ID CE170_MOUSE Reviewed; 1588 AA. AC Q6A065; Q7TQD9; Q8BJW2; Q9D3Z0; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 2. DT 24-JAN-2024, entry version 135. DE RecName: Full=Centrosomal protein of 170 kDa; DE Short=Cep170; GN Name=Cep170; Synonyms=Kiaa0470; 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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1462-1588 (ISOFORMS 1/3). RC STRAIN=C57BL/6J; TISSUE=Muellerian duct, and Testis; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 786-1588 (ISOFORM 1). RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-1102, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443 AND SER-829, AND RP IDENTIFICATION BY 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-358; SER-443; RP SER-829; SER-1008; THR-1012; SER-1102; SER-1150; SER-1155; SER-1229; RP SER-1521 AND SER-1522, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, 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 [9] RP SUBCELLULAR LOCATION. RX PubMed=23386061; DOI=10.1038/emboj.2013.3; RA Kodani A., Salome Sirerol-Piquer M., Seol A., Garcia-Verdugo J.M., RA Reiter J.F.; RT "Kif3a interacts with Dynactin subunit p150 Glued to organize centriole RT subdistal appendages."; RL EMBO J. 32:597-607(2013). RN [10] RP INTERACTION WITH NIN. RX PubMed=27565344; DOI=10.1016/j.cell.2016.07.025; RA Zhang X., Chen M.H., Wu X., Kodani A., Fan J., Doan R., Ozawa M., Ma J., RA Yoshida N., Reiter J.F., Black D.L., Kharchenko P.V., Sharp P.A., RA Walsh C.A.; RT "Cell-type-specific alternative splicing governs cell fate in the RT developing cerebral cortex."; RL Cell 166:1147-1162(2016). RN [11] RP INTERACTION WITH FHDC1. RX PubMed=29742020; DOI=10.1091/mbc.e18-02-0088; RA Copeland S.J., McRae A., Guarguaglini G., Trinkle-Mulcahy L., RA Copeland J.W.; RT "Actin-dependent regulation of cilia length by the inverted formin FHDC1."; RL Mol. Biol. Cell 29:1611-1627(2018). CC -!- FUNCTION: Plays a role in microtubule organization. Required for CC centriole subdistal appendage assembly. {ECO:0000250|UniProtKB:Q5SW79}. CC -!- SUBUNIT: Interacts with CCDC68 and CCDC120; leading to recruitment to CC centrosomes (By similarity). Interacts with PLK1 (By similarity). CC Interacts with NIN (PubMed:27565344). Interacts with FHDC1 CC (PubMed:29742020). Interacts with CCDC61 (By similarity). Interacts CC with TBK1; efficient complex formation may be dependent on the presence CC of CCDC61 (By similarity). {ECO:0000250|UniProtKB:Q5SW79, CC ECO:0000269|PubMed:27565344, ECO:0000269|PubMed:29742020}. CC -!- INTERACTION: CC Q6A065; Q9NRI5: DISC1; Xeno; NbExp=2; IntAct=EBI-2554140, EBI-529989; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000250|UniProtKB:Q5SW79}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome, centriole CC {ECO:0000269|PubMed:23386061}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000250|UniProtKB:Q5SW79}. Note=Associated with the mature mother CC centriole. Associated with spindle microtubules during mitosis (By CC similarity). Localizes to the distal appendage region of the centriole CC (By similarity). Localizes at the centriole proximal ends (By CC similarity). {ECO:0000250|UniProtKB:Q5SW79, CC ECO:0000269|PubMed:23386061}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6A065-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6A065-2; Sequence=VSP_024244, VSP_024245; CC Name=3; CC IsoId=Q6A065-3; Sequence=VSP_024243, VSP_024246; CC -!- PTM: Phosphorylated; probably by PLK1. CC -!- SIMILARITY: Belongs to the CEP170 family. {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; AK016937; BAB30507.2; -; mRNA. DR EMBL; AK078541; BAC37328.1; -; mRNA. DR EMBL; AC113311; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC054781; AAH54781.1; -; mRNA. DR EMBL; BC057019; AAH57019.1; -; mRNA. DR EMBL; AK172953; BAD32231.1; -; mRNA. DR RefSeq; XP_006497000.1; XM_006496937.3. [Q6A065-1] DR AlphaFoldDB; Q6A065; -. DR SMR; Q6A065; -. DR BioGRID; 244244; 48. DR IntAct; Q6A065; 22. DR MINT; Q6A065; -. DR STRING; 10090.ENSMUSP00000141769; -. DR ChEMBL; CHEMBL4879479; -. DR GlyGen; Q6A065; 12 sites, 1 O-linked glycan (12 sites). DR iPTMnet; Q6A065; -. DR PhosphoSitePlus; Q6A065; -. DR SwissPalm; Q6A065; -. DR EPD; Q6A065; -. DR jPOST; Q6A065; -. DR MaxQB; Q6A065; -. DR PaxDb; 10090-ENSMUSP00000059562; -. DR PeptideAtlas; Q6A065; -. DR ProteomicsDB; 281365; -. [Q6A065-1] DR ProteomicsDB; 281366; -. [Q6A065-2] DR ProteomicsDB; 281367; -. [Q6A065-3] DR Pumba; Q6A065; -. DR Antibodypedia; 34708; 141 antibodies from 21 providers. DR Ensembl; ENSMUST00000192961.6; ENSMUSP00000142271.2; ENSMUSG00000057335.12. [Q6A065-2] DR Ensembl; ENSMUST00000194727.6; ENSMUSP00000141793.2; ENSMUSG00000057335.12. [Q6A065-1] DR GeneID; 545389; -. DR UCSC; uc007dub.1; mouse. [Q6A065-3] DR UCSC; uc007duc.1; mouse. [Q6A065-1] DR UCSC; uc007dug.2; mouse. [Q6A065-2] DR AGR; MGI:1918348; -. DR CTD; 9859; -. DR MGI; MGI:1918348; Cep170. DR VEuPathDB; HostDB:ENSMUSG00000057335; -. DR eggNOG; ENOG502QSH8; Eukaryota. DR GeneTree; ENSGT00940000155103; -. DR HOGENOM; CLU_1175117_0_0_1; -. DR InParanoid; Q6A065; -. DR OrthoDB; 5489878at2759; -. DR PhylomeDB; Q6A065; -. DR BioGRID-ORCS; 545389; 2 hits in 77 CRISPR screens. DR ChiTaRS; Cep170; mouse. DR PRO; PR:Q6A065; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q6A065; Protein. DR Bgee; ENSMUSG00000057335; Expressed in cortical plate and 223 other cell types or tissues. DR ExpressionAtlas; Q6A065; baseline and differential. DR GO; GO:0120103; C:centriolar subdistal appendage; ISO:MGI. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR CDD; cd22724; FHA_Cep170A; 1. DR Gene3D; 2.60.200.20; -; 1. DR InterPro; IPR029300; CEP170_C. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR PANTHER; PTHR15715; CENTROSOMAL PROTEIN OF 170 KDA; 1. DR PANTHER; PTHR15715:SF17; CENTROSOMAL PROTEIN OF 170 KDA; 1. DR Pfam; PF15308; CEP170_C; 1. DR Pfam; PF00498; FHA; 1. DR SMART; SM00240; FHA; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR Genevisible; Q6A065; MM. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; KW Phosphoprotein; Reference proteome. FT CHAIN 1..1588 FT /note="Centrosomal protein of 170 kDa" FT /id="PRO_0000282888" FT DOMAIN 23..73 FT /note="FHA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086" FT REGION 121..172 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 299..323 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 338..447 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 461..508 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 602..854 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 844..1588 FT /note="Targeting to microtubules" FT /evidence="ECO:0000250" FT REGION 899..1222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1103..1588 FT /note="Targeting to centrosomes" FT /evidence="ECO:0000250" FT REGION 1228..1247 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1315..1334 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1370..1398 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1511..1540 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1467..1495 FT /evidence="ECO:0000255" FT COMPBIAS 121..135 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 347..415 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 484..498 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 606..635 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 639..692 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 733..757 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 762..777 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 778..792 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 793..823 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 913..940 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 969..991 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1001..1044 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1045..1062 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1066..1087 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1114..1131 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1148..1171 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1188..1222 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1515..1536 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 141 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 355 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 358 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 363 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 443 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 463 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 494 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 498 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 568 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 577 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 628 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 631 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 639 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 662 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 718 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 752 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 829 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 870 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 872 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 906 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 912 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 922 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 925 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 950 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1008 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1012 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1047 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1048 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1102 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1104 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1122 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1123 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1135 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1150 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1155 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1188 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1195 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1200 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1229 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1231 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1241 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1260 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1270 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1362 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5SW79" FT MOD_RES 1521 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1522 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 1..1257 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_024243" FT VAR_SEQ 211..236 FT /note="CSTEAKHVEGQSAAASEEALFPFCRE -> KNTSVAVASNSYWASIYSLNKS FT HSTL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024244" FT VAR_SEQ 237..1588 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024245" FT VAR_SEQ 1344..1353 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_024246" SQ SEQUENCE 1588 AA; 175050 MW; B7140E6F82AF93A7 CRC64; MSLTSWFLVS SGGTRHRLPR EMIFVGRDDC ELMLQSRSVD KQHAVINYDA SMDEHLVKDL GSLNGTFVND VRIPEQTYIT LKLEDKLRFG YDTNLFTVVR GEMRVPEEAL KHEKFTIQLQ LSQKSSESEL PKSASAKGTD SKVEAAAEVQ PRATEALKSE EKPMDVSAMP RGTPLYGQPS WWGDAEEDEQ RAFKANGKPE GKSQEAGASG CSTEAKHVEG QSAAASEEAL FPFCREPSYF EIPTKEFQQP SQIAESTIHE IPTKDTPSSH TAGAGHASFT IEFDDSTPGK VTIRDHVTKF TSDQRHKSKK ASPGTQDLPG IQTGMMAPEN KVADWLAQNN PPQMVWERTE EDSKSIKSDV PVYLKRLKGN KHDDGTQSDS ENAGAHRRCS KRATLEEHLR RHHSEQKKKA QSTEKHQEQA ATSSTHHRGG HGVPHGKLLK QKSEEPSVSL PFLQTALLRS SGSLGHRPSQ EMDVMLKNQA TSASSEKDND DDQSDKGTYT IELENPNSEE VEARKMIDKV FGVDDNQDYN RPIINEKHKG LIKDWALNSA AVVMEERKPL STPGFHNSEE AISSSGSKRW VSQWASLAAN HTRHDPEERL MELSATVENE TDTGDAGVSL RSTSCTTSLA SQGERKRRTL PQLPNEEKLL ESSRAKVVPQ RSEIGEKQDT ELQEKEAQVY QSEKHDADRG LSKMSRAVNG ESPKTGGDGK ALLHSGSSSS KEKSETEKET SLVKQTLAKM QQQEQKEQAQ WTPTKFPSKN ALGHIDKCRE ESSKQESQLL EKVSGHSTSK GDRVIQNESK RRKAEEIPKC QASKGDKKES SKSLVRQGSF TIDKPSSNIP IELIPHINKQ NSSVPTALAL TSASRLRERS DSLDTDSSMD TTLILKDTEA VMAFLEAKLR EDNNKTDEGP DTPSYNRDNS ISPESDVDTA STISLVTGET ERKSTQKRKS FTSLYKDRCS TSSPSKDVTK SGSREKIEKK AKSRSADIGA RADGRKFVQS SGRIRQPSID LTDDDQTSSV PHSAISDIMS SDQETYSCKS HGRTPLTSAD EHNIHSKLEG GKATKSKTSP VASGSTSKST TLPRPRPTRT SLLRRARLGE ASDSELADAD KASVASEVST TSSTSKPPTG RRTISRIDLL AQPRRTRLGS LSARSDSEAT ISRSSASART AEAVIRSGAR LVPSDKLSPR TRANSISRLS DSKVKSMSST HGSPSVNSRW RRFPTDYAST SEDEFGSNRN SPKHTRLRTS PALKTTRMQS TGSAMPASSS FKHRIKEQED YIRDWTAHRE EIARISQDLA LIAREINDVA GEIDSVTSSG TAPSTTVSTA ATTPGSAIDT REEVGDLHGE MHKLVDRVFD ESLNFRKIPP LVHSKTPEGN NGRSVDSRPQ PAEHPDHLTI TRRRTWSRDE VMGDNLLLSS VFQFSRKIRQ SIDKTAGKIR ILFKDKDRNW DDIENKLRAE SEVPIVKTSS MEISSILQEL KRVEKQLQVI NAMIDPDGTL EALNNMGFPN AILPSPPKQK SSPVNNHSSP SQTPALCPPE TRALHPAAAG VAAAASTEFE NAESEADFSI HFNRFNPDGE EEDVTVHE //