ID ADNP_MOUSE Reviewed; 1108 AA. AC Q9Z103; A2BDX0; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2015, sequence version 2. DT 24-JAN-2024, entry version 178. DE RecName: Full=Activity-dependent neuroprotector homeobox protein; DE AltName: Full=Activity-dependent neuroprotective protein; GN Name=Adnp; 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 [MRNA] OF 281-1108, AND SYNTHESIS OF 354-361. RC TISSUE=Brain; RX PubMed=10037502; DOI=10.1046/j.1471-4159.1999.0721283.x; RA Bassan M., Zamostiano R., Davidson A., Pinhasov A., Giladi E., Perl O., RA Bassan H., Blat C., Gibney G., Glazner G., Brenneman D.E., Gozes I.; RT "Complete sequence of a novel protein containing a femtomolar-activity- RT dependent neuroprotective peptide."; RL J. Neurochem. 72:1283-1293(1999). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-959, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-708; SER-737; SER-888; RP SER-904; SER-959 AND SER-1077, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Lung, 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 [5] RP FUNCTION. RX PubMed=23071114; DOI=10.1074/jbc.m112.387027; RA Dresner E., Malishkevich A., Arviv C., Leibman Barak S., Alon S., Ofir R., RA Gothilf Y., Gozes I.; RT "Novel evolutionary-conserved role for the activity-dependent RT neuroprotective protein (ADNP) family that is important for RT erythropoiesis."; RL J. Biol. Chem. 287:40173-40185(2012). RN [6] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-348, AND IDENTIFICATION BY MASS RP 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 [7] RP FUNCTION. RX PubMed=32533114; DOI=10.1038/s41467-020-16799-0; RA Sun X., Peng X., Cao Y., Zhou Y., Sun Y.; RT "ADNP promotes neural differentiation by modulating Wnt/beta-catenin RT signaling."; RL Nat. Commun. 11:2984-2984(2020). CC -!- FUNCTION: May be involved in transcriptional regulation CC (PubMed:23071114, PubMed:32533114). May mediate some of the CC neuroprotective peptide VIP-associated effects involving normal growth CC and cancer proliferation. Positively modulates WNT-beta-catenin/CTNN1B CC signaling, acting by regulating phosphorylation of, and thereby CC stabilizing, CTNNB1 (PubMed:32533114). May be required for neural CC induction and neuronal differentiation (PubMed:32533114). May be CC involved in erythroid differentiation (PubMed:23071114). CC {ECO:0000269|PubMed:23071114, ECO:0000269|PubMed:32533114}. CC -!- SUBUNIT: Interacts (via N-terminal region) with beta-catenin/CTNNB1 CC (via the central armadillo domains); interaction is direct and CC stabilizes CTNNB1 by modulating its phosphorylation by glycogen CC synthase kinase-3 beta GSK3B. {ECO:0000269|PubMed:32533114}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. CC Chromosome {ECO:0000305|PubMed:23071114}. CC -!- TISSUE SPECIFICITY: Expressed in the brain, with a higher expression in CC cerebellum and hippocampus. Weakly expressed in lung, kidney and CC intestine, and expressed at intermediate level in testis. CC -!- INDUCTION: By the neuroprotective peptide VIP. CC -!- MISCELLANEOUS: When isolated from the sequence, the neuroprotective CC peptide provides neuroprotection at subfemtomolar concentrations CC against toxicity associated with tetrodoxin (electrical blockade), the CC amyloid-beta peptide (the Alzheimer disease neurotoxin), N-methyl- CC aspartate (excitotoxicity), and the human immunideficiency virus (HIV) CC envelope protein. 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; BX005039; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF068198; AAD19843.1; -; mRNA. DR CCDS; CCDS38342.1; -. DR RefSeq; NP_001297015.1; NM_001310086.1. DR RefSeq; NP_033758.2; NM_009628.3. DR AlphaFoldDB; Q9Z103; -. DR IntAct; Q9Z103; 3. DR MINT; Q9Z103; -. DR STRING; 10090.ENSMUSP00000085316; -. DR GlyGen; Q9Z103; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Z103; -. DR PhosphoSitePlus; Q9Z103; -. DR EPD; Q9Z103; -. DR jPOST; Q9Z103; -. DR MaxQB; Q9Z103; -. DR PaxDb; 10090-ENSMUSP00000085316; -. DR PeptideAtlas; Q9Z103; -. DR ProteomicsDB; 285555; -. DR Pumba; Q9Z103; -. DR Antibodypedia; 1423; 396 antibodies from 34 providers. DR DNASU; 11538; -. DR Ensembl; ENSMUST00000057793.11; ENSMUSP00000056809.5; ENSMUSG00000051149.16. DR Ensembl; ENSMUST00000088001.6; ENSMUSP00000085316.6; ENSMUSG00000051149.16. DR GeneID; 11538; -. DR KEGG; mmu:11538; -. DR UCSC; uc008oaq.1; mouse. DR AGR; MGI:1338758; -. DR CTD; 23394; -. DR MGI; MGI:1338758; Adnp. DR VEuPathDB; HostDB:ENSMUSG00000051149; -. DR eggNOG; ENOG502QSYX; Eukaryota. DR GeneTree; ENSGT00530000063631; -. DR InParanoid; Q9Z103; -. DR OMA; PYCTFNG; -. DR OrthoDB; 4079234at2759; -. DR PhylomeDB; Q9Z103; -. DR TreeFam; TF328818; -. DR BioGRID-ORCS; 11538; 9 hits in 82 CRISPR screens. DR PRO; PR:Q9Z103; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q9Z103; Protein. DR Bgee; ENSMUSG00000051149; Expressed in embryonic post-anal tail and 85 other cell types or tissues. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0005615; C:extracellular space; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI. DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB. DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0005507; F:copper ion binding; ISO:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:ARUK-UCL. DR GO; GO:0042277; F:peptide binding; ISO:MGI. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:ARUK-UCL. DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl. DR GO; GO:0019934; P:cGMP-mediated signaling; ISO:MGI. DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl. DR GO; GO:0033484; P:intracellular nitric oxide homeostasis; ISO:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB. DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:MGI. DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI. DR GO; GO:0030182; P:neuron differentiation; IMP:UniProtKB. DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI. DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:MGI. DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ARUK-UCL. DR GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl. DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl. DR GO; GO:0007614; P:short-term memory; ISO:MGI. DR CDD; cd00086; homeodomain; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR038861; ADNP/ADNP2. DR InterPro; IPR045762; ADNP_Znf. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR001356; Homeobox_dom. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR15740:SF1; ACTIVITY-DEPENDENT NEUROPROTECTOR HOMEOBOX PROTEIN; 1. DR PANTHER; PTHR15740; NEUROPROTECTIVE PEPTIDE-CONTAINING PROTEIN; 1. DR Pfam; PF19627; ADNP_N; 1. DR Pfam; PF00046; Homeodomain; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00355; ZnF_C2H2; 8. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 1: Evidence at protein level; KW Acetylation; Chromosome; DNA-binding; Homeobox; Isopeptide bond; KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..1108 FT /note="Activity-dependent neuroprotector homeobox protein" FT /id="PRO_0000048808" FT ZN_FING 74..97 FT /note="C2H2-type 1; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 107..129 FT /note="C2H2-type 2; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 165..188 FT /note="C2H2-type 3; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 221..244 FT /note="C2H2-type 4; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 446..468 FT /note="C2H2-type 5; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 488..509 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 511..534 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 621..646 FT /note="C2H2-type 8; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 661..685 FT /note="C2H2-type 9; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT DNA_BIND 753..813 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..685 FT /note="Binds to beta-catenin/CTNNB1" FT /evidence="ECO:0000269|PubMed:32533114" FT REGION 133..154 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 354..361 FT /note="Neuroprotective peptide; contributes to CTNNB1- FT binding, but less effective than whole N-terminal region" FT /evidence="ECO:0000269|PubMed:10037502, FT ECO:0000269|PubMed:32533114" FT REGION 360..438 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 690..711 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 851..1037 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1050..1108 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 391..427 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 692..707 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 851..883 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 940..962 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 978..992 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1009..1029 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1050..1080 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 98 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT MOD_RES 348 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 408 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT MOD_RES 412 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT MOD_RES 607 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT MOD_RES 708 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 737 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 804 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT MOD_RES 875 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT MOD_RES 877 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT MOD_RES 885 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JKL8" FT MOD_RES 888 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 904 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 959 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 961 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT MOD_RES 1041 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT MOD_RES 1048 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT MOD_RES 1077 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CROSSLNK 39 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 72 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 144 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 155 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 203 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 231 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 266 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 274 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 278 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 279 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 311 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 335 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 367 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 407 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 426 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 599 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 605 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 615 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 620 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 631 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 657 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 698 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 715 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 727 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 730 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 744 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 806 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 828 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 834 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 913 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 928 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 941 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 1022 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 1041 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" FT CROSSLNK 1048 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q9H2P0" SQ SEQUENCE 1108 AA; 124308 MW; C69498C5DFC9150B CRC64; MFQLPVNNLG SLRKARKTVK KILSDIGLEY CKEHIEDFKQ FEPNDFYLKN TTWEDVGLWD PSLTKNQDYR TKPFCCSACP FSSKFFSAYK SHFRNVHSED FENRILLNCP YCTFNADKKT LETHIKIFHA PNSSAPSSSL STFKDKNKND GLKPKQADNV EQAVYYCKKC TYRDPLYEIV RKHIYREHFQ HVAAPYIAKA GEKSLNGAVS LGTNAREECN IHCKRCLFMP KSYEALVQHV IEDHERIGYQ VTAMIGHTNV VVPRAKPLML IAPKPQDKKG MGLPPRISSL ASGNVRSLPS QQMVNRLSIP KPNLNSTGVN MMSNVHLQQN NYGVKSVGQS YGVGQSVRLG LGGNAPVSIP QQSQSVKQLL PSGNGRSFGL GAEQRPPAAA RYSLQTANTS LPPGQVKSPS VSQSQASRVL GQSSSKPPPA ATGPPPSNHC ATQKWKICTI CNELFPENVY SVHFEKEHKA EKVPAVANYI MKIHNFTSKC LYCNRYLPTD TLLNHMLIHG LSCPYCRSTF NDVEKMAAHM RMVHIDEEMG PKTDSTLSFD LTLQQGSHTN IHLLVTTYNL RDAPAESVAY HAQNNAPVPP KPQPKVQEKA DVPVKSSPQA AVPYKKDVGK TLCPLCFSIL KGPISDALAH HLRERHQVIQ TVHPVEKKLT YKCIHCLGVY TSNMTASTIT LHLVHCRGVG KTQNGQDKTN APSRLNQSPG LAPVKRTYEQ MEFPLLKKRK LEEDADSPSC FEEKPEEPVV LALDPKGHED DSYEARKSFL TKYFNKQPYP TRREIEKLAA SLWLWKSDIA SHFSNKRKKC VRDCEKYKPG VLLGFNMKEL NKVKHEMDFD AEWLFENHDE KDSRVNASKT VDKKHNLGKE DDSFSDSFEH LEEESNGSGS PFDPVFEVEP KIPSDNLEEP VPKVIPEGAL ESEKLDQKEE EEEEEEEDGS KYETIHLTEE PAKLMHDASD SEVDQDDVVE WKDGASPSES GPGSQQISDF EDNTCEMKPG TWSDESSQSE DARSSKPAAK KKATVQDDTE QLKWKNSSYG KVEGFWSKDQ SQWENASENA ERLPNPQIEW QNSTIDSEDG EQFDSMTDGV ADPMHGSLTG VKLSSQQA //