacts with EMD. Interacts with MLIP. Interacts with
CC DMPK; may regulate nuclear envelope stability. Interacts with SUV39H1;
CC the interaction increases stability of SUV39H1 (By similarity).
CC Interacts with ITSN1 isoform 2 (By similarity). Interacts with IFFO1;
CC the interaction forms an interior nucleoskeleton and the recruitment to
CC DNA double-strand breaks (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P02545}.
CC -!- SUBUNIT: [Isoform Lamin C]: Interacts (via C-terminus) with LEMD2 (via
CC N-terminus) (in vitro). {ECO:0000250|UniProtKB:P02545}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P02545}. Nucleus
CC envelope {ECO:0000250|UniProtKB:P02545}. Nucleus lamina {ECO:0000250}.
CC Nucleus, nucleoplasm {ECO:0000250}. Nucleus matrix
CC {ECO:0000250|UniProtKB:P02545}. Note=Farnesylation of prelamin-A/C
CC facilitates nuclear envelope targeting and subsequent cleavage by
CC ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C,
CC which can then be inserted into the nuclear lamina. EMD is required for
CC proper localization of non-farnesylated prelamin-A/C (By similarity).
CC Phosphorylation status of S-22 determines its localization between
CC double-strand break (DSB) sites and the nuclear matrix (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P02545}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoform A and isoform C are present in equal amounts in the
CC lamina of mammals.;
CC Name=Lamin A;
CC IsoId=P48679-1; Sequence=Displayed;
CC Name=Lamin C;
CC IsoId=P48679-2; Sequence=Not described;
CC -!- PTM: Proteolytic cleavage of the C-terminal of 18 residues of prelamin-
CC A/C results in the production of lamin-A/C. The prelamin-A/C maturation
CC pathway includes farnesylation of CAAX motif, ZMPSTE24/FACE1 mediated
CC cleavage of the last three amino acids, methylation of the C-terminal
CC cysteine and endoproteolytic removal of the last 15 C-terminal amino
CC acids. Proteolytic cleavage requires prior farnesylation and
CC methylation, and absence of these blocks cleavage (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Sumoylation is necessary for the localization to the nuclear
CC envelope. {ECO:0000250}.
CC -!- PTM: Farnesylation of prelamin-A/C facilitates nuclear envelope
CC targeting. {ECO:0000250}.
CC -!- PTM: Increased phosphorylation of the lamins occurs before envelope
CC disintegration and probably plays a role in regulating lamin
CC associations. Phosphorylation status of S-22 determines its
CC localization between double-strand break (DSB) sites and the nuclear
CC matrix (By similarity). {ECO:0000250|UniProtKB:P02545}.
CC -!- MISCELLANEOUS: The structural integrity of the lamina is strictly
CC controlled by the cell cycle, as seen by the disintegration and
CC formation of the nuclear envelope in prophase and telophase,
CC respectively.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA47342.1; Type=Frameshift; Evidence={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; X66870; CAA47342.1; ALT_FRAME; mRNA.
DR EMBL; X76297; CAA53945.1; -; mRNA.
DR PIR; S27267; S27267.
DR AlphaFoldDB; P48679; -.
DR SMR; P48679; -.
DR IntAct; P48679; 3.
DR MINT; P48679; -.
DR STRING; 10116.ENSRNOP00000026705; -.
DR CarbonylDB; P48679; -.
DR iPTMnet; P48679; -.
DR PhosphoSitePlus; P48679; -.
DR jPOST; P48679; -.
DR PaxDb; P48679; -.
DR PRIDE; P48679; -.
DR UCSC; RGD:620456; rat. [P48679-1]
DR RGD; 620456; Lmna.
DR eggNOG; KOG0977; Eukaryota.
DR InParanoid; P48679; -.
DR PhylomeDB; P48679; -.
DR Reactome; R-RNO-352238; Breakdown of the nuclear lamina.
DR Reactome; R-RNO-4419969; Depolymerisation of the Nuclear Lamina.
DR PRO; PR:P48679; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005638; C:lamin filament; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005652; C:nuclear lamina; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IPI:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0090398; P:cellular senescence; IEP:RGD.
DR GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; ISS:UniProtKB.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; ISO:RGD.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; ISO:RGD.
DR GO; GO:1904178; P:negative regulation of adipose tissue development; IMP:RGD.
DR GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; ISO:RGD.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0006998; P:nuclear envelope organization; ISO:RGD.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0051664; P:nuclear pore localization; IBA:GO_Central.
DR GO; GO:0006997; P:nucleus organization; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1900114; P:positive regulation of histone H3-K9 trimethylation; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IBA:GO_Central.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISO:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; ISO:RGD.
DR Gene3D; 2.60.40.1260; -; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF00932; LTD; 1.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF74853; SSF74853; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
DR PROSITE; PS51841; LTD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Direct protein sequencing;
KW Intermediate filament; Isopeptide bond; Lipoprotein; Methylation; Nucleus;
KW Phosphoprotein; Prenylation; Reference proteome; Ubl conjugation.
FT CHAIN 1..662
FT /note="Prelamin-A/C"
FT /id="PRO_0000398841"
FT CHAIN 1..647
FT /note="Lamin-A/C"
FT /id="PRO_0000063813"
FT PROPEP 648..662
FT /note="Removed in Lamin-A/C form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000398842"
FT PROPEP 663..665
FT /note="Removed in Prelamin-A/C form and in Lamin-A/C form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403445"
FT DOMAIN 31..387
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 428..545
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..130
FT /note="Interaction with MLIP"
FT /evidence="ECO:0000250"
FT REGION 1..33
FT /note="Head"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..70
FT /note="Coil 1A"
FT REGION 71..80
FT /note="Linker 1"
FT REGION 81..218
FT /note="Coil 1B"
FT REGION 219..242
FT /note="Linker 2"
FT REGION 243..383
FT /note="Coil 2"
FT REGION 384..665
FT /note="Tail"
FT REGION 384..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 417..422
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 266
FT /note="Heptad change of phase"
FT SITE 325
FT /note="Stutter"
FT /evidence="ECO:0000250"
FT SITE 330
FT /note="Heptad change of phase"
FT SITE 647..648
FT /note="Cleavage; by endoprotease"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 135
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 155
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 171
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 171
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 201
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 260
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 270
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 311
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 450
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 457
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 496
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 505
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 510
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 548
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 662
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 662
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 599
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 599
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CONFLICT 470
FT /note="K -> R (in Ref. 1; CAA47342)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="T -> S (in Ref. 1; CAA47342)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="R -> P (in Ref. 1; CAA47342)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="A -> P (in Ref. 1; CAA47342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 665 AA; 74324 MW; 9CC553005C8534E4 CRC64;
METPSQRRPT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR
LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKELKARN
TKKEGDLLAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALGEAK
KQLQDEMLRR VDAENRLQTL KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR
LADALQELRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA RMQQQLDEYQ
ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQSQ GGGSVTKKRK
LESSESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIK RQNGDDPLMT
YRFPPKFTLK AGQVVTIWAS GAGATHSPPT DLVWKAQNTW GCGTSLRTAL INATGEEVAM
RKLVRSLTMV EDNDDEEEDG DELLHHHRGS HCSSSGDPAE YNLRSRTVLC GTCGQPADKA
ASGSGAQVGG SISSGSSASS VTVTRSFRSV GGSGGGSFGD NLVTRSYLLG NSSPRTQSSQ
NCSIM
