ID LNX1_MOUSE STANDARD; PRT; 728 AA. AC O70263; O70264; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Numb-binding protein 1 (Ligand of Numb-protein X 1). GN Name=Lnx; Synonyms=Lnx1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, RP AND MUTAGENESIS OF TYR-188. RC TISSUE=Brain, and Embryo; RX MEDLINE=98204916; PubMed=9535908; DOI=10.1074/jbc.273.15.9179; RA Dho S.E., Jacob S., Wolting C.D., French M.B., Rohrschneider L.R., RA McGlade C.J.; RT "The mammalian numb phosphotyrosine-binding domain. Characterization RT of binding specificity and identification of a novel PDZ domain- RT containing numb binding protein, LNX."; RL J. Biol. Chem. 273:9179-9187(1998). CC -!- SUBUNIT: Interacts with the phosphotyrosine interaction domain of CC NUMB. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=LNX, LNXp80; CC IsoId=O70263-1; Sequence=Displayed; CC Name=2; Synonyms=LNX-B, LNXp70; CC IsoId=O70263-2; Sequence=VSP_005734; CC -!- TISSUE SPECIFICITY: Both isoforms are expressed in the heart. CC Isoform 1 is also expressed in kidney, lung and skeletal muscle CC while isoform 2 is also expressed in brain. CC -!- SIMILARITY: Contains 4 PDZ/DHR domains. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. 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; AF034745; AAC40075.1; -. DR EMBL; AF034746; AAC40076.1; -. DR PIR; T09457; T09457. DR PIR; T09458; T09458. DR HSSP; Q64512; 1GM1. DR MGD; MGI:1278335; Lnx1. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005615; C:extracellular space; TAS. DR GO; GO:0030165; F:PDZ domain binding; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA. DR GO; GO:0051260; P:protein homooligomerization; IDA. DR GO; GO:0042787; P:protein ubiquitination during ubiquitin-dep...; IDA. DR InterPro; IPR001478; PDZ. DR InterPro; IPR001841; Znf_ring. DR Pfam; PF00595; PDZ; 4. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00228; PDZ; 4. DR SMART; SM00184; RING; 1. DR PROSITE; PS50106; PDZ; 4. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Alternative splicing; Repeat; Zinc-finger. FT ZN_FING 45 83 RING-type. FT DOMAIN 278 362 PDZ 1. FT DOMAIN 385 467 PDZ 2. FT DOMAIN 508 593 PDZ 3. FT DOMAIN 638 723 PDZ 4. FT VARSPLIC 1 131 MNQPDLADDPDPSPEPLCIVCGQNHSPEENHFYTYTEDVDD FT DLICHICLQALLDPLDTPCGHTYCTLCLTNFLVEKDFCPVD FT RKPVVLQHCKKSSILVNKLLNKLLVTCPFTEHCTEVLQRCD FT LQHHFQTS -> MKALLLLVLPWLSPANYIDNVGNLHFLYS FT EL (in isoform 2). FT /FTId=VSP_005734. FT MUTAGEN 188 188 Y->A: Abolishes binding to NUMB protein. FT MUTAGEN 188 188 Y->F: No effect on binding to NUMB FT protein. SQ SEQUENCE 728 AA; 80157 MW; E2914BD364C0CEC4 CRC64; MNQPDLADDP DPSPEPLCIV CGQNHSPEEN HFYTYTEDVD DDLICHICLQ ALLDPLDTPC GHTYCTLCLT NFLVEKDFCP VDRKPVVLQH CKKSSILVNK LLNKLLVTCP FTEHCTEVLQ RCDLQHHFQT SCKGASHYGL TKDRKRRSQD GCPDGCASLM ATTLSPEVSA AATISLMTDE PGLDNPAYVS SVEDGEPVAN SSDSGRSNRT RARPFERSTM RSRSFKKINR ALSALRRTKS GSVVANHVDQ GRDNSENTTV PEVFPRLFHL IPDGEITSIK INRADPSESL SIRLVGGSET PLVHIIIQHI YRDGVIARDG RLLPGDIILK VNGMDISNVP HNYAVRLLRQ PCQVLRLTVL REQKFRSRSN AHVPDSYGPR DDSFHVILNK SSPEEQLGIK LVRRVDEPGV FIFNVLNGGV ADRHGQLEEN DRVLAINGHD LRFGSPESAA HLIQASERRV HLVVSRQVRQ SSPDIFQEAG WISNGQQSPG PGERNTASKP AATCHEKVVS VWKDPSESLG MTVGGGASHR EWDLPIYVIS VEPGGVISRD GRIKTGDILL NVNGIELTEV SRTEAVAILK SAPSSVVLKA LEVKEQEAQE DCSPAALDSN HNVTPPGDWS PSWVMWLELP QYLCNCKDVI LRRNTAGSLG FCIVGGYEEY SGNKPFFIKS IVEGTPAYND GRIRCGDILL AVNGRSTSGM IHACLARMLK ELKGRITLTI ASWPGTFL //