UniProt ID | CAD24_HUMAN | |
---|---|---|
UniProt AC | Q86UP0 | |
Protein Name | Cadherin-24 | |
Gene Name | CDH24 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 819 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . |
|
Protein Description | Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Cadherin-24 mediate strong cell-cell adhesion.. | |
Protein Sequence | MWGLVRLLLAWLGGWGCMGRLAAPARAWAGSREHPGPALLRTRRSWVWNQFFVIEEYAGPEPVLIGKLHSDVDRGEGRTKYLLTGEGAGTVFVIDEATGNIHVTKSLDREEKAQYVLLAQAVDRASNRPLEPPSEFIIKVQDINDNPPIFPLGPYHATVPEMSNVGTSVIQVTAHDADDPSYGNSAKLVYTVLDGLPFFSVDPQTGVVRTAIPNMDRETQEEFLVVIQAKDMGGHMGGLSGSTTVTVTLSDVNDNPPKFPQSLYQFSVVETAGPGTLVGRLRAQDPDLGDNALMAYSILDGEGSEAFSISTDLQGRDGLLTVRKPLDFESQRSYSFRVEATNTLIDPAYLRRGPFKDVASVRVAVQDAPEPPAFTQAAYHLTVPENKAPGTLVGQISAADLDSPASPIRYSILPHSDPERCFSIQPEEGTIHTAAPLDREARAWHNLTVLATELGWSWGPERGWVPLLVAEWSAPAAPPQRSPVGSAVGIPQDSSAQASRVQVAIQTLDENDNAPQLAEPYDTFVCDSAAPGQLIQVIRALDRDEVGNSSHVSFQGPLGPDANFTVQDNRDGSASLLLPSRPAPPRHAPYLVPIELWDWGQPALSSTATVTVSVCRCQPDGSVASCWPEAHLSAAGLSTGALLAIITCVGALLALVVLFVALRRQKQEALMVLEEEDVRENIITYDDEGGGEEDTEAFDITALQNPDGAAPPAPGPPARRDVLPRARVSRQPRPPGPADVAQLLALRLREADEDPGVPPYDSVQVYGYEGRGSSCGSLSSLGSGSEAGGAPGPAEPLDDWGPLFRTLAELYGAKEPPAP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
90 | Phosphorylation | LTGEGAGTVFVIDEA EECCCCCEEEEEEEC | 15.38 | - | |
250 | Phosphorylation | TTVTVTLSDVNDNPP EEEEEEEHHCCCCCC | 30.10 | - | |
258 | Acetylation | DVNDNPPKFPQSLYQ HCCCCCCCCCCCEEE | 71.57 | 20167786 | |
262 | Phosphorylation | NPPKFPQSLYQFSVV CCCCCCCCEEEEEEE | 29.31 | 28111955 | |
264 | Phosphorylation | PKFPQSLYQFSVVET CCCCCCEEEEEEEEE | 16.86 | 28111955 | |
267 | Phosphorylation | PQSLYQFSVVETAGP CCCEEEEEEEEEECC | 15.10 | 28111955 | |
271 | Phosphorylation | YQFSVVETAGPGTLV EEEEEEEEECCCCEE | 25.88 | 28111955 | |
276 | Phosphorylation | VETAGPGTLVGRLRA EEEECCCCEEEEEEE | 22.77 | 28111955 | |
360 | Phosphorylation | GPFKDVASVRVAVQD CCCCCCEEEEEEEEC | 15.42 | 24719451 | |
446 | N-linked_Glycosylation | REARAWHNLTVLATE HHHHHHHHHEEEEHH | 27.06 | UniProtKB CARBOHYD | |
473 | Phosphorylation | PLLVAEWSAPAAPPQ EEEEEEECCCCCCCC | 18.84 | - | |
548 | N-linked_Glycosylation | LDRDEVGNSSHVSFQ CCCCCCCCCCCEEEC | 45.58 | UniProtKB CARBOHYD | |
563 | N-linked_Glycosylation | GPLGPDANFTVQDNR CCCCCCCCCEEEECC | 40.27 | UniProtKB CARBOHYD | |
573 | Phosphorylation | VQDNRDGSASLLLPS EEECCCCCEEEEEEC | 20.97 | - | |
575 | Phosphorylation | DNRDGSASLLLPSRP ECCCCCEEEEEECCC | 22.65 | - | |
580 | Phosphorylation | SASLLLPSRPAPPRH CEEEEEECCCCCCCC | 51.36 | 25278378 |
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 CAD24_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CAD24_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 CAD24_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of CAD24_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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