L1CAM_RAT - dbPTM
L1CAM_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID L1CAM_RAT
UniProt AC Q05695
Protein Name Neural cell adhesion molecule L1
Gene Name L1cam
Organism Rattus norvegicus (Rat).
Sequence Length 1259
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell projection, growth cone . Colocalized with SHTN1 in close apposition with actin filaments in filopodia and lamellipodia of axonal growth cones of hippocampal neurons (PubMed:18519736).
Protein Description Neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. During brain development, critical in multiple processes, including neuronal migration, axonal growth and fasciculation, and synaptogenesis. In the mature brain, plays a role in the dynamics of neuronal structure and function, including synaptic plasticity..
Protein Sequence MVMMLWYVLPLLLCSPCLLIQIPDEYKGHHVLEPPVITEQSPRRLVVFPTDDISLKCEARGRPQVEFRWTKDGIHFKPKEELGVVVHEAPYSGSFTIEGNNSFAQRFQGIYRCYASNNLGTAMSHEIQLVAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAAPLRIYWMNSKILHIKQDERVSMGQNGDLYFANVLTSDNHSDYICNAHFPGTRTIIQKEPIDLRVKPTNSMIDRKPRLLFPTNSSSHLVALQGQSLILECIAEGFPTPTIKWLHPSDPMPTDRVIYQNHNKTLQLLNVGEEDDGEYTCLAENSLGSARHAYYVTVEAAPYWLQKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGMSIEKVNKDQKYRIEQGSLILSNVQPSDTMVTQCEARNQHGLLLANAYIYVVQLPARILTKDNQTYMAVEGSTAYLLCKAFGAPVPSVQWLDEEGTTVLQDERFFPYANGHLGIRDLQANDTGRYFCQAANDQNNVTILANLQVKEATQITQGPRSTIEKKGARVTFTCQASFDPSLQASITWRGDGRDLQERGDSDKYFIEDGQLVIKSLDYSDQGDYSCVASTELDEVESRAQLLVVGSPGPVPHLELSDRHLLKQSQVHLSWSPAEDHNSPIEKYDIEFEDKEMAPEKWFSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVRGEGNETNNMVITWKPLRWMDWNAPQIQYRVQWRPLGKQETWKEQTVSDPFLVVSNTSTFVPYEIKVQAVNNQGKGPEPQVTIGYSGEDYPQVSPELEDITIFNSSTVLVRWRPVDLAQVKGHLRGYNVTYWWKGSQRKHSKRHVHKSHMVVPANTTSAILSGLRPYSSYHVEVQAFNGRGLGPASEWTFSTPEGVPGHPEALHLECQSDTSLLLHWQPPLSHNGVLTGYLLSYHPLDGESKEQLFFNLSDPELRTHNLTNLNPDLQYRFQLQATTHQGPGEAIVREGGTMALFGKPDFGNISVTAGENYSVVSWVPREGQCNFRFHILFKALPEGKVSPDHQPQPQYVSYNQSSYTQWDLQPDTKYEIHLMREKVLLHHLAVKTNGTGPVRVSTTGSFASEGWFIAFVSAIILLLLILLILCFIKRSKGGKYSVKDKEDTQVDSEARPMKDETFGEYRSLESDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVDVQFNEDGSFIGQYSGKKEKEAAGGNDSSGATSPINPAVALE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
100N-linked_GlycosylationGSFTIEGNNSFAQRF
CCEEEECCCHHHHHH
28.34-
202N-linked_GlycosylationANVLTSDNHSDYICN
EEEECCCCCCCCEEC
36.0124090084
246N-linked_GlycosylationPRLLFPTNSSSHLVA
CCEECCCCCCCCEEE
39.88-
293N-linked_GlycosylationRVIYQNHNKTLQLLN
CEEEECCCCEEEECC
46.70-
432N-linked_GlycosylationARILTKDNQTYMAVE
CEEECCCCCEEEEEC
37.34-
489N-linked_GlycosylationGIRDLQANDTGRYFC
EECCCCCCCCCCEEE
34.12-
504N-linked_GlycosylationQAANDQNNVTILANL
ECCCCCCCEEEEEEE
27.03-
670N-linked_GlycosylationSLGKVPGNQTSTTLK
ECCCCCCCCCCCEEE
35.5724090084
725N-linked_GlycosylationVDVRGEGNETNNMVI
CCCCCCCCCCCCEEE
48.9224090084
776N-linked_GlycosylationDPFLVVSNTSTFVPY
CCEEEEECCCCEECE
26.83-
824N-linked_GlycosylationLEDITIFNSSTVLVR
CEEEEEECCCCEEEE
31.06-
848N-linked_GlycosylationKGHLRGYNVTYWWKG
CCHHCCCEEEEEECC
23.60-
875N-linked_GlycosylationSHMVVPANTTSAILS
CCEEECCCCHHHHHH
37.51-
968N-linked_GlycosylationSKEQLFFNLSDPELR
CHHHEEEECCCHHHH
31.16-
978N-linked_GlycosylationDPELRTHNLTNLNPD
CHHHHHCCCCCCCCC
48.2024090084
1021N-linked_GlycosylationFGKPDFGNISVTAGE
ECCCCCCCEEEECCC
24.29-
1029N-linked_GlycosylationISVTAGENYSVVSWV
EEEECCCCEEEEEEC
33.20-
1072N-linked_GlycosylationQPQYVSYNQSSYTQW
CCCEEECCCCCCCCC
27.9624090084
1106N-linked_GlycosylationHHLAVKTNGTGPVRV
EEEEECCCCCCCEEE
40.07-
1153PhosphorylationKRSKGGKYSVKDKED
HHHCCCCCCCCCCCC
23.2118478542
1154PhosphorylationRSKGGKYSVKDKEDT
HHCCCCCCCCCCCCC
26.618663493
1161PhosphorylationSVKDKEDTQVDSEAR
CCCCCCCCCCCCCCC
31.4230240740
1165PhosphorylationKEDTQVDSEARPMKD
CCCCCCCCCCCCCCC
34.0130240740
1174PhosphorylationARPMKDETFGEYRSL
CCCCCCCCCCCEECC
47.2628551015
1178 (in isoform 2)Phosphorylation-13.0922108457
1178PhosphorylationKDETFGEYRSLESDN
CCCCCCCEECCCCCC
13.0915911348
1179 (in isoform 2)Phosphorylation-30.3922108457
1180PhosphorylationETFGEYRSLESDNEE
CCCCCEECCCCCCHH
35.2730240740
1183PhosphorylationGEYRSLESDNEEKAF
CCEECCCCCCHHHHH
51.548592152
1192PhosphorylationNEEKAFGSSQPSLNG
CHHHHHCCCCCCCCC
21.2422673903
1193PhosphorylationEEKAFGSSQPSLNGD
HHHHHCCCCCCCCCC
46.6322673903
1196PhosphorylationAFGSSQPSLNGDIKP
HHCCCCCCCCCCCCC
27.1622673903
1206PhosphorylationGDIKPLGSDDSLADY
CCCCCCCCCCCHHHC
46.0222673903
1209PhosphorylationKPLGSDDSLADYGGS
CCCCCCCCHHHCCCE
30.3722673903
1213PhosphorylationSDDSLADYGGSVDVQ
CCCCHHHCCCEEEEE
20.1322673903
1216PhosphorylationSLADYGGSVDVQFNE
CHHHCCCEEEEEECC
15.6922673903
1226PhosphorylationVQFNEDGSFIGQYSG
EEECCCCCCEEEECC
26.4722673903
1231PhosphorylationDGSFIGQYSGKKEKE
CCCCEEEECCCCCCC
17.7422673903
1232PhosphorylationGSFIGQYSGKKEKEA
CCCEEEECCCCCCCC
35.9322673903
1245PhosphorylationEAAGGNDSSGATSPI
CCCCCCCCCCCCCCC
34.3722108457
1246PhosphorylationAAGGNDSSGATSPIN
CCCCCCCCCCCCCCC
35.0030240740
1249PhosphorylationGNDSSGATSPINPAV
CCCCCCCCCCCCHHH
38.2622108457
1250PhosphorylationNDSSGATSPINPAVA
CCCCCCCCCCCHHHC
24.2122108457

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
1148SPhosphorylationKinaseRPS6KA2F1M7N7
GPS
1153YPhosphorylationKinaseSRCP05480
PSP
1154SPhosphorylationKinaseRPS6KA1Q63531
GPS
1183SPhosphorylationKinaseCSNK2A1P19139
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of L1CAM_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of L1CAM_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of L1CAM_RAT

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Related Literatures of Post-Translational Modification

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