ABLM3_HUMAN
ID ABLM3_HUMAN Reviewed; 683 AA.
AC O94929; A8K121; Q19VH3; Q658S1; Q68CI5; Q9BV32;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Actin-binding LIM protein 3;
DE Short=abLIM-3;
DE AltName: Full=Actin-binding LIM protein family member 3;
GN Name=ABLIM3; Synonyms=KIAA0843; ORFNames=HMFN1661;
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 3), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH F-ACTIN AND ABRA.
RC TISSUE=Heart;
RX PubMed=17194709; DOI=10.1074/jbc.m607549200;
RA Barrientos T., Frank D., Kuwahara K., Bezprozvannaya S., Pipes G.C.T.,
RA Bassel-Duby R., Richardson J.A., Katus H.A., Olson E.N., Frey N.;
RT "Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate
RT with STARS and directly bind F-actin.";
RL J. Biol. Chem. 282:8393-8403(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Hepatoblastoma;
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 117-683 (ISOFORM 3).
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-504, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-504, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282; SER-286; SER-372;
RP SER-373; TYR-376; SER-388; SER-493; SER-503; SER-504; THR-543 AND SER-576,
RP AND 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).
RN [12]
RP STRUCTURE BY NMR OF 610-683.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the villin headpiece domain of human actin-binding
RT LIM protein homologue (KIAA0843 protein).";
RL Submitted (FEB-2004) to the PDB data bank.
CC -!- FUNCTION: May act as scaffold protein. May stimulate ABRA activity and
CC ABRA-dependent SRF transcriptional activity.
CC {ECO:0000269|PubMed:17194709}.
CC -!- SUBUNIT: Directly interacts with F-actin and ABRA.
CC {ECO:0000269|PubMed:17194709}.
CC -!- INTERACTION:
CC O94929; Q9UKT9: IKZF3; NbExp=4; IntAct=EBI-351267, EBI-747204;
CC O94929; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-351267, EBI-2212028;
CC O94929-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-11961672, EBI-11096309;
CC O94929-2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-11961672, EBI-11524452;
CC O94929-2; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-11961672, EBI-744545;
CC O94929-2; Q9HC52: CBX8; NbExp=3; IntAct=EBI-11961672, EBI-712912;
CC O94929-2; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-11961672, EBI-5453285;
CC O94929-2; Q53FT3: HIKESHI; NbExp=3; IntAct=EBI-11961672, EBI-6137602;
CC O94929-2; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-11961672, EBI-747204;
CC O94929-2; Q9NP74: PALMD; NbExp=3; IntAct=EBI-11961672, EBI-2811699;
CC O94929-2; Q13573: SNW1; NbExp=3; IntAct=EBI-11961672, EBI-632715;
CC O94929-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-11961672, EBI-1105213;
CC O94929-2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-11961672, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O94929-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94929-2; Sequence=VSP_012127, VSP_012128, VSP_012130;
CC Name=3;
CC IsoId=O94929-3; Sequence=VSP_012127, VSP_012129;
CC Name=4;
CC IsoId=O94929-4; Sequence=VSP_012126;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in heart and brain.
CC {ECO:0000269|PubMed:17194709}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74866.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ413174; ABD83327.1; -; mRNA.
DR EMBL; AB020650; BAA74866.2; ALT_INIT; mRNA.
DR EMBL; AK289736; BAF82425.1; -; mRNA.
DR EMBL; AB075881; BAD38663.1; -; mRNA.
DR EMBL; BC001665; AAH01665.1; -; mRNA.
DR EMBL; AL833021; CAH56270.1; -; mRNA.
DR CCDS; CCDS4294.1; -. [O94929-1]
DR CCDS; CCDS78071.1; -. [O94929-2]
DR CCDS; CCDS87335.1; -. [O94929-3]
DR RefSeq; NP_001287944.1; NM_001301015.2. [O94929-1]
DR RefSeq; NP_001287947.1; NM_001301018.2.
DR RefSeq; NP_001287956.1; NM_001301027.2.
DR RefSeq; NP_001287957.1; NM_001301028.2. [O94929-2]
DR RefSeq; NP_001332787.1; NM_001345858.1.
DR RefSeq; NP_001332788.1; NM_001345859.1. [O94929-3]
DR RefSeq; NP_001332789.1; NM_001345860.1.
DR RefSeq; NP_001332790.1; NM_001345861.1. [O94929-3]
DR RefSeq; NP_055760.1; NM_014945.4. [O94929-1]
DR PDB; 1UJS; NMR; -; A=609-683.
DR PDB; 2DJ7; NMR; -; A=141-207.
DR PDBsum; 1UJS; -.
DR PDBsum; 2DJ7; -.
DR AlphaFoldDB; O94929; -.
DR BMRB; O94929; -.
DR SMR; O94929; -.
DR BioGRID; 116552; 37.
DR IntAct; O94929; 25.
DR MINT; O94929; -.
DR STRING; 9606.ENSP00000425394; -.
DR CarbonylDB; O94929; -.
DR GlyGen; O94929; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; O94929; -.
DR PhosphoSitePlus; O94929; -.
DR BioMuta; ABLIM3; -.
DR EPD; O94929; -.
DR jPOST; O94929; -.
DR MassIVE; O94929; -.
DR MaxQB; O94929; -.
DR PaxDb; O94929; -.
DR PeptideAtlas; O94929; -.
DR PRIDE; O94929; -.
DR ProteomicsDB; 50565; -. [O94929-1]
DR ProteomicsDB; 50566; -. [O94929-2]
DR ProteomicsDB; 50567; -. [O94929-3]
DR ProteomicsDB; 50568; -. [O94929-4]
DR Antibodypedia; 1195; 164 antibodies from 22 providers.
DR DNASU; 22885; -.
DR Ensembl; ENST00000309868.12; ENSP00000310309.7; ENSG00000173210.20. [O94929-1]
DR Ensembl; ENST00000326685.11; ENSP00000315841.7; ENSG00000173210.20. [O94929-3]
DR Ensembl; ENST00000504238.5; ENSP00000421183.1; ENSG00000173210.20. [O94929-2]
DR Ensembl; ENST00000506113.5; ENSP00000425394.1; ENSG00000173210.20. [O94929-1]
DR Ensembl; ENST00000517451.5; ENSP00000430150.1; ENSG00000173210.20. [O94929-4]
DR GeneID; 22885; -.
DR KEGG; hsa:22885; -.
DR MANE-Select; ENST00000309868.12; ENSP00000310309.7; NM_014945.5; NP_055760.1.
DR UCSC; uc003lpy.3; human. [O94929-1]
DR CTD; 22885; -.
DR DisGeNET; 22885; -.
DR GeneCards; ABLIM3; -.
DR HGNC; HGNC:29132; ABLIM3.
DR HPA; ENSG00000173210; Tissue enhanced (liver).
DR MIM; 611305; gene.
DR neXtProt; NX_O94929; -.
DR OpenTargets; ENSG00000173210; -.
DR PharmGKB; PA134962761; -.
DR VEuPathDB; HostDB:ENSG00000173210; -.
DR eggNOG; KOG1044; Eukaryota.
DR GeneTree; ENSGT00950000182850; -.
DR InParanoid; O94929; -.
DR OMA; XCAGCKE; -.
DR OrthoDB; 192350at2759; -.
DR PhylomeDB; O94929; -.
DR TreeFam; TF318042; -.
DR PathwayCommons; O94929; -.
DR Reactome; R-HSA-418885; DCC mediated attractive signaling.
DR SignaLink; O94929; -.
DR BioGRID-ORCS; 22885; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; ABLIM3; human.
DR EvolutionaryTrace; O94929; -.
DR GeneWiki; ABLIM3; -.
DR GenomeRNAi; 22885; -.
DR Pharos; O94929; Tdark.
DR PRO; PR:O94929; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O94929; protein.
DR Bgee; ENSG00000173210; Expressed in lower esophagus mucosa and 187 other tissues.
DR ExpressionAtlas; O94929; baseline and differential.
DR Genevisible; O94929; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:MGI.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 1.10.950.10; -; 1.
DR InterPro; IPR028449; ABLIM3.
DR InterPro; IPR032402; AbLIM_anchor.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24213:SF0; PTHR24213:SF0; 1.
DR Pfam; PF16182; AbLIM_anchor; 1.
DR Pfam; PF00412; LIM; 4.
DR Pfam; PF02209; VHP; 1.
DR SMART; SM00132; LIM; 4.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR PROSITE; PS51089; HP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; LIM domain;
KW Metal-binding; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..683
FT /note="Actin-binding LIM protein 3"
FT /id="PRO_0000075702"
FT DOMAIN 21..80
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 80..140
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 149..208
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 208..268
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 615..683
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 372..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX8"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX8"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX8"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX8"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 376
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX8"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX8"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX8"
FT MOD_RES 631
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX8"
FT VAR_SEQ 1..514
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15221005"
FT /id="VSP_012126"
FT VAR_SEQ 297..358
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17194709, ECO:0000303|PubMed:17974005"
FT /id="VSP_012127"
FT VAR_SEQ 402..450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012128"
FT VAR_SEQ 402..434
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17194709,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_012129"
FT VAR_SEQ 647..683
FT /note="RHLSQEEFYQVFGMTISEFDRLALWKRNELKKQARLF -> GNFWKSGCL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012130"
FT VARIANT 125
FT /note="G -> D (in dbSNP:rs35907283)"
FT /id="VAR_050143"
FT CONFLICT 227
FT /note="K -> R (in Ref. 3; BAF82425)"
FT /evidence="ECO:0000305"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:2DJ7"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2DJ7"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2DJ7"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2DJ7"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:2DJ7"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2DJ7"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2DJ7"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2DJ7"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:2DJ7"
FT TURN 623..626
FT /evidence="ECO:0007829|PDB:1UJS"
FT TURN 630..633
FT /evidence="ECO:0007829|PDB:1UJS"
FT TURN 642..644
FT /evidence="ECO:0007829|PDB:1UJS"
FT HELIX 645..648
FT /evidence="ECO:0007829|PDB:1UJS"
FT HELIX 653..658
FT /evidence="ECO:0007829|PDB:1UJS"
FT HELIX 662..665
FT /evidence="ECO:0007829|PDB:1UJS"
FT HELIX 670..679
FT /evidence="ECO:0007829|PDB:1UJS"
SQ SEQUENCE 683 AA; 77802 MW; 0392DBD9065EE08A CRC64;
MNTSIPYQQN PYNPRGSSNV IQCYRCGDTC KGEVVRVHNN HFHIRCFTCQ VCGCGLAQSG
FFFKNQEYIC TQDYQQLYGT RCDSCRDFIT GEVISALGRT YHPKCFVCSL CRKPFPIGDK
VTFSGKECVC QTCSQSMASS KPIKIRGPSH CAGCKEEIKH GQSLLALDKQ WHVSCFKCQT
CSVILTGEYI SKDGVPYCES DYHAQFGIKC ETCDRYISGR VLEAGGKHYH PTCARCVRCH
QMFTEGEEMY LTGSEVWHPI CKQAARAEKK LKHRRTSETS ISPPGSSIGS PNRVICAKVD
NEILNYKDLA ALPKVKSIYE VQRPDLISYE PHSRYMSDEM LERCGYGESL GTLSPYSQDI
YENLDLRQRR ASSPGYIDSP TYSRQGMSPT FSRSPHHYYR SGPESGRSSP YHSQLDVRSS
TPTSYQAPKH FHIPAGDSNI YRKPPIYKRH GDLSTATKSK TSEDISQTSK YSPIYSPDPY
YASESEYWTY HGSPKVPRAR RFSSGGEEDD FDRSMHKLQS GIGRLILKEE MKARSSSYAD
PWTPPRSSTS SREALHTAGY EMSLNGSPRS HYLADSDPLI SKSASLPAYR RNGLHRTPSA
DLFHYDSMNA VNWGMREYKI YPYELLLVTT RGRNRLPKDV DRTRLERHLS QEEFYQVFGM
TISEFDRLAL WKRNELKKQA RLF
