| UniProt ID | CNTN4_HUMAN | |
|---|---|---|
| UniProt AC | Q8IWV2 | |
| Protein Name | Contactin-4 | |
| Gene Name | CNTN4 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 1026 | |
| Subcellular Localization |
Cell membrane Lipid-anchor, GPI-anchor. Secreted. |
|
| Protein Description | Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity. May be involved in synaptogenesis.. | |
| Protein Sequence | MRLPWELLVLQSFILCLADDSTLHGPIFIQEPSPVMFPLDSEEKKVKLNCEVKGNPKPHIRWKLNGTDVDTGMDFRYSVVEGSLLINNPNKTQDAGTYQCTATNSFGTIVSREAKLQFAYLDNFKTRTRSTVSVRRGQGMVLLCGPPPHSGELSYAWIFNEYPSYQDNRRFVSQETGNLYIAKVEKSDVGNYTCVVTNTVTNHKVLGPPTPLILRNDGVMGEYEPKIEVQFPETVPTAKGATVKLECFALGNPVPTIIWRRADGKPIARKARRHKSNGILEIPNFQQEDAGLYECVAENSRGKNVARGQLTFYAQPNWIQKINDIHVAMEENVFWECKANGRPKPTYKWLKNGEPLLTRDRIQIEQGTLNITIVNLSDAGMYQCLAENKHGVIFSNAELSVIAVGPDFSRTLLKRVTLVKVGGEVVIECKPKASPKPVYTWKKGRDILKENERITISEDGNLRIINVTKSDAGSYTCIATNHFGTASSTGNLVVKDPTRVMVPPSSMDVTVGESIVLPCQVTHDHSLDIVFTWSFNGHLIDFDRDGDHFERVGGQDSAGDLMIRNIQLKHAGKYVCMVQTSVDRLSAAADLIVRGPPGPPEAVTIDEITDTTAQLSWRPGPDNHSPITMYVIQARTPFSVGWQAVSTVPELIDGKTFTATVVGLNPWVEYEFRTVAANVIGIGEPSRPSEKRRTEEALPEVTPANVSGGGGSKSELVITWETVPEELQNGRGFGYVVAFRPYGKMIWMLTVLASADASRYVFRNESVHPFSPFEVKVGVFNNKGEGPFSPTTVVYSAEEEPTKPPASIFARSLSATDIEVFWASPLEKNRGRIQGYEVKYWRHEDKEENARKIRTVGNQTSTKITNLKGSVLYHLAVKAYNSAGTGPSSATVNVTTRKPPPSQPPGNIIWNSSDSKIILNWDQVKALDNESEVKGYKVLYRWNRQSSTSVIETNKTSVELSLPFDEDYIIEIKPFSDGGDGSSSEQIRIPKISNAYARGSGASTSNACTLSAISTIMISLTARSSL | |
| 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 |
|---|---|---|---|---|---|
| 65 | N-linked_Glycosylation | PHIRWKLNGTDVDTG CCEEEEECCEECCCC | 47.82 | 16335952 | |
| 90 | N-linked_Glycosylation | SLLINNPNKTQDAGT CEEECCCCCCCCCEE | 63.23 | UniProtKB CARBOHYD | |
| 131 | Phosphorylation | FKTRTRSTVSVRRGQ CCCCCCCEEEEECCC | 17.32 | - | |
| 176 | Phosphorylation | RRFVSQETGNLYIAK CCEEECCCCCEEEEE | 24.59 | - | |
| 180 | Phosphorylation | SQETGNLYIAKVEKS ECCCCCEEEEEEEEC | 11.66 | - | |
| 191 | N-linked_Glycosylation | VEKSDVGNYTCVVTN EEECCCCCEEEEEEE | 28.87 | UniProtKB CARBOHYD | |
| 223 | Phosphorylation | NDGVMGEYEPKIEVQ CCCCCCCCCCCEEEE | 31.63 | - | |
| 370 | N-linked_Glycosylation | QIEQGTLNITIVNLS EEECCEEEEEEEEHH | 29.24 | UniProtKB CARBOHYD | |
| 375 | N-linked_Glycosylation | TLNITIVNLSDAGMY EEEEEEEEHHHCCHH | 29.94 | UniProtKB CARBOHYD | |
| 466 | N-linked_Glycosylation | DGNLRIINVTKSDAG CCCEEEEEEECCCCC | 32.79 | UniProtKB CARBOHYD | |
| 474 | Phosphorylation | VTKSDAGSYTCIATN EECCCCCCEEEEEEC | 20.99 | - | |
| 476 | Phosphorylation | KSDAGSYTCIATNHF CCCCCCEEEEEECCC | 10.11 | - | |
| 487 | Phosphorylation | TNHFGTASSTGNLVV ECCCCCCCCCCCEEE | 28.42 | - | |
| 616 | Phosphorylation | TDTTAQLSWRPGPDN CCCEEECCCCCCCCC | 14.68 | 24719451 | |
| 705 | N-linked_Glycosylation | LPEVTPANVSGGGGS CCCCCCCCCCCCCCC | 29.68 | UniProtKB CARBOHYD | |
| 764 | N-linked_Glycosylation | ASRYVFRNESVHPFS HHHEEECCCCCCCCC | 34.14 | UniProtKB CARBOHYD | |
| 824 | Phosphorylation | DIEVFWASPLEKNRG CEEEEEECCCHHCCC | 22.18 | 24719451 | |
| 855 | Phosphorylation | ENARKIRTVGNQTST HHHHEEEECCCCCCC | 35.92 | 19651622 | |
| 858 | N-linked_Glycosylation | RKIRTVGNQTSTKIT HEEEECCCCCCCEEE | 37.31 | UniProtKB CARBOHYD | |
| 862 | Phosphorylation | TVGNQTSTKITNLKG ECCCCCCCEEECCCC | 29.83 | 19651622 | |
| 893 | N-linked_Glycosylation | GPSSATVNVTTRKPP CCCCCEEEEEECCCC | 22.51 | UniProtKB CARBOHYD | |
| 911 | N-linked_Glycosylation | PPGNIIWNSSDSKII CCCCEEECCCCCEEE | 22.64 | UniProtKB CARBOHYD | |
| 929 | N-linked_Glycosylation | DQVKALDNESEVKGY HHEEECCCHHHHCCE | 56.39 | UniProtKB CARBOHYD | |
| 954 | N-linked_Glycosylation | STSVIETNKTSVELS CCEEEECCCCEEEEE | 32.58 | UniProtKB CARBOHYD | |
| 1000 | GPI-anchor | SNAYARGSGASTSNA CCCCCCCCCCCCCCC | 26.15 | - | |
| 1015 | Phosphorylation | CTLSAISTIMISLTA HHHHHHHHHHHHHHH | 14.40 | - | |
| 1021 | Phosphorylation | STIMISLTARSSL-- HHHHHHHHHHHCC-- | 17.15 | - |
| 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 CNTN4_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CNTN4_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 CNTN4_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CNTN4_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65, AND MASS SPECTROMETRY. | |