ABLM2_HUMAN
ID ABLM2_HUMAN Reviewed; 611 AA.
AC Q6H8Q1; E9PF39; Q08E71; Q19VH0; Q6H8Q0; Q6NX73; Q8N3C5; Q8N9E9; Q8N9G2;
AC Q96JL7;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Actin-binding LIM protein 2;
DE Short=abLIM-2;
DE AltName: Full=Actin-binding LIM protein family member 2;
GN Name=ABLIM2; Synonyms=KIAA1808;
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 7), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH ABRA AND F-ACTIN.
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 [MRNA] (ISOFORMS 1 AND 2).
RA Klimov E.A., Rakhmanaliev E.R., Rudco O.I.;
RT "Structure and transcriptional activity of the ABLIM2 gene of human, mouse
RT and rat.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 8).
RC TISSUE=PNS;
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 34-611 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 390-572 (ISOFORM 5).
RC TISSUE=Amygdala;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [9]
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).
RN [10]
RP STRUCTURE BY NMR OF 73-140 AND 212-271, AND ZINC-BINDING SITES.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the LIM domain of the human actin binding LIM
RT protein 2.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [11]
RP VARIANTS [LARGE SCALE ANALYSIS] ARG-227 AND MET-274.
RX PubMed=18772397; DOI=10.1126/science.1164368;
RA Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
RA Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T.,
RA Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y.,
RA Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M.,
RA Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E.,
RA Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B.,
RA Velculescu V.E., Kinzler K.W.;
RT "Core signaling pathways in human pancreatic cancers revealed by global
RT genomic analyses.";
RL Science 321:1801-1806(2008).
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: Interacts with F-actin and ABRA.
CC {ECO:0000269|PubMed:17194709}.
CC -!- INTERACTION:
CC Q6H8Q1-8; A0A0S2Z5Z3: C6orf142; NbExp=3; IntAct=EBI-16436655, EBI-16435510;
CC Q6H8Q1-8; A0A0S2Z6I7: C6orf142; NbExp=4; IntAct=EBI-16436655, EBI-16435493;
CC Q6H8Q1-8; P28329-3: CHAT; NbExp=3; IntAct=EBI-16436655, EBI-25837549;
CC Q6H8Q1-8; G5E9A7: DMWD; NbExp=3; IntAct=EBI-16436655, EBI-10976677;
CC Q6H8Q1-8; P22607: FGFR3; NbExp=3; IntAct=EBI-16436655, EBI-348399;
CC Q6H8Q1-8; P14136: GFAP; NbExp=3; IntAct=EBI-16436655, EBI-744302;
CC Q6H8Q1-8; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-16436655, EBI-1055254;
CC Q6H8Q1-8; P02545: LMNA; NbExp=3; IntAct=EBI-16436655, EBI-351935;
CC Q6H8Q1-8; P35240: NF2; NbExp=3; IntAct=EBI-16436655, EBI-1014472;
CC Q6H8Q1-8; Q9BZ23-2: PANK2; NbExp=3; IntAct=EBI-16436655, EBI-25929070;
CC Q6H8Q1-8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-16436655, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In skeletal muscle, sarcomeric or
CC cosarcomeric localization. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q6H8Q1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6H8Q1-2; Sequence=VSP_012117;
CC Name=3;
CC IsoId=Q6H8Q1-3; Sequence=VSP_012113, VSP_012115, VSP_012117;
CC Name=4;
CC IsoId=Q6H8Q1-4; Sequence=VSP_012112, VSP_012113, VSP_012114,
CC VSP_012116;
CC Name=5;
CC IsoId=Q6H8Q1-5; Sequence=VSP_012116, VSP_012117;
CC Name=6;
CC IsoId=Q6H8Q1-6; Sequence=VSP_012113, VSP_012115, VSP_012116,
CC VSP_012118, VSP_012119;
CC Name=7;
CC IsoId=Q6H8Q1-7; Sequence=VSP_012115;
CC Name=8;
CC IsoId=Q6H8Q1-8; Sequence=VSP_012115, VSP_012116, VSP_012117;
CC Name=9;
CC IsoId=Q6H8Q1-9; Sequence=VSP_046646, VSP_012116;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle.
CC {ECO:0000269|PubMed:17194709}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH67214.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ413177; ABD83330.1; -; mRNA.
DR EMBL; AJ748600; CAG38375.1; -; mRNA.
DR EMBL; AJ748601; CAG38376.1; -; mRNA.
DR EMBL; AK094754; BAC04414.1; -; mRNA.
DR EMBL; AK094798; BAC04427.1; -; mRNA.
DR EMBL; AC097381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067214; AAH67214.1; ALT_INIT; mRNA.
DR EMBL; BC122567; AAI22568.1; -; mRNA.
DR EMBL; AB058711; BAB47437.1; -; mRNA.
DR EMBL; AL834195; CAD38885.2; -; mRNA.
DR CCDS; CCDS47011.1; -. [Q6H8Q1-7]
DR CCDS; CCDS47012.1; -. [Q6H8Q1-2]
DR CCDS; CCDS47013.1; -. [Q6H8Q1-1]
DR CCDS; CCDS47014.1; -. [Q6H8Q1-9]
DR CCDS; CCDS47015.1; -. [Q6H8Q1-3]
DR CCDS; CCDS47016.1; -. [Q6H8Q1-6]
DR CCDS; CCDS54719.1; -. [Q6H8Q1-8]
DR CCDS; CCDS68669.1; -. [Q6H8Q1-4]
DR RefSeq; NP_001123555.1; NM_001130083.1. [Q6H8Q1-9]
DR RefSeq; NP_001123556.1; NM_001130084.1. [Q6H8Q1-1]
DR RefSeq; NP_001123557.1; NM_001130085.1. [Q6H8Q1-2]
DR RefSeq; NP_001123558.1; NM_001130086.1. [Q6H8Q1-7]
DR RefSeq; NP_001123559.1; NM_001130087.1. [Q6H8Q1-3]
DR RefSeq; NP_001123560.1; NM_001130088.1. [Q6H8Q1-6]
DR RefSeq; NP_001273617.1; NM_001286688.1. [Q6H8Q1-4]
DR RefSeq; NP_115808.3; NM_032432.4. [Q6H8Q1-8]
DR PDB; 1V6G; NMR; -; A=73-140.
DR PDB; 1WIG; NMR; -; A=212-271.
DR PDB; 2L3X; NMR; -; A=546-611.
DR PDBsum; 1V6G; -.
DR PDBsum; 1WIG; -.
DR PDBsum; 2L3X; -.
DR AlphaFoldDB; Q6H8Q1; -.
DR BMRB; Q6H8Q1; -.
DR SMR; Q6H8Q1; -.
DR BioGRID; 124086; 14.
DR IntAct; Q6H8Q1; 15.
DR STRING; 9606.ENSP00000393511; -.
DR GlyGen; Q6H8Q1; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q6H8Q1; -.
DR PhosphoSitePlus; Q6H8Q1; -.
DR BioMuta; ABLIM2; -.
DR DMDM; 56404514; -.
DR EPD; Q6H8Q1; -.
DR jPOST; Q6H8Q1; -.
DR MassIVE; Q6H8Q1; -.
DR MaxQB; Q6H8Q1; -.
DR PeptideAtlas; Q6H8Q1; -.
DR PRIDE; Q6H8Q1; -.
DR ProteomicsDB; 20020; -.
DR ProteomicsDB; 66340; -. [Q6H8Q1-1]
DR ProteomicsDB; 66341; -. [Q6H8Q1-2]
DR ProteomicsDB; 66342; -. [Q6H8Q1-3]
DR ProteomicsDB; 66343; -. [Q6H8Q1-4]
DR ProteomicsDB; 66344; -. [Q6H8Q1-5]
DR ProteomicsDB; 66345; -. [Q6H8Q1-6]
DR ProteomicsDB; 66346; -. [Q6H8Q1-7]
DR ProteomicsDB; 66347; -. [Q6H8Q1-8]
DR Antibodypedia; 22725; 51 antibodies from 15 providers.
DR DNASU; 84448; -.
DR Ensembl; ENST00000341937.9; ENSP00000342813.5; ENSG00000163995.21. [Q6H8Q1-1]
DR Ensembl; ENST00000361581.9; ENSP00000355003.5; ENSG00000163995.21. [Q6H8Q1-2]
DR Ensembl; ENST00000361737.9; ENSP00000354887.5; ENSG00000163995.21. [Q6H8Q1-3]
DR Ensembl; ENST00000407564.7; ENSP00000384658.3; ENSG00000163995.21. [Q6H8Q1-8]
DR Ensembl; ENST00000428004.6; ENSP00000389410.2; ENSG00000163995.21. [Q6H8Q1-6]
DR Ensembl; ENST00000447017.7; ENSP00000393511.2; ENSG00000163995.21. [Q6H8Q1-9]
DR Ensembl; ENST00000505872.5; ENSP00000421283.1; ENSG00000163995.21. [Q6H8Q1-7]
DR Ensembl; ENST00000514025.5; ENSP00000423661.1; ENSG00000163995.21. [Q6H8Q1-4]
DR GeneID; 84448; -.
DR KEGG; hsa:84448; -.
DR MANE-Select; ENST00000447017.7; ENSP00000393511.2; NM_001130083.2; NP_001123555.1. [Q6H8Q1-9]
DR UCSC; uc003gkj.5; human. [Q6H8Q1-1]
DR CTD; 84448; -.
DR DisGeNET; 84448; -.
DR GeneCards; ABLIM2; -.
DR HGNC; HGNC:19195; ABLIM2.
DR HPA; ENSG00000163995; Group enriched (skeletal muscle, tongue).
DR MIM; 612544; gene.
DR neXtProt; NX_Q6H8Q1; -.
DR OpenTargets; ENSG00000163995; -.
DR PharmGKB; PA134940437; -.
DR VEuPathDB; HostDB:ENSG00000163995; -.
DR eggNOG; KOG1044; Eukaryota.
DR GeneTree; ENSGT00950000182850; -.
DR HOGENOM; CLU_001357_12_3_1; -.
DR InParanoid; Q6H8Q1; -.
DR OMA; XNANLAP; -.
DR OrthoDB; 192350at2759; -.
DR PhylomeDB; Q6H8Q1; -.
DR TreeFam; TF318042; -.
DR PathwayCommons; Q6H8Q1; -.
DR Reactome; R-HSA-418885; DCC mediated attractive signaling.
DR SignaLink; Q6H8Q1; -.
DR BioGRID-ORCS; 84448; 9 hits in 1073 CRISPR screens.
DR ChiTaRS; ABLIM2; human.
DR EvolutionaryTrace; Q6H8Q1; -.
DR GenomeRNAi; 84448; -.
DR Pharos; Q6H8Q1; Tdark.
DR PRO; PR:Q6H8Q1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6H8Q1; protein.
DR Bgee; ENSG00000163995; Expressed in tibialis anterior and 159 other tissues.
DR ExpressionAtlas; Q6H8Q1; baseline and differential.
DR Genevisible; Q6H8Q1; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0030032; P:lamellipodium assembly; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.950.10; -; 1.
DR InterPro; IPR028450; ABLIM2.
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:SF6; PTHR24213:SF6; 2.
DR Pfam; PF16182; AbLIM_anchor; 2.
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; Alternative splicing; Cytoplasm; LIM domain; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..611
FT /note="Actin-binding LIM protein 2"
FT /id="PRO_0000075699"
FT DOMAIN 22..81
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 81..141
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 151..210
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 210..270
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 543..611
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 269..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC51"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BL65"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BL65"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC51"
FT MOD_RES 472
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BL65"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC51"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC51"
FT VAR_SEQ 1..243
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012112"
FT VAR_SEQ 349
FT /note="E -> ESPQLLSPTPTE (in isoform 3, isoform 4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012113"
FT VAR_SEQ 389..422
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012114"
FT VAR_SEQ 389
FT /note="P -> PAGTVSVGTSSCLSLSQHPSPTSVFRHHYIPYFR (in isoform
FT 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_046646"
FT VAR_SEQ 390..441
FT /note="Missing (in isoform 3, isoform 6, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17194709"
FT /id="VSP_012115"
FT VAR_SEQ 459
FT /note="K -> KQ (in isoform 4, isoform 5, isoform 6, isoform
FT 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_012116"
FT VAR_SEQ 506..545
FT /note="RFPYSKSDPLPGHGKNGLDQRNANLAPCGADPDASWGMRE -> Q (in
FT isoform 2, isoform 3, isoform 5 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:11347906,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2"
FT /id="VSP_012117"
FT VAR_SEQ 507..510
FT /note="FPYS -> EWFF (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012118"
FT VAR_SEQ 511..611
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012119"
FT VARIANT 227
FT /note="G -> R (in a pancreatic ductal adenocarcinoma
FT sample; somatic mutation; dbSNP:rs757430763)"
FT /evidence="ECO:0000269|PubMed:18772397"
FT /id="VAR_062665"
FT VARIANT 274
FT /note="K -> M (in a pancreatic ductal adenocarcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:18772397"
FT /id="VAR_062666"
FT CONFLICT 240
FT /note="R -> G (in Ref. 3; BAC04414)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="D -> G (in Ref. 3; BAC04414)"
FT /evidence="ECO:0000305"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1V6G"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1V6G"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1V6G"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1V6G"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1V6G"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1V6G"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1V6G"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1V6G"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1V6G"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1V6G"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1WIG"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1WIG"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1WIG"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1WIG"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:1WIG"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:1WIG"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1WIG"
FT HELIX 551..554
FT /evidence="ECO:0007829|PDB:2L3X"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:2L3X"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:2L3X"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:2L3X"
FT HELIX 573..576
FT /evidence="ECO:0007829|PDB:2L3X"
FT HELIX 579..586
FT /evidence="ECO:0007829|PDB:2L3X"
FT HELIX 590..595
FT /evidence="ECO:0007829|PDB:2L3X"
FT HELIX 598..607
FT /evidence="ECO:0007829|PDB:2L3X"
SQ SEQUENCE 611 AA; 67812 MW; 225A4E25646B370B CRC64;
MSAVSQPQAA PSPLEKSPST AILCNTCGNV CKGEVLRVQD KYFHIKCFVC KACGCDLAEG
GFFVRQGEYI CTLDYQRLYG TRCFSCDQFI EGEVVSALGK TYHPDCFVCA VCRLPFPPGD
RVTFNGKECM CQKCSLPVSV GSSAHLSQGL RSCGGCGTEI KNGQALVALD KHWHLGCFKC
KSCGKLLNAE YISKDGLPYC EADYHAKFGI RCDSCEKYIT GRVLEAGEKH YHPSCALCVR
CGQMFAEGEE MYLQGSSIWH PACRQAARTE DRNKETRTSS ESIISVPASS TSGSPSRVIY
AKLGGEILDY RDLAALPKSK AIYDIDRPDM ISYSPYISHS AGDRQSYGEG DQDDRSYKQC
RTSSPSSTGS VSLGRYTPTS RSPQHYSRPG SESGRSTPSL SVLSDSKPPP STYQQAPRHF
HVPDTGVKDN IYRKPPIYRQ HAARRSDGED GSLDQDNRKK SSWLMLKGDA DTRTNSPDLD
TQSLSHSSGT DRDPLQRMAG DSFHSRFPYS KSDPLPGHGK NGLDQRNANL APCGADPDAS
WGMREYKIYP YDSLIVTNRI RVKLPKDVDR TRLERHLSPE EFQEVFGMSI EEFDRLALWK
RNDLKKKALL F
