AKA12_MOUSE
ID AKA12_MOUSE Reviewed; 1684 AA.
AC Q9WTQ5; Q80SS4; Q810D4; Q8BPK4; Q99MP1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=A-kinase anchor protein 12;
DE Short=AKAP-12;
DE AltName: Full=Germ cell lineage protein gercelin;
DE AltName: Full=Src-suppressed C kinase substrate;
DE Short=SSeCKS;
GN Name=Akap12; Synonyms=Gag12, Ssecks;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11429284; DOI=10.1016/s0925-4773(01)00384-7;
RA Camus A., Mesbah K., Rallu M., Babinet C., Barra J.;
RT "Gene trap insertion reveals two open reading frames in the mouse SSeCKS
RT gene: the form predominantly detected in the nervous system is suppressed
RT by the insertion while the other, specific of the testis, remains
RT expressed.";
RL Mech. Dev. 105:79-91(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=11799143; DOI=10.1177/002215540205000212;
RA Kitamura H., Okita K., Fujikura D., Mori K., Iwanaga T., Saito M.;
RT "Induction of Src-suppressed C kinase substrate (SSeCKS) in vascular
RT endothelial cells by bacterial lipopolysaccharide.";
RL J. Histochem. Cytochem. 50:245-255(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Nishina Y., Motoda Y.;
RT "Mouse testicular cell specific gene, GAG12.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Tsuchida J., Tanaka H., Yomogida K., Nozaki M., Maeda N., Matsui Y.,
RA Nishimune Y.;
RT "Molecular cloning and characterization of the mouse germ cell lineage
RT protein cDNA, gercelin, encoding the cytoplasmic AKAP, Gercelin / SSeCKS
RT and the potential germ cell-specific nuclear antigen, GENA.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-605 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-1684 (ISOFORMS 1/2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682; SER-683 AND SER-684, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-353, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-22; SER-27; SER-234;
RP SER-270; SER-273; SER-350; SER-371; SER-467; SER-489; SER-584; SER-631;
RP SER-634; SER-637; SER-682; SER-733; SER-767; SER-786; THR-871; SER-873;
RP SER-1351 AND SER-1645, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- FUNCTION: Anchoring protein that mediates the subcellular
CC compartmentation of protein kinase A (PKA) and protein kinase C (PKC).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds to dimeric RII-alpha regulatory subunit of PKC.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Membrane
CC {ECO:0000250|UniProtKB:Q02952}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q02952}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q9WTQ5-1; Sequence=Displayed;
CC Name=2; Synonyms=Gamma;
CC IsoId=Q9WTQ5-2; Sequence=VSP_028135;
CC -!- TISSUE SPECIFICITY: Isoform 1 is predominantly found in the nervous
CC system. Isoform 3 is testis specific. {ECO:0000269|PubMed:11429284}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC66465.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF326228; AAK16150.1; -; mRNA.
DR EMBL; AF326230; AAK16152.1; -; mRNA.
DR EMBL; AB020886; BAA76894.1; -; mRNA.
DR EMBL; AB025278; BAC66465.1; ALT_FRAME; mRNA.
DR EMBL; AB051563; BAB72161.1; -; mRNA.
DR EMBL; AB070852; BAB72164.1; -; mRNA.
DR EMBL; AB070853; BAB72165.1; -; mRNA.
DR EMBL; AK053844; BAC35553.1; -; mRNA.
DR EMBL; BC042461; AAH42461.1; -; mRNA.
DR EMBL; BC043939; AAH43939.1; -; mRNA.
DR CCDS; CCDS56673.1; -. [Q9WTQ5-1]
DR RefSeq; NP_112462.1; NM_031185.3. [Q9WTQ5-1]
DR AlphaFoldDB; Q9WTQ5; -.
DR BioGRID; 219914; 15.
DR ELM; Q9WTQ5; -.
DR IntAct; Q9WTQ5; 11.
DR STRING; 10090.ENSMUSP00000035829; -.
DR iPTMnet; Q9WTQ5; -.
DR PhosphoSitePlus; Q9WTQ5; -.
DR SwissPalm; Q9WTQ5; -.
DR CPTAC; non-CPTAC-3631; -.
DR EPD; Q9WTQ5; -.
DR jPOST; Q9WTQ5; -.
DR MaxQB; Q9WTQ5; -.
DR PaxDb; Q9WTQ5; -.
DR PeptideAtlas; Q9WTQ5; -.
DR PRIDE; Q9WTQ5; -.
DR ProteomicsDB; 285794; -. [Q9WTQ5-1]
DR ProteomicsDB; 285795; -. [Q9WTQ5-2]
DR Antibodypedia; 1199; 236 antibodies from 38 providers.
DR DNASU; 83397; -.
DR Ensembl; ENSMUST00000045730; ENSMUSP00000035829; ENSMUSG00000038587. [Q9WTQ5-1]
DR Ensembl; ENSMUST00000215696; ENSMUSP00000150261; ENSMUSG00000038587. [Q9WTQ5-2]
DR GeneID; 83397; -.
DR KEGG; mmu:83397; -.
DR UCSC; uc007ehh.1; mouse. [Q9WTQ5-1]
DR CTD; 9590; -.
DR MGI; MGI:1932576; Akap12.
DR VEuPathDB; HostDB:ENSMUSG00000038587; -.
DR eggNOG; ENOG502RDV6; Eukaryota.
DR GeneTree; ENSGT00730000111244; -.
DR HOGENOM; CLU_002691_0_0_1; -.
DR InParanoid; Q9WTQ5; -.
DR OMA; AWEPVEL; -.
DR PhylomeDB; Q9WTQ5; -.
DR TreeFam; TF105411; -.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 83397; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Akap12; mouse.
DR PRO; PR:Q9WTQ5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9WTQ5; protein.
DR Bgee; ENSMUSG00000038587; Expressed in efferent duct and 242 other tissues.
DR ExpressionAtlas; Q9WTQ5; baseline and differential.
DR Genevisible; Q9WTQ5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0008179; F:adenylate cyclase binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051018; F:protein kinase A binding; IEA:InterPro.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; TAS:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0035733; P:hepatic stellate cell activation; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0043116; P:negative regulation of vascular permeability; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0061870; P:positive regulation of hepatic stellate cell migration; ISO:MGI.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR GO; GO:1900143; P:positive regulation of oligodendrocyte apoptotic process; ISO:MGI.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IEA:InterPro.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:MGI.
DR GO; GO:0090036; P:regulation of protein kinase C signaling; IEA:InterPro.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR InterPro; IPR028540; AKAP12.
DR InterPro; IPR001573; AKAP_WSK.
DR InterPro; IPR018459; RII-bd_1.
DR PANTHER; PTHR23209; PTHR23209; 1.
DR Pfam; PF10522; RII_binding_1; 1.
DR Pfam; PF03832; WSK; 3.
DR PROSITE; PS51893; AKAP_CAM_BD; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT CHAIN 2..1684
FT /note="A-kinase anchor protein 12"
FT /id="PRO_0000304941"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..543
FT /note="Involved in PKC-binding"
FT /evidence="ECO:0000250"
FT REGION 296..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1514
FT /note="RII-binding"
FT /evidence="ECO:0000250"
FT REGION 1568..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 593..613
FT /note="AKAP CaM-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT MOTIF 740..760
FT /note="AKAP CaM-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT MOTIF 781..801
FT /note="AKAP CaM-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1568..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1649..1684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 353
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 628
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17622165,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17622165"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17622165"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 871
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 1351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 1357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 1546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 1645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT CROSSLNK 1030
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11429284, ECO:0000303|Ref.4"
FT /id="VSP_028135"
SQ SEQUENCE 1684 AA; 180695 MW; E569D55762FCB19E CRC64;
MGAGSSTEQR SPEQPAESDT PSELELSGHG PAAEASGAAG DPADADPATK LPQKNGQLSA
VNGVAEQEDV HVQEESQDGQ EEEVTVEDVG QRESEDVKEK DRAKEMAASS TVVEDITKDE
QEETPEIIEQ IPASESNVEE MAQAAESQAN DVGFKKVFKF VGFKFTVKKD KNEKSDTVQL
LTVKKDEGEG AEASVGAGDH QEPGVETVGE SASKESELKQ STEKQEGTLK QAQSSTEIPL
QAESGQGTEE EAAKDGEENR EKEPTKPLES PTSPVSNETT SSFKKFFTHG WAGWRKKTSF
KKPKEDDLET SEKRKEQEAE KVDEEEGEKT EPAPAEEQEP AEGTDQARLS ADYEKVELPL
EDQVGDLEAL SEKCAPLATE VFDEKTEAHQ EVVAEVHVST VEKMTKGQGG AEVEGDVVVE
GSGESLPPEK LAETQEVPQE AEPVEELMKT KEVCVSGGDH TQLTDLSPEE KMLPKHPEGI
VSEVEMLSSQ ERIKVQGSPL KKLFSSSGLK KLSGKKQKGK RGGGGGDEEP GEYQHIQTES
PESADEQKGE SSASSPEEPE EIACLEKGPS EAPQEAEAEE GATSDGEKKR EGITPWASFK
KMVTPKKRVR RPSESDKEEE LDKVKSATLS STESTASGMQ DEVRAVGEEQ RSEEPKRRVD
TSVSWEALIC VGSSKKRARK ASSSDDEGGP RTLGGDGHRA EEASKDKEAD ALPASTQEQD
QAHGSSSPEP AGSPSEGEGV STWESFKRLV TPRKKSKSKL EERAEDSGAE QLASEIEPSR
EESWVSIKKF IPGRRKKRAD GKQEQAAVED SGPGEINEDD PDVPAVVPLS EYDAVEREKL
EAQRAQENVE LPQLKGAVYV SEELSKTLVH TVSVAVIDGT RAVTSAEERS PSWISASMTE
PLEHAEGVAT PPVGEVTEKD ITAEATPALA QTLPGGKDAH DDIVTSEVDF TSEAVTAAET
TEALRAEELT EASGAEETTD MVSAVSQLSD SPDTTEEATP VQEVEGGMLD TEEQERQTQA
VLQAVADKVK EDSQVPATQT LQRAGPKALE KVEEVEEDSE VLATEKEKDV VPEGPVQEAE
TEHLAQGSET VQATPESLEV PEVTEDVDRA TTCQVIKHQQ LMEQAVAPES SETLTDSETN
GSTPLADSDT PNGTQQDETV DSQDSNAIAA VKQSQVTEEE AAAAQTEGPS TPSSFPAQEE
HREKPGRDVL EPTQALAAGA VPILAKAEVG QEGEAGQFDG EKVKDGQCVK ELEVPVHTGP
NSQKTADLTR DSEVMEVARC QETESNEEQS ISPEKREMGT DVEKEETETK TEQASEEHEQ
ETAAPEHEGT HPKPVLTADM PHSERGKALG SLEGSPSLPD QDKADCIEVQ VQSSDTPVTQ
TTEAVKKVEE TVATSEMDES LECAGAQSLP AEKLSETGGY GTLQHGEDTV PQGPESQAES
IPIIVTPAPE SILHSDLQRE VSASQKQRSD EDNKPDAGPD AAGKESAARE KILRAEPEIL
ELESKSNKIV QSVIQTAVDQ FARTETAPET HASDLQNQVP VMQADSQGAQ QMLDKDESDL
QVSPQDGTLS AVAQEGLAVS DSSEGMSKAS EMITTLAVES ASVKESVEKL PLQCKDEKEH
AADGPQHQSL AKAEADASGN LTKESPDTNG PKLTEEGDAL KEEMNKAQTE EDDLQEPKGD
LTES
