LYSM2_HUMAN
ID LYSM2_HUMAN Reviewed; 215 AA.
AC Q8IV50; Q5CZ88; Q8WTV3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=LysM and putative peptidoglycan-binding domain-containing protein 2;
GN Name=LYSMD2;
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).
RA Ding P., Han W., Wang Y., Rui M., Chen Y., Wang L., Ma D.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hypothalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-215 (ISOFORMS 1/2).
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 [4]
RP IDENTIFICATION BY 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-24; SER-33 AND SER-57,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, 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).
CC -!- INTERACTION:
CC Q8IV50-2; Q96LK0: CEP19; NbExp=3; IntAct=EBI-19761491, EBI-741885;
CC Q8IV50-2; Q13115: DUSP4; NbExp=3; IntAct=EBI-19761491, EBI-6591081;
CC Q8IV50-2; Q8WX39: LCN9; NbExp=3; IntAct=EBI-19761491, EBI-19762110;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IV50-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IV50-2; Sequence=VSP_020123;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY125955; AAM94507.1; -; mRNA.
DR EMBL; BC022075; AAH22075.1; -; mRNA.
DR EMBL; BC033515; AAH33515.1; -; mRNA.
DR EMBL; CR936638; CAI56778.1; -; mRNA.
DR CCDS; CCDS10143.1; -. [Q8IV50-1]
DR CCDS; CCDS45259.1; -. [Q8IV50-2]
DR RefSeq; NP_001137389.1; NM_001143917.1. [Q8IV50-2]
DR RefSeq; NP_699205.1; NM_153374.2. [Q8IV50-1]
DR RefSeq; XP_016877546.1; XM_017022057.1.
DR AlphaFoldDB; Q8IV50; -.
DR SMR; Q8IV50; -.
DR BioGRID; 129172; 18.
DR IntAct; Q8IV50; 15.
DR STRING; 9606.ENSP00000267838; -.
DR iPTMnet; Q8IV50; -.
DR PhosphoSitePlus; Q8IV50; -.
DR BioMuta; LYSMD2; -.
DR DMDM; 74728034; -.
DR EPD; Q8IV50; -.
DR jPOST; Q8IV50; -.
DR MassIVE; Q8IV50; -.
DR MaxQB; Q8IV50; -.
DR PaxDb; Q8IV50; -.
DR PeptideAtlas; Q8IV50; -.
DR PRIDE; Q8IV50; -.
DR ProteomicsDB; 70660; -. [Q8IV50-1]
DR ProteomicsDB; 70661; -. [Q8IV50-2]
DR Antibodypedia; 24890; 42 antibodies from 17 providers.
DR DNASU; 256586; -.
DR Ensembl; ENST00000267838.7; ENSP00000267838.3; ENSG00000140280.14. [Q8IV50-1]
DR Ensembl; ENST00000454181.6; ENSP00000410424.2; ENSG00000140280.14. [Q8IV50-2]
DR Ensembl; ENST00000560491.2; ENSP00000453933.1; ENSG00000140280.14. [Q8IV50-2]
DR GeneID; 256586; -.
DR KEGG; hsa:256586; -.
DR MANE-Select; ENST00000267838.7; ENSP00000267838.3; NM_153374.3; NP_699205.1.
DR UCSC; uc002abi.4; human. [Q8IV50-1]
DR CTD; 256586; -.
DR GeneCards; LYSMD2; -.
DR HGNC; HGNC:28571; LYSMD2.
DR HPA; ENSG00000140280; Low tissue specificity.
DR neXtProt; NX_Q8IV50; -.
DR OpenTargets; ENSG00000140280; -.
DR PharmGKB; PA142671494; -.
DR VEuPathDB; HostDB:ENSG00000140280; -.
DR eggNOG; ENOG502S0XR; Eukaryota.
DR GeneTree; ENSGT00940000160054; -.
DR HOGENOM; CLU_079453_1_0_1; -.
DR InParanoid; Q8IV50; -.
DR OMA; DGETANQ; -.
DR OrthoDB; 1553362at2759; -.
DR PhylomeDB; Q8IV50; -.
DR TreeFam; TF318444; -.
DR PathwayCommons; Q8IV50; -.
DR SignaLink; Q8IV50; -.
DR BioGRID-ORCS; 256586; 7 hits in 1077 CRISPR screens.
DR GenomeRNAi; 256586; -.
DR Pharos; Q8IV50; Tdark.
DR PRO; PR:Q8IV50; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8IV50; protein.
DR Bgee; ENSG00000140280; Expressed in pons and 188 other tissues.
DR ExpressionAtlas; Q8IV50; baseline and differential.
DR Genevisible; Q8IV50; HS.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR045030; LYSM1-4.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR20932; PTHR20932; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..215
FT /note="LysM and putative peptidoglycan-binding domain-
FT containing protein 2"
FT /id="PRO_0000248002"
FT DOMAIN 71..115
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020123"
FT VARIANT 107
FT /note="I -> V (in dbSNP:rs3751593)"
FT /id="VAR_027198"
FT VARIANT 164
FT /note="S -> F (in dbSNP:rs7168775)"
FT /id="VAR_027199"
SQ SEQUENCE 215 AA; 23463 MW; A87E666478E903AC CRC64;
MADSSPALSL REGGPRAPRP SAPSPPPRSR SGSESEEAEL SLSLARTKTR SYGSTASVRA
PLGAGVIERH VEHRVRAGDT LQGIALKYGV TMEQIKRANK LFTNDCIFLK KTLNIPVISE
KPLLFNGLNS IDSPENETAD NSFSQEEEPV VAGEDLPPPS PQESDVQPVQ PEEVSARDFL
QRLDLQIKLS TQAAKKLKEE SRDEESPYAT SLYHS