CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-026550
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell adhesion molecule 1 
Protein Synonyms/Alias
 Protein Cadm1 
Gene Name
 Cadm1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
184ATTIRWFKGNKELKGacetylation[1]
471GQNNSEEKKEYFI**ubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Disulfide bond; Immunoglobulin domain; Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 476 AA 
Protein Sequence
MASPVLPSGS QCAAAAAVAA AAAPPGLRLR LLLLLLSAAA LIPTGDGQNL FTKDVTVIEG 60
EVATISCQVN KSDDSVIQLL NPNRQTIYFR DFRPLKDSRF QLLNFSSSEL KVSLTNVSIS 120
DEGRYFCQLY TDPPQESYTT ITVLVPPRNL MIDIQKDTAV EGEEIEVNCT AMASKPATTI 180
RWFKGNKELK GKSEVEEWSD MYTVTSQLML KVHKEDDGVP VICQVEHPAV TGNLQTQRYL 240
EVQYKPQVQI QMTYPLQGLT REGDAFELTC EATGKPQPVM VTWVRVDDEM PQHAVLSGPN 300
LFINNLNKTD NGTYRCEASN TVGKAHSDYM LYVYDPPTTI PPPTTTTTTT TTTTTTTTIL 360
TIITDTTATT EPAVHGLTQL PNSAEELDSE DLSDSRAGEE GAIGAVDHAV IGGVVAVVVF 420
AMLCLLIILG RYFARHKGTY FTHEAKGADD AADADTAIIN AEGGQNNSEE KKEYFI 476 
Gene Ontology
 GO:0030424; C:axon; IEA:Compara.
 GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
 GO:0005911; C:cell-cell junction; ISS:UniProtKB.
 GO:0030425; C:dendrite; IEA:Compara.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0043005; C:neuron projection; IDA:RGD.
 GO:0008021; C:synaptic vesicle; IEA:Compara.
 GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
 GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0005102; F:receptor binding; ISS:UniProtKB.
 GO:0007420; P:brain development; IEP:RGD.
 GO:0016338; P:calcium-independent cell-cell adhesion; IEA:Compara.
 GO:0008037; P:cell recognition; ISS:UniProtKB.
 GO:0051606; P:detection of stimulus; ISS:UniProtKB.
 GO:0007157; P:heterophilic cell-cell adhesion; ISS:UniProtKB.
 GO:0007156; P:homophilic cell adhesion; ISS:UniProtKB.
 GO:0001889; P:liver development; IMP:RGD.
 GO:0050715; P:positive regulation of cytokine secretion; IEA:Compara.
 GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; ISS:UniProtKB.
 GO:0007416; P:synapse assembly; IEA:Compara.
 GO:0009826; P:unidimensional cell growth; IEA:Compara. 
Interpro
 IPR013162; CD80_C2-set.
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR003599; Ig_sub.
 IPR003598; Ig_sub2.
 IPR013106; Ig_V-set.
 IPR003585; Neurexin-like. 
Pfam
 PF08205; C2-set_2
 PF07686; V-set 
SMART
 SM00294; 4.1m
 SM00409; IG
 SM00408; IGc2 
PROSITE
 PS50835; IG_LIKE 
PRINTS