| 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 | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 37 | Phosphorylation | VGPLYARSLGASSYY CHHHHHHHCCCHHHH | 24.00 | 22617229 | |
| 43 | Phosphorylation | RSLGASSYYSLLTAP HHCCCHHHHHHHHHH | 8.45 | 22617229 | |
| 45 | Phosphorylation | LGASSYYSLLTAPRF CCCHHHHHHHHHHHH | 14.52 | 22617229 | |
| 48 | Phosphorylation | SSYYSLLTAPRFARL HHHHHHHHHHHHHHH | 39.65 | 22617229 | |
| 59 | Phosphorylation | FARLHGISGWSPRIG HHHHCCCCCCCCCCC | 38.51 | - | |
| 62 | Phosphorylation | LHGISGWSPRIGDPN HCCCCCCCCCCCCCC | 14.07 | 24719451 | |
| 120 | N-linked_Glycosylation | PFYQRGHNSTFFGNV CCEECCCCCCCCCCC | 45.64 | UniProtKB CARBOHYD | |
| 128 | N-linked_Glycosylation | STFFGNVNESAVVRH CCCCCCCCCCCEEEC | 41.32 | UniProtKB CARBOHYD | |
| 202 | Phosphorylation | LWDVFAFSFKTEEKD HHHEEEEEEECCCCC | 23.54 | 24719451 | |
| 276 | N-linked_Glycosylation | DRFGRDVNFTLDGYV ECCCCEEEEECCHHE | 28.60 | UniProtKB CARBOHYD | |
| 299 | Phosphorylation | FERLNLDTEMFIGGL HHHCCCCHHHHHHHH | 32.30 | - | |
| 316 | Phosphorylation | AARKNLAYRHNFRGC HHHHHHHHHCCCCHH | 18.64 | 28509920 | |
| 420 | N-linked_Glycosylation | TLSEGQVNVSIAQSG EECCCEEEEEEECCC | 17.58 | UniProtKB CARBOHYD | |
| 437 | Phosphorylation | KLQFAAGYRLNDGFW EEEEEEEEECCCCCC | 13.75 | 23403867 | |
| 489 | Methylation | YFFGGCPKPASRWDC EECCCCCCCCCCCCC | 58.24 | - | |
| 499 | N-linked_Glycosylation | SRWDCHSNQTAFHGC CCCCCCCCCHHHCHH | 21.40 | UniProtKB CARBOHYD | |
| 518 | N-linked_Glycosylation | KVDGQLVNLTLVEGR EECCEEEEEEEECCC | 35.58 | UniProtKB CARBOHYD | |
| 597 | N-linked_Glycosylation | LSGKTSGNFTIDPDG CCCCCCCCEEECCCC | 30.56 | UniProtKB CARBOHYD | |
| 653 | N-linked_Glycosylation | LGAIQYWNASWEEVS HHEEEHHHCCHHHHH | 21.11 | UniProtKB CARBOHYD | |
| 664 | N-linked_Glycosylation | EEVSALANASQHCEQ HHHHHHHHHHHHHHH | 40.76 | UniProtKB CARBOHYD | |
| 763 | N-linked_Glycosylation | QVVIGDTNRSTSEAQ EEEECCCCCCCCHHH | 40.42 | UniProtKB CARBOHYD | |
| 779 | Phosphorylation | FLRPLRCYGDRNSWN EEEEEEECCCCCCCE | 18.67 | 29978859 | |
| 784 | Phosphorylation | RCYGDRNSWNTISFH EECCCCCCCEEEEEE | 23.69 | 29978859 | |
| 787 | Phosphorylation | GDRNSWNTISFHTGA CCCCCCEEEEEECCC | 16.25 | 29978859 | |
| 789 | Phosphorylation | RNSWNTISFHTGAAL CCCCEEEEEECCCCC | 14.67 | 29978859 | |
| 792 | Phosphorylation | WNTISFHTGAALRFP CEEEEEECCCCCCCC | 26.89 | 29978859 | |
| 804 | N-linked_Glycosylation | RFPPIRANHSLDVSF CCCCCCCCCCEEEEE | 18.55 | UniProtKB CARBOHYD | |
| 843 | N-linked_Glycosylation | PYVRVELNTSRDVVF CEEEEEECCCCEEEE | 23.62 | UniProtKB CARBOHYD | |
| 860 | N-linked_Glycosylation | DVGNGDENLTVHSDD ECCCCCCCEEEEECC | 45.83 | UniProtKB CARBOHYD | |
| 885 | Ubiquitination | VRAEINVKQARLRVD EEEEEECCCCEEECC | 33.48 | - | |
| 940 | Phosphorylation | AMRLNGVTLNLEGRA EEEECCEEEEEECCC | 16.01 | - | |
| 948 | N-linked_Glycosylation | LNLEGRANASEGTSP EEEECCCCCCCCCCC | 42.51 | UniProtKB CARBOHYD | |
| 950 | Phosphorylation | LEGRANASEGTSPNC EECCCCCCCCCCCCC | 36.04 | 22210691 | |
| 953 | Phosphorylation | RANASEGTSPNCTGH CCCCCCCCCCCCCCC | 36.64 | 22210691 | |
| 954 | Phosphorylation | ANASEGTSPNCTGHC CCCCCCCCCCCCCCC | 25.60 | 22210691 | |
| 956 | N-linked_Glycosylation | ASEGTSPNCTGHCAH CCCCCCCCCCCCCCC | 35.43 | UniProtKB CARBOHYD | |
| 1011 | Phosphorylation | EPGTWMRYNLQSALR CCCCHHHHHHHHHHH | 12.24 | 27642862 | |
| 1015 | Phosphorylation | WMRYNLQSALRSAAR HHHHHHHHHHHHHHH | 32.22 | 30206219 | |
| 1019 | Phosphorylation | NLQSALRSAAREFSH HHHHHHHHHHHHHHH | 27.42 | 30206219 | |
| 1078 | N-linked_Glycosylation | GYRGPVYNVTGEEVS CCCCCEEECCCCEEE | 25.71 | UniProtKB CARBOHYD | |
| 1087 | Phosphorylation | TGEEVSFSFSTSSAP CCCEEEEEEECCCCC | 15.69 | - | |
| 1122 | Phosphorylation | DGTLQLRYQLGTSPY CCEEEEEEECCCCCE | 19.38 | 23663014 | |
| 1126 | Phosphorylation | QLRYQLGTSPYVYQL EEEEECCCCCEEEEE | 34.81 | 23663014 | |
| 1127 | Phosphorylation | LRYQLGTSPYVYQLT EEEECCCCCEEEEEE | 16.66 | 23663014 | |
| 1129 | Phosphorylation | YQLGTSPYVYQLTTR EECCCCCEEEEEECC | 16.14 | 23663014 | |
| 1131 | Phosphorylation | LGTSPYVYQLTTRPV CCCCCEEEEEECCCC | 7.61 | 23663014 | |
| 1134 | Phosphorylation | SPYVYQLTTRPVTDG CCEEEEEECCCCCCC | 12.77 | 23663014 | |
| 1135 | Phosphorylation | PYVYQLTTRPVTDGQ CEEEEEECCCCCCCC | 41.38 | 23663014 | |
| 1147 | N-linked_Glycosylation | DGQPHSINITRVYRN CCCCCEEEEEEEEEC | 32.37 | UniProtKB CARBOHYD | |
| 1149 | Phosphorylation | QPHSINITRVYRNLF CCCEEEEEEEEECEE | 15.03 | - | |
| 1170 | Phosphorylation | PLTEQKFSLLVDSQL ECCCHHEEEHHHCCC | 28.03 | 26471730 | |
| 1211 | Phosphorylation | PGFSGCLSGVRFNNV CCCCCCCCCCEECCC | 39.04 | 24719451 | |
| 1331 | Ubiquitination | HEYHPGSKPPLPTSG CCCCCCCCCCCCCCC | 57.48 | 30230243 | |
| 1381 | Phosphorylation | LPQILEESRSE---- HHHHHHHHHCC---- | 31.56 | 30108239 | |
| 1383 | Phosphorylation | QILEESRSE------ HHHHHHHCC------ | 57.86 | 30108239 |
| 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 !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CNTP1_HUMAN !! | ||||||
* 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 !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RTN4_HUMAN | RTN4 | physical | 14592966 | |
| KCNA1_HUMAN | KCNA1 | physical | 14592966 | |
| KCNA2_HUMAN | KCNA2 | physical | 14592966 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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