CE170_MOUSE
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 03-AUG-2022, entry version 127.
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}.
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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; 43.
DR IntAct; Q6A065; 22.
DR MINT; Q6A065; -.
DR STRING; 10090.ENSMUSP00000059562; -.
DR iPTMnet; Q6A065; -.
DR PhosphoSitePlus; Q6A065; -.
DR SwissPalm; Q6A065; -.
DR EPD; Q6A065; -.
DR jPOST; Q6A065; -.
DR MaxQB; Q6A065; -.
DR PaxDb; Q6A065; -.
DR PeptideAtlas; Q6A065; -.
DR PRIDE; Q6A065; -.
DR ProteomicsDB; 281365; -. [Q6A065-1]
DR ProteomicsDB; 281366; -. [Q6A065-2]
DR ProteomicsDB; 281367; -. [Q6A065-3]
DR Antibodypedia; 34708; 116 antibodies from 21 providers.
DR Ensembl; ENSMUST00000192961; ENSMUSP00000142271; ENSMUSG00000057335. [Q6A065-2]
DR Ensembl; ENSMUST00000194727; ENSMUSP00000141793; ENSMUSG00000057335. [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 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 OMA; IDKCRED; -.
DR OrthoDB; 83451at2759; -.
DR PhylomeDB; Q6A065; -.
DR BioGRID-ORCS; 545389; 2 hits in 72 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 220 other tissues.
DR ExpressionAtlas; Q6A065; baseline and differential.
DR Genevisible; Q6A065; MM.
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; cd00060; FHA; 1.
DR InterPro; IPR026644; CEP170.
DR InterPro; IPR029300; CEP170_C.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR15715:SF17; PTHR15715:SF17; 1.
DR Pfam; PF15308; CEP170_C; 1.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
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
