true2005-02-152024-01-24190LIN7C_HUMANComplete sequencing and characterization of 21,243 full-length human cDNAs.Ota T.Suzuki Y.Nishikawa T.Otsuki T.Sugiyama T.Irie R.Wakamatsu A.Hayashi K.Sato H.Nagai K.Kimura K.Makita H.Sekine M.Obayashi M.Nishi T.Shibahara T.Tanaka T.Ishii S.Yamamoto J.Saito K.Kawai Y.Isono Y.Nakamura Y.Nagahari K.Murakami K.Yasuda T.Iwayanagi T.Wagatsuma M.Shiratori A.Sudo H.Hosoiri T.Kaku Y.Kodaira H.Kondo H.Sugawara M.Takahashi M.Kanda K.Yokoi T.Furuya T.Kikkawa E.Omura Y.Abe K.Kamihara K.Katsuta N.Sato K.Tanikawa M.Yamazaki M.Ninomiya K.Ishibashi T.Yamashita H.Murakawa K.Fujimori K.Tanai H.Kimata M.Watanabe M.Hiraoka S.Chiba Y.Ishida S.Ono Y.Takiguchi S.Watanabe S.Yosida M.Hotuta T.Kusano J.Kanehori K.Takahashi-Fujii A.Hara H.Tanase T.-O.Nomura Y.Togiya S.Komai F.Hara R.Takeuchi K.Arita M.Imose N.Musashino K.Yuuki H.Oshima A.Sasaki N.Aotsuka S.Yoshikawa Y.Matsunawa H.Ichihara T.Shiohata N.Sano S.Moriya S.Momiyama H.Satoh N.Takami S.Terashima Y.Suzuki O.Nakagawa S.Senoh A.Mizoguchi H.Goto Y.Shimizu F.Wakebe H.Hishigaki H.Watanabe T.Sugiyama A.Takemoto M.Kawakami B.Yamazaki M.'Watanabe K.Kumagai A.Itakura S.Fukuzumi Y.Fujimori Y.Komiyama M.Tashiro H.Tanigami A.Fujiwara T.Ono T.Yamada K.Fujii Y.Ozaki K.Hirao M.Ohmori Y.Kawabata A.Hikiji T.Kobatake N.Inagaki H.Ikema Y.Okamoto S.Okitani R.Kawakami T.Noguchi S.Itoh T.Shigeta K.Senba T.Matsumura K.Nakajima Y.Mizuno T.Morinaga M.Sasaki M.Togashi T.Oyama M.Hata H.Watanabe M.'Komatsu T.Mizushima-Sugano J.Satoh T.Shirai Y.Takahashi Y.Nakagawa K.Okumura K.Nagase T.Nomura N.Kikuchi H.Masuho Y.Yamashita R.Nakai K.Yada T.Nakamura Y.'Ohara O.Isogai T.Sugano S.doi:10.1038/ng12852004Nat. Genet.3640-45NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]PlacentaThe status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]UterusBienvenut W.V.Lao L.Ryan K.M.2009-06UniProtKBPROTEIN SEQUENCE OF 2-12; 17-23 AND 77-92CLEAVAGE OF INITIATOR METHIONINEACETYLATION AT ALA-2IDENTIFICATION BY MASS SPECTROMETRYOsteosarcomaPolar expression of ErbB-2/HER2 in epithelia. Bimodal regulation by Lin-7.Shelly M.Mosesson Y.Citri A.Lavi S.Zwang Y.Melamed-Book N.Aroeti B.Yarden Y.doi:10.1016/j.devcel.2003.08.0012003Dev. Cell5475-486SUBCELLULAR LOCATIONINTERACTION WITH EGFRThe stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 that regulates the stability and localization of DLG1 to cell junctions.Bohl J.Brimer N.Lyons C.Vande Pol S.B.doi:10.1074/jbc.m6100022002007J. Biol. Chem.2829392-9400INTERACTION WITH DLG1 AND MPP7Initial characterization of the human central proteome.Burkard T.R.Planyavsky M.Kaupe I.Breitwieser F.P.Buerckstuemmer T.Bennett K.L.Superti-Furga G.Colinge J.doi:10.1186/1752-0509-5-172011BMC Syst. Biol.517IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P.Lasa M.Polevoda B.Gazquez C.Elosegui-Artola A.Kim D.S.De Juan-Pardo E.Demeyer K.Hole K.Larrea E.Timmerman E.Prieto J.Arnesen T.Sherman F.Gevaert K.Aldabe R.doi:10.1073/pnas.12103031092012Proc. Natl. Acad. Sci. U.S.A.10912449-12454ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]N-terminome analysis of the human mitochondrial proteome.Vaca Jacome A.S.Rabilloud T.Schaeffer-Reiss C.Rompais M.Ayoub D.Lane L.Bairoch A.Van Dorsselaer A.Carapito C.doi:10.1002/pmic.2014006172015Proteomics152519-2524IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Structural basis for tandem L27 domain-mediated polymerization.Yang X.Xie X.Chen L.Zhou H.Wang Z.Zhao W.Tian R.Zhang R.Tian C.Long J.Shen Y.doi:10.1096/fj.10-1638572010FASEB J.244806-4815X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 3-64 IN COMPLEX WITH MPP7 AND DLG1SUBUNIT2.95A=3-64124LIN-10-LIN-2-LIN-7 complex, LIN7C variant641 site, 1 O-linked glycan (1 site)154 antibodies from 27 providershumanLIN7CLow tissue specificitygeneEukaryotaDopamine Neurotransmitter Release CycleNeurexins and neuroliginsAssembly and cell surface presentation of NMDA receptors49 hits in 1156 CRISPR screenshumanTbioProteinExpressed in esophagus squamous epithelium and 205 other cell types or tissuesbaseline and differentialHSPDZ_signalingL27 domainL27_CL27_domL27_dom_sfLIN7PDZPDZ_sfPROTEIN LIN-7 HOMOLOGPROTEIN LIN-7 HOMOLOG CL27PDZLin-7_homologueL27PDZL27 domainPDZ domain-likeL27PDZProtein lin-7 homolog CLin-7CMammalian lin-seven protein 3MALS-3Vertebrate lin-7 homolog 3Veli-3LIN7CMALS3VELI3Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.Forms a complex with CASK and APBA1 or CASKIN1 (By similarity). Component of the brain-specific heterotrimeric complex (LIN-10-LIN-2-LIN-7 complex) composed of at least APBA1, CASK, and LIN7, which associates with the motor protein KIF17 to transport vesicles along microtubules (By similarity). Can also interact with other modular proteins containing protein-protein interaction domains like PALS1, PALS2, MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts with DLG4 and GRIN2B as well as CDH1 and CTNNB1, the channels KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and SLC6A12/BGT-1 via its PDZ domain. The association of LIN7A with cadherin and beta-catenin is calcium-dependent, occurs at synaptic junctions and requires the actin cytoskeleton. Interacts with EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains. Associates with KIF17 via APBA1. Interacts with HTR4 (By similarity). Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). Interacts with MAPK12 (By similarity).Mainly basolateral in renal epithelial cells.The kinase interacting site is required for proper delivery of ERBB2 to the basolateral membrane.The PDZ domain regulates endocytosis and recycling of the receptor at the membrane.The L27 domain mediates interaction with CASK and is involved in the formation of multimeric complexes and the association of LIN7 to membranes.Belongs to the lin-7 family.Removed1Protein lin-7 homolog C217032197L271065PDZ93175Kinase interacting site13N-acetylalanine72633434560false7false7false4false4false6false3MPP2MPP3MPP7PALS1PALS2YES12000-10-01121834f88092c4bee682ffc3278bff2bcf08feMAALGEPVRLERDICRAIELLEKLQRSGEVPPQKLQALQRVLQSEFCNAVREVYEHVYETVDISSSPEVRANATAKATVAAFAASEGHSHPRVVELPKTEEGLGFNIMGGKEQNSPIYISRIIPGGIADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGKVKLVVRYTPKVLEEMESRFEKMRSAKRRQQTtruetruetruetruetruetruetruetruetruetruetruetruetrue