LPP_HUMAN
ID LPP_HUMAN Reviewed; 612 AA.
AC Q93052; A1L4L6; D3DNV6; Q8NFX5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Lipoma-preferred partner;
DE AltName: Full=LIM domain-containing preferred translocation partner in lipoma;
GN Name=LPP;
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 [GENOMIC DNA / MRNA], CHROMOSOMAL TRANSLOCATION WITH
RP HMGA2, AND TISSUE SPECIFICITY.
RC TISSUE=Small intestine;
RX PubMed=8812423; DOI=10.1006/geno.1996.0432;
RA Petit M.M.R., Mols R., Schoenmakers E.F., Mandahl N., Van de Ven W.J.M.;
RT "LPP, the preferred fusion partner gene of HMGIC in lipomas, is a novel
RT member of the LIM protein gene family.";
RL Genomics 36:118-129(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) 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].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 276-371.
RX PubMed=12063392; DOI=10.1159/000059338;
RA Lemke I., Rogalla P., Bullerdiek J.;
RT "A novel LPP fusion gene indicates the crucial role of truncated LPP
RT proteins in lipomas and pulmonary chondroid hamartomas.";
RL Cytogenet. Cell Genet. 95:153-156(2001).
RN [6]
RP CHROMOSOMAL TRANSLOCATION WITH HMGA2.
RX PubMed=9772904; DOI=10.1016/s0165-4608(98)00038-7;
RA Petit M.M., Swarts S., Bridge J.A., Van de Ven W.J.M.;
RT "Expression of reciprocal fusion transcripts of the HMGIC and LPP genes in
RT parosteal lipoma.";
RL Cancer Genet. Cytogenet. 106:18-23(1998).
RN [7]
RP CHROMOSOMAL TRANSLOCATION WITH HMGA2.
RX PubMed=11066083;
RX DOI=10.1002/1098-2264(2000)9999:9999<1::aid-gcc1043>3.0.co;2-n;
RA Rogalla P., Lemke I., Kazmierczak B., Bullerdiek J.;
RT "An identical HMGIC-LPP fusion transcript is consistently expressed in
RT pulmonary chondroid hamartomas with t(3;12)(q27-28;q14-15).";
RL Genes Chromosomes Cancer 29:363-366(2000).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP VASP.
RX PubMed=10637295; DOI=10.1091/mbc.11.1.117;
RA Petit M.M., Fradelizi J., Golsteyn R.M., Ayoubi T.A., Menichi B.,
RA Louvard D., Van de Ven W.J.M., Friederich E.;
RT "LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear
RT export signal and transcriptional activation capacity.";
RL Mol. Biol. Cell 11:117-129(2000).
RN [9]
RP CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
RX PubMed=11433529; DOI=10.1002/gcc.1157;
RA Daheron L., Veinstein A., Brizard F., Drabkin H., Lacotte L., Guilhot F.,
RA Larsen C.J., Brizard A., Roche J.;
RT "Human LPP gene is fused to MLL in a secondary acute leukemia with a
RT t(3;11) (q28;q23).";
RL Genes Chromosomes Cancer 31:382-389(2001).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH VASP AND ACTN1.
RX PubMed=12441356; DOI=10.1074/jbc.m206106200;
RA Petit M.M., Meulemans S.M., Van de Ven W.J.M.;
RT "The focal adhesion and nuclear targeting capacity of the LIM-containing
RT lipoma-preferred partner (LPP) protein.";
RL J. Biol. Chem. 278:2157-2168(2003).
RN [11]
RP INTERACTION WITH ACTN1.
RX PubMed=12615977; DOI=10.1242/jcs.00309;
RA Li B., Zhuang L., Reinhard M., Trueb B.;
RT "The lipoma preferred partner LPP interacts with alpha-actinin.";
RL J. Cell Sci. 116:1359-1366(2003).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=12522270; DOI=10.1073/pnas.2436191100;
RA Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C.,
RA Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
RT "Profiling of tyrosine phosphorylation pathways in human cells using mass
RT spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP INTERACTION WITH SCRIB, AND MUTAGENESIS.
RX PubMed=15649318; DOI=10.1186/1471-2121-6-1;
RA Petit M.M.R., Meulemans S.M.P., Alen P., Ayoubi T.A.Y., Jansen E.,
RA Van de Ven W.J.M.;
RT "The tumor suppressor Scrib interacts with the zyxin-related protein LPP,
RT which shuttles between cell adhesion sites and the nucleus.";
RL BMC Cell Biol. 6:1-1(2005).
RN [15]
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, AND IDENTIFICATION BY
RP MASS 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 [18]
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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, 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).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-327, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
CC -!- FUNCTION: May play a structural role at sites of cell adhesion in
CC maintaining cell shape and motility. In addition to these structural
CC functions, it may also be implicated in signaling events and activation
CC of gene transcription. May be involved in signal transduction from cell
CC adhesion sites to the nucleus allowing successful integration of
CC signals arising from soluble factors and cell-cell adhesion sites. Also
CC suggested to serve as a scaffold protein upon which distinct protein
CC complexes are assembled in the cytoplasm and in the nucleus.
CC {ECO:0000269|PubMed:10637295}.
CC -!- SUBUNIT: Interacts with VASP, with PDZ domains of SCRIB and with
CC ACTN1/alpha-actinin. {ECO:0000269|PubMed:10637295,
CC ECO:0000269|PubMed:12441356, ECO:0000269|PubMed:12615977,
CC ECO:0000269|PubMed:15649318}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell junction. Cell membrane.
CC Note=Found in the nucleus, in the cytoplasm and at cell adhesion sites.
CC Shuttles between the cytoplasm and the nucleus. It has been found in
CC sites of cell adhesion such as cell-to-cell contact and focal adhesion
CC which are membrane attachment sites of cells to the extracellular
CC matrix. Mainly nuclear when fused with HMGA2/HMGIC and KMT2A/MLL1.
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues but no or
CC very low expression in brain and peripheral leukocytes.
CC {ECO:0000269|PubMed:10637295, ECO:0000269|PubMed:8812423}.
CC -!- DISEASE: Note=A chromosomal aberration involving LPP is associated with
CC a subclass of benign mesenchymal tumors known as lipomas. Translocation
CC t(3;12)(q27-q28;q13-q15) with HMGA2 is shown in lipomas.
CC -!- DISEASE: Note=A chromosomal aberration involving LPP is associated with
CC pulmonary chondroid hamartomas. Translocation t(3;12)(q27-q28;q14-q15)
CC with HMGA2 is detected in pulmonary chondroid hamartomas.
CC -!- DISEASE: Note=A chromosomal aberration involving LPP is associated with
CC parosteal lipomas. Translocation t(3;12)(q28;q14) with HMGA2 is also
CC shown in one parosteal lipoma.
CC -!- DISEASE: Note=A chromosomal aberration involving LPP is associated with
CC acute monoblastic leukemia. Translocation t(3;11)(q28;q23) with
CC KMT2A/MLL1 is associated with acute monoblastic leukemia.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LPPID72.html";
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DR EMBL; U49957; AAC50738.1; -; mRNA.
DR EMBL; U49968; AAC50739.1; -; Genomic_DNA.
DR EMBL; U49960; AAC50739.1; JOINED; Genomic_DNA.
DR EMBL; U49961; AAC50739.1; JOINED; Genomic_DNA.
DR EMBL; U49962; AAC50739.1; JOINED; Genomic_DNA.
DR EMBL; U49963; AAC50739.1; JOINED; Genomic_DNA.
DR EMBL; U49964; AAC50739.1; JOINED; Genomic_DNA.
DR EMBL; U49965; AAC50739.1; JOINED; Genomic_DNA.
DR EMBL; U49966; AAC50739.1; JOINED; Genomic_DNA.
DR EMBL; U49967; AAC50739.1; JOINED; Genomic_DNA.
DR EMBL; CR457074; CAG33355.1; -; mRNA.
DR EMBL; CH471052; EAW78127.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78128.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78133.1; -; Genomic_DNA.
DR EMBL; BC130584; AAI30585.1; -; mRNA.
DR EMBL; AF393503; AAM73685.1; ALT_TERM; mRNA.
DR CCDS; CCDS3291.1; -.
DR RefSeq; NP_001161143.1; NM_001167671.2.
DR RefSeq; NP_005569.1; NM_005578.4.
DR RefSeq; XP_005247503.1; XM_005247446.4.
DR RefSeq; XP_005247507.1; XM_005247450.4.
DR RefSeq; XP_005247508.1; XM_005247451.4.
DR RefSeq; XP_005247510.1; XM_005247453.2.
DR RefSeq; XP_011511122.1; XM_011512820.2.
DR RefSeq; XP_011511129.1; XM_011512827.2.
DR RefSeq; XP_011511130.1; XM_011512828.2.
DR RefSeq; XP_011511133.1; XM_011512831.2.
DR RefSeq; XP_011511135.1; XM_011512833.2.
DR RefSeq; XP_011511136.1; XM_011512834.2.
DR RefSeq; XP_016861866.1; XM_017006377.1.
DR RefSeq; XP_016861867.1; XM_017006378.1.
DR RefSeq; XP_016861868.1; XM_017006379.1.
DR RefSeq; XP_016861869.1; XM_017006380.1.
DR AlphaFoldDB; Q93052; -.
DR SMR; Q93052; -.
DR BioGRID; 110208; 98.
DR CORUM; Q93052; -.
DR IntAct; Q93052; 24.
DR MINT; Q93052; -.
DR STRING; 9606.ENSP00000482472; -.
DR GlyGen; Q93052; 11 sites, 2 O-linked glycans (11 sites).
DR iPTMnet; Q93052; -.
DR MetOSite; Q93052; -.
DR PhosphoSitePlus; Q93052; -.
DR BioMuta; LPP; -.
DR DMDM; 74751663; -.
DR EPD; Q93052; -.
DR jPOST; Q93052; -.
DR MassIVE; Q93052; -.
DR MaxQB; Q93052; -.
DR PaxDb; Q93052; -.
DR PeptideAtlas; Q93052; -.
DR PRIDE; Q93052; -.
DR ProteomicsDB; 75690; -.
DR Antibodypedia; 2772; 272 antibodies from 41 providers.
DR DNASU; 4026; -.
DR Ensembl; ENST00000617246.5; ENSP00000478901.1; ENSG00000145012.14.
DR Ensembl; ENST00000640853.1; ENSP00000491657.1; ENSG00000145012.14.
DR GeneID; 4026; -.
DR KEGG; hsa:4026; -.
DR MANE-Select; ENST00000617246.5; ENSP00000478901.1; NM_001375462.1; NP_001362391.1.
DR UCSC; uc032sne.1; human.
DR CTD; 4026; -.
DR DisGeNET; 4026; -.
DR GeneCards; LPP; -.
DR HGNC; HGNC:6679; LPP.
DR HPA; ENSG00000145012; Low tissue specificity.
DR MalaCards; LPP; -.
DR MIM; 600700; gene.
DR neXtProt; NX_Q93052; -.
DR OpenTargets; ENSG00000145012; -.
DR PharmGKB; PA30440; -.
DR VEuPathDB; HostDB:ENSG00000145012; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000156022; -.
DR InParanoid; Q93052; -.
DR OMA; FNPYKQM; -.
DR PhylomeDB; Q93052; -.
DR TreeFam; TF320310; -.
DR PathwayCommons; Q93052; -.
DR SignaLink; Q93052; -.
DR SIGNOR; Q93052; -.
DR BioGRID-ORCS; 4026; 10 hits in 1081 CRISPR screens.
DR ChiTaRS; LPP; human.
DR GeneWiki; LPP_(gene); -.
DR GenomeRNAi; 4026; -.
DR Pharos; Q93052; Tbio.
DR PRO; PR:Q93052; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q93052; protein.
DR Bgee; ENSG00000145012; Expressed in saphenous vein and 212 other tissues.
DR ExpressionAtlas; Q93052; baseline and differential.
DR Genevisible; Q93052; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR InterPro; IPR028771; LPP.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24207:SF0; PTHR24207:SF0; 1.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cell adhesion; Cell junction; Cell membrane;
KW Chromosomal rearrangement; Cytoplasm; Isopeptide bond; LIM domain;
KW Membrane; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation; Zinc.
FT CHAIN 1..612
FT /note="Lipoma-preferred partner"
FT /id="PRO_0000075832"
FT DOMAIN 414..473
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 474..534
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 535..603
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 371..372
FT /note="Breakpoint for translocation to form HMGA2-LPP"
FT SITE 470..471
FT /note="Breakpoint for translocation to form HMGA2-LPP and
FT KMT2A/MLL1-LPP"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFW7"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI07"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI07"
FT MOD_RES 244
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFW7"
FT MOD_RES 301
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFW7"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VARIANT 146
FT /note="T -> A (in dbSNP:rs35417432)"
FT /id="VAR_050150"
FT VARIANT 259
FT /note="S -> P (in dbSNP:rs35940579)"
FT /id="VAR_050151"
FT VARIANT 346
FT /note="Y -> H (in dbSNP:rs7645635)"
FT /id="VAR_034070"
FT MUTAGEN 610
FT /note="T->A: Abolishes binding to SCRIB."
FT /evidence="ECO:0000269|PubMed:15649318"
FT MUTAGEN 612
FT /note="L->A: Abolishes binding to SCRIB."
FT /evidence="ECO:0000269|PubMed:15649318"
SQ SEQUENCE 612 AA; 65746 MW; 439CE0101FDE4DDD CRC64;
MSHPSWLPPK STGEPLGHVP ARMETTHSFG NPSISVSTQQ PPKKFAPVVA PKPKYNPYKQ
PGGEGDFLPP PPPPLDDSSA LPSISGNFPP PPPLDEEAFK VQGNPGGKTL EERRSSLDAE
IDSLTSILAD LECSSPYKPR PPQSSTGSTA SPPVSTPVTG HKRMVIPNQP PLTATKKSTL
KPQPAPQAGP IPVAPIGTLK PQPQPVPASY TTASTSSRPT FNVQVKSAQP SPHYMAAPSS
GQIYGSGPQG YNTQPVPVSG QCPPPSTRGG MDYAYIPPPG LQPEPGYGYA PNQGRYYEGY
YAAGPGYGGR NDSDPTYGQQ GHPNTWKREP GYTPPGAGNQ NPPGMYPVTG PKKTYITDPV
SAPCAPPLQP KGGHSGQLGP SSVAPSFRPE DELEHLTKKM LYDMENPPAD EYFGRCARCG
ENVVGEGTGC TAMDQVFHVD CFTCIICNNK LRGQPFYAVE KKAYCEPCYI NTLEQCNVCS
KPIMERILRA TGKAYHPHCF TCVMCHRSLD GIPFTVDAGG LIHCIEDFHK KFAPRCSVCK
EPIMPAPGQE ETVRIVALDR DFHVHCYRCE DCGGLLSEGD NQGCYPLDGH ILCKTCNSAR
IRVLTAKAST DL
