CPLM-022166

Genbank Nucleotide ID

Protein lin-7 homolog C

Protein Synonyms/Alias

Lin-7C; Mammalian lin-seven protein 3; MALS-3; Vertebrate lin-7 homolog 3; Veli-3

Homo sapiens (Human)

Position	Peptide	Type	References
23	RAIELLEKLQRSGEV	ubiquitination	[1, 2, 3, 4]
34	SGEVPPQKLQALQRV	ubiquitination	[1, 4]
76	VRANATAKATVAAFA	ubiquitination	[3, 4, 5, 6, 7]
111	GFNIMGGKEQNSPIY	ubiquitination	[3]
161	EKAVELLKAAQGKVK	ubiquitination	[2]
176	LVVRYTPKVLEEMES	ubiquitination	[1, 3, 4, 6]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]

Functional Description

Plays 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 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.

DOMAIN 10 65 L27.
DOMAIN 93 175 PDZ.
MOTIF 2 13 Kinase interacting site (By similarity).
MOD_RES 2 2 N-acetylalanine.

3D-structure; Acetylation; Cell junction; Cell membrane; Complete proteome; Direct protein sequencing; Exocytosis; Membrane; Postsynaptic cell membrane; Protein transport; Reference proteome; Synapse; Synaptosome; Tight junction; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
GO:0007269; P:neurotransmitter secretion; IEA:Compara.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.

IPR004172; L27.
IPR014775; L27_C.
IPR017365; Lin-7_homologue.
IPR001478; PDZ.

PF02828; L27
PF00595; PDZ

SM00569; L27
SM00228; PDZ

PS51022; L27
PS50106; PDZ