SI1L1_MOUSE
ID SI1L1_MOUSE Reviewed; 1782 AA.
AC Q8C0T5; Q6PDI8; Q80U02; Q8C026;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Signal-induced proliferation-associated 1-like protein 1;
DE Short=SIPA1-like protein 1;
GN Name=Sipa1l1; Synonyms=Kiaa0440;
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 1).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, 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 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 [3]
RP PROTEIN SEQUENCE OF 18-28; 1379-1408 AND 1468-1482, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-1782 (ISOFORM 1).
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 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 INTERACTION WITH EPHA4.
RX PubMed=18094260; DOI=10.1523/jneurosci.2746-07.2007;
RA Richter M., Murai K.K., Bourgin C., Pak D.T., Pasquale E.B.;
RT "The EphA4 receptor regulates neuronal morphology through SPAR-mediated
RT inactivation of Rap GTPases.";
RL J. Neurosci. 27:14205-14215(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1547, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1528, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1528, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-288; SER-1127;
RP SER-1410; SER-1412; SER-1547; SER-1564; SER-1582; SER-1624; SER-1626;
RP SER-1629; SER-1687; SER-1690; SER-1707; SER-1708 AND SER-1712, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC 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 [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1580, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes
CC reorganization of the actin cytoskeleton and recruits DLG4 to F-actin.
CC Contributes to the regulation of dendritic spine morphogenesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DLG4, PDLIM5, PDLIM7 and LZTS3. Interacts with
CC the actin cytoskeleton (By similarity). Interacts (via PDZ domain) with
CC EPHA4 (via PDZ motif); controls neuronal morphology through regulation
CC of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases.
CC {ECO:0000250, ECO:0000269|PubMed:18094260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Postsynaptic density {ECO:0000250}. Synapse, synaptosome {ECO:0000250}.
CC Note=Associated with the actin cytoskeleton. Detected at synapses and
CC dendritic spines of cultured hippocampal neurons (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=E6TP1 alpha;
CC IsoId=Q8C0T5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0T5-2; Sequence=VSP_010918, VSP_010919;
CC -!- PTM: Ubiquitinated and degraded by the SCF(BTRC) following
CC phosphorylation by PLK2. {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-1328 by CDK5, creating a docking site for
CC the POLO box domains of PLK2. Subsequently, PLK2 binds and
CC phosphorylates SIPA1L1, leading to ubiquitination and degradation by
CC the proteasome (By similarity). {ECO:0000250}.
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DR EMBL; AK029889; BAC26660.1; -; mRNA.
DR EMBL; AK032493; BAC27896.1; -; mRNA.
DR EMBL; BC058681; AAH58681.1; -; mRNA.
DR EMBL; AK122284; BAC65566.1; -; mRNA.
DR CCDS; CCDS26026.1; -. [Q8C0T5-1]
DR CCDS; CCDS49105.1; -. [Q8C0T5-2]
DR RefSeq; NP_001161455.1; NM_001167983.1. [Q8C0T5-2]
DR RefSeq; NP_766167.2; NM_172579.3. [Q8C0T5-1]
DR RefSeq; XP_011242371.1; XM_011244069.2. [Q8C0T5-1]
DR RefSeq; XP_017170514.1; XM_017315025.1. [Q8C0T5-1]
DR AlphaFoldDB; Q8C0T5; -.
DR SMR; Q8C0T5; -.
DR BioGRID; 229945; 15.
DR IntAct; Q8C0T5; 4.
DR MINT; Q8C0T5; -.
DR STRING; 10090.ENSMUSP00000061014; -.
DR iPTMnet; Q8C0T5; -.
DR PhosphoSitePlus; Q8C0T5; -.
DR SwissPalm; Q8C0T5; -.
DR EPD; Q8C0T5; -.
DR jPOST; Q8C0T5; -.
DR MaxQB; Q8C0T5; -.
DR PaxDb; Q8C0T5; -.
DR PeptideAtlas; Q8C0T5; -.
DR PRIDE; Q8C0T5; -.
DR ProteomicsDB; 261033; -. [Q8C0T5-1]
DR ProteomicsDB; 261034; -. [Q8C0T5-2]
DR Antibodypedia; 132; 56 antibodies from 24 providers.
DR DNASU; 217692; -.
DR Ensembl; ENSMUST00000053969; ENSMUSP00000061014; ENSMUSG00000042700. [Q8C0T5-1]
DR Ensembl; ENSMUST00000166429; ENSMUSP00000131030; ENSMUSG00000042700. [Q8C0T5-1]
DR Ensembl; ENSMUST00000222298; ENSMUSP00000152356; ENSMUSG00000042700. [Q8C0T5-2]
DR Ensembl; ENSMUST00000222714; ENSMUSP00000152212; ENSMUSG00000042700. [Q8C0T5-1]
DR GeneID; 217692; -.
DR KEGG; mmu:217692; -.
DR UCSC; uc007ocu.2; mouse. [Q8C0T5-1]
DR UCSC; uc007ocw.2; mouse. [Q8C0T5-2]
DR CTD; 26037; -.
DR MGI; MGI:2443679; Sipa1l1.
DR VEuPathDB; HostDB:ENSMUSG00000042700; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00940000155944; -.
DR HOGENOM; CLU_002127_0_1_1; -.
DR InParanoid; Q8C0T5; -.
DR OMA; CHLPAMS; -.
DR OrthoDB; 28453at2759; -.
DR PhylomeDB; Q8C0T5; -.
DR TreeFam; TF318626; -.
DR BioGRID-ORCS; 217692; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Sipa1l1; mouse.
DR PRO; PR:Q8C0T5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8C0T5; protein.
DR Bgee; ENSMUSG00000042700; Expressed in olfactory tubercle and 232 other tissues.
DR ExpressionAtlas; Q8C0T5; baseline and differential.
DR Genevisible; Q8C0T5; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0050770; P:regulation of axonogenesis; IDA:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; ISO:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR InterPro; IPR030770; SIPA1L1.
DR InterPro; IPR021818; SIPA1L_C.
DR PANTHER; PTHR15711:SF10; PTHR15711:SF10; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR Pfam; PF11881; SPAR_C; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTPase activation; Methylation; Phosphoprotein;
KW Reference proteome; Synapse; Synaptosome; Ubl conjugation.
FT CHAIN 1..1782
FT /note="Signal-induced proliferation-associated 1-like
FT protein 1"
FT /id="PRO_0000056747"
FT DOMAIN 599..816
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT DOMAIN 953..1031
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1625..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1713..1773
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1305
FT /note="Phosphoserine; by PLK2"
FT /evidence="ECO:0000250|UniProtKB:O35412"
FT MOD_RES 1309
FT /note="Phosphothreonine; by PLK2"
FT /evidence="ECO:0000250|UniProtKB:O35412"
FT MOD_RES 1328
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O35412"
FT MOD_RES 1345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 1530
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1580
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1712
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1736..1751
FT /note="EKEDKAQLQAEVEHLR -> VNALRKRRQGPAAGGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010918"
FT VAR_SEQ 1752..1782
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010919"
FT CONFLICT 855
FT /note="S -> N (in Ref. 1; BAC26660)"
FT /evidence="ECO:0000305"
FT CONFLICT 1204
FT /note="W -> C (in Ref. 1; BAC65566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1782 AA; 197031 MW; A5BBD8CD69A481FC CRC64;
MTSLKRSQTE RPVTADRASV VSTDGAPKVH TDDFYMRRFR SQNGSLGSSV MAAVGPPRSE
GPHHITSTPG VPKMGVRARI ADWPPRKENV KESSRSSQEI ETSSCLESLS SKGSPVSQGS
SVSLNSNDSA MLKSIQNTLK NKTGPAESMD SRFLMPEAYP SSPRKALRRI RQRSNSDITI
SELDVDSFDE CISPTYKSGP SLHREYGSTS SIDKQGTSGD SFFDLLKGYK DDRSDRGPTP
TKLSDFLITG GGKGSGFSLD VIDGPISQRE NLRLFKEREK PLKRRSKSET GDSSIFRKLR
NAKGEELGKS SDLEDNRSED SVRPWTCPKC FAHYDVQSIL FDLNEAIMNR HNVIKRRNTT
TGASAAAVAS LVSGPLSHSA SFSSPMGSTE DLNSKGSLGM DQGDDKSNEL VMSCPYFRNE
IGGEGERKIS LSKSNSGSFS GCESTSFESA LSSHCTNAGV AVLEVPKESL MLHLDRVKRY
TVEHVDLGAY YYRKFFYQKE HWNYFGADEN LGPVAVSIRR EKPEDMKENG SPYNYRIIFR
TSELMTLRGS VLEDAIPSTA KHSTARGLPL KEVLEHVIPE LNVQCLRLAF NTPKVTEQLM
KLDEQGLNYQ QKVGIMYCKA GQSTEEEMYN NESAGPAFEE FLQLLGERVR LKGFEKYRAQ
LDTKTDSTGT HSLYTTYKDY EIMFHVSTML PYTPNNKQQL LRKRHIGNDI VTIVFQEPGA
QPFSPKNIRS HFQHVFVIVR AHNPCTESVC YSVAVTRSRD VPSFGPPIPK GVTFPKSNVF
RDFLLAKVIN AENAAHKSEK FRAMATRTRQ EYLKDLAEKN VTNTPIDPSG KFPFISLASK
KKEKSKPYPG AELSSMGAIV WAVRAKDYNK AMEFDCLLGI SSEFIVLIEQ ETKSVAFNCS
CRDVIGWTSS DTSLKIFYER GECVSVESFI SGEDIKEIVR RLQFVSKGCE SVEMTLRRNG
LGQLGFHVNY EGIVADVEPY GYAWQAGLRQ GSRLVEICKV AVATLSHEQM IDLLRTSVTV
KVVIIPPHDD CTPRRSCSET YRMPVMEYQM NEGISYEFKF PFRNNNKWQR NASKGAHSPQ
VPSQLQSPMT SRLNAGKGDG KMPPPERAAN IPRSISSDGR PLERRLSPGS DIYVTVSSMA
LARSQCRNSP SNLSSSSETG SGGGTYRQKS MPEGFGVSRR SPASIDRQNT QSDISGSGKS
TPSWQRSEDS LADQMEPTCH LPAVSKVLPA FRESPSGRLM RQDPVVHLSP NKQGHSDSHY
SSHSSSNTLS SNASSAHSDE KWYDGDRTES DLNSYNYLQG TSADSGIDTA SYGPSHGSTA
SLGASTSSPR SGPGKEKVAP LWHSSSEVLS LADRTLETEG HGMDRKAESS LSLDIHSKSQ
GGSSPLSREN STFSINDAAS HTSTMSSRHS ASPVVFSSAR SSPKEELHPT ASSQLAPSFS
SSSSSSSGPR TFYPRQGATS KYLIGWKKPE GTINSVGFMD TRKRHQSDGN EIAHTRLRAS
TRDLQASPKP TSKSTIEEDL KKLIDLESPT PESQKNFKFH ALSSPQSPFP TTPTSRRALH
RTLSDESIYS SQREHFFTSR ASLLDQALPN DVLFSSTYPS LPKSLPLRRP SYTLGMKSLH
GEFSASDSSL TDIQETRRQP IPDPGLMPLP DAASDLDWSN LVDAAKAYEV QRASFFAASD
ENHRPLSAAS NSDQLEEQAL VQMKSYSSKD PSPTLASKVD QLEGMLKMLR EDLKKEKEDK
AQLQAEVEHL REDNLRLQEE SQNASDKLKK FTEWVFNTID MS
