CTR9_MOUSE
ID CTR9_MOUSE Reviewed; 1173 AA.
AC Q62018; Q3UFF5; Q3UY40; Q66JX4; Q7TPS6; Q8BND9; Q8BRD1; Q8C9W7; Q8C9Y3;
AC Q8CHI1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=RNA polymerase-associated protein CTR9 homolog;
DE AltName: Full=SH2 domain-binding protein 1;
DE AltName: Full=Tetratricopeptide repeat-containing, SH2-binding phosphoprotein of 150 kDa;
DE Short=TPR-containing, SH2-binding phosphoprotein of 150 kDa;
DE Short=p150TSP;
GN Name=Ctr9; Synonyms=Kiaa0155, Sh2bp1;
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 1), SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RC TISSUE=Lymphoma;
RX PubMed=8636124; DOI=10.1074/jbc.271.12.6952;
RA Malek S.N., Yang C.H., Earnshaw W.C., Kozak C.A., Desiderio S.;
RT "p150TSP, a conserved nuclear phosphoprotein that contains multiple
RT tetratricopeptide repeats and binds specifically to SH2 domains.";
RL J. Biol. Chem. 271:6952-6962(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1-955 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Olfactory bulb, Pancreas, Spinal ganglion, and Thymus;
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 MRNA] OF 1-936 (ISOFORM 1).
RC STRAIN=129, and C3H/He; TISSUE=Mammary tumor, and Osteoblast;
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 705-1173 (ISOFORM 3), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH STAT3.
RX PubMed=17911113; DOI=10.1074/jbc.m705411200;
RA Youn M.Y., Yoo H.S., Kim M.J., Hwang S.Y., Choi Y., Desiderio S.V.,
RA Yoo J.Y.;
RT "hCTR9, a component of Paf1 complex, participates in the transcription of
RT interleukin 6-responsive genes through regulation of STAT3-DNA
RT interactions.";
RL J. Biol. Chem. 282:34727-34734(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, 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 [8]
RP FUNCTION.
RX PubMed=19345177; DOI=10.1016/j.stem.2009.03.009;
RA Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M., Heninger A.K.,
RA de Vries I., Kittler R., Junqueira M., Shevchenko A., Schulz H., Hubner N.,
RA Doss M.X., Sachinidis A., Hescheler J., Iacone R., Anastassiadis K.,
RA Stewart A.F., Pisabarro M.T., Caldarelli A., Poser I., Theis M.,
RA Buchholz F.;
RT "A genome-scale RNAi screen for Oct4 modulators defines a role of the Paf1
RT complex for embryonic stem cell identity.";
RL Cell Stem Cell 4:403-415(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-970;
RP SER-1037; SER-1039; SER-1041; SER-1079; SER-1083 AND SER-1085, 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 [11]
RP INTERACTION WITH SETD5.
RX PubMed=27864380; DOI=10.1242/dev.141465;
RA Osipovich A.B., Gangula R., Vianna P.G., Magnuson M.A.;
RT "Setd5 is essential for mammalian development and the co-transcriptional
RT regulation of histone acetylation.";
RL Development 143:4595-4607(2016).
RN [12]
RP SUBUNIT.
RX PubMed=27749823; DOI=10.1038/ncb3424;
RA Strikoudis A., Lazaris C., Trimarchi T., Galvao Neto A.L., Yang Y.,
RA Ntziachristos P., Rothbart S., Buckley S., Dolgalev I., Stadtfeld M.,
RA Strahl B.D., Dynlacht B.D., Tsirigos A., Aifantis I.;
RT "Regulation of transcriptional elongation in pluripotency and cell
RT differentiation by the PHD-finger protein Phf5a.";
RL Nat. Cell Biol. 18:1127-1138(2016).
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II and is implicated
CC in regulation of development and maintenance of embryonic stem cell
CC pluripotency. PAF1C associates with RNA polymerase II through
CC interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-
CC 5'-phosphorylated forms and is involved in transcriptional elongation,
CC acting both independently and synergistically with TCEA1 and in
CC cooperation with the DSIF complex and HTATSF1. PAF1C is required for
CC transcription of Hox and Wnt target genes. PAF1C is involved in
CC hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1.
CC PAF1C is involved in histone modifications such as ubiquitination of
CC histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C
CC recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2
CC enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of
CC 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
CC ubiquitination is proposed to be coupled to transcription. PAF1C is
CC involved in mRNA 3' end formation probably through association with
CC cleavage and poly(A) factors. Required for mono- and trimethylation on
CC histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79'
CC (H3K4me3). Required for Hox gene transcription (By similarity).
CC Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on
CC genes involved in stem cell pluripotency; this function is synergistic
CC with CXXC1 indicative for an involvement of the SET1 complex. Involved
CC in transcriptional regulation of IL6-responsive genes and in JAK-STAT
CC pathway; may regulate DNA-association of STAT3.
CC {ECO:0000250|UniProtKB:Q6PD62, ECO:0000269|PubMed:17911113,
CC ECO:0000269|PubMed:19345177}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and WDR61 (By similarity). The PAF1 complex interacts
CC with PHF5A (PubMed:27749823). Interacts with KMT2A/MLL1 (By
CC similarity). Interacts with STAT3 (PubMed:17911113). Interacts with
CC SETD5 (PubMed:27864380). Interacts with ERCC6 (By similarity).
CC {ECO:0000250|UniProtKB:Q6PD62, ECO:0000269|PubMed:17911113,
CC ECO:0000269|PubMed:27749823, ECO:0000269|PubMed:27864380}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:8636124}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q62018-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62018-2; Sequence=VSP_017846, VSP_017847;
CC Name=3;
CC IsoId=Q62018-3; Sequence=VSP_017848, VSP_017849;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12465718}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53910.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 937.; Evidence={ECO:0000305};
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DR EMBL; L49502; AAC42083.1; -; mRNA.
DR EMBL; AK040205; BAC30540.1; -; mRNA.
DR EMBL; AK040331; BAC30566.1; -; mRNA.
DR EMBL; AK045101; BAC32223.1; -; mRNA.
DR EMBL; AK083921; BAC39065.2; -; mRNA.
DR EMBL; AK134990; BAE22373.1; -; mRNA.
DR EMBL; AK148536; BAE28606.1; -; mRNA.
DR EMBL; BC053910; AAH53910.1; ALT_SEQ; mRNA.
DR EMBL; BC080719; AAH80719.1; -; mRNA.
DR EMBL; AB093211; BAC41395.1; -; Transcribed_RNA.
DR CCDS; CCDS21750.1; -. [Q62018-1]
DR PIR; T42719; T42719.
DR RefSeq; NP_033457.2; NM_009431.2. [Q62018-1]
DR AlphaFoldDB; Q62018; -.
DR SMR; Q62018; -.
DR BioGRID; 204339; 21.
DR IntAct; Q62018; 6.
DR MINT; Q62018; -.
DR STRING; 10090.ENSMUSP00000005749; -.
DR iPTMnet; Q62018; -.
DR PhosphoSitePlus; Q62018; -.
DR EPD; Q62018; -.
DR jPOST; Q62018; -.
DR MaxQB; Q62018; -.
DR PaxDb; Q62018; -.
DR PeptideAtlas; Q62018; -.
DR PRIDE; Q62018; -.
DR ProteomicsDB; 285416; -. [Q62018-1]
DR ProteomicsDB; 285417; -. [Q62018-2]
DR ProteomicsDB; 285418; -. [Q62018-3]
DR Antibodypedia; 24416; 202 antibodies from 27 providers.
DR Ensembl; ENSMUST00000005749; ENSMUSP00000005749; ENSMUSG00000005609. [Q62018-1]
DR GeneID; 22083; -.
DR KEGG; mmu:22083; -.
DR UCSC; uc009jfw.1; mouse. [Q62018-2]
DR UCSC; uc009jfx.1; mouse. [Q62018-1]
DR CTD; 9646; -.
DR MGI; MGI:109345; Ctr9.
DR VEuPathDB; HostDB:ENSMUSG00000005609; -.
DR eggNOG; KOG2002; Eukaryota.
DR GeneTree; ENSGT00390000005097; -.
DR HOGENOM; CLU_006386_0_0_1; -.
DR InParanoid; Q62018; -.
DR OMA; MSNCIEI; -.
DR PhylomeDB; Q62018; -.
DR TreeFam; TF314342; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR BioGRID-ORCS; 22083; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Ctr9; mouse.
DR PRO; PR:Q62018; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q62018; protein.
DR Bgee; ENSMUSG00000005609; Expressed in placenta labyrinth and 262 other tissues.
DR Genevisible; Q62018; MM.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0042169; F:SH2 domain binding; IDA:MGI.
DR GO; GO:0001832; P:blastocyst growth; IMP:MGI.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0001711; P:endodermal cell fate commitment; IMP:UniProtKB.
DR GO; GO:0033523; P:histone H2B ubiquitination; ISO:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0010390; P:histone monoubiquitination; ISO:MGI.
DR GO; GO:0001826; P:inner cell mass cell differentiation; IMP:MGI.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; ISO:MGI.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:2001168; P:positive regulation of histone H2B ubiquitination; ISO:MGI.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:2001162; P:positive regulation of histone H3-K79 methylation; ISS:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IMP:UniProtKB.
DR GO; GO:2000653; P:regulation of genetic imprinting; IMP:MGI.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 5.
DR InterPro; IPR031101; Ctr9.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14027; PTHR14027; 1.
DR Pfam; PF13181; TPR_8; 3.
DR SMART; SM00028; TPR; 10.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 10.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Transcription; Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..1173
FT /note="RNA polymerase-associated protein CTR9 homolog"
FT /id="PRO_0000231589"
FT REPEAT 41..75
FT /note="TPR 1"
FT REPEAT 129..162
FT /note="TPR 2"
FT REPEAT 163..196
FT /note="TPR 3"
FT REPEAT 198..231
FT /note="TPR 4"
FT REPEAT 235..268
FT /note="TPR 5"
FT REPEAT 306..339
FT /note="TPR 6"
FT REPEAT 341..374
FT /note="TPR 7"
FT REPEAT 412..444
FT /note="TPR 8"
FT REPEAT 451..484
FT /note="TPR 9"
FT REPEAT 497..530
FT /note="TPR 10"
FT REPEAT 531..564
FT /note="TPR 11"
FT REPEAT 566..598
FT /note="TPR 12"
FT REPEAT 613..646
FT /note="TPR 13"
FT REPEAT 647..680
FT /note="TPR 14"
FT REPEAT 681..714
FT /note="TPR 15"
FT REPEAT 717..750
FT /note="TPR 16"
FT REGION 892..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1061
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 925
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PD62"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PD62"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PD62"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PD62"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PD62"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PD62"
FT VAR_SEQ 704..721
FT /note="YENCLRKFYKHQNTEVVL -> VTSLLLRIVACNVEPWLP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017846"
FT VAR_SEQ 722..1173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017847"
FT VAR_SEQ 816..860
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12465718"
FT /id="VSP_017848"
FT VAR_SEQ 995..1032
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12465718"
FT /id="VSP_017849"
FT CONFLICT 144
FT /note="K -> Q (in Ref. 1; AAC42083)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="R -> S (in Ref. 3; AAH53910)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="E -> Q (in Ref. 2; BAC32223)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="D -> Y (in Ref. 3; AAH53910)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="V -> I (in Ref. 2; BAE22373)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="Q -> R (in Ref. 3; AAH80719)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="E -> K (in Ref. 3; AAH80719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1173 AA; 133408 MW; 2FB84564F1BEFD79 CRC64;
MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF
VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE KNKDNKKDLI TQATLLYTMA
DKIIMYDQNH LLGRACFCLL EGDKMDQADA QFHFVLNQSP NNIPALLGKA CISFNKKDYR
GALAYYKKAL RTNPGCPAEV RLGMGHCFVK LNKLEKARLA FSRALELNSK CVGALVGLAV
LELNNKEADS IKNGVQLLSR AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE
VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFASSSF VLPFFGLGQM YIYRGDKENA
SQCFEKVLKA YPNNYETMKI LGSLYAASED QEKRDIAKGH LKKVTEQYPD DVEAWIELAQ
ILEQTDIQGA LSAYGTATRI LQEKVQADVP PEILNNVGAL HFRLGNLGEA KKYFLASLDR
AKAEAEHDEH YYNAISVTTS YNLARLYEAM CEFHEAEKLY KNILREHPNY VDCYLRLGAM
ARDKGNFYEA SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPATQSD
TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDAKNLYAA NGIGAVLAHK
GYFREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA VQMYENCLRK FYKHQNTEVV
LYLARALFKC GKLQECKQTL LKARHVAPSD TVLMFNVALV LQRLATSVLK DEKSNLKEVL
NAVKELELAH RYFSYLSKVG DKMRFDLALA ASEARQCSDL LSQAQYHVAR ARKQDEEERE
LRAKQEQEKE LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNILM FTGETEATKE
KKRGGGGGRR SKKGGEFDEF VNDDTDDDLP VSKKKKRRKG SGSEQEGEEE EGGERKKKRR
RRPPKGEEGS EEEETENGPK PKKRRPPRAE KKKAPKPERL PPSMKGKIKS KAIISSSDDS
SDEDKLKIAD EGHPRNSNSD SDDDERPNRR ASSESDSDDN QNKSGSEAGS PRRSGRQESD
EDSDSDQPSR KRRRSGSEQS DNESVQSGRS PSGASENEND SRPASPSAES DHESEQGSDN
EGSGQGSGNE SEPEGSNNEA SDRGSEHGSD DSD
