AKAP8_MOUSE
ID AKAP8_MOUSE Reviewed; 687 AA.
AC Q9DBR0; Q9R0L8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=A-kinase anchor protein 8;
DE Short=AKAP-8;
DE AltName: Full=A-kinase anchor protein 95 kDa;
DE Short=AKAP 95;
GN Name=Akap8; Synonyms=Akap95;
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].
RA Hattori A., Seki N., Hayashi A., Kozuma S., Muramatsu M., Miyajima N.,
RA Saito T.;
RT "Mouse AKAP95.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Thymus;
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 [3]
RP INTERACTION WITH MYCBP.
RX PubMed=12414807; DOI=10.1074/jbc.m206387200;
RA Furusawa M., Taira T., Iguchi-Ariga S.M., Ariga H.;
RT "AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus,
RT respectively, and inhibits cAMP-dependent protein kinase activity by
RT preventing binding of its catalytic subunit to A-kinase-anchoring protein
RT (AKAP) complex.";
RL J. Biol. Chem. 277:50885-50892(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12082153; DOI=10.1242/jcs.115.14.2931;
RA Bomar J., Moreira P., Balise J.J., Collas P.;
RT "Differential regulation of maternal and paternal chromosome condensation
RT in mitotic zygotes.";
RL J. Cell Sci. 115:2931-2940(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH CCND1.
RX PubMed=14641107; DOI=10.1042/bj20031765;
RA Arsenijevic T., Degraef C., Dumont J.E., Roger P.P., Pirson I.;
RT "A novel partner for D-type cyclins: protein kinase A-anchoring protein
RT AKAP95.";
RL Biochem. J. 378:673-679(2004).
RN [6]
RP INTERACTION WITH CASP3.
RX PubMed=16227597; DOI=10.1128/mcb.25.21.9469-9477.2005;
RA Kamada S., Kikkawa U., Tsujimoto Y., Hunter T.;
RT "A-kinase-anchoring protein 95 functions as a potential carrier for the
RT nuclear translocation of active caspase 3 through an enzyme-substrate-like
RT association.";
RL Mol. Cell. Biol. 25:9469-9477(2005).
RN [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH FIGN, AND DISRUPTION PHENOTYPE.
RX PubMed=16751186; DOI=10.1074/jbc.m603626200;
RA Yang Y., Mahaffey C.L., Berube N., Frankel W.N.;
RT "Interaction between fidgetin and protein kinase A-anchoring protein AKAP95
RT is critical for palatogenesis in the mouse.";
RL J. Biol. Chem. 281:22352-22359(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320 AND SER-325, 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 [9]
RP FUNCTION, INTERACTION WITH NFKB1, AND SUBCELLULAR LOCATION.
RX PubMed=19531803; DOI=10.1126/scisignal.2000202;
RA Wall E.A., Zavzavadjian J.R., Chang M.S., Randhawa B., Zhu X., Hsueh R.C.,
RA Liu J., Driver A., Bao X.R., Sternweis P.C., Simon M.I., Fraser I.D.;
RT "Suppression of LPS-induced TNF-alpha production in macrophages by cAMP is
RT mediated by PKA-AKAP95-p105.";
RL Sci. Signal. 2:RA28-RA28(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-320; SER-325 AND
RP SER-336, AND 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 [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-109; ARG-232 AND ARG-276, AND
RP 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).
CC -!- FUNCTION: Anchoring protein that mediates the subcellular
CC compartmentation of cAMP-dependent protein kinase (PKA type II). Acts
CC as an anchor for a PKA-signaling complex onto mitotic chromosomes,
CC which is required for maintenance of chromosomes in a condensed form
CC throughout mitosis. Recruits condensin complex subunit NCAPD2 to
CC chromosomes required for chromatin condensation; the function appears
CC to be independent from PKA-anchoring (By similarity). Specifically
CC involved in recruitment of CAPD2 to, and condensation of maternal but
CC not paternal chromosomes (PubMed:12082153). May help to deliver cyclin
CC D/E to CDK4 to facilitate cell cycle progression (PubMed:14641107).
CC Required for cell cycle G2/M transition and histone deacetylation
CC during mitosis. In mitotic cells recruits HDAC3 to the vicinity of
CC chromatin leading to deacetylation and subsequent phosphorylation at
CC 'Ser-10' of histone H3; in this function may act redundantly with
CC AKAP8L. Involved in nuclear retention of RPS6KA1 upon ERK activation
CC thus inducing cell proliferation. May be involved in regulation of DNA
CC replication by acting as scaffold for MCM2. Enhances HMT activity of
CC the KMT2 family MLL4/WBP7 complex and is involved in transcriptional
CC regulation. In a teratocarcinoma cell line is involved in retinoic
CC acid-mediated induction of developmental genes implicating H3 'Lys-4'
CC methylation. May be involved in recruitment of active CASP3 to the
CC nucleus in apoptotic cells. May act as a carrier protein of GJA1 for
CC its transport to the nucleus. May play a repressive role in the
CC regulation of rDNA transcription. Preferentially binds GC-rich DNA in
CC vitro. In cells, associates with ribosomal RNA (rRNA) chromatin,
CC preferentially with rRNA promoter and transcribed regions (By
CC similarity). Involved in modulation of Toll-like receptor signaling.
CC Required for the cAMP-dependent suppression of TNF-alpha in early
CC stages of LPS-induced macrophage activation; the function probably
CC implicates targeting of PKA to NFKB1 (PubMed:19531803).
CC {ECO:0000250|UniProtKB:O43823, ECO:0000250|UniProtKB:Q63014}.
CC -!- SUBUNIT: Binds to the PKA RII-alpha regulatory subunit PRKAR2A (By
CC similarity). Interacts (via C-terminus) with FIGN (PubMed:16751186).
CC Interacts with NCAPD2, CCND3, CCNE1, MCM2, RPS6KA1, DDX5, PDE4A (By
CC similarity). Interacts with MYCBP; MYCBP is translocated to the nucleus
CC and the interaction prevents the association of the PKA catalytic
CC subunit leading to suppression of PKA activity (PubMed:12414807).
CC Interacts with CCND1, CASP3 (PubMed:14641107, PubMed:16227597).
CC Interacts with NFKB1; detetcted in the cytoplasm (PubMed:19531803).
CC Interacts with DPY30; mediating AKAP8 association with at least the
CC MLL4/WBP7 HMT complex. Interacts with HDAC3; increased during mitosis.
CC Interacts with GJA1; in the nucleus and in the nuclear membrane; the
CC nuclear association increases with progress of cell cycle G1, S and G2
CC phase and decreases in M phase (By similarity).
CC {ECO:0000250|UniProtKB:O43823, ECO:0000250|UniProtKB:Q5VK71,
CC ECO:0000250|UniProtKB:Q63014, ECO:0000269|PubMed:12414807,
CC ECO:0000269|PubMed:14641107, ECO:0000269|PubMed:16227597,
CC ECO:0000269|PubMed:16751186, ECO:0000269|PubMed:19531803}.
CC -!- INTERACTION:
CC Q9DBR0; Q9ERZ6: Fign; NbExp=4; IntAct=EBI-4285802, EBI-11111349;
CC Q9DBR0; P25799: Nfkb1; NbExp=4; IntAct=EBI-4285802, EBI-643958;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16751186}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:O43823}. Cytoplasm
CC {ECO:0000269|PubMed:19531803}. Note=Associated with the nuclear matrix
CC (By similarity). Exhibits partial localization to the nucleolus in
CC interphase, possibly to the fibrillary center and/or to the dense
CC fibrillary component (By similarity). Redistributed and detached from
CC condensed chromatin during mitosis (By similarity). Localizes
CC specifically to the vicinity of the meiotic spindle in metaphase II
CC oocytes (PubMed:12082153). {ECO:0000250|UniProtKB:O43823,
CC ECO:0000269|PubMed:12082153}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed in metaphase II oocytes. Strongly
CC up-regulated after fertilization at the pronuclear stage and restricted
CC to the female pronucleus. Subsequently localized to the nucleus of each
CC blastomere and on condensed chromosomes in mitotic cells.
CC {ECO:0000269|PubMed:12082153}.
CC -!- PTM: Phosphorylated on tyrosine residues probably by SRC subfamily
CC protein kinases; multiple phosphorylation is leading to dissociation
CC from nuclear structures implicated in chromatin structural changes.
CC {ECO:0000250|UniProtKB:O43823}.
CC -!- DISRUPTION PHENOTYPE: AKAP8 and FIGN double mutant mice die soon after
CC birth due to cleft palate. {ECO:0000269|PubMed:16751186}.
CC -!- SIMILARITY: Belongs to the AKAP95 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01140}.
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DR EMBL; AB028920; BAA84710.1; -; mRNA.
DR EMBL; AK004801; BAB23574.1; -; mRNA.
DR EMBL; AK089092; BAC40746.1; -; mRNA.
DR CCDS; CCDS37555.1; -.
DR RefSeq; NP_062748.2; NM_019774.5.
DR AlphaFoldDB; Q9DBR0; -.
DR BioGRID; 207953; 30.
DR IntAct; Q9DBR0; 27.
DR MINT; Q9DBR0; -.
DR STRING; 10090.ENSMUSP00000002699; -.
DR iPTMnet; Q9DBR0; -.
DR PhosphoSitePlus; Q9DBR0; -.
DR EPD; Q9DBR0; -.
DR jPOST; Q9DBR0; -.
DR MaxQB; Q9DBR0; -.
DR PaxDb; Q9DBR0; -.
DR PRIDE; Q9DBR0; -.
DR ProteomicsDB; 285797; -.
DR Antibodypedia; 1427; 356 antibodies from 36 providers.
DR DNASU; 56399; -.
DR Ensembl; ENSMUST00000002699; ENSMUSP00000002699; ENSMUSG00000024045.
DR GeneID; 56399; -.
DR KEGG; mmu:56399; -.
DR UCSC; uc008bwg.2; mouse.
DR CTD; 10270; -.
DR MGI; MGI:1928488; Akap8.
DR VEuPathDB; HostDB:ENSMUSG00000024045; -.
DR eggNOG; ENOG502QZY2; Eukaryota.
DR GeneTree; ENSGT00530000063777; -.
DR HOGENOM; CLU_024193_1_0_1; -.
DR InParanoid; Q9DBR0; -.
DR OMA; EFCDSGR; -.
DR OrthoDB; 902224at2759; -.
DR PhylomeDB; Q9DBR0; -.
DR TreeFam; TF105407; -.
DR BioGRID-ORCS; 56399; 1 hit in 63 CRISPR screens.
DR ChiTaRS; Akap8; mouse.
DR PRO; PR:Q9DBR0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9DBR0; protein.
DR Bgee; ENSMUSG00000024045; Expressed in retinal neural layer and 282 other tissues.
DR ExpressionAtlas; Q9DBR0; baseline and differential.
DR Genevisible; Q9DBR0; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0001939; C:female pronucleus; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0051059; F:NF-kappaB binding; IDA:UniProtKB.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0044839; P:cell cycle G2/M phase transition; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0033127; P:regulation of histone phosphorylation; ISO:MGI.
DR InterPro; IPR007071; AKAP95.
DR InterPro; IPR034736; ZF_C2H2_AKAP95.
DR PANTHER; PTHR12190; PTHR12190; 1.
DR Pfam; PF04988; AKAP95; 1.
DR PROSITE; PS51799; ZF_C2H2_AKAP95; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Immunity; Innate immunity; Isopeptide bond;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transport; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..687
FT /note="A-kinase anchor protein 8"
FT /id="PRO_0000075382"
FT ZN_FING 389..411
FT /note="C2H2 AKAP95-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT ZN_FING 478..501
FT /note="C2H2 AKAP95-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT REGION 1..210
FT /note="Interaction with DPY30"
FT /evidence="ECO:0000250|UniProtKB:O43823"
FT REGION 1..195
FT /note="Interaction with MCM2"
FT /evidence="ECO:0000250|UniProtKB:O43823"
FT REGION 105..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..201
FT /note="Interaction with DDX5"
FT /evidence="ECO:0000250|UniProtKB:Q63014"
FT REGION 185..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..447
FT /note="Involved in chromatin-binding"
FT /evidence="ECO:0000250|UniProtKB:O43823"
FT REGION 522..565
FT /note="Involved in condensin complex recruitment"
FT /evidence="ECO:0000250|UniProtKB:O43823"
FT REGION 568..585
FT /note="RII-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63014"
FT REGION 572..589
FT /note="Required for interaction with MYCBP"
FT /evidence="ECO:0000269|PubMed:12414807"
FT REGION 624..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 286..303
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O43823,
FT ECO:0000250|UniProtKB:Q63014"
FT COMPBIAS 194..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 109
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43823"
FT MOD_RES 232
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 276
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 552
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63014"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63014"
FT CROSSLNK 314
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43823"
FT CONFLICT 323
FT /note="D -> G (in Ref. 1; BAA84710)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="K -> E (in Ref. 1; BAA84710)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="D -> G (in Ref. 1; BAA84710)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="V -> A (in Ref. 1; BAA84710)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="A -> T (in Ref. 1; BAA84710)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="E -> G (in Ref. 1; BAA84710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 76294 MW; BC1E320216A47E10 CRC64;
MEQGYGGYGA WSAGPANTQG TYGSGMTSWQ GYENYNYYNA QNTSVPAGTP YSYGPASWEA
TKTNDGGLAA GSPAMHVASF APEPCTDNSD SLIAKINQRL DMLSKEGGRG GISSGGEGVQ
DRDSSFRFQP YESYDARPCI PEHNPYRPGY GYDYDFDLGT DRNGSFGGTF NDCRDPAPER
GSLDGFLRGR GQGRFQDRSN SSTFIRSDPF MPPSASEPLS TTWNELNYMG GRGLGGPSTS
RPPPSLFSQS MAPDYSMMGM QGVGGFGGTM PYGCGRSQTR IRDWPRRRGF ERFGPDNMGR
KRKQFPLYEE PDAKLARADS DGDLSENDDG AGDLRSGDEE FRGEDDLCDS RKQRGEKEDE
DEDVKKRREK QRRRDRMRDR AADRIQFACS VCKFRSFEDE EIQKHLQSKF HKETLRFIST
KLPDKTVEFL QEYIINRNKK IEKRRQELLE KESPKPKPDP FKGIGQEHFF KKIEAAHCLA
CDMLIPAQHQ LLQRHLHSVD HNHNRRLAAE QFKKTSLHVA KSVLNNKHIV KMLEKYLKGE
DPFVNETADL ETEGDENVGE EKEETPEEVA AEVLAEVITA AVKAVEGEGE PAAAHSDVLT
EVEGPVDTAE ASSDPHTEKL LEEQTCEAAS ETRSIEDKTR GEAAEARNEA AMPTADAGST
LPVIAIPGIM EDELEQTGAE AKDIPTE
