ID PRP4B_MOUSE Reviewed; 1007 AA.
AC Q61136; B2RUN6; O88378; Q8BND8; Q8R4Y5; Q9CTL9; Q9CTT0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 24-JAN-2024, entry version 191.
DE RecName: Full=Serine/threonine-protein kinase PRP4 homolog;
DE EC=2.7.11.1;
DE AltName: Full=PRP4 pre-mRNA-processing factor 4 homolog;
DE AltName: Full=Pre-mRNA protein kinase;
GN Name=Prpf4b; Synonyms=Cbp143, Prp4h, Prp4k, Prp4m, Prpk;
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].
RX PubMed=12077342; DOI=10.1128/mcb.22.14.5141-5156.2002;
RA Dellaire G., Makarov E.M., Cowger J.J.M., Longman D., Sutherland H.G.E.,
RA Luehrmann R., Torchia J., Bickmore W.A.;
RT "Mammalian PRP4 kinase copurifies and interacts with components of both the
RT U5 snRNP and the N-CoR deacetylase complexes.";
RL Mol. Cell. Biol. 22:5141-5156(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, Spinal ganglion, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 185-1007.
RX PubMed=9701556; DOI=10.1242/jcs.111.17.2575;
RA Tate P., Lee M., Tweedie S., Skarnes W.C., Bickmore W.A.;
RT "Capturing novel mouse genes encoding chromosomal and other nuclear
RT proteins.";
RL J. Cell Sci. 111:2575-2585(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 512-1007.
RX PubMed=9102632; DOI=10.1093/nar/25.5.1028;
RA Gross T., Lutzelberger M., Wiegmann H., Klingenhoff A., Shenoy S.,
RA Kaeufer N.F.;
RT "Functional analysis of the fission yeast Prp4 protein kinase involved in
RT pre-mRNA splicing and isolation of a putative mammalian homologue.";
RL Nucleic Acids Res. 25:1028-1035(1997).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-94; SER-431; SER-437
RP AND TYR-849, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-33; SER-88;
RP SER-94; TYR-141; SER-143; SER-145; SER-578; SER-580 AND TYR-849, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBUNIT: Identified in the spliceosome C complex (By similarity).
CC Interacts with Clk1 C-terminus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated by Clk1.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF283466; AAM19102.1; -; mRNA.
DR EMBL; AK020579; BAB32137.3; -; mRNA.
DR EMBL; AK021274; BAB32358.3; -; mRNA.
DR EMBL; AK083926; BAC39069.1; -; mRNA.
DR EMBL; CH466546; EDL40895.1; -; Genomic_DNA.
DR EMBL; BC141272; AAI41273.1; -; mRNA.
DR EMBL; BC141273; AAI41274.1; -; mRNA.
DR EMBL; AF033663; AAC32042.1; -; mRNA.
DR EMBL; U48737; AAB03269.1; -; mRNA.
DR CCDS; CCDS26448.1; -.
DR RefSeq; NP_038858.2; NM_013830.2.
DR RefSeq; XP_017170914.1; XM_017315425.1.
DR RefSeq; XP_017170915.1; XM_017315426.1.
DR RefSeq; XP_017170916.1; XM_017315427.1.
DR RefSeq; XP_017170917.1; XM_017315428.1.
DR RefSeq; XP_017170918.1; XM_017315429.1.
DR RefSeq; XP_017170919.1; XM_017315430.1.
DR RefSeq; XP_017170920.1; XM_017315431.1.
DR RefSeq; XP_017170921.1; XM_017315432.1.
DR RefSeq; XP_017170922.1; XM_017315433.1.
DR RefSeq; XP_017170923.1; XM_017315434.1.
DR RefSeq; XP_017170924.1; XM_017315435.1.
DR RefSeq; XP_017170925.1; XM_017315436.1.
DR RefSeq; XP_017170926.1; XM_017315437.1.
DR AlphaFoldDB; Q61136; -.
DR SMR; Q61136; -.
DR BioGRID; 202400; 33.
DR IntAct; Q61136; 2.
DR MINT; Q61136; -.
DR STRING; 10090.ENSMUSP00000077019; -.
DR GlyGen; Q61136; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q61136; -.
DR PhosphoSitePlus; Q61136; -.
DR EPD; Q61136; -.
DR jPOST; Q61136; -.
DR MaxQB; Q61136; -.
DR PaxDb; 10090-ENSMUSP00000077019; -.
DR ProteomicsDB; 291666; -.
DR Pumba; Q61136; -.
DR Antibodypedia; 9532; 193 antibodies from 27 providers.
DR DNASU; 19134; -.
DR Ensembl; ENSMUST00000077853.5; ENSMUSP00000077019.4; ENSMUSG00000021413.10.
DR Ensembl; ENSMUST00000222509.2; ENSMUSP00000152654.2; ENSMUSG00000021413.10.
DR GeneID; 19134; -.
DR KEGG; mmu:19134; -.
DR UCSC; uc007qbp.2; mouse.
DR AGR; MGI:109584; -.
DR CTD; 8899; -.
DR MGI; MGI:109584; Prpf4b.
DR VEuPathDB; HostDB:ENSMUSG00000021413; -.
DR eggNOG; KOG0670; Eukaryota.
DR GeneTree; ENSGT00940000155562; -.
DR HOGENOM; CLU_000288_5_3_1; -.
DR InParanoid; Q61136; -.
DR OMA; YDKGAAY; -.
DR OrthoDB; 232702at2759; -.
DR PhylomeDB; Q61136; -.
DR TreeFam; TF315246; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 19134; 13 hits in 82 CRISPR screens.
DR ChiTaRS; Prpf4b; mouse.
DR PRO; PR:Q61136; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61136; Protein.
DR Bgee; ENSMUSG00000021413; Expressed in bone fossa and 262 other cell types or tissues.
DR ExpressionAtlas; Q61136; baseline and differential.
DR Genevisible; Q61136; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005694; C:chromosome; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14135; STKc_PRP4; 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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR044092; STKc_PRP4.
DR PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR PANTHER; PTHR24058:SF103; MITOGEN-ACTIVATED PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Isopeptide bond; Kinase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Spliceosome;
KW Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT CHAIN 2..1007
FT /note="Serine/threonine-protein kinase PRP4 homolog"
FT /id="PRO_0000086587"
FT DOMAIN 687..1006
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..59
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..499
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 815
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 693..701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 717
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RKH1"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 100
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 141
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 717
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT MOD_RES 849
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RKH1"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT CROSSLNK 593
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13523"
FT CONFLICT 185..187
FT /note="SKS -> IPG (in Ref. 5; AAC32042)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="K -> I (in Ref. 5; AAC32042)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="R -> K (in Ref. 1; AAM19102 and 5; AAC32042)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="F -> L (in Ref. 6; AAB03269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1007 AA; 116976 MW; 18E1B7371E17AB4C CRC64;
MAATEPPSLR EQAEMDDADN SEKSVNEENG EVSEDQSQNK HSRHKKKKHK HRSKHKKHKH
SSEEDRDKKH KHKHKHKKHK RKEVIEASDK EGLSPAKRTK LDDLALLEDL EKQRALIKAE
LDNELMEGKV QSGMGLILQG YESGSEEEGE IHEKARNGNR SSTRSSSTRG KLEITDNKNS
AKKRSKSRSK ERTRHRSDKR KSKGAGEMLR EKANRSKSKE RRKSKSPSKR SKSQDQARKS
KSPPLRRRSQ EKVGKARSPA EEKMKSEEKG KIKDRKKSPI VNERSRDRSK KSKSPVDLRD
KSKDRRSRSK ERKSKRSEID KEKKPIKSPS KDASSGKENR SPSRRPGRSP KRRSLSPKLR
DKSRRSRSPL LNDRRSKQSK SPSRTLSPGR RAKSRSLERK RREPERRRLS SPRTRPRDDI
LGRCERSKDA SPINRWSPTR RRSRSPIRRR SRSPLRRSRS PRRRSRSPRR RDRSRRSRSR
LRRRSRSRGG HRRRSRSKVK EDKFKGSLSE GMKVEQESSS DDNLEDFDVE EEDEEALIEQ
RRIQRQAIVQ KYKYLAEDSN ISVPSEPSSP QSSTRSRSPS PDDILERVAA DVKEYERENV
DTFEASVKAK HNLMTVEQNN GSSQKKILAP DMFTESDDMF AAYFDSARLR AAGIGKDFKE
NPNLRDNWTD AEGYYRVNIG EVLDKRYNVY GYTGQGVFSN VVRARDNARA NQEVAVKIIR
NNELMQKTGL KELEFLKKLN DADPDDKFHC LRLFRHFYHK QHLCLVFEPL SMNLREVLKK
YGKDVGLHIK AVRSYSQQLF LALKLLKRCN ILHADIKPDN ILVNESKTIL KLCDFGSASH
VADNDITPYL VSRFYRAPEI IIGKSYDYGI DMWSVGCTLY ELYTGKILFP GKTNNHMLKL
AMDLKGKMPN KMIRKGVFKD QHFDQNLNFM YIEVDKVTER EKVTVMSTIN PTKDLLADLI
GCQRLPEDQR KKVHQLKDLL DQILMLDPAK RISINQALQH AFIQEKI
//
