CDK13_MOUSE
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 03-AUG-2022, entry version 157.
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, 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 [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 iPTMnet; Q69ZA1; -.
DR PhosphoSitePlus; Q69ZA1; -.
DR EPD; Q69ZA1; -.
DR jPOST; Q69ZA1; -.
DR MaxQB; Q69ZA1; -.
DR PaxDb; Q69ZA1; -.
DR PeptideAtlas; Q69ZA1; -.
DR PRIDE; Q69ZA1; -.
DR ProteomicsDB; 280038; -. [Q69ZA1-1]
DR ProteomicsDB; 280039; -. [Q69ZA1-2]
DR Antibodypedia; 26726; 208 antibodies from 28 providers.
DR DNASU; 69562; -.
DR Ensembl; ENSMUST00000042365; ENSMUSP00000036013; ENSMUSG00000041297. [Q69ZA1-1]
DR Ensembl; ENSMUST00000223490; ENSMUSP00000152820; ENSMUSG00000041297. [Q69ZA1-2]
DR GeneID; 69562; -.
DR KEGG; mmu:69562; -.
DR UCSC; uc007poc.2; mouse. [Q69ZA1-1]
DR UCSC; uc007pod.2; mouse. [Q69ZA1-2]
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; REAPQAY; -.
DR OrthoDB; 925637at2759; -.
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 78 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 225 other tissues.
DR ExpressionAtlas; Q69ZA1; baseline and differential.
DR Genevisible; Q69ZA1; MM.
DR GO; GO:0002945; C:cyclin K-CDK13 complex; ISO:MGI.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
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; IBA:GO_Central.
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:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:MGI.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 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
