ID   CDK12_MOUSE             Reviewed;        1484 AA.
AC   Q14AX6; A2A530; A2A531; B1AQH7; Q6ZQ27; Q8R457;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   02-SEP-2026, entry version 152.
DE   RecName: Full=Cyclin-dependent kinase 12;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=Cdc2-related kinase, arginine/serine-rich;
DE            Short=CrkRS;
DE   AltName: Full=Cell division cycle 2-related protein kinase 7;
DE            Short=CDC2-related protein kinase 7;
DE   AltName: Full=Cell division protein kinase 12;
GN   Name=Cdk12; Synonyms=Crk7, Crkrs, Kiaa0904;
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 2).
RC   STRAIN=BALB/cJ;
RA   Lin S.-F., Chen H.-H., Fann M.-J.;
RT   "Characterization of a putative SR-related protein kinase that is
RT   differentially expressed in the embryonic nervous system.";
RL   Submitted (JAN-2002) 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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-1484 (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382; SER-384 AND SER-1079,
RP   AND IDENTIFICATION BY 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-382 AND SER-384, AND
RP   IDENTIFICATION BY 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-248; SER-382;
RP   SER-384; SER-677; SER-681; THR-889; SER-1079; THR-1240 AND THR-1242,
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1240 AND THR-1242 (ISOFORM
RP   3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=22012619; DOI=10.1101/gad.16962311;
RA   Blazek D., Kohoutek J., Bartholomeeusen K., Johansen E., Hulinkova P.,
RA   Luo Z., Cimermancic P., Ule J., Peterlin B.M.;
RT   "The Cyclin K/Cdk12 complex maintains genomic stability via regulation of
RT   expression of DNA damage response genes.";
RL   Genes Dev. 25:2158-2172(2011).
CC   -!- FUNCTION: Cyclin-dependent kinase that phosphorylates the C-terminal
CC       domain (CTD) of the large subunit of RNA polymerase II (POLR2A),
CC       thereby acting as a key regulator of transcription elongation.
CC       Regulates the expression of genes involved in DNA repair and is
CC       required for the maintenance of genomic stability. Preferentially
CC       phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated
CC       at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA
CC       splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation
CC       of MAP kinase activity, possibly leading to affect the response to
CC       estrogen inhibitors. {ECO:0000269|PubMed:22012619}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed
CC         RNA polymerase] + ADP + H(+); Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC         COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC         ChEBI:CHEBI:456216; EC=2.7.11.23;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC   -!- SUBUNIT: Interacts with CCNL1 and CCNL2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}. Note=Colocalized with nuclear speckles throughout
CC       interphase. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q14AX6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14AX6-2; Sequence=VSP_030285, VSP_030287;
CC       Name=3;
CC         IsoId=Q14AX6-3; Sequence=VSP_030286;
CC   -!- PTM: Phosphorylation at Thr-889 increases kinase activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM21270.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY072295; AAL69526.1; -; mRNA.
DR   EMBL; AL591205; CAM21267.1; -; Genomic_DNA.
DR   EMBL; AL591205; CAM21268.1; -; Genomic_DNA.
DR   EMBL; AL591205; CAM21269.1; -; Genomic_DNA.
DR   EMBL; AL591205; CAM21270.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC116645; AAI16646.1; -; mRNA.
DR   EMBL; AK129237; BAC98047.1; -; mRNA.
DR   CCDS; CCDS25342.1; -. [Q14AX6-2]
DR   CCDS; CCDS48901.1; -. [Q14AX6-1]
DR   CCDS; CCDS48902.1; -. [Q14AX6-3]
DR   RefSeq; NP_001103096.1; NM_001109626.1. [Q14AX6-1]
DR   RefSeq; NP_001103098.1; NM_001109628.1. [Q14AX6-3]
DR   RefSeq; NP_081228.2; NM_026952.2. [Q14AX6-2]
DR   RefSeq; XP_030102133.1; XM_030246273.1. [Q14AX6-1]
DR   RefSeq; XP_030102134.1; XM_030246274.2. [Q14AX6-1]
DR   RefSeq; XP_030102135.1; XM_030246275.2. [Q14AX6-3]
DR   AlphaFoldDB; Q14AX6; -.
DR   SMR; Q14AX6; -.
DR   BioGRID; 213247; 20.
DR   ComplexPortal; CPX-251; Cyclin K-CDK12 complex.
DR   FunCoup; Q14AX6; 3425.
DR   STRING; 10090.ENSMUSP00000103162; -.
DR   BindingDB; Q14AX6; -.
DR   ChEMBL; CHEMBL5465307; -.
DR   GlyGen; Q14AX6; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; Q14AX6; -.
DR   PhosphoSitePlus; Q14AX6; -.
DR   jPOST; Q14AX6; -.
DR   PaxDb; 10090-ENSMUSP00000103162; -.
DR   PeptideAtlas; Q14AX6; -.
DR   ProteomicsDB; 283768; -. [Q14AX6-1]
DR   ProteomicsDB; 283769; -. [Q14AX6-2]
DR   ProteomicsDB; 283770; -. [Q14AX6-3]
DR   Pumba; Q14AX6; -.
DR   Antibodypedia; 2096; 238 antibodies from 33 providers.
DR   DNASU; 69131; -.
DR   Ensembl; ENSMUST00000003203.14; ENSMUSP00000003203.8; ENSMUSG00000003119.15. [Q14AX6-2]
DR   Ensembl; ENSMUST00000107538.2; ENSMUSP00000103162.2; ENSMUSG00000003119.15. [Q14AX6-1]
DR   Ensembl; ENSMUST00000107539.8; ENSMUSP00000103163.2; ENSMUSG00000003119.15. [Q14AX6-3]
DR   GeneID; 69131; -.
DR   KEGG; mmu:69131; -.
DR   UCSC; uc007lfr.2; mouse. [Q14AX6-1]
DR   UCSC; uc007lfs.2; mouse. [Q14AX6-2]
DR   UCSC; uc007lfu.2; mouse. [Q14AX6-3]
DR   AGR; MGI:1098802; -.
DR   CTD; 51755; -.
DR   MGI; MGI:1098802; Cdk12.
DR   VEuPathDB; HostDB:ENSMUSG00000003119; -.
DR   eggNOG; KOG0600; Eukaryota.
DR   GeneTree; ENSGT00940000157595; -.
DR   HOGENOM; CLU_004166_2_1_1; -.
DR   InParanoid; Q14AX6; -.
DR   OMA; HWGAPAQ; -.
DR   OrthoDB; 28397at2759; -.
DR   PhylomeDB; Q14AX6; -.
DR   Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   BioGRID-ORCS; 69131; 25 hits in 84 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:Q14AX6; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q14AX6; protein.
DR   Bgee; ENSMUSG00000003119; Expressed in animal zygote and 224 other cell types or tissues.
DR   GO; GO:0002944; C:cyclin K-CDK12 complex; ISO:MGI.
DR   GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR   GO; GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030332; F:cyclin binding; ISO:MGI.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; ISS:HGNC-UCL.
DR   GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; ISS:UniProtKB.
DR   GO; GO:0071391; P:cellular response to estrogen stimulus; ISO:GO_Central.
DR   GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:GO_Central.
DR   GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; ISO:GO_Central.
DR   GO; GO:0043405; P:regulation of MAP kinase activity; ISS:UniProtKB.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISO:GO_Central.
DR   GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR   CDD; cd07864; STKc_CDK12; 1.
DR   FunFam; 1.10.510.10:FF:000102; cyclin-dependent kinase 12 isoform X1; 1.
DR   FunFam; 3.30.200.20:FF:000074; cyclin-dependent kinase 12 isoform X2; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR050108; CDK.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF126; CYCLIN-DEPENDENT KINASE 12; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Isopeptide bond; Kinase;
KW   mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..1484
FT                   /note="Cyclin-dependent kinase 12"
FT                   /id="PRO_0000314470"
FT   DOMAIN          723..1016
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1156..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1219..1363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1437..1484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..13
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..49
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..84
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..119
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..224
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..304
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..349
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..380
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..570
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..681
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1079
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1156..1167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1264..1277
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1444..1454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1467..1484
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        855
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         729..737
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         752
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         810..815
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1036
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         57
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         73
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         311
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         317
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         331
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         340
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         399
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         511
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         610
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         640
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3MJK5"
FT   MOD_RES         677
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         681
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         688
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         885
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         889
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1049
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   MOD_RES         1079
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1240
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1242
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        262
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   CROSSLNK        506
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   CROSSLNK        651
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT   VAR_SEQ         1250..1258
FT                   /note="ACPPHILPP -> GKQTGHESH (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT                   /id="VSP_030285"
FT   VAR_SEQ         1250..1258
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_030286"
FT   VAR_SEQ         1259..1484
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT                   /id="VSP_030287"
FT   CONFLICT        346
FT                   /note="L -> I (in Ref. 1; AAL69526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="R -> S (in Ref. 1; AAL69526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        377
FT                   /note="R -> H (in Ref. 1; AAL69526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425..427
FT                   /note="ILP -> FCL (in Ref. 4; BAC98047)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        496
FT                   /note="G -> V (in Ref. 1; AAL69526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        562
FT                   /note="L -> V (in Ref. 1; AAL69526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        854
FT                   /note="R -> Q (in Ref. 1; AAL69526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        863
FT                   /note="L -> V (in Ref. 1; AAL69526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        870
FT                   /note="K -> R (in Ref. 1; AAL69526)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q14AX6-3:1240
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q14AX6-3:1242
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   1484 AA;  163681 MW;  5FCEE8D1903DF803 CRC64;
     MPNSERHGGK KDGSGGASGT SQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDVGLVTPEA
     ASLGTIIKPL VEYDDISSDS DTFSDDTAFK SDRRENEERR GTDRSDRLHR HRHHQHRRSR
     DLLKTKQTEK EKNQEVSKSG SMKDRVSGSS KRSVEGSDDY GKAQLSKSGS KESRSSKMHK
     EKTRKERELK SGYKDRSKSH RKRETPKSYK TVASPKRRSR SPHRKWSDSS KQDDSPSGAS
     YGQDYDLSPP RSHTSSNYDS YKKSPGSTSR RQSISPPYKE PSAYQSSTRS PSPYSRRQRS
     VSPYSRRRSS SYERSGSYSG RSPSPYGRRR SSSPFLSKRS LSRSPLPSRK SMKSRSRSPA
     YSRHSSSHSK KKRSGSRSRH SSISPVRLPL NSSLGAELSR KKKERAAAAA AAKMDGKESK
     SSPIILPKKE KLEVKESGLE SKKLPRSIKS EKSTPDTELV TVAHSNPEVK HCLDTGKVRL
     DENLQKHPAK DLKAQGTKDV KPVAPKEVIV TSKETETSEK ETLPPLPTIT SPPPLPATTP
     PPQTPPLPPL PPLPAIPLQP PLPPPQPPFS QVPVSSTSIL PSSPHPRTST LSSQTNSQPP
     VQVSMKTQVS ITAAIPHLKT STLPPLPLPP LLPGDDDMDS PKETLPSKPA KKEKEQRTRH
     LLTDLPLPPE LPGGDPSPPD SPEPKAITPP QQPYKKRPKI CCPRYGERRQ TESDWGKRCV
     DKFDIIGIIG EGTYGQVYKA KDKDTGELVA LKKVRLDNEK EGFPITAIRE IKILRQLVHQ
     SVVNMKEIVT DKQDALDFKK DKGAFYLVFE YMDHDLMGLL ESGLVHFSED HIKSFMKQLM
     EGLDYCHKKN FLHRDIKCSN ILLNNSGQIK LADFGLARLY NSEESRPYTN KVITLWYRPP
     ELLLGEERYT PAIDVWSCGC ILGELFTKKP IFQANLELAQ LELISRLCGS PCPAVWPDVI
     KLPYFNTMKP KKQYRRRLRE EFSFIPSAAL DLLDHMLTLD PSKRCTAEQT LQSDFLKDVE
     LSKMAPPDLP HWQDCHELWS KKRRRQRQSG IVIEDPPPSK ASRKETTSGT TAEPVKNNSP
     APPQPAPVKA EPGPGDAVGL GDITQQLNQS ELAVLLNLLQ SQTDLSIPQM AQLLNIHSNP
     EMQQQLEALN QSISALTEAS SQQQDSESIA PEESLKEVPS VPVVLPPAEQ TTPEASNTPA
     DMQNVLAVLL SQLMKTQEPA GNLEENTNDK NSGPQGPRRT PTMPQEEAAA CPPHILPPEK
     RPPEPPGPPP PPPPPPLVEG DLSSAPQELN PAVTAALLQL LSQPEAEPPG HLPHEHQALR
     PMEYSTRSHP NRTYGNTDGP ETGFSSADTD ERSSGPALTE SLVQTPVKNR TFSGSVSHLG
     ESNSYQGTGS VQFPGDQDLR FTRVPLALHS VVGQPFLKSE GNSNSVVHAE TKLQNYGELG
     PGTTGANSSG TTLQWGGPAQ SYGKPYRGAA RVLPRGGRGR GVPY
//