NCHL1_MOUSE - dbPTM
NCHL1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCHL1_MOUSE
UniProt AC P70232
Protein Name Neural cell adhesion molecule L1-like protein
Gene Name Chl1
Organism Mus musculus (Mouse).
Sequence Length 1209
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Soluble forms produced by cleavage/shedding also exist.
Processed neural cell adhesion molecule L1-like protein: Secreted, extracellular space, extracellular matrix.
Protein Description Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons as well as in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane..
Protein Sequence MMELPLCGRGLILSLIFLLLKLSAAEIPLSVQQVPTIVKQSYVQVAFPFDEYFQIECEAKGNPEPIFSWTKDDKPFDLSDPRIIAANNSGTFKIPNEGHISHFQGKYRCFASNRLGTAVSEEIEFIVPGVPKFPKEKIEPIDVEEGDSIVLPCNPPKGLPPLHIYWMNIELEHIEQDERVYMSQRGDLYFANVEENDSRNDYCCFAAFPKLRTIVQKMPMKLTVNSSNSIKQRKPKLLLPPAQMGSLSAKTVLKGDTLLLECFAEGLPTPHIQWSKPGSELPEGRATIEVHEKTLKIENISYQDRGNYRCTANNLLGKASHDFHVTVEEPPRWKKKPQSAVYSTGSSGILLCEAEGEPQPTIKWRLNGLPIEKHPFPGDFMFPREISFTNLLPNHTGVYQCEASNIHGTILANANIDVIDVIPLIKTKNEENYATVVGYSAFLHCEYFASPKATVVWEVADETHPLEGDRYHTHENGTLEIYRTTEEDAGSYSCWVDNAMGKAVITANLDIRNATKLRVSPKNPRIPKSHVLELYCESQCDSHLKHSLKLSWSKDGEAFEMNGTEDGRIVIDGAYLTISNITAEDQGVYSCSAQTSLDSTSEKTQVTVLGVPDPPGNLHLSERQNRSVRLSWEAGDDHNSKISEYIVEFEGNREEPGKWEELTRVQGEETDVVLSLAPYVRYQFRVTAVNEVGRSHASLPSDHHETPPAAPDKNPQNIRVQASQPKEMIIKWEPLKSMEQNGPGLEYKVSWKPQGAPEEWEEEIVTNHTLRVMTPTVYAPYDVKVQAINQLGSSPDPQPVTLYSGEDYPSTAPVIQRVDVMNSTLVKVTWSSIPKETVHGLLRGYQINWWKTKSLLDGRTHPKEVNILRFSGQRNSGMVPSLDPFSEFHLTVLAYNSKGAGPESEPYIFQTPEGVPEQPSFLKVIKVDKDTATLSWGLPKKLNGNLTGYLLQYQIINDTYELGELNEINVTTPSKSSWHLSNLNSTTKYKFYLRACTSRGCGKPISEEGATLGEGSKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDNDSIFQDVIETRGREYAGLYDDISTQGWFIGLMCAIALLTLILLTICFVKRNRGGKYSVKEKEDLHPDPEVQSAKDETFGEYSDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNEDGSFIGAYTGAKEKGSVESNGSSTATFPLRA
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
87N-linked_GlycosylationDPRIIAANNSGTFKI
CCCEEEECCCCCEEC
-
91PhosphorylationIAANNSGTFKIPNEG
EEECCCCCEECCCCC
22871156
101PhosphorylationIPNEGHISHFQGKYR
CCCCCCCCEECCEEE
22871156
225N-linked_GlycosylationMPMKLTVNSSNSIKQ
CCCEEEECCCCHHHC
-
231 (in isoform 2)Phosphorylation-23375375
233 (in isoform 2)Phosphorylation-23375375
234 (in isoform 2)Phosphorylation-23375375
235 (in isoform 2)Phosphorylation-23375375
236 (in isoform 2)Phosphorylation-23375375
299N-linked_GlycosylationEKTLKIENISYQDRG
ECEEEEECCCCCCCC
-
476N-linked_GlycosylationDRYHTHENGTLEIYR
CEEEECCCCEEEEEE
-
506PhosphorylationAMGKAVITANLDIRN
CCCCEEEEECCCCCC
28059163
562N-linked_GlycosylationDGEAFEMNGTEDGRI
CCCCEEECCCCCCCE
-
580N-linked_GlycosylationGAYLTISNITAEDQG
CCEEEEECCCHHHCC
-
767N-linked_GlycosylationWEEEIVTNHTLRVMT
HHHHHHHCCEEEEEC
-
822N-linked_GlycosylationIQRVDVMNSTLVKVT
EEEEECCCCEEEEEE
-
926AcetylationPSFLKVIKVDKDTAT
CCEEEEEEECCCCCE
19843315
929AcetylationLKVIKVDKDTATLSW
EEEEEECCCCCEEEC
19843325
945N-linked_GlycosylationLPKKLNGNLTGYLLQ
CCCCCCCCCCCEEEE
-
1003AcetylationCTSRGCGKPISEEGA
HCCCCCCCCCCCCCC
23864654
1019 (in isoform 2)Acetylation--
1027N-linked_GlycosylationRKITEGVNVTQKIHP
HHHCCCCCCCCEECC
-
1032 (in isoform 2)Acetylation--
1128PhosphorylationHPDPEVQSAKDETFG
CCCHHHCCCCCCCCC
25521595
1133PhosphorylationVQSAKDETFGEYSDS
HCCCCCCCCCCCCCC
30372032
1137PhosphorylationKDETFGEYSDSDEKP
CCCCCCCCCCCCCCC
25177544
1138PhosphorylationDETFGEYSDSDEKPL
CCCCCCCCCCCCCCC
30372032
1140PhosphorylationTFGEYSDSDEKPLKG
CCCCCCCCCCCCCCH
27742792
1148PhosphorylationDEKPLKGSLRSLNRN
CCCCCCHHHHHHHCC
25521595
1151PhosphorylationPLKGSLRSLNRNMQP
CCCHHHHHHHCCCCC
25521595
1159PhosphorylationLNRNMQPTESADSLV
HHCCCCCCCCCHHHH
21183079
1161PhosphorylationRNMQPTESADSLVEY
CCCCCCCCCHHHHHH
19060867
1164PhosphorylationQPTESADSLVEYGEG
CCCCCCHHHHHHCCC
19060867
1168PhosphorylationSADSLVEYGEGDQSI
CCHHHHHHCCCCCEE
20415495
1174PhosphorylationEYGEGDQSIFNEDGS
HHCCCCCEEECCCCC
-
1181PhosphorylationSIFNEDGSFIGAYTG
EEECCCCCEEEEECC
16141072
1194PhosphorylationTGAKEKGSVESNGSS
CCCCCCCCCCCCCCC
21183079
1197PhosphorylationKEKGSVESNGSSTAT
CCCCCCCCCCCCCEE
29899451
1200PhosphorylationGSVESNGSSTATFPL
CCCCCCCCCCEEEEC
29899451
1201PhosphorylationSVESNGSSTATFPLR
CCCCCCCCCEEEECC
22807455
1202PhosphorylationVESNGSSTATFPLRA
CCCCCCCCEEEECCC
21183079

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

Oops, there are no upstream regulatory protein records of NCHL1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCHL1_MOUSE !!

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 NCHL1_MOUSE !!

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

Oops, there are no PPI records of NCHL1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NCHL1_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP