LARP1_MOUSE
ID LARP1_MOUSE Reviewed; 1072 AA.
AC Q6ZQ58; A2AFQ8; J3QNB1; Q7TSF7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=La-related protein 1;
DE AltName: Full=La ribonucleoprotein domain family member 1;
GN Name=Larp1; Synonyms=Kiaa0731, Larp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Limb;
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 [LARGE SCALE MRNA] OF 709-1072 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=10878606;
RX DOI=10.1002/1097-0177(200007)218:3<401::aid-dvdy1009>3.0.co;2-6;
RA Chauvet S., Maurel-Zaffran C., Miassod R., Jullien N., Pradel J.,
RA Aragnol D.;
RT "dlarp, a new candidate Hox target in Drosophila whose orthologue in mouse
RT is expressed at sites of epithelium/mesenchymal interactions.";
RL Dev. Dyn. 218:401-413(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-503; SER-604; SER-608;
RP THR-626 AND SER-751, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-503; SER-604 AND SER-608, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-302; THR-503 AND
RP SER-525, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-81; THR-196; SER-198;
RP SER-201; SER-299; SER-302; THR-503; SER-525; SER-604; SER-608; THR-626;
RP SER-743; SER-830; THR-842 AND SER-845, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-213, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: RNA-binding protein that regulates the translation of
CC specific target mRNA species downstream of the mTORC1 complex, in
CC function of growth signals and nutrient availability. Interacts on the
CC one hand with the 3' poly-A tails that are present in all mRNA
CC molecules, and on the other hand with the 7-methylguanosine cap
CC structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP)
CC motif, which is present in mRNAs encoding ribosomal proteins and
CC several components of the translation machinery. The interaction with
CC the 5' end of mRNAs containing a 5'TOP motif leads to translational
CC repression by preventing the binding of EIF4G1. When mTORC1 is
CC activated, LARP1 is phosphorylated and dissociates from the 5'
CC untranslated region (UTR) of mRNA. Does not prevent binding of EIF4G1
CC to mRNAs that lack a 5'TOP motif. Interacts with the free 40S ribosome
CC subunit and with ribosomes, both monosomes and polysomes. Under normal
CC nutrient availability, interacts primarily with the 3' untranslated
CC region (UTR) of mRNAs encoding ribosomal proteins and increases protein
CC synthesis. Associates with actively translating ribosomes and
CC stimulates translation of mRNAs containing a 5'TOP motif, thereby
CC regulating protein synthesis, and as a consequence, cell growth and
CC proliferation. Stabilizes mRNAs species with a 5'TOP motif, which is
CC required to prevent apoptosis. {ECO:0000250|UniProtKB:Q6PKG0}.
CC -!- SUBUNIT: Interacts with PABPC1/PABP. Interacts with EIF4A1. Interacts
CC with RPTOR. Recruited to the active mTORC1 complex via interaction with
CC RPTOR. Inhibition of mTORC1 activity strongly reduces interaction with
CC RPTOR and the mTORC1 complex. Identified in a complex with mRNA,
CC PABPC1, EIF4E and EIF4G1. Found in a complex with PABPC1 and SHFL.
CC {ECO:0000250|UniProtKB:Q6PKG0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10878606}.
CC Cytoplasmic granule {ECO:0000250|UniProtKB:Q6PKG0}. Note=Colocalizes
CC with RPTOR and PABPC1 in cytoplasmic granules that resemble stress
CC granules. {ECO:0000250|UniProtKB:Q6PKG0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZQ58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZQ58-2; Sequence=VSP_015116;
CC -!- DEVELOPMENTAL STAGE: At 10.5 dpc, expressed in dorsal root ganglia,
CC spinal cord, and branchial arches. At 14.5 dpc, expressed in olfactory
CC epithelium and cranial sensory ganglia. Also expressed in salivary
CC glands, lungs, gut, kidney, teeth and vibrissae.
CC {ECO:0000269|PubMed:10878606}.
CC -!- DOMAIN: The C-terminal region mediates interaction with the mRNA and
CC polysomes. It is required for translational repression of mRNAs with a
CC 5'TOP motif. {ECO:0000250|UniProtKB:Q6PKG0}.
CC -!- DOMAIN: The N-terminal region mediates interaction with PABPC1.
CC {ECO:0000250|UniProtKB:Q6PKG0}.
CC -!- PTM: Phosphorylated on multiple Ser and Thr residues in response to
CC active mTORC1. Phosphorylation is important for interaction with RPTOR
CC and the mTORC1 complex. Phosphorylation promotes dissociation from the
CC 5'UTR of mRNA molecules with a 5'TOP motif.
CC {ECO:0000250|UniProtKB:Q6PKG0}.
CC -!- SIMILARITY: Belongs to the LARP family. {ECO:0000305}.
CC -!- CAUTION: Conflicting results are reported regarding the interaction
CC with PABPC1. Some studies found that the interaction depends on the
CC presence of mRNA; others found that the interaction is direct and does
CC not depend on the presence of mRNA. {ECO:0000250|UniProtKB:Q6PKG0}.
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DR EMBL; AL672182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053449; AAH53449.1; -; mRNA.
DR EMBL; AK129202; BAC98012.1; -; mRNA.
DR CCDS; CCDS56771.1; -. [Q6ZQ58-1]
DR RefSeq; NP_082727.1; NM_028451.1. [Q6ZQ58-1]
DR AlphaFoldDB; Q6ZQ58; -.
DR SMR; Q6ZQ58; -.
DR BioGRID; 215803; 32.
DR IntAct; Q6ZQ58; 4.
DR MINT; Q6ZQ58; -.
DR STRING; 10090.ENSMUSP00000136673; -.
DR iPTMnet; Q6ZQ58; -.
DR PhosphoSitePlus; Q6ZQ58; -.
DR SwissPalm; Q6ZQ58; -.
DR EPD; Q6ZQ58; -.
DR jPOST; Q6ZQ58; -.
DR MaxQB; Q6ZQ58; -.
DR PaxDb; Q6ZQ58; -.
DR PeptideAtlas; Q6ZQ58; -.
DR PRIDE; Q6ZQ58; -.
DR ProteomicsDB; 264836; -. [Q6ZQ58-1]
DR ProteomicsDB; 264837; -. [Q6ZQ58-2]
DR Antibodypedia; 28316; 146 antibodies from 27 providers.
DR Ensembl; ENSMUST00000178636; ENSMUSP00000136673; ENSMUSG00000037331. [Q6ZQ58-1]
DR GeneID; 73158; -.
DR KEGG; mmu:73158; -.
DR UCSC; uc007jah.2; mouse. [Q6ZQ58-1]
DR CTD; 23367; -.
DR MGI; MGI:1890165; Larp1.
DR VEuPathDB; HostDB:ENSMUSG00000037331; -.
DR eggNOG; KOG2590; Eukaryota.
DR GeneTree; ENSGT00940000159577; -.
DR InParanoid; Q6ZQ58; -.
DR OMA; GGHFDYQ; -.
DR OrthoDB; 258488at2759; -.
DR TreeFam; TF314516; -.
DR BioGRID-ORCS; 73158; 8 hits in 71 CRISPR screens.
DR ChiTaRS; Larp1; mouse.
DR PRO; PR:Q6ZQ58; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6ZQ58; protein.
DR Bgee; ENSMUSG00000037331; Expressed in primitive streak and 280 other tissues.
DR ExpressionAtlas; Q6ZQ58; baseline and differential.
DR Genevisible; Q6ZQ58; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:0031931; C:TORC1 complex; ISO:MGI.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000339; F:RNA cap binding; ISS:UniProtKB.
DR GO; GO:0008494; F:translation activator activity; ISS:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0072752; P:cellular response to rapamycin; ISS:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISO:MGI.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:MGI.
DR GO; GO:1990928; P:response to amino acid starvation; ISS:UniProtKB.
DR GO; GO:0031929; P:TOR signaling; ISS:UniProtKB.
DR GO; GO:0038202; P:TORC1 signaling; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006607; DM15.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR Pfam; PF05383; La; 1.
DR SMART; SM00684; DM15; 3.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond; Methylation;
KW Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT CHAIN 2..1072
FT /note="La-related protein 1"
FT /id="PRO_0000207610"
FT DOMAIN 372..462
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT REGION 1..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..550
FT /note="Required for interaction with PABPC1"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT REGION 289..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..1072
FT /note="Required for interaction with RPTOR and for
FT repression of mRNAs with a 5'TOP motif"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT REGION 737..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..1000
FT /note="Interaction with mRNA"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT REGION 933..976
FT /note="Interaction with 7-methylguanosine mRNA cap
FT structure"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT REGION 1003..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 503
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 626
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 701
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 746
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 747
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 754
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 759
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 762
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 765
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 774
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 822
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 842
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 869
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 994
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT CROSSLNK 508
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT CROSSLNK 680
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT VAR_SEQ 1..1006
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015116"
SQ SEQUENCE 1072 AA; 121125 MW; BAFCE019DF683870 CRC64;
MATQVEPLLP AGAPLLQAEE HGLARKKPAP DAQAESGPGD GGGEPDGGVR RPRPACARPG
RDGAERESPR PPAAAEAPAG SDGEDGGRRD FVEAPPPKVN PWTKHAPPPA AVNGQPPPEP
SAPAKVVRAA APKPRKGSKV GDFGDAVNWP TPGEIAHKSV QPQSHKPQPA RKLPPKKDMK
EQEKGDGSDS KESPKTKSDE SGEEKNGDED CQRGGQKKKG SKHKWVPLQI DMKPEVPREK
LASRPTRPQE PRHTPAVRGE MKGSEPATYM PVSVAPPTPA WQPETKVEPA WHDQDETSSV
KSDGAGGARA SFRGRGRGRG RGRGRGRGGT RTHFDYQFGY RKFDGTEGPR THKYMNNITY
YFDNVSSNEI YSMDQELLKD YIKRQIEYYF SVDNLERDFF LRRKMDADGF LPITLIASFH
RVQALTTDIS LIFAALKDSK VVEMVEEKVR RREEPEKWPL PGPPIVDYSQ TDFSQLLNCP
EFVPRQHYQK ETESAPGSPR AVTPVPTKTE EVSNLKTLPK GLSASLPDLD SESWIEVKKR
PRPSPARPKK PEEPRFSHPT ALPQQLPSQQ LMSKDQDEQE ELDFLFDEEM EQMDGRKNTF
TAWSEEDSDY EIDDRDVNKI LIVTQTPPYM RRHPGGDRTG NHTSRAKMSA ELAKVINDGL
FYYEQDLWTE KFEPEYSQIK QEVENFKKVN MISREQFDTL TPEPPVDPNQ EVPPGPPRFQ
QVPTDALANK LFGAPEPSTI ARSLPTTVPE SPNYRNARTP RTPRTPQLKD SSQTPRFYPV
VKEGRTLDAK MPRKRKTRHS SNPPLESHVG WVMDSREHRP RTASISSSPS EGTPAVGSYG
CTPQSLPKFQ HPSHELLKEN GFTQHVYHKY RRRCLNERKR LGIGQSQEMN TLFRFWSFFL
RDHFNKKMYE EFKQLALEDA KEGYRYGLEC LFRYYSYGLE KKFRLDIFKD FQEETVKDYE
AGQLYGLEKF WAFLKYSKAK NLDIDPKLQE YLGKFRRLED FRVDPPMGEE GNHKRHPVVA
GGSGEGRKRC PSQSSSRPAT GISQPPTTPT GQATREDAKW TSQHSDTLTL RK
