ID NFIC_HUMAN Reviewed; 508 AA. AC P08651; A8K1H0; B7Z4U5; B7Z9C3; K7EMU1; P08652; Q14932; Q9UPJ3; Q9UPJ9; AC Q9UPK0; Q9UPK1; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 27-MAR-2024, entry version 222. DE RecName: Full=Nuclear factor 1 C-type; DE Short=NF1-C; DE Short=Nuclear factor 1/C; DE AltName: Full=CCAAT-box-binding transcription factor; DE Short=CTF; DE AltName: Full=Nuclear factor I/C; DE Short=NF-I/C; DE Short=NFI-C; DE AltName: Full=TGGCA-binding protein; GN Name=NFIC; Synonyms=NFI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND PARTIAL PROTEIN RP SEQUENCE. RX PubMed=3398920; DOI=10.1038/334218a0; RA Santoro C., Mermod N., Andrews P.C., Tjian R.; RT "A family of human CCAAT-box-binding proteins active in transcription and RT DNA replication: cloning and expression of multiple cDNAs."; RL Nature 334:218-224(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). RX PubMed=8710515; DOI=10.1093/nar/24.12.2416; RA Wenzelides S., Altmann S., Wendler W., Winnacker E.L.; RT "CTF5 -- a new transcriptional activator of the NFI/CTF family."; RL Nucleic Acids Res. 24:2416-2421(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 6). RC TISSUE=Caudate nucleus, Heart, and Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Uterus; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-323; SER-333 AND RP SER-339, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-194; SER-323; SER-333; SER-337; SER-339; SER-343 AND RP SER-487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305; SER-323; SER-333; RP SER-339 AND SER-343, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-304; SER-333; RP SER-339; SER-343; SER-475 AND SER-477, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-365; ARG-395 AND ARG-451, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [16] RP 9AATAD MOTIF. RX PubMed=31375868; DOI=10.1007/s00018-019-03251-w; RA Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.; RT "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with RT valines and intron reservoirs."; RL Cell. Mol. Life Sci. 77:1793-1810(2020). CC -!- FUNCTION: Recognizes and binds the palindromic sequence 5'- CC TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the CC origin of replication of adenovirus type 2. These proteins are CC individually capable of activating transcription and replication. CC -!- SUBUNIT: Binds DNA as a homodimer. CC -!- INTERACTION: CC P08651; O00712: NFIB; NbExp=5; IntAct=EBI-741360, EBI-10963452; CC P08651-5; P07101-3: TH; NbExp=3; IntAct=EBI-18939222, EBI-12001016; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=4; CC IsoId=P08651-1; Sequence=Displayed; CC Name=1; CC IsoId=P08651-2; Sequence=VSP_003552; CC Name=2; CC IsoId=P08651-3; Sequence=VSP_003552, VSP_003555, VSP_003556; CC Name=3; CC IsoId=P08651-4; Sequence=VSP_003552, VSP_003553, VSP_003555, CC VSP_003556; CC Name=5; CC IsoId=P08651-5; Sequence=VSP_003554; CC Name=6; CC IsoId=P08651-6; Sequence=VSP_047539; CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large CC number of yeast and animal transcription factors. CC {ECO:0000269|PubMed:31375868}. CC -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE- CC ProRule:PRU00436}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X12492; CAA31012.1; -; mRNA. DR EMBL; X92857; CAA63440.1; -; mRNA. DR EMBL; AK289885; BAF82574.1; -; mRNA. DR EMBL; AK297867; BAH12681.1; -; mRNA. DR EMBL; AK304816; BAH14259.1; -; mRNA. DR EMBL; AC005514; AAC32593.1; -; Genomic_DNA. DR EMBL; AC005514; AAC32594.1; -; Genomic_DNA. DR EMBL; AC005551; AAC33190.1; -; Genomic_DNA. DR EMBL; AC005551; AAC33191.1; -; Genomic_DNA. DR EMBL; AC005551; AAC33192.1; -; Genomic_DNA. DR EMBL; AC005778; AAC62842.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69325.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69326.1; -; Genomic_DNA. DR EMBL; BC012120; AAH12120.1; -; mRNA. DR CCDS; CCDS12107.1; -. [P08651-5] DR CCDS; CCDS45914.1; -. [P08651-2] DR CCDS; CCDS58640.1; -. [P08651-3] DR CCDS; CCDS59330.1; -. [P08651-1] DR CCDS; CCDS59331.1; -. [P08651-6] DR PIR; B33416; B33416. DR PIR; S01038; S01038. DR RefSeq; NP_001231931.1; NM_001245002.1. [P08651-1] DR RefSeq; NP_001231933.1; NM_001245004.1. [P08651-6] DR RefSeq; NP_001231934.1; NM_001245005.1. [P08651-3] DR RefSeq; NP_005588.2; NM_005597.3. [P08651-5] DR RefSeq; NP_995315.1; NM_205843.2. [P08651-2] DR RefSeq; XP_016882324.1; XM_017026835.1. DR AlphaFoldDB; P08651; -. DR SMR; P08651; -. DR BioGRID; 110854; 200. DR DIP; DIP-44692N; -. DR IntAct; P08651; 144. DR MINT; P08651; -. DR STRING; 9606.ENSP00000396843; -. DR GlyCosmos; P08651; 1 site, 1 glycan. DR GlyGen; P08651; 9 sites, 1 O-linked glycan (9 sites). DR iPTMnet; P08651; -. DR PhosphoSitePlus; P08651; -. DR SwissPalm; P08651; -. DR BioMuta; NFIC; -. DR DMDM; 14195672; -. DR EPD; P08651; -. DR jPOST; P08651; -. DR MassIVE; P08651; -. DR MaxQB; P08651; -. DR PaxDb; 9606-ENSP00000396843; -. DR PeptideAtlas; P08651; -. DR ProteomicsDB; 52148; -. [P08651-1] DR ProteomicsDB; 52149; -. [P08651-2] DR ProteomicsDB; 52150; -. [P08651-3] DR ProteomicsDB; 52151; -. [P08651-4] DR ProteomicsDB; 52152; -. [P08651-5] DR Pumba; P08651; -. DR Antibodypedia; 23195; 333 antibodies from 31 providers. DR DNASU; 4782; -. DR Ensembl; ENST00000341919.7; ENSP00000342194.2; ENSG00000141905.19. [P08651-5] DR Ensembl; ENST00000395111.7; ENSP00000378543.2; ENSG00000141905.19. [P08651-3] DR Ensembl; ENST00000443272.3; ENSP00000396843.2; ENSG00000141905.19. [P08651-1] DR Ensembl; ENST00000586919.5; ENSP00000465177.1; ENSG00000141905.19. [P08651-4] DR Ensembl; ENST00000589123.5; ENSP00000465655.1; ENSG00000141905.19. [P08651-2] DR Ensembl; ENST00000590282.5; ENSP00000466647.1; ENSG00000141905.19. [P08651-6] DR GeneID; 4782; -. DR KEGG; hsa:4782; -. DR MANE-Select; ENST00000443272.3; ENSP00000396843.2; NM_001245002.2; NP_001231931.1. DR UCSC; uc002lxo.3; human. [P08651-1] DR AGR; HGNC:7786; -. DR CTD; 4782; -. DR DisGeNET; 4782; -. DR GeneCards; NFIC; -. DR HGNC; HGNC:7786; NFIC. DR HPA; ENSG00000141905; Tissue enriched (skeletal). DR MIM; 600729; gene. DR neXtProt; NX_P08651; -. DR OpenTargets; ENSG00000141905; -. DR PharmGKB; PA31592; -. DR VEuPathDB; HostDB:ENSG00000141905; -. DR eggNOG; KOG3663; Eukaryota. DR GeneTree; ENSGT00950000182916; -. DR HOGENOM; CLU_012576_3_0_1; -. DR InParanoid; P08651; -. DR OMA; HISISVK; -. DR OrthoDB; 5392447at2759; -. DR PhylomeDB; P08651; -. DR PathwayCommons; P08651; -. DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination. DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation. DR SignaLink; P08651; -. DR SIGNOR; P08651; -. DR BioGRID-ORCS; 4782; 31 hits in 1180 CRISPR screens. DR ChiTaRS; NFIC; human. DR GeneWiki; NFIC_(gene); -. DR GenomeRNAi; 4782; -. DR Pharos; P08651; Tbio. DR PRO; PR:P08651; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P08651; Protein. DR Bgee; ENSG00000141905; Expressed in nipple and 205 other cell types or tissues. DR ExpressionAtlas; P08651; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR InterPro; IPR000647; CTF/NFI. DR InterPro; IPR020604; CTF/NFI_DNA-bd-dom. DR InterPro; IPR019739; CTF/NFI_DNA-bd_CS. DR InterPro; IPR019548; CTF/NFI_DNA-bd_N. DR InterPro; IPR003619; MAD_homology1_Dwarfin-type. DR PANTHER; PTHR11492:SF2; NUCLEAR FACTOR 1 C-TYPE; 1. DR PANTHER; PTHR11492; NUCLEAR FACTOR I; 1. DR Pfam; PF00859; CTF_NFI; 1. DR Pfam; PF03165; MH1; 1. DR Pfam; PF10524; NfI_DNAbd_pre-N; 1. DR SMART; SM00523; DWA; 1. DR PROSITE; PS00349; CTF_NFI_1; 1. DR PROSITE; PS51080; CTF_NFI_2; 1. DR Genevisible; P08651; HS. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; Direct protein sequencing; KW DNA replication; DNA-binding; Methylation; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..508 FT /note="Nuclear factor 1 C-type" FT /id="PRO_0000100199" FT DNA_BIND 1..195 FT /note="CTF/NF-I" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00436" FT REGION 190..209 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 267..348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 438..495 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 404..412 FT /note="9aaTAD" FT /evidence="ECO:0000269|PubMed:31375868" FT COMPBIAS 194..209 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 267..281 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 297..317 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 329..348 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 462..484 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 194 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 294 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 300 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P70255" FT MOD_RES 302 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P70255" FT MOD_RES 304 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 305 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 323 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 333 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 337 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 339 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 343 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 365 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 365 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 395 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 451 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 475 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 477 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 487 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT VAR_SEQ 1..10 FT /note="MYSSPLCLTQ -> M (in isoform 1, isoform 2 and isoform FT 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:3398920" FT /id="VSP_003552" FT VAR_SEQ 188..211 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:3398920" FT /id="VSP_003553" FT VAR_SEQ 424..508 FT /note="LNGSGQLKMPSHCLSAQMLAPPPPGLPRLALPPATKPATTSEGGATSPTSPS FT YSPPDTSPANRSFVGLGPRDPAGIYQAQSWYLG -> PTLRPTRPLQTVPLWD (in FT isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047539" FT VAR_SEQ 424..503 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8710515" FT /id="VSP_003554" FT VAR_SEQ 424..439 FT /note="LNGSGQLKMPSHCLSA -> PTLRPTRPLQTVPLWD (in isoform 2 FT and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:3398920" FT /id="VSP_003555" FT VAR_SEQ 440..508 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:3398920" FT /id="VSP_003556" FT VARIANT 417 FT /note="A -> S (in dbSNP:rs10412720)" FT /id="VAR_057656" FT CONFLICT 130 FT /note="L -> P (in Ref. 3; BAH12681)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="D -> V (in Ref. 2; CAA63440)" FT /evidence="ECO:0000305" FT CONFLICT 329 FT /note="E -> K (in Ref. 3; BAH12681)" FT /evidence="ECO:0000305" FT CONFLICT 353 FT /note="H -> Y (in Ref. 3; BAH12681)" FT /evidence="ECO:0000305" SQ SEQUENCE 508 AA; 55675 MW; 3D0F97DA0F3AF992 CRC64; MYSSPLCLTQ DEFHPFIEAL LPHVRAFAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE LLGEKPEVKQ KWASRLLAKL RKDIRPECRE DFVLSITGKK APGCVLSNPD QKGKMRRIDC LRQADKVWRL DLVMVILFKG IPLESTDGER LVKAAQCGHP VLCVQPHHIG VAVKELDLYL AYFVRERDAE QSGSPRTGMG SDQEDSKPIT LDTTDFQESF VTSGVFSVTE LIQVSRTPVV TGTGPNFSLG ELQGHLAYDL NPASTGLRRT LPSTSSSGSK RHKSGSMEED VDTSPGGDYY TSPSSPTSSS RNWTEDMEGG ISSPVKKTEM DKSPFNSPSP QDSPRLSSFT QHHRPVIAVH SGIARSPHPS SALHFPTTSI LPQTASTYFP HTAIRYPPHL NPQDPLKDLV SLACDPASQQ PGPLNGSGQL KMPSHCLSAQ MLAPPPPGLP RLALPPATKP ATTSEGGATS PTSPSYSPPD TSPANRSFVG LGPRDPAGIY QAQSWYLG //