ID CING_HUMAN Reviewed; 1203 AA. AC Q9P2M7; A6H8L3; A7MD22; Q5T386; Q9NR25; DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 3. DT 24-JAN-2024, entry version 167. DE RecName: Full=Cingulin {ECO:0000305}; GN Name=CGN {ECO:0000312|HGNC:HGNC:17429}; Synonyms=KIAA1319; 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] (ISOFORM 1), AND SUBUNIT. RC TISSUE=Neuroepithelium; RX PubMed=11042084; DOI=10.1006/jsbi.2000.4284; RA Citi S., D'Atri F., Parry D.A.D.; RT "Human and Xenopus cingulin share a modular organization of the coiled-coil RT rod domain: predictions for intra- and intermolecular assembly."; RL J. Struct. Biol. 131:135-145(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hippocampus; 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=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). 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] (ISOFORMS 1 AND 2). 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 PROTEIN SEQUENCE OF 374-382. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP INTERACTION WITH TJP1. RX PubMed=12023291; DOI=10.1074/jbc.m203717200; RA D'Atri F., Nadalutti F., Citi S.; RT "Evidence for a functional interaction between cingulin and ZO-1 in RT cultured cells."; RL J. Biol. Chem. 277:27757-27764(2002). RN [9] RP IDENTIFICATION BY 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-1182, AND RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-165, AND RP IDENTIFICATION BY 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 [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-579, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-258, AND RP 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-140; SER-155; RP SER-165; SER-214; SER-217 AND THR-712, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-137; SER-140; RP SER-258; SER-276; SER-1175 AND SER-1176, 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 [18] RP INTERACTION WITH SPEF1, AND SUBCELLULAR LOCATION. RX PubMed=31473225; DOI=10.1053/j.gastro.2019.08.031; RA Tapia R., Perez-Yepez E.A., Carlino M.J., Karandikar U.C., Kralicek S.E., RA Estes M.K., Hecht G.A.; RT "Sperm Flagellar 1 Binds Actin in Intestinal Epithelial Cells and RT Contributes to Formation of Filopodia and Lamellipodia."; RL Gastroenterology 157:1544-1555(2019). CC -!- FUNCTION: Probably plays a role in the formation and regulation of the CC tight junction (TJ) paracellular permeability barrier. CC -!- SUBUNIT: Homodimer (PubMed:11042084). Interacts with TJP1/ZO1 CC (PubMed:12023291). Interacts with SPEF1 (PubMed:31473225). CC {ECO:0000269|PubMed:12023291, ECO:0000269|PubMed:31473225, CC ECO:0000303|PubMed:11042084}. CC -!- INTERACTION: CC Q9P2M7; P31947: SFN; NbExp=4; IntAct=EBI-79537, EBI-476295; CC Q9P2M7; P63104: YWHAZ; NbExp=4; IntAct=EBI-79537, EBI-347088; CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction CC {ECO:0000250|UniProtKB:P59242}. Note=Localizes to the apical junction CC complex composed of tight and adherens junctions (By similarity). CC Colocalizes with SPEF1 at sites of cell-cell contact in intestinal CC epithelial cells (PubMed:12023291). {ECO:0000250|UniProtKB:P59242, CC ECO:0000269|PubMed:12023291}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9P2M7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P2M7-2; Sequence=VSP_037039, VSP_037040; CC -!- TISSUE SPECIFICITY: Localized on the cytoplasmic face of tight CC junctions of polarized epithelia and some endothelia. Expressed in CC pancreas, kidney, liver and lung, but not in skeletal muscle, placenta, CC brain or heart. CC -!- DOMAIN: Deletion of the TJP1/ZO1 interaction motif (ZIM) decreases but CC does not abolish colocalization with TJP1/ZO1. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the cingulin family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI46658.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA92557.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AF263462; AAF74498.1; -; mRNA. DR EMBL; AB037740; BAA92557.1; ALT_INIT; mRNA. DR EMBL; AK290007; BAF82696.1; -; mRNA. DR EMBL; AL365436; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW53434.1; -; Genomic_DNA. DR EMBL; BC146657; AAI46658.1; ALT_INIT; mRNA. DR EMBL; BC152445; AAI52446.1; -; mRNA. DR CCDS; CCDS999.1; -. [Q9P2M7-1] DR RefSeq; NP_065821.1; NM_020770.2. [Q9P2M7-1] DR RefSeq; XP_005245422.1; XM_005245365.4. [Q9P2M7-1] DR AlphaFoldDB; Q9P2M7; -. DR SMR; Q9P2M7; -. DR BioGRID; 121589; 149. DR DIP; DIP-30947N; -. DR IntAct; Q9P2M7; 40. DR MINT; Q9P2M7; -. DR STRING; 9606.ENSP00000271636; -. DR iPTMnet; Q9P2M7; -. DR MetOSite; Q9P2M7; -. DR PhosphoSitePlus; Q9P2M7; -. DR BioMuta; CGN; -. DR DMDM; 27923755; -. DR EPD; Q9P2M7; -. DR jPOST; Q9P2M7; -. DR MassIVE; Q9P2M7; -. DR MaxQB; Q9P2M7; -. DR PaxDb; 9606-ENSP00000271636; -. DR PeptideAtlas; Q9P2M7; -. DR ProteomicsDB; 83849; -. [Q9P2M7-1] DR ProteomicsDB; 83850; -. [Q9P2M7-2] DR Pumba; Q9P2M7; -. DR Antibodypedia; 34064; 127 antibodies from 23 providers. DR DNASU; 57530; -. DR Ensembl; ENST00000271636.12; ENSP00000271636.7; ENSG00000143375.15. [Q9P2M7-1] DR GeneID; 57530; -. DR KEGG; hsa:57530; -. DR MANE-Select; ENST00000271636.12; ENSP00000271636.7; NM_020770.3; NP_065821.1. DR UCSC; uc009wmw.4; human. [Q9P2M7-1] DR AGR; HGNC:17429; -. DR CTD; 57530; -. DR DisGeNET; 57530; -. DR GeneCards; CGN; -. DR HGNC; HGNC:17429; CGN. DR HPA; ENSG00000143375; Tissue enhanced (intestine). DR MIM; 609473; gene. DR neXtProt; NX_Q9P2M7; -. DR OpenTargets; ENSG00000143375; -. DR PharmGKB; PA134938123; -. DR VEuPathDB; HostDB:ENSG00000143375; -. DR eggNOG; ENOG502R9EI; Eukaryota. DR GeneTree; ENSGT00940000154489; -. DR HOGENOM; CLU_002036_0_0_1; -. DR InParanoid; Q9P2M7; -. DR OMA; HWREMFQ; -. DR OrthoDB; 4226071at2759; -. DR PhylomeDB; Q9P2M7; -. DR TreeFam; TF332247; -. DR PathwayCommons; Q9P2M7; -. DR Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition). DR SignaLink; Q9P2M7; -. DR BioGRID-ORCS; 57530; 12 hits in 1149 CRISPR screens. DR ChiTaRS; CGN; human. DR GeneWiki; Cingulin; -. DR GenomeRNAi; 57530; -. DR Pharos; Q9P2M7; Tbio. DR PRO; PR:Q9P2M7; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9P2M7; Protein. DR Bgee; ENSG00000143375; Expressed in pancreatic ductal cell and 148 other cell types or tissues. DR ExpressionAtlas; Q9P2M7; baseline and differential. DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0016459; C:myosin complex; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR InterPro; IPR002928; Myosin_tail. DR PANTHER; PTHR46349:SF4; CINGULIN; 1. DR PANTHER; PTHR46349; CINGULIN-LIKE PROTEIN 1-RELATED; 1. DR Pfam; PF01576; Myosin_tail_1; 1. DR Genevisible; Q9P2M7; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell junction; Coiled coil; KW Direct protein sequencing; Phosphoprotein; Reference proteome; KW Tight junction. FT CHAIN 1..1203 FT /note="Cingulin" FT /id="PRO_0000089763" FT REGION 7..357 FT /note="Head" FT REGION 25..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 54..67 FT /note="Interaction with TJP1/ZO1" FT /evidence="ECO:0000269|PubMed:12023291" FT REGION 89..127 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 186..266 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1034..1053 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1154..1181 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1161..1203 FT /note="Tail" FT COILED 358..1160 FT /evidence="ECO:0000255" FT MOTIF 48..62 FT /note="ZIM" FT COMPBIAS 109..124 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 200..233 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 234..266 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 95 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P59242" FT MOD_RES 96 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P59242" FT MOD_RES 135 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 137 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 155 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 214 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 217 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 258 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 276 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 338 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P59242" FT MOD_RES 351 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P59242" FT MOD_RES 579 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 712 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1175 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1176 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1182 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 704..777 FT /note="KMVAEAEATVLGQRRAAVETTLRETQEENDEFRRRILGLEQQLKETRGLVDG FT GEAVEARLRDKLQRLEAEKQQL -> RGVGTGLRRWRLRVSGGLRSQRVWKVTCHGYVL FT TSSWVLGMWFKEARIWQGEDTCICVGVGFSEKRLAGGSCSL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_037039" FT VAR_SEQ 778..1203 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_037040" FT VARIANT 485 FT /note="R -> Q (in dbSNP:rs12038198)" FT /id="VAR_057809" SQ SEQUENCE 1203 AA; 137057 MW; 0AE294110E605765 CRC64; MEQAPNMAEP RGPVDHGVQI RFITEPVSGA EMGTLRRGGR RPAKDARAST YGVAVRVQGI AGQPFVVLNS GEKGGDSFGV QIKGANDQGA SGALSSDLEL PENPYSQVKG FPAPSQSSTS DEEPGAYWNG KLLRSHSQAS LAGPGPVDPS NRSNSMLELA PKVASPGSTI DTAPLSSVDS LINKFDSQLG GQARGRTGRR TRMLPPEQRK RSKSLDSRLP RDTFEERERQ STNHWTSSTK YDNHVGTSKQ PAQSQNLSPL SGFSRSRQTQ DWVLQSFEEP RRSAQDPTML QFKSTPDLLR DQQEAAPPGS VDHMKATIYG ILREGSSESE TSVRRKVSLV LEKMQPLVMV SSGSTKAVAG QGELTRKVEE LQRKLDEEVK KRQKLEPSQV GLERQLEEKT EECSRLQELL ERRKGEAQQS NKELQNMKRL LDQGEDLRHG LETQVMELQN KLKHVQGPEP AKEVLLKDLL ETRELLEEVL EGKQRVEEQL RLRERELTAL KGALKEEVAS RDQEVEHVRQ QYQRDTEQLR RSMQDATQDH AVLEAERQKM SALVRGLQRE LEETSEETGH WQSMFQKNKE DLRATKQELL QLRMEKEEME EELGEKIEVL QRELEQARAS AGDTRQVEVL KKELLRTQEE LKELQAERQS QEVAGRHRDR ELEKQLAVLR VEADRGRELE EQNLQLQKTL QQLRQDCEEA SKAKMVAEAE ATVLGQRRAA VETTLRETQE ENDEFRRRIL GLEQQLKETR GLVDGGEAVE ARLRDKLQRL EAEKQQLEEA LNASQEEEGS LAAAKRALEA RLEEAQRGLA RLGQEQQTLN RALEEEGKQR EVLRRGKAEL EEQKRLLDRT VDRLNKELEK IGEDSKQALQ QLQAQLEDYK EKARREVADA QRQAKDWASE AEKTSGGLSR LQDEIQRLRQ ALQASQAERD TARLDKELLA QRLQGLEQEA ENKKRSQDDR ARQLKGLEEK VSRLETELDE EKNTVELLTD RVNRGRDQVD QLRTELMQER SARQDLECDK ISLERQNKDL KTRLASSEGF QKPSASLSQL ESQNQLLQER LQAEEREKTV LQSTNRKLER KVKELSIQIE DERQHVNDQK DQLSLRVKAL KRQVDEAEEE IERLDGLRKK AQREVEEQHE VNEQLQARIK SLEKDSWRKA SRSAAESALK NEGLSSDEEF DSVYDPSSIA SLLTESNLQT SSC //