FOXK2_MOUSE
ID FOXK2_MOUSE Reviewed; 651 AA.
AC Q3UCQ1; A2AN27; B5AZX0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Forkhead box protein K2 {ECO:0000305};
DE AltName: Full=Cellular transcription factor ILF-1 {ECO:0000303|PubMed:16376864};
DE AltName: Full=Interleukin enhancer-binding factor 1 {ECO:0000303|PubMed:16376864};
GN Name=Foxk2 {ECO:0000303|Ref.1, ECO:0000312|MGI:MGI:1916087};
GN Synonyms=Ilf1 {ECO:0000303|PubMed:16376864};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Midbrain;
RA Wijchers P.J.E.C., van der Heidee L.P., van den Akker W.M.R., Adolfs Y.,
RA Durston A.J., Hoekman M.F.M., Burbach J.P.H., Smidt M.P.;
RT "Foxk2 is the mammalian homolog of yeast Fkh2, but is functionally
RT distinct.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3] {ECO:0000312|EMBL:BAE29561.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-651 (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE29561.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE29561.1};
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16376864; DOI=10.1016/j.brainres.2005.11.022;
RA Wijchers P.J.E.C., Hoekman M.F.M., Burbach J.P.H., Smidt M.P.;
RT "Identification of forkhead transcription factors in cortical and
RT dopaminergic areas of the adult murine brain.";
RL Brain Res. 1068:23-33(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364; SER-389; SER-415;
RP SER-419 AND SER-590, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, and Spleen;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SIN3A.
RX PubMed=25402684; DOI=10.1038/ncb3062;
RA Bowman C.J., Ayer D.E., Dynlacht B.D.;
RT "Foxk proteins repress the initiation of starvation-induced atrophy and
RT autophagy programs.";
RL Nat. Cell Biol. 16:1202-1214(2014).
RN [8]
RP FUNCTION.
RX PubMed=29861159; DOI=10.1016/j.molcel.2018.04.024;
RA He L., Gomes A.P., Wang X., Yoon S.O., Lee G., Nagiec M.J., Cho S.,
RA Chavez A., Islam T., Yu Y., Asara J.M., Kim B.Y., Blenis J.;
RT "mTORC1 promotes metabolic reprogramming by the suppression of GSK3-
RT dependent foxk1 phosphorylation.";
RL Mol. Cell 70:949-960(2018).
RN [9]
RP FUNCTION.
RX PubMed=30700909; DOI=10.1038/s41586-019-0900-5;
RA Sukonina V., Ma H., Zhang W., Bartesaghi S., Subhash S., Heglind M.,
RA Foyn H., Betz M.J., Nilsson D., Lidell M.E., Naumann J., Haufs-Brusberg S.,
RA Palmgren H., Mondal T., Beg M., Jedrychowski M.P., Tasken K., Pfeifer A.,
RA Peng X.R., Kanduri C., Enerbaeck S.;
RT "FOXK1 and FOXK2 regulate aerobic glycolysis.";
RL Nature 566:279-283(2019).
CC -!- FUNCTION: Transcriptional regulator involved in different processes
CC such as glucose metabolism, aerobic glycolysis and autophagy
CC (PubMed:25402684, PubMed:29861159, PubMed:30700909). Recognizes and
CC binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act
CC as a transcription activator or repressor, depending on the context
CC (PubMed:25402684, PubMed:29861159, PubMed:30700909). Together with
CC FOXK1, acts as a key regulator of metabolic reprogramming towards
CC aerobic glycolysis, a process in which glucose is converted to lactate
CC in the presence of oxygen (PubMed:30700909). Acts by promoting
CC expression of enzymes for glycolysis (such as hexokinase-2 (HK2),
CC phosphofructokinase, pyruvate kinase (PKLR) and lactate dehydrogenase),
CC while suppressing further oxidation of pyruvate in the mitochondria by
CC up-regulating pyruvate dehydrogenase kinases PDK1 and PDK4
CC (PubMed:30700909). Probably plays a role in gluconeogenesis during
CC overnight fasting, when lactate from white adipose tissue and muscle is
CC the main substrate (PubMed:30700909). Together with FOXK1, acts as a
CC negative regulator of autophagy in skeletal muscle: in response to
CC starvation, enters the nucleus, binds the promoters of autophagy genes
CC and represses their expression, preventing proteolysis of skeletal
CC muscle proteins (PubMed:25402684). In addition to the 5'-GTAAACA-3' DNA
CC motif, also binds the 5'-TGANTCA-3' palindromic DNA motif, and co-
CC associates with JUN/AP-1 to activate transcription (By similarity).
CC Also able to bind to a minimal DNA heteroduplex containing a G/T-
CC mismatch with 5'-TRT[G/T]NB-3' sequence (By similarity). Binds to NFAT-
CC like motifs (purine-rich) in the IL2 promoter (By similarity).
CC Positively regulates WNT/beta-catenin signaling by translocating DVL
CC proteins into the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:Q01167, ECO:0000269|PubMed:25402684,
CC ECO:0000269|PubMed:29861159, ECO:0000269|PubMed:30700909}.
CC -!- SUBUNIT: Component of SIN3A-, but not SIN3B-, containing multiprotein
CC complexes (PubMed:25402684). Interacts with DVL1, DVL2 (when
CC phosphorylated) and DVL3; the interaction induces DVL2 nuclear
CC translocation (By similarity). Interacts with SUDS3 (By similarity).
CC Interacts with BAP1 (when phosphorylated); leading to recruit the PR-
CC DUB complex and repress FOXK2 target genes (By similarity).
CC {ECO:0000250|UniProtKB:Q01167, ECO:0000269|PubMed:25402684}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089,
CC ECO:0000269|PubMed:16376864, ECO:0000269|PubMed:25402684}. Cytoplasm
CC {ECO:0000269|PubMed:25402684}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UCQ1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3UCQ1-2; Sequence=VSP_052236;
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of adult brain regions,
CC namely the piriform cortex, the major islands of Calleja and cells
CC lining the lateral ventricles, the bed nucleus of stria terminalis, the
CC paraventricular thalamic nucleus, habenula and all structures of the
CC hippocampus. Also present in the hypothalamus, cerebral cortex and in
CC the Purkinje cell layer in the cerebellum. Additionally expressed in
CC dopamine neurons of the substantia and more sparsely in the ventral
CC tegmental area. {ECO:0000269|PubMed:16376864}.
CC -!- DEVELOPMENTAL STAGE: At 12.5 dpc, expressed ubiquitously in the
CC developing central nervous system. This pattern persists at 14.5 dpc
CC and 16.5 dpc, with expression levels varying.
CC {ECO:0000269|PubMed:16376864}.
CC -!- DOMAIN: The C-terminal part of the DNA-binding domain may contribute to
CC DNA recognition specificity. {ECO:0000250|UniProtKB:Q01167}.
CC -!- PTM: Hyperphosphorylated during mitosis by CDK1 and, to a lower extent,
CC CDK2. Phosphorylation at Ser-364 and Ser-419 affects stability by
CC promoting degradation. {ECO:0000250|UniProtKB:Q01167}.
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DR EMBL; EU882160; ACG63496.1; -; mRNA.
DR EMBL; AL808021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK150439; BAE29561.1; -; mRNA.
DR CCDS; CCDS36393.2; -. [Q3UCQ1-1]
DR RefSeq; NP_001074401.2; NM_001080932.2. [Q3UCQ1-1]
DR RefSeq; XP_006534145.1; XM_006534082.1.
DR AlphaFoldDB; Q3UCQ1; -.
DR BMRB; Q3UCQ1; -.
DR SMR; Q3UCQ1; -.
DR BioGRID; 213075; 1.
DR STRING; 10090.ENSMUSP00000101719; -.
DR iPTMnet; Q3UCQ1; -.
DR PhosphoSitePlus; Q3UCQ1; -.
DR EPD; Q3UCQ1; -.
DR jPOST; Q3UCQ1; -.
DR MaxQB; Q3UCQ1; -.
DR PaxDb; Q3UCQ1; -.
DR PeptideAtlas; Q3UCQ1; -.
DR PRIDE; Q3UCQ1; -.
DR ProteomicsDB; 267498; -. [Q3UCQ1-1]
DR ProteomicsDB; 267499; -. [Q3UCQ1-2]
DR Antibodypedia; 33026; 241 antibodies from 30 providers.
DR DNASU; 68837; -.
DR Ensembl; ENSMUST00000106113; ENSMUSP00000101719; ENSMUSG00000039275. [Q3UCQ1-1]
DR GeneID; 68837; -.
DR KEGG; mmu:68837; -.
DR UCSC; uc007mvs.1; mouse. [Q3UCQ1-2]
DR UCSC; uc011yjl.1; mouse. [Q3UCQ1-1]
DR CTD; 3607; -.
DR MGI; MGI:1916087; Foxk2.
DR VEuPathDB; HostDB:ENSMUSG00000039275; -.
DR eggNOG; KOG2294; Eukaryota.
DR GeneTree; ENSGT00940000155709; -.
DR HOGENOM; CLU_022344_0_0_1; -.
DR InParanoid; Q3UCQ1; -.
DR OMA; LMTDNSQ; -.
DR OrthoDB; 1270467at2759; -.
DR PhylomeDB; Q3UCQ1; -.
DR TreeFam; TF325718; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR BioGRID-ORCS; 68837; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Foxk2; mouse.
DR PRO; PR:Q3UCQ1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3UCQ1; protein.
DR Bgee; ENSMUSG00000039275; Expressed in floor plate of midbrain and 266 other tissues.
DR Genevisible; Q3UCQ1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0061621; P:canonical glycolysis; IDA:UniProtKB.
DR GO; GO:0001678; P:cellular glucose homeostasis; IDA:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IDA:UniProtKB.
DR CDD; cd00059; FH; 1.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR018122; TF_fork_head_CS_1.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond;
KW Magnesium; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..651
FT /note="Forkhead box protein K2"
FT /id="PRO_0000261668"
FT DOMAIN 48..119
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DNA_BIND 249..344
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..162
FT /note="Required for interaction with DVL2 and SUDS3"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT REGION 150..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..309
FT /note="DNA-binding; major groove"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT REGION 319..323
FT /note="DNA-binding; minor groove"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT REGION 339..344
FT /note="DNA-binding; minor groove"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT REGION 350..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT MOD_RES 135
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT CROSSLNK 518
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01167"
FT VAR_SEQ 517..586
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052236"
FT CONFLICT 104
FT /note="L -> M (in Ref. 3; BAE29561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 651 AA; 68446 MW; DFD83C2A8EF52EF0 CRC64;
MAAAAALSGA GAPPAGGGAG GGGSPPGGWA VARLEGREFE YLMKKRSVTI GRNSSQGSVD
VSMGHSSFIS RRHLEIFTPP GGGHSAAAPE PAQPRPDAGG DFYLRCLGKN GVFVDGVFQR
RGAPPLQLPR VCTFRFPSTN IKITFTALSS EKREKQEAPE SPVKPVQPHI SPLTINIPDT
MAHLISPLPS PTGTISAANS CPSSPRGAGS SGYKVGRVMP SDLSLMADNS QPENEKEASG
GDSPKDDSKP PYSYAQLIVQ AITMAPDKQL TLNGIYTHIT KNYPYYRTAD KGWQNSIRHN
LSLNRYFIKV PRSQEEPGKG SFWRIDPASE SKLVEQAFRK RRPRGVPCFR TPLGPLSSRS
APASPNHAGV LSAHSSGAQT PESLSREGSP APLEPEPGAS QPKLAVIQEA RFAQSAPGSP
LSSQPVLITV QRQLPPAIKP VTYTVATPVT TPTSQPPVVQ TVHVVHQIPA VSVTSVAGLA
PANTYTVAGQ AVVTQAAVLA PPNPEPQENG DHREVRVKVE PVPAISPATL GAASRIIQTS
QGTPVQTVTI VQQAPLGQHQ LPIKTVTQNG AHVVPMPTAV HSQVNNAAAS PLHMLATHAS
ASASLPTKRQ NGDQAEQPEL KRVKAEDGES IVIALSVDAP PAAVREKAIQ N
