SI1L2_HUMAN
ID SI1L2_HUMAN Reviewed; 1722 AA.
AC Q9P2F8; Q2TV88; Q5VXR7; Q5VXR8; Q641Q4; Q8NA38; Q96DZ3; Q9H9F6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Signal-induced proliferation-associated 1-like protein 2;
DE Short=SIPA1-like protein 2;
GN Name=SIPA1L2; Synonyms=KIAA1389;
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 VARIANT ALA-1322.
RA Matsuura K., Kohu K., Akiyama T.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-1322.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-1722 (ISOFORM 1), AND VARIANT
RP ALA-1322.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1065-1722 (ISOFORM 2), AND
RP VARIANT ALA-1322.
RC TISSUE=Ovary, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1478, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-1478, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-1488, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1461, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1461; SER-1549 AND SER-1552,
RP AND 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-1029, 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 [14]
RP IDENTIFICATION BY MASS 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 [15]
RP IDENTIFICATION BY MASS 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).
CC -!- INTERACTION:
CC Q9P2F8-2; Q9Y2T2: AP3M1; NbExp=6; IntAct=EBI-10326741, EBI-2371151;
CC Q9P2F8-2; P26196: DDX6; NbExp=5; IntAct=EBI-10326741, EBI-351257;
CC Q9P2F8-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-10326741, EBI-11955057;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2F8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2F8-2; Sequence=VSP_010920, VSP_010921, VSP_010922;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92627.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14273.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY168879; AAO12530.1; -; mRNA.
DR EMBL; AK022852; BAB14273.1; ALT_INIT; mRNA.
DR EMBL; AK093191; BAC04090.1; -; mRNA.
DR EMBL; AL356965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB037810; BAA92627.1; ALT_INIT; mRNA.
DR EMBL; CH471098; EAW69972.1; -; Genomic_DNA.
DR EMBL; BC013119; AAH13119.2; -; mRNA.
DR EMBL; BC082251; AAH82251.1; -; mRNA.
DR CCDS; CCDS41474.1; -. [Q9P2F8-1]
DR RefSeq; NP_065859.3; NM_020808.4. [Q9P2F8-1]
DR RefSeq; XP_005273268.1; XM_005273211.2.
DR RefSeq; XP_005273269.1; XM_005273212.4. [Q9P2F8-1]
DR RefSeq; XP_005273270.1; XM_005273213.4. [Q9P2F8-1]
DR RefSeq; XP_011542545.1; XM_011544243.2. [Q9P2F8-1]
DR RefSeq; XP_016857385.1; XM_017001896.1. [Q9P2F8-1]
DR AlphaFoldDB; Q9P2F8; -.
DR SMR; Q9P2F8; -.
DR BioGRID; 121621; 114.
DR IntAct; Q9P2F8; 48.
DR MINT; Q9P2F8; -.
DR STRING; 9606.ENSP00000355589; -.
DR iPTMnet; Q9P2F8; -.
DR PhosphoSitePlus; Q9P2F8; -.
DR BioMuta; SIPA1L2; -.
DR DMDM; 85681894; -.
DR EPD; Q9P2F8; -.
DR jPOST; Q9P2F8; -.
DR MassIVE; Q9P2F8; -.
DR MaxQB; Q9P2F8; -.
DR PaxDb; Q9P2F8; -.
DR PeptideAtlas; Q9P2F8; -.
DR PRIDE; Q9P2F8; -.
DR ProteomicsDB; 83807; -. [Q9P2F8-1]
DR ProteomicsDB; 83808; -. [Q9P2F8-2]
DR Antibodypedia; 11728; 139 antibodies from 27 providers.
DR DNASU; 57568; -.
DR Ensembl; ENST00000308942.4; ENSP00000309102.4; ENSG00000116991.12. [Q9P2F8-2]
DR Ensembl; ENST00000366630.5; ENSP00000355589.1; ENSG00000116991.12. [Q9P2F8-1]
DR Ensembl; ENST00000674635.1; ENSP00000502693.1; ENSG00000116991.12. [Q9P2F8-1]
DR GeneID; 57568; -.
DR KEGG; hsa:57568; -.
DR MANE-Select; ENST00000674635.1; ENSP00000502693.1; NM_020808.5; NP_065859.3.
DR UCSC; uc001hvf.4; human. [Q9P2F8-1]
DR CTD; 57568; -.
DR DisGeNET; 57568; -.
DR GeneCards; SIPA1L2; -.
DR HGNC; HGNC:23800; SIPA1L2.
DR HPA; ENSG00000116991; Tissue enhanced (brain).
DR MIM; 611609; gene.
DR neXtProt; NX_Q9P2F8; -.
DR OpenTargets; ENSG00000116991; -.
DR PharmGKB; PA134933243; -.
DR VEuPathDB; HostDB:ENSG00000116991; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00940000157388; -.
DR HOGENOM; CLU_002127_0_2_1; -.
DR InParanoid; Q9P2F8; -.
DR OMA; GSRSMIH; -.
DR OrthoDB; 28453at2759; -.
DR PhylomeDB; Q9P2F8; -.
DR TreeFam; TF318626; -.
DR PathwayCommons; Q9P2F8; -.
DR SignaLink; Q9P2F8; -.
DR BioGRID-ORCS; 57568; 5 hits in 1064 CRISPR screens.
DR ChiTaRS; SIPA1L2; human.
DR GeneWiki; SIPA1L2; -.
DR GenomeRNAi; 57568; -.
DR Pharos; Q9P2F8; Tbio.
DR PRO; PR:Q9P2F8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9P2F8; protein.
DR Bgee; ENSG00000116991; Expressed in left ventricle myocardium and 181 other tissues.
DR ExpressionAtlas; Q9P2F8; baseline and differential.
DR Genevisible; Q9P2F8; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
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; IPR031203; SIPA1L2.
DR InterPro; IPR021818; SIPA1L_C.
DR PANTHER; PTHR15711:SF7; PTHR15711:SF7; 1.
DR Pfam; PF00595; PDZ; 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; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1722
FT /note="Signal-induced proliferation-associated 1-like
FT protein 2"
FT /id="PRO_0000056749"
FT DOMAIN 595..812
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT DOMAIN 950..1026
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1654..1712
FT /evidence="ECO:0000255"
FT COMPBIAS 43..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TE4"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TE4"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JCS6"
FT MOD_RES 1461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TE4"
FT MOD_RES 1478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18220336"
FT MOD_RES 1488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TE4"
FT VAR_SEQ 1..926
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010920"
FT VAR_SEQ 927..940
FT /note="NCAEDIREIVQRLV -> MSPCFSFIGCKLCS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010921"
FT VAR_SEQ 1588..1605
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010922"
FT VARIANT 49
FT /note="T -> A (in dbSNP:rs16857502)"
FT /id="VAR_049153"
FT VARIANT 1322
FT /note="T -> A (in dbSNP:rs2275307)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.4"
FT /id="VAR_049154"
FT VARIANT 1403
FT /note="S -> L (in dbSNP:rs1547742)"
FT /id="VAR_049155"
FT VARIANT 1424
FT /note="M -> L (in dbSNP:rs3210731)"
FT /id="VAR_061183"
FT VARIANT 1639
FT /note="G -> S (in dbSNP:rs2275303)"
FT /id="VAR_049156"
FT CONFLICT 1288
FT /note="S -> P (in Ref. 2; BAB14273)"
FT /evidence="ECO:0000305"
FT CONFLICT 1308
FT /note="D -> V (in Ref. 2; BAB14273)"
FT /evidence="ECO:0000305"
FT CONFLICT 1702
FT /note="T -> I (in Ref. 2; BAB14273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1722 AA; 190438 MW; C99E808CD6B156B1 CRC64;
MSDPRQSQEE KHKLGRASSK FKDPPRIMQS DDYFARKFKA INGNMGPTTS LNASNSNETG
GGGPANGTPA VPKMGVRARV SEWPPKKDCS KELTCKALWE SRSQTSYESI TSVLQNGQSD
QSEGQQDEQL DLDFVEAKYT IGDIFVHSPQ RGLHPIRQRS NSDVTISDID AEDVLDQNAV
NPNTGAALHR EYGSTSSIDR QGLSGENFFA MLRGYRVENY DHKAMVPFGF PEFFRCDPAI
SPSLHAAAQI SRGEFVRISG LDYVDSALLM GRDRDKPFKR RLKSESVETS LFRKLRTVKS
EHETFKFTSE LEESRLERGI RPWNCQRCFA HYDVQSILFN INEAMATRAN VGKRKNITTG
ASAASQTQMP TGQTGNCESP LGSKEDLNSK ENLDADEGDG KSNDLVLSCP YFRNETGGEG
DRRIALSRAN SSSFSSGESC SFESSLSSHC TNAGVSVLEV PRENQPIHRE KVKRYIIEHI
DLGAYYYRKF FYGKEHQNYF GIDENLGPVA VSIRREKVED AKEKEGSQFN YRVAFRTSEL
TTLRGAILED AIPSTARHGT ARGLPLKEVL EYVIPELSIQ CLRQASNSPK VSEQLLKLDE
QGLSFQHKIG ILYCKAGQST EEEMYNNETA GPAFEEFLDL LGQRVRLKGF SKYRAQLDNK
TDSTGTHSLY TTYKDYELMF HVSTLLPYMP NNRQQLLRKR HIGNDIVTIV FQEPGALPFT
PKSIRSHFQH VFVIVKVHNP CTENVCYSVG VSRSKDVPPF GPPIPKGVTF PKSAVFRDFL
LAKVINAENA AHKSEKFRAM ATRTRQEYLK DLAENFVTTA TVDTSVKFSF ITLGAKKKEK
VKPRKDAHLF SIGAIMWHVI ARDFGQSADI ECLLGISNEF IMLIEKDSKN VVFNCSCRDV
IGWTSGLVSI KVFYERGECV LLSSVDNCAE DIREIVQRLV IVTRGCETVE MTLRRNGLGQ
LGFHVNFEGI VADVEPFGFA WKAGLRQGSR LVEICKVAVA TLTHEQMIDL LRTSVTVKVV
IIQPHDDGSP RRGCSELCRI PMVEYKLDSE GTPCEYKTPF RRNTTWHRVP TPALQPLSRA
SPIPGTPDRL PCQQLLQQAQ AAIPRSTSFD RKLPDGTRSS PSNQSSSSDP GPGGSGPWRP
QVGYDGCQSP LLLEHQGSGP LECDGARERE DTMEASRHPE TKWHGPPSKV LGSYKERALQ
KDGSCKDSPN KLSHIGDKSC SSHSSSNTLS SNTSSNSDDK HFGSGDLMDP ELLGLTYIKG
ASTDSGIDTA PCMPATILGP VHLAGSRSLI HSRAEQWADA ADVSGPDDEP AKLYSVHGYA
STISAGSAAE GSMGDLSEIS SHSSGSHHSG SPSAHCSKSS GSLDSSKVYI VSHSSGQQVP
GSMSKPYHRQ GAVNKYVIGW KKSEGSPPPE EPEVTECPGM YSEMDVMSTA TQHQTVVGDA
VAETQHVLSK EDFLKLMLPD SPLVEEGRRK FSFYGNLSPR RSLYRTLSDE SICSNRRGSS
FGSSRSSVLD QALPNDILFS TTPPYHSTLP PRAHPAPSMG SLRNEFWFSD GSLSDKSKCA
DPGLMPLPDT ATGLDWTHLV DAARAFEGLD SDEELGLLCH HTSYLDQRVA SFCTLTDMQH
GQDLEGAQEL PLCVDPGSGK EFMDTTGERS PSPLTGKVNQ LELILRQLQT DLRKEKQDKA
VLQAEVQHLR QDNMRLQEES QTATAQLRKF TEWFFTTIDK KS
