GGYF2_MOUSE
ID GGYF2_MOUSE Reviewed; 1291 AA.
AC Q6Y7W8; Q0VGQ7; Q3UNS2; Q63ZU9; Q80TV1; Q8K0R0; Q8R0A3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=GRB10-interacting GYF protein 2 {ECO:0000303|PubMed:12771153};
DE AltName: Full=PERQ amino acid-rich with GYF domain-containing protein 2;
DE AltName: Full=Trinucleotide repeat-containing gene 15 protein;
GN Name=Gigyf2 {ECO:0000303|PubMed:12771153};
GN Synonyms=Kiaa0642, Perq2, Tnrc15;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION
RP WITH GRB10, AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=12771153; DOI=10.1074/jbc.m211572200;
RA Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A., Smith R.J.;
RT "Two novel proteins that are linked to insulin-like growth factor (IGF-I)
RT receptors by the Grb10 adapter and modulate IGF-I signaling.";
RL J. Biol. Chem. 278:31564-31573(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Eye, and Mammary gland;
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 1-878 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 244-1291 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=19744960; DOI=10.1093/hmg/ddp430;
RA Giovannone B., Tsiaras W.G., de la Monte S., Klysik J., Lautier C.,
RA Karashchuk G., Goldwurm S., Smith R.J.;
RT "GIGYF2 gene disruption in mice results in neurodegeneration and altered
RT insulin-like growth factor signaling.";
RL Hum. Mol. Genet. 18:4629-4639(2009).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-30 AND THR-383, AND
RP IDENTIFICATION BY MASS 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 [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-107; ARG-119; ARG-121 AND
RP ARG-150, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
RN [9]
RP FUNCTION, AND INTERACTION WITH ZFP36.
RX PubMed=26763119; DOI=10.1261/rna.054833.115;
RA Fu R., Olsen M.T., Webb K., Bennett E.J., Lykke-Andersen J.;
RT "Recruitment of the 4EHP-GYF2 cap-binding complex to tetraproline motifs of
RT tristetraprolin promotes repression and degradation of mRNAs with AU-rich
RT elements.";
RL RNA 22:373-382(2016).
CC -!- FUNCTION: Key component of the 4EHP-GYF2 complex, a multiprotein
CC complex that acts as a repressor of translation initiation
CC (PubMed:26763119). In the 4EHP-GYF2 complex, acts as a factor that
CC bridges EIF4E2 to ZFP36/TTP, linking translation repression with mRNA
CC decay (PubMed:26763119). Also recruits and bridges the association of
CC the 4EHP complex with the decapping effector protein DDX6, which is
CC required for the ZFP36/TTP-mediated down-regulation of AU-rich mRNA (By
CC similarity). May act cooperatively with GRB10 to regulate tyrosine
CC kinase receptor signaling, including IGF1 and insulin receptors
CC (PubMed:12771153). {ECO:0000250|UniProtKB:Q6Y7W6,
CC ECO:0000269|PubMed:12771153, ECO:0000269|PubMed:26763119}.
CC -!- SUBUNIT: Component of the 4EHP-GYF2 complex, at least composed of
CC EIF4E2, GIGYF2 and ZNF598 (PubMed:26763119). Interacts (via the 4EHP-
CC binding motif) with EIF4E2; the interaction is direct (By similarity).
CC Interacts with ZFP36/TTP (via P-P-P-P-G repeats); the interaction is
CC direct (PubMed:26763119). Interacts with GRB10 (PubMed:12771153).
CC Interacts (via DDX6 motif) with DDX6 (via RecA-like domain 2) (By
CC similarity). {ECO:0000250|UniProtKB:Q6Y7W6,
CC ECO:0000269|PubMed:12771153, ECO:0000269|PubMed:26763119}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6Y7W8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6Y7W8-2; Sequence=VSP_022247;
CC -!- TISSUE SPECIFICITY: Expressed in heart, liver, kidney and brain as well
CC as in testis (PubMed:12771153). {ECO:0000269|PubMed:12771153}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in embryonic tissues, including
CC strong expression in the central nervous system.
CC {ECO:0000269|PubMed:19744960}.
CC -!- DISRUPTION PHENOTYPE: Mice undergo normal embryonic development, but
CC fail to feed and die within the first 2 postnatal days. Heterozygous
CC mice survive to adulthood with no evident metabolic or growth defects.
CC At 12-15 months of age, heterozygous mice show motor dysfunction
CC associated with histopathologic evidence of neurodegeneration and rare
CC intracytoplasmic Lewy body-like inclusions in spinal anterior horn
CC motor neurons. {ECO:0000269|PubMed:19744960}.
CC -!- SIMILARITY: Belongs to the GIGYF family. {ECO:0000305}.
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DR EMBL; AY176043; AAO46887.1; -; mRNA.
DR EMBL; BC027137; AAH27137.1; -; mRNA.
DR EMBL; BC030845; AAH30845.1; -; mRNA.
DR EMBL; BC082811; AAH82811.1; -; mRNA.
DR EMBL; BC089036; AAH89036.1; -; mRNA.
DR EMBL; AK144058; BAE25675.1; -; mRNA.
DR EMBL; AK122337; BAC65619.1; -; mRNA.
DR CCDS; CCDS15133.1; -. [Q6Y7W8-1]
DR RefSeq; NP_001103682.1; NM_001110212.2.
DR RefSeq; NP_666224.3; NM_146112.4. [Q6Y7W8-1]
DR RefSeq; XP_006529527.1; XM_006529464.2. [Q6Y7W8-1]
DR RefSeq; XP_006529528.1; XM_006529465.3. [Q6Y7W8-1]
DR AlphaFoldDB; Q6Y7W8; -.
DR SMR; Q6Y7W8; -.
DR BioGRID; 230615; 18.
DR IntAct; Q6Y7W8; 3.
DR MINT; Q6Y7W8; -.
DR STRING; 10090.ENSMUSP00000027475; -.
DR iPTMnet; Q6Y7W8; -.
DR PhosphoSitePlus; Q6Y7W8; -.
DR EPD; Q6Y7W8; -.
DR jPOST; Q6Y7W8; -.
DR MaxQB; Q6Y7W8; -.
DR PaxDb; Q6Y7W8; -.
DR PeptideAtlas; Q6Y7W8; -.
DR PRIDE; Q6Y7W8; -.
DR ProteomicsDB; 267443; -. [Q6Y7W8-1]
DR ProteomicsDB; 267444; -. [Q6Y7W8-2]
DR Antibodypedia; 62944; 90 antibodies from 25 providers.
DR DNASU; 227331; -.
DR Ensembl; ENSMUST00000027475; ENSMUSP00000027475; ENSMUSG00000048000. [Q6Y7W8-1]
DR Ensembl; ENSMUST00000174501; ENSMUSP00000133327; ENSMUSG00000048000. [Q6Y7W8-1]
DR GeneID; 227331; -.
DR KEGG; mmu:227331; -.
DR UCSC; uc007bwt.2; mouse. [Q6Y7W8-1]
DR CTD; 26058; -.
DR MGI; MGI:2138584; Gigyf2.
DR VEuPathDB; HostDB:ENSMUSG00000048000; -.
DR eggNOG; KOG1862; Eukaryota.
DR GeneTree; ENSGT00940000156108; -.
DR HOGENOM; CLU_007300_0_0_1; -.
DR InParanoid; Q6Y7W8; -.
DR OMA; AIEMTEW; -.
DR OrthoDB; 412069at2759; -.
DR PhylomeDB; Q6Y7W8; -.
DR TreeFam; TF325513; -.
DR BioGRID-ORCS; 227331; 13 hits in 75 CRISPR screens.
DR ChiTaRS; Gigyf2; mouse.
DR PRO; PR:Q6Y7W8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6Y7W8; protein.
DR Bgee; ENSMUSG00000048000; Expressed in animal zygote and 246 other tissues.
DR ExpressionAtlas; Q6Y7W8; baseline and differential.
DR Genevisible; Q6Y7W8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990635; C:proximal dendrite; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031982; C:vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070064; F:proline-rich region binding; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0007631; P:feeding behavior; IMP:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:MGI.
DR GO; GO:0061157; P:mRNA destabilization; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0050881; P:musculoskeletal movement; IMP:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0016441; P:post-transcriptional gene silencing; ISO:MGI.
DR GO; GO:0019538; P:protein metabolic process; IMP:MGI.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Methylation;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT CHAIN 2..1291
FT /note="GRB10-interacting GYF protein 2"
FT /id="PRO_0000270838"
FT DOMAIN 534..582
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 112..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..564
FT /note="Required for GRB10-binding"
FT /evidence="ECO:0000269|PubMed:12771153"
FT REGION 732..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 281..311
FT /note="DDX6 binding motif"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT COMPBIAS 148..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 107
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 119
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 121
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT MOD_RES 150
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT MOD_RES 383
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT MOD_RES 1276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT CROSSLNK 1129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W6"
FT VAR_SEQ 1..868
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022247"
FT CONFLICT 13
FT /note="E -> G (in Ref. 3; BAE25675)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="P -> S (in Ref. 4; BAC65619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1291 AA; 149193 MW; D05938427E72580A CRC64;
MAAETQTLNF GPEWLRALSS GGSITSPPLS PALPKYKLAD YRYGREEMLA LFLKDYKIPF
DLLEKEFLPI LQEEPLPPLA LVPFTEEEQR NFSMSVNSAA VLRLTGRGGG GGTVVGAPRG
RSSSRGRGRG RGECGFYQRS FDEVEGVFGR GGGREMHRSQ SWEERGDRRF EKPGRKDVGR
PNFEESGPTS VGRKHEFIRS ESENWRIFRE EQNGEDEDGG WRLAGSRRDG ERWRPHSPDG
PRSTGWREHM ERRRRFEFDF RDRDDERGYR RVRSGSGSID DDRDSLPEWC LEDAEEEMGT
FDSSGAFLSL KKVQKEPIPE EQEMDFRPVE EGEERSDSDS SHNEEAKEPD KTNRREGEKT
DRAGAEASEE VPQTSLSSAR PGTPSDHQPQ EATQFERKDE PKAEQVEKAE EENRSENSLS
AKVPSRGDET VPASQQPSTP LPPDTASPLL ILSPPVPTPS SASRPVETAA VEAPGMSSVS
TEPDDEEGLK HLEQQAEKMV AYLQDSALDD ERLTSKLQEH RAKGVSIPLM HEAMQKWYYK
DPQGEIQGPF NNQEMAEWFQ AGYFTMSLLV KRACDESFQP LGDIMKMWGR VPFSPGPAPP
PHMGELDQER LTRQQELTAL YQMQHLQYQQ FLIQQQYAQV LAQQQKAALS SQQQQQLALL
LQQFQALKMR MSDQNIIPSV TRSVSVPDTG SIWELQPAAS QPAVWEGGSV WDLPLDTTAP
GPSLEQLQQL EKAKAAKLEQ ERREAEMRAK REEEERKRQE ELRRQQEEIL RRQQEEERKR
REEEELARRK QEEALRRQRE QEIALRRQRE EEERQQQEEA LRRLEERRRE EEERRKQEEL
LRKQEEEAAK WAREEEEAQR RLEENRLRME EEAARLRHEE EERKRKELEL QRQKDLMRQR
QQQQEALRRL QQQQQQQQLA QMKLPSSSTW GQQSNTATCQ SQATLSLAEI QKLEEERERQ
LREEQRRQQR ELMKALQQQQ QQQQQQKLSG WGNVSKPAGT TKSLLEIQQE EARQMQKQQQ
QQQQQQQQHQ QSNRARNSTH SNLHTSLGNS VWGSINTGPS NQWASELVSS IWSNADTKNS
NMGFWDDAVK EVGPRNSTNK NKNNASLSKS VGVSNRQNKK VEEEEKLLKL FQGVNKAQDG
FTQWCEQMLH ALNTANNLDV PTFVSFLKEV ESPYEVHDYT RAYLGDTSEA KEFAKQFLER
RAKQKVNQQR QQQQQQQQQQ DSVWGMNHST LHSVFQTNQS NNQQSNFEAV QSGKKKKKQK
MVRADPSLLG FSVNASSERL NMGEIETLDD Y
