LRRF2_HUMAN
ID LRRF2_HUMAN Reviewed; 721 AA.
AC Q9Y608; A8K649; A8MXR0; B4DY63; Q68CV3; Q9NXH5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Leucine-rich repeat flightless-interacting protein 2;
DE Short=LRR FLII-interacting protein 2;
GN Name=LRRFIP2;
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), REGION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH FLII.
RC TISSUE=Skeletal muscle;
RX PubMed=10366446; DOI=10.1006/geno.1999.5817;
RA Fong K.S.K., de Couet H.G.;
RT "Novel proteins interacting with the leucine-rich repeat domain of human
RT flightless-I identified by the yeast two-hybrid system.";
RL Genomics 58:146-157(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC TISSUE=Colon mucosa, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 PROTEIN SEQUENCE OF 186-218 AND 326-345, PHOSPHORYLATION AT SER-190 AND
RP SER-202, MUTAGENESIS OF SER-190; SER-200 AND SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=21220426; DOI=10.1074/jbc.m110.168179;
RA Gunawardena H.P., Huang Y., Kenjale R., Wang H., Xie L., Chen X.;
RT "Unambiguous characterization of site-specific phosphorylation of leucine-
RT rich repeat Fli-I-interacting protein 2 (LRRFIP2) in Toll-like receptor 4
RT (TLR4)-mediated signaling.";
RL J. Biol. Chem. 286:10897-10910(2011).
RN [7]
RP FUNCTION, AND INTERACTION WITH DVL3.
RX PubMed=15677333; DOI=10.1073/pnas.0409472102;
RA Liu J., Bang A.G., Kintner C., Orth A.P., Chanda S.K., Ding S.,
RA Schultz P.G.;
RT "Identification of the Wnt signaling activator leucine-rich repeat in
RT Flightless interaction protein 2 by a genome-wide functional analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1927-1932(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-96 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-168 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-96 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-168 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
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 [14]
RP FUNCTION, AND INTERACTION WITH FLII AND MYD88.
RX PubMed=19265123; DOI=10.4049/jimmunol.0802260;
RA Dai P., Jeong S.Y., Yu Y., Leng T., Wu W., Xie L., Chen X.;
RT "Modulation of TLR signaling by multiple MyD88-interacting partners
RT including leucine-rich repeat Fli-I-interacting proteins.";
RL J. Immunol. 182:3450-3460(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-324 AND SER-328, AND
RP IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-328, 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 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-96 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-168 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-320; SER-324 AND
RP SER-328, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-324 AND SER-328,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 (ISOFORM 5), AND
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).
CC -!- FUNCTION: May function as activator of the canonical Wnt signaling
CC pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
CC Positively regulates Toll-like receptor (TLR) signaling in response to
CC agonist probably by competing with the negative FLII regulator for
CC MYD88-binding. {ECO:0000269|PubMed:15677333,
CC ECO:0000269|PubMed:19265123}.
CC -!- SUBUNIT: Interacts (via N-terminus) with DVL3. Interacts with FLII.
CC Weakly interacts with MYD88 in resting cells. Following LPS-
CC stimulation, the interaction with MYD88 is rapidly enhanced; the
CC complex gradually dissociates to basal levels after 6 hours of
CC stimulation. Interaction with MYD88 is regulated by LPS-induced
CC phosphorylation at Ser-202. In the presence of LPS, competes with FLII
CC for MYD88-binding. {ECO:0000269|PubMed:10366446,
CC ECO:0000269|PubMed:15677333, ECO:0000269|PubMed:19265123}.
CC -!- INTERACTION:
CC Q9Y608; Q8N5M1: ATPAF2; NbExp=4; IntAct=EBI-1023718, EBI-1166928;
CC Q9Y608; Q92997: DVL3; NbExp=2; IntAct=EBI-1023718, EBI-739789;
CC Q9Y608-2; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-12696250, EBI-1166928;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9Y608-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y608-2; Sequence=VSP_019675, VSP_019676, VSP_019677;
CC Name=3;
CC IsoId=Q9Y608-3; Sequence=VSP_019674;
CC Name=4;
CC IsoId=Q9Y608-4; Sequence=VSP_019675, VSP_019677;
CC Name=5;
CC IsoId=Q9Y608-5; Sequence=VSP_056969, VSP_056970, VSP_056971,
CC VSP_056972, VSP_019676, VSP_056973;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in heart and
CC skeletal muscle. {ECO:0000269|PubMed:10366446}.
CC -!- PTM: Ser-190 and Ser-202 are phosphorylated in response to LPS
CC stimulation. Ser-202 phosphorylation regulates the LPS-induced
CC interaction with MYD88. {ECO:0000269|PubMed:21220426}.
CC -!- SIMILARITY: Belongs to the LRRFIP family. {ECO:0000305}.
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DR EMBL; AF115509; AAD41257.1; -; mRNA.
DR EMBL; AK000255; BAA91035.1; -; mRNA.
DR EMBL; AK291514; BAF84203.1; -; mRNA.
DR EMBL; AK302282; BAG63625.1; -; mRNA.
DR EMBL; CR749705; CAH18481.1; -; mRNA.
DR EMBL; AC006583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053668; AAH53668.1; -; mRNA.
DR CCDS; CCDS2664.1; -. [Q9Y608-1]
DR CCDS; CCDS2665.1; -. [Q9Y608-2]
DR CCDS; CCDS46791.1; -. [Q9Y608-4]
DR CCDS; CCDS63592.1; -. [Q9Y608-5]
DR PIR; T50611; T50611.
DR RefSeq; NP_001127841.1; NM_001134369.2. [Q9Y608-4]
DR RefSeq; NP_001269620.1; NM_001282691.1. [Q9Y608-5]
DR RefSeq; NP_001335239.1; NM_001348310.1. [Q9Y608-4]
DR RefSeq; NP_001335240.1; NM_001348311.1. [Q9Y608-2]
DR RefSeq; NP_006300.1; NM_006309.3. [Q9Y608-1]
DR RefSeq; NP_060194.1; NM_017724.2. [Q9Y608-2]
DR RefSeq; XP_005265596.1; XM_005265539.2. [Q9Y608-1]
DR RefSeq; XP_005265597.1; XM_005265540.1. [Q9Y608-1]
DR RefSeq; XP_011532519.1; XM_011534217.1. [Q9Y608-1]
DR RefSeq; XP_011532520.1; XM_011534218.1. [Q9Y608-1]
DR RefSeq; XP_011532521.1; XM_011534219.1. [Q9Y608-1]
DR RefSeq; XP_016862973.1; XM_017007484.1. [Q9Y608-4]
DR AlphaFoldDB; Q9Y608; -.
DR SMR; Q9Y608; -.
DR BioGRID; 114643; 110.
DR IntAct; Q9Y608; 54.
DR MINT; Q9Y608; -.
DR STRING; 9606.ENSP00000338727; -.
DR iPTMnet; Q9Y608; -.
DR MetOSite; Q9Y608; -.
DR PhosphoSitePlus; Q9Y608; -.
DR BioMuta; LRRFIP2; -.
DR DMDM; 74721508; -.
DR EPD; Q9Y608; -.
DR jPOST; Q9Y608; -.
DR MassIVE; Q9Y608; -.
DR MaxQB; Q9Y608; -.
DR PaxDb; Q9Y608; -.
DR PeptideAtlas; Q9Y608; -.
DR PRIDE; Q9Y608; -.
DR ProteomicsDB; 2344; -.
DR ProteomicsDB; 86571; -. [Q9Y608-1]
DR ProteomicsDB; 86572; -. [Q9Y608-2]
DR ProteomicsDB; 86573; -. [Q9Y608-3]
DR ProteomicsDB; 86574; -. [Q9Y608-4]
DR Antibodypedia; 28249; 192 antibodies from 25 providers.
DR DNASU; 9209; -.
DR Ensembl; ENST00000336686.9; ENSP00000338727.4; ENSG00000093167.18. [Q9Y608-1]
DR Ensembl; ENST00000354379.8; ENSP00000346349.4; ENSG00000093167.18. [Q9Y608-2]
DR Ensembl; ENST00000396428.6; ENSP00000379705.2; ENSG00000093167.18. [Q9Y608-5]
DR Ensembl; ENST00000421276.6; ENSP00000416364.2; ENSG00000093167.18. [Q9Y608-4]
DR Ensembl; ENST00000440230.5; ENSP00000405480.1; ENSG00000093167.18. [Q9Y608-4]
DR GeneID; 9209; -.
DR KEGG; hsa:9209; -.
DR MANE-Select; ENST00000336686.9; ENSP00000338727.4; NM_006309.4; NP_006300.1.
DR UCSC; uc003cgs.4; human. [Q9Y608-1]
DR CTD; 9209; -.
DR DisGeNET; 9209; -.
DR GeneCards; LRRFIP2; -.
DR HGNC; HGNC:6703; LRRFIP2.
DR HPA; ENSG00000093167; Low tissue specificity.
DR MIM; 614043; gene.
DR neXtProt; NX_Q9Y608; -.
DR OpenTargets; ENSG00000093167; -.
DR PharmGKB; PA30466; -.
DR VEuPathDB; HostDB:ENSG00000093167; -.
DR eggNOG; KOG2010; Eukaryota.
DR GeneTree; ENSGT00530000063564; -.
DR HOGENOM; CLU_018871_2_0_1; -.
DR InParanoid; Q9Y608; -.
DR OMA; CIRIERD; -.
DR OrthoDB; 1434475at2759; -.
DR PhylomeDB; Q9Y608; -.
DR TreeFam; TF314109; -.
DR PathwayCommons; Q9Y608; -.
DR SignaLink; Q9Y608; -.
DR SIGNOR; Q9Y608; -.
DR BioGRID-ORCS; 9209; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; LRRFIP2; human.
DR GenomeRNAi; 9209; -.
DR Pharos; Q9Y608; Tbio.
DR PRO; PR:Q9Y608; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y608; protein.
DR Bgee; ENSG00000093167; Expressed in buccal mucosa cell and 197 other tissues.
DR ExpressionAtlas; Q9Y608; baseline and differential.
DR Genevisible; Q9Y608; HS.
DR GO; GO:0030275; F:LRR domain binding; IPI:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR019139; LRRFIP1/2.
DR PANTHER; PTHR19212; PTHR19212; 1.
DR Pfam; PF09738; LRRFIP; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..721
FT /note="Leucine-rich repeat flightless-interacting protein
FT 2"
FT /id="PRO_0000245246"
FT REGION 1..370
FT /note="DVL3-binding"
FT REGION 232..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..49
FT /evidence="ECO:0000255"
FT COILED 349..524
FT /evidence="ECO:0000255"
FT COILED 566..714
FT /evidence="ECO:0000255"
FT COMPBIAS 232..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21220426"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21220426"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91WK0"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91WK0"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91WK0"
FT VAR_SEQ 1..621
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019674"
FT VAR_SEQ 60..291
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019675"
FT VAR_SEQ 60..76
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056969"
FT VAR_SEQ 111..124
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056970"
FT VAR_SEQ 146..202
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056971"
FT VAR_SEQ 220..291
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056972"
FT VAR_SEQ 346..369
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019676"
FT VAR_SEQ 457..521
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019677"
FT VAR_SEQ 489..522
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056973"
FT VARIANT 143
FT /note="K -> E (in dbSNP:rs34902788)"
FT /id="VAR_050001"
FT MUTAGEN 190
FT /note="S->A: No change in LPS-induced NFKB activity."
FT /evidence="ECO:0000269|PubMed:21220426"
FT MUTAGEN 200
FT /note="S->A: No change in LPS-induced NFKB activity."
FT /evidence="ECO:0000269|PubMed:21220426"
FT MUTAGEN 202
FT /note="S->A: Reduction in LPS-induced NFKB activity."
FT /evidence="ECO:0000269|PubMed:21220426"
FT MUTAGEN 202
FT /note="S->E: No change in LPS-induced NFKB activity.
FT Interacts with MYD88 in an LPS-inducible manner."
FT /evidence="ECO:0000269|PubMed:21220426"
FT MOD_RES Q9Y608-2:96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y608-2:101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q9Y608-5:168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y608-5:173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 721 AA; 82171 MW; 94B18B274656CB0B CRC64;
MGTPASGRKR TPVKDRFSAE DEALSNIARE AEARLAAKRA ARAEARDIRM RELERQQKEY
SLHSFDRKWG QIQKWLEDSE RARYSHRSSH HRPYLGVEDA LSIRSVGSHR YDMFKDRSSR
LSSLNHSYSH SHGMKKRSSD SHKDLLSGLY FDQRNYSSLR HSKPTSAYYT RQSSSLYSDP
LATYKSDRAS PTANSGLLRS ASLASLYNGG LYNPYGPRTP SECSYYSSRI SSARSSPGFT
NDDTASIVSS DRASRGRRES VVSAADYFSR SNRRGSVVSE VDDISIPDLS SLDEKSDKQY
AENYTRPSSR NSASATTPLS GNSSRRGSGD TSSLIDPDTS LSELRDIYDL KDQIQDVEGR
YMQGLKELKE SLSEVEEKYK KAMVSNAQLD NEKNNLIYQV DTLKDVIEEQ EEQMAEFYRE
NEEKSKELER QKHMCSVLQH KMEELKEGLR QRDELIEEKQ RMQQKIDTMT KEVFDLQETL
LWKDKKIGAL EKQKEYIACL RNERDMLREE LADLQETVKT GEKHGLVIIP DGTPNGDVSH
EPVAGAITVV SQEAAQVLES AGEGPLDVRL RKLAGEKEEL LSQIRKLKLQ LEEERQKCSR
NDGTVGDLAG LQNGSDLQFI EMQRDANRQI SEYKFKLSKA EQDITTLEQS ISRLEGQVLR
YKTAAENAEK VEDELKAEKR KLQRELRTAL DKIEEMEMTN SHLAKRLEKM KANRTALLAQ
Q
