LIMD2_HUMAN
ID LIMD2_HUMAN Reviewed; 127 AA.
AC Q9BT23; D3DU16; Q96S91;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=LIM domain-containing protein 2 {ECO:0000305};
GN Name=LIMD2 {ECO:0000312|HGNC:HGNC:28142}; ORFNames=SB143;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Li N., Zhang W., Zhang M., Wan T., Cao X.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7] {ECO:0007744|PDB:2LZU}
RP STRUCTURE BY NMR OF 33-104 IN COMPLEX WITH ZINC, ZINC-BINDING, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=24590809; DOI=10.1158/0008-5472.can-13-1275;
RA Peng H., Talebzadeh-Farrooji M., Osborne M.J., Prokop J.W., McDonald P.C.,
RA Karar J., Hou Z., He M., Kebebew E., Orntoft T., Herlyn M., Caton A.J.,
RA Fredericks W., Malkowicz B., Paterno C.S., Carolin A.S., Speicher D.W.,
RA Skordalakes E., Huang Q., Dedhar S., Borden K.L., Rauscher F.J. III;
RT "LIMD2 is a small LIM-only protein overexpressed in metastatic lesions that
RT regulates cell motility and tumor progression by directly binding to and
RT activating the integrin-linked kinase.";
RL Cancer Res. 74:1390-1403(2014).
CC -!- FUNCTION: Acts as an activator of the protein-kinase ILK, thereby
CC regulating cell motility (PubMed:24590809).
CC {ECO:0000269|PubMed:24590809}.
CC -!- SUBUNIT: Interacts with ILK (PubMed:24590809).
CC {ECO:0000269|PubMed:24590809}.
CC -!- INTERACTION:
CC Q9BT23; P60900: PSMA6; NbExp=3; IntAct=EBI-2805292, EBI-357793;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24590809}. Nucleus
CC {ECO:0000269|PubMed:24590809}. Note=Mainly found in cytoplasm,
CC concentrated in membrane ruffles and in streaks reminiscent of focal
CC adhesion plaques (PubMed:24590809). Also found in nucleus
CC (PubMed:24590809). {ECO:0000269|PubMed:24590809}.
CC -!- INDUCTION: Over-expressed in breast, bladder, melanoma and thyroid
CC cancer cell lines and tumors (at protein level).
CC {ECO:0000269|PubMed:24590809}.
CC -!- MISCELLANEOUS: May play a role in tumor progression via its ability to
CC activate the ILK protein-kinase activity.
CC {ECO:0000269|PubMed:24590809}.
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DR EMBL; AK092301; BAC03855.1; -; mRNA.
DR EMBL; AY037154; AAK67634.1; -; mRNA.
DR EMBL; CH471109; EAW94291.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94292.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94294.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94295.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94296.1; -; Genomic_DNA.
DR EMBL; BC004400; AAH04400.1; -; mRNA.
DR EMBL; BC051812; AAH51812.1; -; mRNA.
DR CCDS; CCDS11641.1; -.
DR RefSeq; NP_085053.1; NM_030576.3.
DR RefSeq; XP_005257760.1; XM_005257703.1.
DR RefSeq; XP_005257762.1; XM_005257705.3.
DR RefSeq; XP_006722187.1; XM_006722124.1.
DR PDB; 2LZU; NMR; -; A=33-104.
DR PDBsum; 2LZU; -.
DR AlphaFoldDB; Q9BT23; -.
DR BMRB; Q9BT23; -.
DR SMR; Q9BT23; -.
DR BioGRID; 123306; 17.
DR IntAct; Q9BT23; 2.
DR STRING; 9606.ENSP00000259006; -.
DR iPTMnet; Q9BT23; -.
DR PhosphoSitePlus; Q9BT23; -.
DR BioMuta; LIMD2; -.
DR DMDM; 74752322; -.
DR EPD; Q9BT23; -.
DR MassIVE; Q9BT23; -.
DR MaxQB; Q9BT23; -.
DR PaxDb; Q9BT23; -.
DR PeptideAtlas; Q9BT23; -.
DR PRIDE; Q9BT23; -.
DR ProteomicsDB; 78944; -.
DR Antibodypedia; 45674; 89 antibodies from 19 providers.
DR DNASU; 80774; -.
DR Ensembl; ENST00000259006.8; ENSP00000259006.3; ENSG00000136490.9.
DR Ensembl; ENST00000578061.5; ENSP00000464003.1; ENSG00000136490.9.
DR Ensembl; ENST00000578402.5; ENSP00000462707.1; ENSG00000136490.9.
DR GeneID; 80774; -.
DR KEGG; hsa:80774; -.
DR MANE-Select; ENST00000259006.8; ENSP00000259006.3; NM_030576.4; NP_085053.1.
DR UCSC; uc002jbj.5; human.
DR CTD; 80774; -.
DR DisGeNET; 80774; -.
DR GeneCards; LIMD2; -.
DR HGNC; HGNC:28142; LIMD2.
DR HPA; ENSG00000136490; Tissue enhanced (bone marrow, lymphoid tissue).
DR neXtProt; NX_Q9BT23; -.
DR OpenTargets; ENSG00000136490; -.
DR PharmGKB; PA143485528; -.
DR VEuPathDB; HostDB:ENSG00000136490; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000158377; -.
DR InParanoid; Q9BT23; -.
DR OMA; MFQDAGA; -.
DR OrthoDB; 1583903at2759; -.
DR PhylomeDB; Q9BT23; -.
DR PathwayCommons; Q9BT23; -.
DR SignaLink; Q9BT23; -.
DR BioGRID-ORCS; 80774; 20 hits in 1072 CRISPR screens.
DR ChiTaRS; LIMD2; human.
DR GenomeRNAi; 80774; -.
DR Pharos; Q9BT23; Tbio.
DR PRO; PR:Q9BT23; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BT23; protein.
DR Bgee; ENSG00000136490; Expressed in granulocyte and 100 other tissues.
DR ExpressionAtlas; Q9BT23; baseline and differential.
DR Genevisible; Q9BT23; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd09486; LIM_Eplin_like_1; 1.
DR InterPro; IPR044115; LIM_LIMD2.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00132; LIM; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; LIM domain; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..127
FT /note="LIM domain-containing protein 2"
FT /id="PRO_0000251207"
FT DOMAIN 38..98
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24590809,
FT ECO:0007744|PDB:2LZU"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24590809,
FT ECO:0007744|PDB:2LZU"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24590809,
FT ECO:0007744|PDB:2LZU"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24590809,
FT ECO:0007744|PDB:2LZU"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24590809,
FT ECO:0007744|PDB:2LZU"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24590809,
FT ECO:0007744|PDB:2LZU"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24590809,
FT ECO:0007744|PDB:2LZU"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24590809,
FT ECO:0007744|PDB:2LZU"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CONFLICT 6
FT /note="G -> E (in Ref. 2; AAK67634)"
FT /evidence="ECO:0000305"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2LZU"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2LZU"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2LZU"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2LZU"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2LZU"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2LZU"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2LZU"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2LZU"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:2LZU"
SQ SEQUENCE 127 AA; 14070 MW; B63174FCF0486956 CRC64;
MFQAAGAAQA TPSHDAKGGG SSTVQRSKSF SLRAQVKETC AACQKTVYPM ERLVADKLIF
HNSCFCCKHC HTKLSLGSYA ALHGEFYCKP HFQQLFKSKG NYDEGFGRKQ HKELWAHKEV
DPGTKTA
