ID   CDK13_MOUSE             Reviewed;        1511 AA.
AC   Q69ZA1; E9QKZ6; Q80V11; Q8BZG1; Q8K0A4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Cyclin-dependent kinase 13;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=CDC2-related protein kinase 5;
DE   AltName: Full=Cell division cycle 2-like protein kinase 5;
DE   AltName: Full=Cell division protein kinase 13;
GN   Name=Cdk13; Synonyms=Cdc2l5, Kiaa1791;
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 MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
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] OF 295-1511 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 891-1511 (ISOFORMS 1 AND 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   [5]
RP   FUNCTION, AND INTERACTION WITH CCNL1 AND CCNL2.
RX   PubMed=17261272; DOI=10.1016/j.bbrc.2007.01.049;
RA   Chen H.H., Wong Y.H., Geneviere A.M., Fann M.J.;
RT   "CDK13/CDC2L5 interacts with L-type cyclins and regulates alternative
RT   splicing.";
RL   Biochem. Biophys. Res. Commun. 354:735-740(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, 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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-343; SER-384;
RP   SER-398; SER-438; SER-440; SER-526 AND THR-1058, AND IDENTIFICATION BY MASS
RP   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   [9]
RP   INTERACTION WITH CCNK.
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 which displays CTD kinase activity
CC       and is required for RNA splicing. Has CTD kinase activity by
CC       hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of
CC       the largest RNA polymerase II subunit RPB1, thereby acting as a key
CC       regulator of transcription elongation. Required for RNA splicing,
CC       probably by phosphorylating SRSF1/SF2. Required during hematopoiesis.
CC       {ECO:0000269|PubMed:17261272}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC         [DNA-directed RNA polymerase]; 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=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; 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=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.22;
CC   -!- SUBUNIT: Interacts with C1QBP (By similarity). Interacts with CCNK,
CC       CCNL1 and CCNL2. {ECO:0000250, ECO:0000269|PubMed:17261272,
CC       ECO:0000269|PubMed:22012619}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q69ZA1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69ZA1-2; Sequence=VSP_013580;
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=AAH32179.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC29077.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC29077.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAD32543.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK173265; BAD32543.1; ALT_INIT; mRNA.
DR   EMBL; AC154219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK035493; BAC29077.1; ALT_SEQ; mRNA.
DR   EMBL; BC032179; AAH32179.1; ALT_INIT; mRNA.
DR   EMBL; BC051093; AAH51093.1; -; mRNA.
DR   CCDS; CCDS36604.1; -. [Q69ZA1-1]
DR   CCDS; CCDS88417.1; -. [Q69ZA1-2]
DR   RefSeq; NP_001074527.1; NM_001081058.2. [Q69ZA1-1]
DR   RefSeq; NP_081394.1; NM_027118.1. [Q69ZA1-2]
DR   AlphaFoldDB; Q69ZA1; -.
DR   SMR; Q69ZA1; -.
DR   BioGRID; 213532; 5.
DR   ComplexPortal; CPX-366; Cyclin K-Cdk13 complex.
DR   IntAct; Q69ZA1; 1.
DR   STRING; 10090.ENSMUSP00000036013; -.
DR   GlyGen; Q69ZA1; 14 sites, 1 O-linked glycan (14 sites).
DR   iPTMnet; Q69ZA1; -.
DR   PhosphoSitePlus; Q69ZA1; -.
DR   EPD; Q69ZA1; -.
DR   jPOST; Q69ZA1; -.
DR   MaxQB; Q69ZA1; -.
DR   PaxDb; 10090-ENSMUSP00000036013; -.
DR   PeptideAtlas; Q69ZA1; -.
DR   ProteomicsDB; 280038; -. [Q69ZA1-1]
DR   ProteomicsDB; 280039; -. [Q69ZA1-2]
DR   Pumba; Q69ZA1; -.
DR   Antibodypedia; 26726; 222 antibodies from 28 providers.
DR   DNASU; 69562; -.
DR   Ensembl; ENSMUST00000042365.9; ENSMUSP00000036013.8; ENSMUSG00000041297.9. [Q69ZA1-1]
DR   Ensembl; ENSMUST00000223490.2; ENSMUSP00000152820.2; ENSMUSG00000041297.9. [Q69ZA1-2]
DR   GeneID; 69562; -.
DR   KEGG; mmu:69562; -.
DR   UCSC; uc007poc.2; mouse. [Q69ZA1-1]
DR   UCSC; uc007pod.2; mouse. [Q69ZA1-2]
DR   AGR; MGI:1916812; -.
DR   CTD; 8621; -.
DR   MGI; MGI:1916812; Cdk13.
DR   VEuPathDB; HostDB:ENSMUSG00000041297; -.
DR   eggNOG; KOG0600; Eukaryota.
DR   GeneTree; ENSGT00940000157852; -.
DR   HOGENOM; CLU_004166_3_0_1; -.
DR   InParanoid; Q69ZA1; -.
DR   OMA; GHMHGQT; -.
DR   OrthoDB; 5402490at2759; -.
DR   PhylomeDB; Q69ZA1; -.
DR   TreeFam; TF101060; -.
DR   Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 69562; 17 hits in 83 CRISPR screens.
DR   ChiTaRS; Cdk13; mouse.
DR   PRO; PR:Q69ZA1; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q69ZA1; Protein.
DR   Bgee; ENSMUSG00000041297; Expressed in undifferentiated genital tubercle and 228 other cell types or tissues.
DR   ExpressionAtlas; Q69ZA1; baseline and differential.
DR   GO; GO:0002945; C:cyclin K-CDK13 complex; ISO:MGI.
DR   GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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:0000380; P:alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
DR   GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:MGI.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:MGI.
DR   GO; GO:0009966; P:regulation of signal transduction; ISO:MGI.
DR   CDD; cd07864; STKc_CDK12; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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:SF459; CYCLIN-DEPENDENT KINASE 13; 1.
DR   Pfam; PF12330; Haspin_kinase; 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.
DR   Genevisible; Q69ZA1; MM.
PE   1: Evidence at protein level;
KW   Acetylation; 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..1511
FT                   /note="Cyclin-dependent kinase 13"
FT                   /id="PRO_0000085712"
FT   DOMAIN          705..998
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          30..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1048..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1138..1168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1465..1511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..59
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..434
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1074
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1140..1168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1197..1211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1233..1256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1465..1497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        837
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         711..719
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         734
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         396
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         526
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         557
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         588
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         871
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         1048
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   MOD_RES         1058
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1245
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   CROSSLNK        520
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   CROSSLNK        548
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q14004"
FT   VAR_SEQ         1079..1138
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15368895,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_013580"
FT   CONFLICT        73
FT                   /note="A -> V (in Ref. 1; BAD32543)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="Q -> R (in Ref. 1; BAD32543)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        637
FT                   /note="E -> K (in Ref. 3; BAC29077)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1009
FT                   /note="P -> L (in Ref. 1; BAD32543)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1206
FT                   /note="E -> K (in Ref. 4; AAH32179)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1400
FT                   /note="A -> P (in Ref. 4; AAH51093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1464
FT                   /note="N -> D (in Ref. 3; BAC29077)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1511 AA;  164553 MW;  EAF4438ABB5063CE CRC64;
     MPSSSDTALG GGGGLSWAEK KLEERRKRRR FLSPQQPPLL LPLLQPQLLQ PPPPPPPLLF
     LAAPGAAAAA AAAAAASSSC FSPGPPLEVK RLARGKRRPG GRQKRRRGPR AGQEAEKRRV
     FSLPQPQQDG GGGASSGGGV TPLVEYEDVS SQSEQGLLLG GASAATAATA AGGTGGNGGS
     PASSSGTQRR AEGSERRPRR DRRSSSGRSK ERHREHRRRD GTRSGSEASK ARSRHGHSGE
     ERAEAAKSGS SSSSGGRRKS ASATSSSSSS RKDRDLKAHR SRTKSSKEPP SAYKEPPKAY
     REDKSEPKAY RRRQRSLSPL GGRDESPVSH RASQSLRSRK SPSPAGGGSS PYSRRLPRSP
     SPYSRRRSPS YSRHSSYERG GDVSPSPYSS SSWRRSRSPY SPVLRRSAKS RSRSPYSSRH
     SRSRSRHRLS RSRSRHSSIS PSTLTLKSSL AAELNKNKKA RAAEAARAAE AAKAAEAAKA
     AEAAAKAAKA SNASTPTKGN TETGASVSQT NHVKEVKKLK TEHAPSPSSG GTVKSDKAKT
     KPPLQVTKVD NNLTVEKATK KTVVGKESKP AATKEEPVST KEKSKPLTPS TGAKEKEQHV
     ALVTSTLPPL PLPPMLPEDK DADSLRGNIS VKAVKKEVEK KLRCLLADLP LPPELPGGDD
     LSKSPEEKKT AAQLHSKRRP KICGPRYGEI KEKDIDWGKR CVDKFDIIGI IGEGTYGQVY
     KARDKDTGEM VALKKVRLDN EKEGFPITAI REIKILRQLT HQSIINMKEI VTDKEDALDF
     KKDKGAFYLV FEYMDHDLMG LLESGLVHFN ENHIKSFMRQ LMEGLDYCHK KNFLHRDIKC
     SNILLNNRGQ IKLADFGLAR LYSSEESRPY TNKVITLWYR PPELLLGEER YTPAIDVWSC
     GCILGELFTK KPIFQANQEL AQLELISRIC GSPCPAVWPD VIKLPYFNTM KPKKQYRRKL
     REEFVFIPAA ALDLFDYMLA LDPSKRCTAE QALQCEFLRD VEPSKMPPPD LPLWQDCHEL
     WSKKRRRQKQ MGMTDDLSTI KAPRKDLSLG LDDSRTNTPQ GVLPPAQLKS QSNSNVAPVI
     TGPGQPLNHS ELAILLNLLQ SKSSVNMADF VQVLNIKVNS ETQQQLNKIN LPAGILATGE
     KQTDPSTPQQ ESSKSLGGVQ PSQTIQPKVE TDAAQAAVQS AFAVLLTQLI KAQQSKQKDA
     MLEERENGSG HEAPLQLRPP LEPSTPGSGQ DDLIQHQDRR ILELTPEPDR PRILPPDQRP
     PEPPEPPPVT EEDLDYRTEN QHVPTTSSSL TDPHAGVKAA LLQLLAQHQP QDDPKREGGI
     DYPTGDTYVP SSDYKDNFGS SFSAAPYVSS DGLGSSSAAA PLEARSFIGN SDIQSLDNYS
     TASSHTGGPP QTSAFTESFA SSVAGYGDIY LNAGPMLFSG DKDHRFEYSH GPITVLTNSN
     DPSTGPESTH PLPAKMHNYN YGGNLQENPG GPSLMHGQTW TSPAQGPGYS QGYRGHISTS
     AGRGRGRGLP Y
//