CNTP1_HUMAN - dbPTM
CNTP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNTP1_HUMAN
UniProt AC P78357
Protein Name Contactin-associated protein 1
Gene Name CNTNAP1
Organism Homo sapiens (Human).
Sequence Length 1384
Subcellular Localization Membrane
Single-pass type I membrane protein . Cell junction, paranodal septate junction .
Protein Description Required, with CNTNAP2, for radial and longitudinal organization of myelinated axons. Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the paranodal region of the axo-glial junction. In association with contactin involved in the signaling between axons and myelinating glial cells..
Protein Sequence MMHLRLFCILLAAVSGAEGWGYYGCDEELVGPLYARSLGASSYYSLLTAPRFARLHGISGWSPRIGDPNPWLQIDLMKKHRIRAVATQGSFNSWDWVTRYMLLYGDRVDSWTPFYQRGHNSTFFGNVNESAVVRHDLHFHFTARYIRIVPLAWNPRGKIGLRLGLYGCPYKADILYFDGDDAISYRFPRGVSRSLWDVFAFSFKTEEKDGLLLHAEGAQGDYVTLELEGAHLLLHMSLGSSPIQPRPGHTTVSAGGVLNDQHWHYVRVDRFGRDVNFTLDGYVQRFILNGDFERLNLDTEMFIGGLVGAARKNLAYRHNFRGCIENVIFNRVNIADLAVRRHSRITFEGKVAFRCLDPVPHPINFGGPHNFVQVPGFPRRGRLAVSFRFRTWDLTGLLLFSRLGDGLGHVELTLSEGQVNVSIAQSGRKKLQFAAGYRLNDGFWHEVNFVAQENHAVISIDDVEGAEVRVSYPLLIRTGTSYFFGGCPKPASRWDCHSNQTAFHGCMELLKVDGQLVNLTLVEGRRLGFYAEVLFDTCGITDRCSPNMCEHDGRCYQSWDDFICYCELTGYKGETCHTPLYKESCEAYRLSGKTSGNFTIDPDGSGPLKPFVVYCDIRENRAWTVVRHDRLWTTRVTGSSMERPFLGAIQYWNASWEEVSALANASQHCEQWIEFSCYNSRLLNTAGGYPYSFWIGRNEEQHFYWGGSQPGIQRCACGLDRSCVDPALYCNCDADQPQWRTDKGLLTFVDHLPVTQVVIGDTNRSTSEAQFFLRPLRCYGDRNSWNTISFHTGAALRFPPIRANHSLDVSFYFRTSAPSGVFLENMGGPYCQWRRPYVRVELNTSRDVVFAFDVGNGDENLTVHSDDFEFNDDEWHLVRAEINVKQARLRVDHRPWVLRPMPLQTYIWMEYDQPLYVGSAELKRRPFVGCLRAMRLNGVTLNLEGRANASEGTSPNCTGHCAHPRLPCFHGGRCVERYSYYTCDCDLTAFDGPYCNHDIGGFFEPGTWMRYNLQSALRSAAREFSHMLSRPVPGYEPGYIPGYDTPGYVPGYHGPGYRLPDYPRPGRPVPGYRGPVYNVTGEEVSFSFSTSSAPAVLLYVSSFVRDYMAVLIKDDGTLQLRYQLGTSPYVYQLTTRPVTDGQPHSINITRVYRNLFIQVDYFPLTEQKFSLLVDSQLDSPKALYLGRVMETGVIDPEIQRYNTPGFSGCLSGVRFNNVAPLKTHFRTPRPMTAELAEALRVQGELSESNCGAMPRLVSEVPPELDPWYLPPDFPYYHDEGWVAILLGFLVAFLLLGLVGMLVLFYLQNHRYKGSYHTNEPKAAHEYHPGSKPPLPTSGPAQVPTPTAAPNQAPASAPAPAPTPAPAPGPRDQNLPQILEESRSE
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
37PhosphorylationVGPLYARSLGASSYY
CHHHHHHHCCCHHHH
24.0022617229
43PhosphorylationRSLGASSYYSLLTAP
HHCCCHHHHHHHHHH
8.4522617229
45PhosphorylationLGASSYYSLLTAPRF
CCCHHHHHHHHHHHH
14.5222617229
48PhosphorylationSSYYSLLTAPRFARL
HHHHHHHHHHHHHHH
39.6522617229
59PhosphorylationFARLHGISGWSPRIG
HHHHCCCCCCCCCCC
38.51-
62PhosphorylationLHGISGWSPRIGDPN
HCCCCCCCCCCCCCC
14.0724719451
120N-linked_GlycosylationPFYQRGHNSTFFGNV
CCEECCCCCCCCCCC
45.64UniProtKB CARBOHYD
128N-linked_GlycosylationSTFFGNVNESAVVRH
CCCCCCCCCCCEEEC
41.32UniProtKB CARBOHYD
202PhosphorylationLWDVFAFSFKTEEKD
HHHEEEEEEECCCCC
23.5424719451
276N-linked_GlycosylationDRFGRDVNFTLDGYV
ECCCCEEEEECCHHE
28.60UniProtKB CARBOHYD
299PhosphorylationFERLNLDTEMFIGGL
HHHCCCCHHHHHHHH
32.30-
316PhosphorylationAARKNLAYRHNFRGC
HHHHHHHHHCCCCHH
18.6428509920
420N-linked_GlycosylationTLSEGQVNVSIAQSG
EECCCEEEEEEECCC
17.58UniProtKB CARBOHYD
437PhosphorylationKLQFAAGYRLNDGFW
EEEEEEEEECCCCCC
13.7523403867
489MethylationYFFGGCPKPASRWDC
EECCCCCCCCCCCCC
58.24-
499N-linked_GlycosylationSRWDCHSNQTAFHGC
CCCCCCCCCHHHCHH
21.40UniProtKB CARBOHYD
518N-linked_GlycosylationKVDGQLVNLTLVEGR
EECCEEEEEEEECCC
35.58UniProtKB CARBOHYD
597N-linked_GlycosylationLSGKTSGNFTIDPDG
CCCCCCCCEEECCCC
30.56UniProtKB CARBOHYD
653N-linked_GlycosylationLGAIQYWNASWEEVS
HHEEEHHHCCHHHHH
21.11UniProtKB CARBOHYD
664N-linked_GlycosylationEEVSALANASQHCEQ
HHHHHHHHHHHHHHH
40.76UniProtKB CARBOHYD
763N-linked_GlycosylationQVVIGDTNRSTSEAQ
EEEECCCCCCCCHHH
40.42UniProtKB CARBOHYD
779PhosphorylationFLRPLRCYGDRNSWN
EEEEEEECCCCCCCE
18.6729978859
784PhosphorylationRCYGDRNSWNTISFH
EECCCCCCCEEEEEE
23.6929978859
787PhosphorylationGDRNSWNTISFHTGA
CCCCCCEEEEEECCC
16.2529978859
789PhosphorylationRNSWNTISFHTGAAL
CCCCEEEEEECCCCC
14.6729978859
792PhosphorylationWNTISFHTGAALRFP
CEEEEEECCCCCCCC
26.8929978859
804N-linked_GlycosylationRFPPIRANHSLDVSF
CCCCCCCCCCEEEEE
18.55UniProtKB CARBOHYD
843N-linked_GlycosylationPYVRVELNTSRDVVF
CEEEEEECCCCEEEE
23.62UniProtKB CARBOHYD
860N-linked_GlycosylationDVGNGDENLTVHSDD
ECCCCCCCEEEEECC
45.83UniProtKB CARBOHYD
885UbiquitinationVRAEINVKQARLRVD
EEEEEECCCCEEECC
33.48-
940PhosphorylationAMRLNGVTLNLEGRA
EEEECCEEEEEECCC
16.01-
948N-linked_GlycosylationLNLEGRANASEGTSP
EEEECCCCCCCCCCC
42.51UniProtKB CARBOHYD
950PhosphorylationLEGRANASEGTSPNC
EECCCCCCCCCCCCC
36.0422210691
953PhosphorylationRANASEGTSPNCTGH
CCCCCCCCCCCCCCC
36.6422210691
954PhosphorylationANASEGTSPNCTGHC
CCCCCCCCCCCCCCC
25.6022210691
956N-linked_GlycosylationASEGTSPNCTGHCAH
CCCCCCCCCCCCCCC
35.43UniProtKB CARBOHYD
1011PhosphorylationEPGTWMRYNLQSALR
CCCCHHHHHHHHHHH
12.2427642862
1015PhosphorylationWMRYNLQSALRSAAR
HHHHHHHHHHHHHHH
32.2230206219
1019PhosphorylationNLQSALRSAAREFSH
HHHHHHHHHHHHHHH
27.4230206219
1078N-linked_GlycosylationGYRGPVYNVTGEEVS
CCCCCEEECCCCEEE
25.71UniProtKB CARBOHYD
1087PhosphorylationTGEEVSFSFSTSSAP
CCCEEEEEEECCCCC
15.69-
1122PhosphorylationDGTLQLRYQLGTSPY
CCEEEEEEECCCCCE
19.3823663014
1126PhosphorylationQLRYQLGTSPYVYQL
EEEEECCCCCEEEEE
34.8123663014
1127PhosphorylationLRYQLGTSPYVYQLT
EEEECCCCCEEEEEE
16.6623663014
1129PhosphorylationYQLGTSPYVYQLTTR
EECCCCCEEEEEECC
16.1423663014
1131PhosphorylationLGTSPYVYQLTTRPV
CCCCCEEEEEECCCC
7.6123663014
1134PhosphorylationSPYVYQLTTRPVTDG
CCEEEEEECCCCCCC
12.7723663014
1135PhosphorylationPYVYQLTTRPVTDGQ
CEEEEEECCCCCCCC
41.3823663014
1147N-linked_GlycosylationDGQPHSINITRVYRN
CCCCCEEEEEEEEEC
32.37UniProtKB CARBOHYD
1149PhosphorylationQPHSINITRVYRNLF
CCCEEEEEEEEECEE
15.03-
1170PhosphorylationPLTEQKFSLLVDSQL
ECCCHHEEEHHHCCC
28.0326471730
1211PhosphorylationPGFSGCLSGVRFNNV
CCCCCCCCCCEECCC
39.0424719451
1331UbiquitinationHEYHPGSKPPLPTSG
CCCCCCCCCCCCCCC
57.4830230243
1381PhosphorylationLPQILEESRSE----
HHHHHHHHHCC----
31.5630108239
1383PhosphorylationQILEESRSE------
HHHHHHHCC------
57.8630108239

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 CNTP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNTP1_HUMAN !!

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 CNTP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RTN4_HUMANRTN4physical
14592966
KCNA1_HUMANKCNA1physical
14592966
KCNA2_HUMANKCNA2physical
14592966

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNTP1_HUMAN

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Related Literatures of Post-Translational Modification

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