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-MAY-2023, entry version 179.
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 SKIC8 (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   ProteomicsDB; 285416; -. [Q62018-1]
DR   ProteomicsDB; 285417; -. [Q62018-2]
DR   ProteomicsDB; 285418; -. [Q62018-3]
DR   Antibodypedia; 24416; 203 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000005749.6; ENSMUSP00000005749.6; ENSMUSG00000005609.17.
DR   GeneID; 22083; -.
DR   KEGG; mmu:22083; -.
DR   UCSC; uc009jfw.1; mouse. [Q62018-2]
DR   UCSC; uc009jfx.1; mouse. [Q62018-1]
DR   AGR; MGI:109345; -.
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; EHWLTIA; -.
DR   OrthoDB; 3573659at2759; -.
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 81 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; ISO:MGI.
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: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:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
DR   GO; GO:2001162; P:positive regulation of histone H3-K79 methylation; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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:0019827; P:stem cell population maintenance; IMP:UniProtKB.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; 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; Tetratricopeptide repeat domain; 5.
DR   InterPro; IPR031101; Ctr9.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR14027; RNA POLYMERASE-ASSOCIATED PROTEIN CTR9; 1.
DR   PANTHER; PTHR14027:SF2; RNA POLYMERASE-ASSOCIATED PROTEIN CTR9 HOMOLOG; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF13181; TPR_8; 3.
DR   SMART; SM00028; TPR; 10.
DR   SUPFAM; SSF81901; HCP-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 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
//