CLAP1_MOUSE
ID CLAP1_MOUSE Reviewed; 1535 AA.
AC Q80TV8; Q505G6; Q6DI75; Q6PG14; Q8BNS4; Q99JH5; Q99JI2; Q9CVU1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=CLIP-associating protein 1;
DE AltName: Full=Cytoplasmic linker-associated protein 1;
GN Name=Clasp1; Synonyms=Kiaa0622;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-306 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1251-1535 (ISOFORMS 1/2), INTERACTION WITH CLIP2 AND RSN, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11290329; DOI=10.1016/s0092-8674(01)00288-4;
RA Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
RA Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
RA Galjart N.;
RT "Clasps are CLIP-115 and -170 associating proteins involved in the regional
RT regulation of microtubule dynamics in motile fibroblasts.";
RL Cell 104:923-935(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-393 (ISOFORMS 1/2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1187-1535 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-1535 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 985-1535 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 997-1535 (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Salivary gland;
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 [6]
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1220, AND IDENTIFICATION BY
RP 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 [8]
RP INTERACTION WITH MACF1.
RX PubMed=18854161; DOI=10.1016/j.cell.2008.07.045;
RA Wu X., Kodama A., Fuchs E.;
RT "ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has
RT ATPase activity.";
RL Cell 135:137-148(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-545; SER-548;
RP SER-600; SER-636; SER-688; SER-820; SER-1088; THR-1092 AND SER-1110,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1139 (ISOFORM 2), 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).
CC -!- FUNCTION: Microtubule plus-end tracking protein that promotes the
CC stabilization of dynamic microtubules. Involved in the nucleation of
CC noncentrosomal microtubules originating from the trans-Golgi network
CC (TGN). Required for the polarization of the cytoplasmic microtubule
CC arrays in migrating cells towards the leading edge of the cell. May act
CC at the cell cortex to enhance the frequency of rescue of depolymerizing
CC microtubules by attaching their plus-ends to cortical platforms
CC composed of ERC1 and PHLDB2. This cortical microtubule stabilizing
CC activity is regulated at least in part by phosphatidylinositol 3-kinase
CC signaling. Also performs a similar stabilizing function at the
CC kinetochore which is essential for the bipolar alignment of chromosomes
CC on the mitotic spindle (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ERC1, MAPRE1, MAPRE3, microtubules, and PHLDB2.
CC The interaction with ERC1 may be mediated by PHLDB2. Interacts with
CC GCC2; recruits CLASP1 to Golgi membranes (By similarity). Interacts
CC with CLIP2 and RSN. Interacts with MACF1. {ECO:0000250,
CC ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:18854161}.
CC -!- INTERACTION:
CC Q80TV8; O55156: Clip2; Xeno; NbExp=3; IntAct=EBI-908322, EBI-349416;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Golgi apparatus, trans-Golgi
CC network {ECO:0000250}. Note=Localizes to microtubule plus ends.
CC Localizes to centrosomes, kinetochores and the mitotic spindle from
CC prometaphase. Subsequently localizes to the spindle midzone from
CC anaphase and to the midbody from telophase. In migrating cells
CC localizes to the plus ends of microtubules within the cell body and to
CC the entire microtubule lattice within the lamella. Localizes to the
CC cell cortex and this requires ERC1 and PHLDB2. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80TV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TV8-2; Sequence=VSP_022390, VSP_022391, VSP_022392;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and heart and at lower
CC levels in kidney, lung, skeletal muscle and testis.
CC {ECO:0000269|PubMed:11290329}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24639.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC38020.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AC109294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ276962; CAC35162.1; -; mRNA.
DR EMBL; AJ288061; CAC35163.1; -; mRNA.
DR EMBL; AK006534; BAB24639.2; ALT_INIT; mRNA.
DR EMBL; AK080782; BAC38020.1; ALT_SEQ; mRNA.
DR EMBL; AK122330; BAC65612.1; -; mRNA.
DR EMBL; BC057312; AAH57312.1; -; mRNA.
DR EMBL; BC075708; AAH75708.1; -; mRNA.
DR EMBL; BC094554; AAH94554.1; -; mRNA.
DR RefSeq; NP_001280229.1; NM_001293300.1.
DR RefSeq; NP_001280230.1; NM_001293301.1.
DR RefSeq; NP_083985.2; NM_029709.2.
DR AlphaFoldDB; Q80TV8; -.
DR SMR; Q80TV8; -.
DR BioGRID; 218270; 35.
DR IntAct; Q80TV8; 11.
DR STRING; 10090.ENSMUSP00000140019; -.
DR iPTMnet; Q80TV8; -.
DR PhosphoSitePlus; Q80TV8; -.
DR SwissPalm; Q80TV8; -.
DR EPD; Q80TV8; -.
DR jPOST; Q80TV8; -.
DR MaxQB; Q80TV8; -.
DR PaxDb; Q80TV8; -.
DR PeptideAtlas; Q80TV8; -.
DR PRIDE; Q80TV8; -.
DR ProteomicsDB; 285464; -. [Q80TV8-1]
DR ProteomicsDB; 285465; -. [Q80TV8-2]
DR GeneID; 76707; -.
DR KEGG; mmu:76707; -.
DR CTD; 23332; -.
DR MGI; MGI:1923957; Clasp1.
DR eggNOG; KOG2956; Eukaryota.
DR InParanoid; Q80TV8; -.
DR OrthoDB; 66632at2759; -.
DR PhylomeDB; Q80TV8; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 76707; 2 hits in 19 CRISPR screens.
DR ChiTaRS; Clasp1; mouse.
DR PRO; PR:Q80TV8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80TV8; protein.
DR GO; GO:0045180; C:basal cortex; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0031592; C:centrosomal corona; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:InterPro.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0002162; F:dystroglycan binding; ISO:MGI.
DR GO; GO:0043515; F:kinetochore binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0051010; F:microtubule plus-end binding; ISO:MGI.
DR GO; GO:0030953; P:astral microtubule organization; ISO:MGI.
DR GO; GO:0051301; P:cell division; ISO:MGI.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; ISO:MGI.
DR GO; GO:0051294; P:establishment of spindle orientation; ISO:MGI.
DR GO; GO:0010458; P:exit from mitosis; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR GO; GO:0031111; P:negative regulation of microtubule polymerization or depolymerization; ISO:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; ISO:MGI.
DR GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISO:MGI.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0010470; P:regulation of gastrulation; ISO:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0006903; P:vesicle targeting; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028399; CLASP_1.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR21567:SF28; PTHR21567:SF28; 1.
DR Pfam; PF12348; CLASP_N; 2.
DR SMART; SM01349; TOG; 4.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus; Kinetochore;
KW Microtubule; Mitosis; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1535
FT /note="CLIP-associating protein 1"
FT /id="PRO_0000272274"
FT REPEAT 87..124
FT /note="HEAT 1"
FT REPEAT 163..200
FT /note="HEAT 2"
FT REPEAT 405..440
FT /note="HEAT 3"
FT REPEAT 441..477
FT /note="HEAT 4"
FT REPEAT 971..1008
FT /note="HEAT 5"
FT REPEAT 1339..1376
FT /note="HEAT 6"
FT REPEAT 1457..1494
FT /note="HEAT 7"
FT REGION 237..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..782
FT /note="Interaction with microtubules, MAPRE1 and MAPRE3"
FT /evidence="ECO:0000250"
FT REGION 1078..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1535
FT /note="Interaction with CLIP2 and RSN"
FT /evidence="ECO:0000269|PubMed:11290329"
FT REGION 1251..1535
FT /note="Interaction with PHLDB2"
FT /evidence="ECO:0000250"
FT REGION 1253..1535
FT /note="Localization to kinetochores"
FT /evidence="ECO:0000250"
FT COILED 1296..1327
FT /evidence="ECO:0000255"
FT COMPBIAS 250..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 656
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 708
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1088
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1092
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1096
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 1110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z460"
FT MOD_RES 1220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT VAR_SEQ 770
FT /note="L -> LASRRHSRSTSALSTAESVGQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022390"
FT VAR_SEQ 805
FT /note="L -> LLLGDARSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022391"
FT VAR_SEQ 1120..1158
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022392"
FT CONFLICT 1231
FT /note="I -> K (in Ref. 3; BAB24639)"
FT /evidence="ECO:0000305"
FT CONFLICT 1417
FT /note="P -> S (in Ref. 5; AAH75708)"
FT /evidence="ECO:0000305"
FT MOD_RES Q80TV8-2:1139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1535 AA; 169227 MW; 5EE40CCE493C64D2 CRC64;
MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDRQKSADL EHDQTLLDKL VDGLATSWVN
SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD
QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN
SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANEKN
FDDEDSVDGN RPSSASSSSS KAPSSSRRNV NLGTTRRLMS SSLGSKSSAA KEGAGAVDEE
DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD
NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN
SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL
ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL
KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTASR GSTVSTKSVS TTGSLQRSRS
DIDVNAAASA KSKVSSSSGS PAFSSAAALP PGSYASLGRI RTRRQSSGST TNVASTPDSR
GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGLAGG SSRGPPVTPS SEKRSKIPRS
QGCSRETSPN RIGLARSSRI PRPSMSQGCS RDTSRESSRD TSPARGFTPL DRFGLGQSGR
IPGSVNAMRV LSTSTDLEAA VADALKKPVR RRYEPYGMYS DDDANSDASS VCSERSYGSR
NGGIPHYLRQ TEDVAEVLNH CASSNWSERK EGLLGLQNLL KSQRTLSRVE LKRLCEIFTR
MFADPHSKRV FSMFLETLVD FIIIHKDDLQ DWLFVLLTQL LKKMGADLLG SVQAKVQKAL
DVTRDSFPFD QQFNILMRFI VDQTQTPNLK VKVAILKYIE SLARQMDPTD FVNSSETRLA
VSRIITWTTE PKSSDVRKAA QIVLISLFEL NTPEFTMLLG ALPKTFQDGA TKLLHNHLKN
SSNTGVGSPS NTIGRTPSRH PSSRTSPLTS PTNCSHGGLS PSRLWGWSAD GLSKPPPPFS
QPNSIPTAPS HKTLRRSYSP SMLDYDTENL NSEEIYSSLR GVTEAIEKFS FRSQEDLNEP
IKRDGKKDCD IVSRDGGAAS PATEGRGGSE IEGGRMALDN KTSLLNTQPP RAFPGPRARE
YNPYPYSDTI NTYDKTALKE AVFDDDMEQL RDVPIDHSDL VADLLKELSN HNERVEERKG
ALLELLKITR EDSLGVWEEH FKTILLLLLE TLGDKDHSIR ALALRVLREI LRNQPARFKN
YAELTIMKTL EAHKDSHKEV VRAAEEAAST LASSIHPEQC IKVLCPIIQT ADYPINLAAI
KMQTKVVERI TKESLLQLLV DIIPGLLQGY DNTESSVRKA SVFCLVAIYS VIGEDLKPHL
AQLTGSKMKL LNLYIKRAQT TNSNSSSSSD VSTHS
