ID ABLM1_HUMAN Reviewed; 778 AA.
AC O14639; A6NI16; A6NJ06; A8MXA9; B3KVH2; Q15039; Q5JVV1; Q5JVV2; Q5T6N2;
AC Q5T6N3; Q5T6N5; Q68CQ9; Q9BUP1;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 3.
DT 27-MAR-2024, entry version 209.
DE RecName: Full=Actin-binding LIM protein 1;
DE Short=abLIM-1;
DE AltName: Full=Actin-binding LIM protein family member 1;
DE AltName: Full=Actin-binding double zinc finger protein;
DE AltName: Full=LIMAB1;
DE AltName: Full=Limatin;
GN Name=ABLIM1; Synonyms=ABLIM, KIAA0059, LIMAB1;
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), FUNCTION, ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=9245787; DOI=10.1083/jcb.138.3.575;
RA Roof D.J., Hayes A., Adamian M., Chishti A.H., Li T.;
RT "Molecular characterization of abLIM, a novel actin-binding and double zinc
RT finger protein.";
RL J. Cell Biol. 138:575-588(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
RC TISSUE=Pericardium, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Retina;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Kidney;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-396, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP INTERACTION WITH ABRA.
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-435; SER-455;
RP SER-458; SER-587; SER-640 AND SER-655, AND IDENTIFICATION BY MASS
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; TYR-373; SER-426;
RP SER-431; THR-433 AND SER-435, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-640, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND IDENTIFICATION BY
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; SER-431; SER-435;
RP SER-452; SER-455; SER-458; SER-587 AND SER-655, AND IDENTIFICATION BY MASS
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426; SER-435; SER-455 AND
RP SER-706, 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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-620, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May act as scaffold protein (By similarity). May play a role
CC in the development of the retina. Has been suggested to play a role in
CC axon guidance. {ECO:0000250, ECO:0000269|PubMed:9245787}.
CC -!- SUBUNIT: Binds F-actin. Interacts with ABRA.
CC {ECO:0000269|PubMed:17194709}.
CC -!- INTERACTION:
CC O14639; Q9H257: CARD9; NbExp=3; IntAct=EBI-487024, EBI-751319;
CC O14639; O95751: LDOC1; NbExp=2; IntAct=EBI-487024, EBI-740738;
CC O14639; P31947: SFN; NbExp=5; IntAct=EBI-487024, EBI-476295;
CC O14639; P62258: YWHAE; NbExp=6; IntAct=EBI-487024, EBI-356498;
CC O14639-4; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-11030084, EBI-10961624;
CC O14639-4; Q14192: FHL2; NbExp=3; IntAct=EBI-11030084, EBI-701903;
CC O14639-4; O75031: HSF2BP; NbExp=3; IntAct=EBI-11030084, EBI-7116203;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Associated with the cytoskeleton. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O14639-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14639-2; Sequence=VSP_012100;
CC Name=3;
CC IsoId=O14639-3; Sequence=VSP_012099, VSP_012102;
CC Name=4;
CC IsoId=O14639-4; Sequence=VSP_012099, VSP_012101, VSP_012102;
CC Name=5;
CC IsoId=O14639-5; Sequence=VSP_012099, VSP_041185, VSP_012102;
CC Name=6;
CC IsoId=O14639-6; Sequence=VSP_012100, VSP_041185, VSP_057209;
CC -!- TISSUE SPECIFICITY: Detected in liver, heart, skeletal muscle, brain
CC and retina, where it is concentrated in the inner segment and in the
CC outer plexiform layers. {ECO:0000269|PubMed:9245787}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06681.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF005654; AAC51676.1; -; mRNA.
DR EMBL; D31883; BAA06681.2; ALT_INIT; mRNA.
DR EMBL; AK098277; BAG53605.1; -; mRNA.
DR EMBL; AK122891; BAG53784.1; -; mRNA.
DR EMBL; CR749819; CAH18679.1; -; mRNA.
DR EMBL; AL133384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002448; AAH02448.1; -; mRNA.
DR CCDS; CCDS31288.1; -. [O14639-2]
DR CCDS; CCDS31289.1; -. [O14639-5]
DR CCDS; CCDS7590.1; -. [O14639-1]
DR CCDS; CCDS81508.1; -. [O14639-4]
DR CCDS; CCDS81509.1; -. [O14639-6]
DR RefSeq; NP_001003407.1; NM_001003407.1. [O14639-2]
DR RefSeq; NP_001309811.1; NM_001322882.1. [O14639-6]
DR RefSeq; NP_001309821.1; NM_001322892.1. [O14639-3]
DR RefSeq; NP_001309822.1; NM_001322893.1. [O14639-3]
DR RefSeq; NP_001309825.1; NM_001322896.1. [O14639-4]
DR RefSeq; NP_002304.3; NM_002313.5. [O14639-1]
DR RefSeq; NP_006711.3; NM_006720.3. [O14639-5]
DR AlphaFoldDB; O14639; -.
DR SMR; O14639; -.
DR BioGRID; 110171; 188.
DR IntAct; O14639; 103.
DR MINT; O14639; -.
DR STRING; 9606.ENSP00000277895; -.
DR GlyConnect; 2904; 1 O-GlcNAc glycan (1 site).
DR GlyCosmos; O14639; 15 sites, 2 glycans.
DR GlyGen; O14639; 18 sites, 2 O-linked glycans (18 sites).
DR iPTMnet; O14639; -.
DR PhosphoSitePlus; O14639; -.
DR BioMuta; ABLIM1; -.
DR CPTAC; CPTAC-957; -.
DR EPD; O14639; -.
DR jPOST; O14639; -.
DR MassIVE; O14639; -.
DR MaxQB; O14639; -.
DR PaxDb; 9606-ENSP00000277895; -.
DR PeptideAtlas; O14639; -.
DR ProteomicsDB; 48133; -. [O14639-1]
DR ProteomicsDB; 48134; -. [O14639-2]
DR ProteomicsDB; 48135; -. [O14639-3]
DR ProteomicsDB; 48136; -. [O14639-4]
DR ProteomicsDB; 48137; -. [O14639-5]
DR ProteomicsDB; 64602; -.
DR Pumba; O14639; -.
DR Antibodypedia; 31944; 223 antibodies from 28 providers.
DR DNASU; 3983; -.
DR Ensembl; ENST00000369253.6; ENSP00000358257.2; ENSG00000099204.22. [O14639-4]
DR Ensembl; ENST00000369256.6; ENSP00000358260.3; ENSG00000099204.22. [O14639-6]
DR Ensembl; ENST00000392952.7; ENSP00000376679.3; ENSG00000099204.22. [O14639-5]
DR Ensembl; ENST00000392955.7; ENSP00000376682.4; ENSG00000099204.22. [O14639-2]
DR Ensembl; ENST00000533213.7; ENSP00000433629.3; ENSG00000099204.22. [O14639-1]
DR GeneID; 3983; -.
DR KEGG; hsa:3983; -.
DR MANE-Select; ENST00000533213.7; ENSP00000433629.3; NM_002313.7; NP_002304.3.
DR UCSC; uc057wcr.1; human. [O14639-1]
DR AGR; HGNC:78; -.
DR CTD; 3983; -.
DR DisGeNET; 3983; -.
DR GeneCards; ABLIM1; -.
DR HGNC; HGNC:78; ABLIM1.
DR HPA; ENSG00000099204; Low tissue specificity.
DR MIM; 602330; gene.
DR neXtProt; NX_O14639; -.
DR OpenTargets; ENSG00000099204; -.
DR PharmGKB; PA35023; -.
DR VEuPathDB; HostDB:ENSG00000099204; -.
DR eggNOG; KOG1044; Eukaryota.
DR GeneTree; ENSGT00950000182850; -.
DR HOGENOM; CLU_001357_12_2_1; -.
DR InParanoid; O14639; -.
DR OMA; RDYNERH; -.
DR OrthoDB; 370973at2759; -.
DR PhylomeDB; O14639; -.
DR TreeFam; TF318042; -.
DR PathwayCommons; O14639; -.
DR Reactome; R-HSA-418885; DCC mediated attractive signaling.
DR SignaLink; O14639; -.
DR BioGRID-ORCS; 3983; 12 hits in 1147 CRISPR screens.
DR ChiTaRS; ABLIM1; human.
DR GeneWiki; ABLIM1; -.
DR GenomeRNAi; 3983; -.
DR Pharos; O14639; Tbio.
DR PRO; PR:O14639; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O14639; Protein.
DR Bgee; ENSG00000099204; Expressed in left ventricle myocardium and 215 other cell types or tissues.
DR ExpressionAtlas; O14639; baseline and differential.
DR Genevisible; O14639; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
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:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:MGI.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd09327; LIM1_abLIM; 1.
DR CDD; cd09328; LIM2_abLIM; 1.
DR CDD; cd09329; LIM3_abLIM; 1.
DR CDD; cd09330; LIM4_abLIM; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR Gene3D; 1.10.950.10; Villin headpiece domain; 1.
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; ACTIN-BINDING LIM PROTEIN; 1.
DR PANTHER; PTHR24213:SF18; ACTIN-BINDING LIM PROTEIN 1; 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 6.
DR SUPFAM; SSF47050; VHP, Villin headpiece domain; 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 Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Zinc.
FT CHAIN 1..778
FT /note="Actin-binding LIM protein 1"
FT /id="PRO_0000075697"
FT DOMAIN 97..156
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 156..216
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 224..283
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 283..343
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 710..778
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 339..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 590..614
FT /evidence="ECO:0000255"
FT COMPBIAS 351..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4G5"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 373
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 396
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 439
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4G5"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4G5"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 620
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..316
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_012099"
FT VAR_SEQ 1..81
FT /note="MPAFLGLKCLGKLCSSEKSKVTSSERTSARGSNRKRLIVEDRRVSGTSFTAH
FT RRATITHLLYLCPKDYCPRGRVCNSVDPF -> MLMTLEMTELTDPHHTMGDYK (in
FT isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:7584044"
FT /id="VSP_012100"
FT VAR_SEQ 347
FT /note="R -> RLPNIRRSSSDFFYSKSLIRRTGRSPSLQ (in isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041185"
FT VAR_SEQ 348..373
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012101"
FT VAR_SEQ 480..514
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_012102"
FT VAR_SEQ 531
FT /note="H -> HDA (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057209"
FT VARIANT 434
FT /note="P -> T (in dbSNP:rs11593544)"
FT /id="VAR_050141"
FT VARIANT 637
FT /note="R -> G (in dbSNP:rs7091419)"
FT /id="VAR_050142"
FT CONFLICT 499
FT /note="R -> L (in Ref. 1; AAC51676)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="A -> R (in Ref. 1; AAC51676)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="K -> E (in Ref. 2; BAA06681)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="V -> I (in Ref. 2; BAA06681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 87688 MW; EBC2F14BE558752B CRC64;
MPAFLGLKCL GKLCSSEKSK VTSSERTSAR GSNRKRLIVE DRRVSGTSFT AHRRATITHL
LYLCPKDYCP RGRVCNSVDP FVAHPQDPHH PSEKPVIHCH KCGEPCKGEV LRVQTKHFHI
KCFTCKVCGC DLAQGGFFIK NGEYLCTLDY QRMYGTRCHG CGEFVEGEVV TALGKTYHPN
CFACTICKRP FPPGDRVTFN GRDCLCQLCA QPMSSSPKET TFSSNCAGCG RDIKNGQALL
ALDKQWHLGC FKCKSCGKVL TGEYISKDGA PYCEKDYQGL FGVKCEACHQ FITGKVLEAG
DKHYHPSCAR CSRCNQMFTE GEEMYLQGST VWHPDCKQST KTEEKLRPTR TSSESIYSRP
GSSIPGSPGH TIYAKVDNEI LDYKDLAAIP KVKAIYDIER PDLITYEPFY TSGYDDKQER
QSLGESPRTL SPTPSAEGYQ DVRDRMIHRS TSQGSINSPV YSRHSYTPTT SRSPQHFHRP
GNEPSSGRNS PLPYRPDSRP LTPTYAQAPK HFHVPDQGIN IYRKPPIYKQ HAALAAQSKS
SEDIIKFSKF PAAQAPDPSE TPKIETDHWP GPPSFAVVGP DMKRRSSGRE EDDEELLRRR
QLQEEQLMKL NSGLGQLILK EEMEKESRER SSLLASRYDS PINSASHIPS SKTASLPGYG
RNGLHRPVST DFAQYNSYGD VSGGVRDYQT LPDGHMPAMR MDRGVSMPNM LEPKIFPYEM
LMVTNRGRNK ILREVDRTRL ERHLAPEVFR EIFGMSIQEF DRLPLWRRND MKKKAKLF
//
