SHRM3_HUMAN
ID SHRM3_HUMAN Reviewed; 1996 AA.
AC Q8TF72; Q5QTQ3; Q6ZRW3; Q96IR9; Q9P247;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein Shroom3;
DE AltName: Full=Shroom-related protein;
DE Short=hShrmL;
GN Name=SHROOM3; Synonyms=KIAA1481, SHRML; ORFNames=MSTP013;
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 VARIANTS ALA-279; ALA-469 AND
RP LEU-1290.
RA Koide M., Iio A., Obata K., Inagaki M., Yokota M., Ono T., Tuan R.S.;
RT "Molecular cloning of FKBP12-associated protein.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 617-1996 (ISOFORM 1), AND VARIANT
RP LEU-1290.
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1230-1996 (ISOFORM 1).
RC TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1799-1996 (ISOFORM 1).
RC TISSUE=Aorta;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W., Liu S.,
RA Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y.,
RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NOMENCLATURE.
RX PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P., Schiaffino M.V.,
RA Smith P., Staub O., Hildebrand J.D., Wallingford J.B.;
RT "A new standard nomenclature for proteins related to Apx and Shroom.";
RL BMC Cell Biol. 7:18-18(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND SER-913, 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-439; SER-443; SER-910;
RP SER-913 AND SER-1221, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-910, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND SER-970, AND
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 [13]
RP INTERACTION WITH ROCK1.
RX PubMed=22493320; DOI=10.1091/mbc.e11-11-0937;
RA Mohan S., Rizaldy R., Das D., Bauer R.J., Heroux A., Trakselis M.A.,
RA Hildebrand J.D., VanDemark A.P.;
RT "Structure of Shroom domain 2 reveals a three-segmented coiled-coil
RT required for dimerization, Rock binding, and apical constriction.";
RL Mol. Biol. Cell 23:2131-2142(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816; SER-890; SER-910;
RP SER-913; SER-1221 AND SER-1441, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1441, AND IDENTIFICATION BY
RP 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).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Controls cell shape changes in the neuroepithelium during
CC neural tube closure. Induces apical constriction in epithelial cells by
CC promoting the apical accumulation of F-actin and myosin II, and
CC probably by bundling stress fibers (By similarity). Induces apicobasal
CC cell elongation by redistributing gamma-tubulin and directing the
CC assembly of robust apicobasal microtubule arrays (By similarity).
CC {ECO:0000250|UniProtKB:Q27IV2, ECO:0000250|UniProtKB:Q9QXN0}.
CC -!- SUBUNIT: Interacts with F-actin (By similarity). Interacts with ROCK1
CC (PubMed:22493320). {ECO:0000250|UniProtKB:Q9QXN0,
CC ECO:0000269|PubMed:22493320}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q9QXN0}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9QXN0}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9QXN0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9QXN0}. Note=Colocalizes with F-actin in stress
CC fibers and adherens junctions. {ECO:0000250|UniProtKB:Q9QXN0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TF72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TF72-2; Sequence=VSP_024965, VSP_024966, VSP_024967,
CC VSP_024968;
CC -!- DOMAIN: The ASD1 domain mediates F-actin binding. {ECO:0000250}.
CC -!- DOMAIN: The ASD2 domain mediates the interaction with ROCK1 and is
CC required for apical constriction induction.
CC {ECO:0000250|UniProtKB:Q9QXN0}.
CC -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator. Met-2
CC is more conserved than Met-1 among the orthologs. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13515.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB84689.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB055660; BAB84689.1; ALT_INIT; mRNA.
DR EMBL; AK127929; BAC87195.1; -; mRNA.
DR EMBL; AC096743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB040914; BAA96005.1; -; mRNA.
DR EMBL; BC007291; AAH07291.1; -; mRNA.
DR EMBL; AF109367; AAQ13515.1; ALT_INIT; mRNA.
DR CCDS; CCDS3579.2; -. [Q8TF72-1]
DR RefSeq; NP_065910.3; NM_020859.3. [Q8TF72-1]
DR PDB; 6FBB; X-ray; 1.30 A; P=1240-1244.
DR PDB; 6FCP; X-ray; 1.45 A; P=1233-1247.
DR PDBsum; 6FBB; -.
DR PDBsum; 6FCP; -.
DR AlphaFoldDB; Q8TF72; -.
DR SMR; Q8TF72; -.
DR BioGRID; 121665; 56.
DR IntAct; Q8TF72; 28.
DR MINT; Q8TF72; -.
DR STRING; 9606.ENSP00000296043; -.
DR iPTMnet; Q8TF72; -.
DR PhosphoSitePlus; Q8TF72; -.
DR SwissPalm; Q8TF72; -.
DR BioMuta; SHROOM3; -.
DR DMDM; 300669666; -.
DR EPD; Q8TF72; -.
DR jPOST; Q8TF72; -.
DR MassIVE; Q8TF72; -.
DR MaxQB; Q8TF72; -.
DR PaxDb; Q8TF72; -.
DR PeptideAtlas; Q8TF72; -.
DR PRIDE; Q8TF72; -.
DR ProteomicsDB; 74572; -. [Q8TF72-1]
DR ProteomicsDB; 74573; -. [Q8TF72-2]
DR Antibodypedia; 62376; 59 antibodies from 19 providers.
DR DNASU; 57619; -.
DR Ensembl; ENST00000296043.7; ENSP00000296043.6; ENSG00000138771.16. [Q8TF72-1]
DR GeneID; 57619; -.
DR KEGG; hsa:57619; -.
DR MANE-Select; ENST00000296043.7; ENSP00000296043.6; NM_020859.4; NP_065910.3.
DR UCSC; uc011cbx.3; human. [Q8TF72-1]
DR CTD; 57619; -.
DR DisGeNET; 57619; -.
DR GeneCards; SHROOM3; -.
DR HGNC; HGNC:30422; SHROOM3.
DR HPA; ENSG00000138771; Low tissue specificity.
DR MIM; 604570; gene.
DR neXtProt; NX_Q8TF72; -.
DR OpenTargets; ENSG00000138771; -.
DR PharmGKB; PA147357295; -.
DR VEuPathDB; HostDB:ENSG00000138771; -.
DR eggNOG; ENOG502QUU2; Eukaryota.
DR GeneTree; ENSGT00940000157778; -.
DR HOGENOM; CLU_002434_1_0_1; -.
DR InParanoid; Q8TF72; -.
DR OMA; DKKHQDL; -.
DR OrthoDB; 29607at2759; -.
DR PhylomeDB; Q8TF72; -.
DR TreeFam; TF333370; -.
DR PathwayCommons; Q8TF72; -.
DR SignaLink; Q8TF72; -.
DR BioGRID-ORCS; 57619; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; SHROOM3; human.
DR GeneWiki; SHROOM3; -.
DR GenomeRNAi; 57619; -.
DR Pharos; Q8TF72; Tbio.
DR PRO; PR:Q8TF72; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8TF72; protein.
DR Bgee; ENSG00000138771; Expressed in ileal mucosa and 173 other tissues.
DR ExpressionAtlas; Q8TF72; baseline and differential.
DR Genevisible; Q8TF72; HS.
DR GO; GO:0005912; C:adherens junction; ISS:HGNC-UCL.
DR GO; GO:0043296; C:apical junction complex; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:HGNC-UCL.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISS:HGNC-UCL.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0045176; P:apical protein localization; ISS:HGNC-UCL.
DR GO; GO:0000902; P:cell morphogenesis; ISS:HGNC-UCL.
DR GO; GO:0043482; P:cellular pigment accumulation; ISS:HGNC-UCL.
DR GO; GO:0002064; P:epithelial cell development; IEA:InterPro.
DR GO; GO:0001843; P:neural tube closure; IEA:InterPro.
DR GO; GO:0007389; P:pattern specification process; ISS:HGNC-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR014800; ASD1_dom.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR030494; Shrm3.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 1.
DR PANTHER; PTHR15012:SF33; PTHR15012:SF33; 1.
DR Pfam; PF08688; ASD1; 1.
DR Pfam; PF08687; ASD2; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51306; ASD1; 1.
DR PROSITE; PS51307; ASD2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell junction;
KW Cell membrane; Cell shape; Cytoplasm; Cytoskeleton; Developmental protein;
KW Membrane; Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1996
FT /note="Protein Shroom3"
FT /id="PRO_0000286066"
FT DOMAIN 25..110
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 928..1030
FT /note="ASD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT DOMAIN 1669..1957
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 150..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1627..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXN0"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXN0"
FT MOD_RES 1072
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXN0"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024965"
FT VAR_SEQ 126..153
FT /note="SPEHLTSGPQHRKAAWSGGVKLRLKHRR -> MAFYSTPEYDIQLARGLLSG
FT MFLFATRR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024966"
FT VAR_SEQ 277..311
FT /note="ISGRERSGSMDNTSARGGLLEGMRQADIRYVKTVY -> KRVKTRDLPGSQS
FT PGRAISRKTTMPTSGGGWREKA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024967"
FT VAR_SEQ 312..1996
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024968"
FT VARIANT 147
FT /note="L -> H (in dbSNP:rs3821979)"
FT /id="VAR_032062"
FT VARIANT 279
FT /note="G -> A (in dbSNP:rs344140)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_032063"
FT VARIANT 469
FT /note="P -> A (in dbSNP:rs344141)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_032064"
FT VARIANT 1290
FT /note="P -> L (in dbSNP:rs3733242)"
FT /evidence="ECO:0000269|PubMed:10819331, ECO:0000269|Ref.1"
FT /id="VAR_032065"
FT CONFLICT 153
FT /note="R -> S (in Ref. 1; BAB84689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1996 AA; 216857 MW; 735F6CD20FF64BC6 CRC64;
MMRTTEDFHK PSATLNSNTA TKGRYIYLEA FLEGGAPWGF TLKGGLEHGE PLIISKVEEG
GKADTLSSKL QAGDEVVHIN EVTLSSSRKE AVSLVKGSYK TLRLVVRRDV CTDPGHADTG
ASNFVSPEHL TSGPQHRKAA WSGGVKLRLK HRRSEPAGRP HSWHTTKSGE KQPDASMMQI
SQGMIGPPWH QSYHSSSSTS DLSNYDHAYL RRSPDQCSSQ GSMESLEPSG AYPPCHLSPA
KSTGSIDQLS HFHNKRDSAY SSFSTSSSIL EYPHPGISGR ERSGSMDNTS ARGGLLEGMR
QADIRYVKTV YDTRRGVSAE YEVNSSALLL QGREARASAN GQGYDKWSNI PRGKGVPPPS
WSQQCPSSLE TATDNLPPKV GAPLPPARSD SYAAFRHRER PSSWSSLDQK RLCRPQANSL
GSLKSPFIEE QLHTVLEKSP ENSPPVKPKH NYTQKAQPGQ PLLPTSIYPV PSLEPHFAQV
PQPSVSSNGM LYPALAKESG YIAPQGACNK MATIDENGNQ NGSGRPGFAF CQPLEHDLLS
PVEKKPEATA KYVPSKVHFC SVPENEEDAS LKRHLTPPQG NSPHSNERKS THSNKPSSHP
HSLKCPQAQA WQAGEDKRSS RLSEPWEGDF QEDHNANLWR RLEREGLGQS LSGNFGKTKS
AFSSLQNIPE SLRRHSSLEL GRGTQEGYPG GRPTCAVNTK AEDPGRKAAP DLGSHLDRQV
SYPRPEGRTG ASASFNSTDP SPEEPPAPSH PHTSSLGRRG PGPGSASALQ GFQYGKPHCS
VLEKVSKFEQ REQGSQRPSV GGSGFGHNYR PHRTVSTSST SGNDFEETKA HIRFSESAEP
LGNGEQHFKN GELKLEEASR QPCGQQLSGG ASDSGRGPQR PDARLLRSQS TFQLSSEPER
EPEWRDRPGS PESPLLDAPF SRAYRNSIKD AQSRVLGATS FRRRDLELGA PVASRSWRPR
PSSAHVGLRS PEASASASPH TPRERHSVTP AEGDLARPVP PAARRGARRR LTPEQKKRSY
SEPEKMNEVG IVEEAEPAPL GPQRNGMRFP ESSVADRRRL FERDGKACST LSLSGPELKQ
FQQSALADYI QRKTGKRPTS AAGCSLQEPG PLRERAQSAY LQPGPAALEG SGLASASSLS
SLREPSLQPR REATLLPATV AETQQAPRDR SSSFAGGRRL GERRRGDLLS GANGGTRGTQ
RGDETPREPS SWGARAGKSM SAEDLLERSD VLAGPVHVRS RSSPATADKR QDVLLGQDSG
FGLVKDPCYL AGPGSRSLSC SERGQEEMLP LFHHLTPRWG GSGCKAIGDS SVPSECPGTL
DHQRQASRTP CPRPPLAGTQ GLVTDTRAAP LTPIGTPLPS AIPSGYCSQD GQTGRQPLPP
YTPAMMHRSN GHTLTQPPGP RGCEGDGPEH GVEEGTRKRV SLPQWPPPSR AKWAHAARED
SLPEESSAPD FANLKHYQKQ QSLPSLCSTS DPDTPLGAPS TPGRISLRIS ESVLRDSPPP
HEDYEDEVFV RDPHPKATSS PTFEPLPPPP PPPPSQETPV YSMDDFPPPP PHTVCEAQLD
SEDPEGPRPS FNKLSKVTIA RERHMPGAAH VVGSQTLASR LQTSIKGSEA ESTPPSFMSV
HAQLAGSLGG QPAPIQTQSL SHDPVSGTQG LEKKVSPDPQ KSSEDIRTEA LAKEIVHQDK
SLADILDPDS RLKTTMDLME GLFPRDVNLL KENSVKRKAI QRTVSSSGCE GKRNEDKEAV
SMLVNCPAYY SVSAPKAELL NKIKEMPAEV NEEEEQADVN EKKAELIGSL THKLETLQEA
KGSLLTDIKL NNALGEEVEA LISELCKPNE FDKYRMFIGD LDKVVNLLLS LSGRLARVEN
VLSGLGEDAS NEERSSLYEK RKILAGQHED ARELKENLDR RERVVLGILA NYLSEEQLQD
YQHFVKMKST LLIEQRKLDD KIKLGQEQVK CLLESLPSDF IPKAGALALP PNLTSEPIPA
GGCTFSGIFP TLTSPL
