| UniProt ID | HECAM_MOUSE | |
|---|---|---|
| UniProt AC | Q640R3 | |
| Protein Name | Hepatocyte cell adhesion molecule | |
| Gene Name | Hepacam {ECO:0000312|MGI:MGI:1920177} | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 418 | |
| Subcellular Localization |
Cytoplasm. Membrane Single-pass type I membrane protein Cytoplasmic side . Colocalizes with CDH1. |
|
| Protein Description | Involved in regulating cell motility and cell-matrix interactions. May inhibit cell growth through suppression of cell proliferation (By similarity).. | |
| Protein Sequence | MKRERGALSRASRALRLSPFVYLLLIQPVPLEGVNITSPVRLIHGTVGKSALLSVQYSSTSSDKPVVKWQLKRDKPVTVVQSIGTEVIGTLRPDYRDRIRLFENGSLLLSDLQLADEGTYEVEISITDDTFTGEKTINLTVDVPISRPQVLVASTTVLELSEAFTLNCSHENGTKPSYTWLKDGKPLLNDSRMLLSPDQKVLTITRVLMEDDDLYSCVVENPISQVRSLPVKITVYRRSSLYIILSTGGIFLLVTLVTVCACWKPSKKSRKKRKLEKQNSLEYMDQNDDRLKSEADTLPRSGEQERKNPMALYILKDKDSSEPDENPATEPRSTTEPGPPGYSVSPPVPGRSPGLPIRSARRYPRSPARSPATGRTHTSPPRAPSSPGRSRSSSRSLRTAGVQRIREQDESGQVEISA | |
| 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 |
|---|---|---|---|---|---|
| 35 | N-linked_Glycosylation | PVPLEGVNITSPVRL CCCCCCCCCCCCEEE | 42.55 | - | |
| 138 | N-linked_Glycosylation | FTGEKTINLTVDVPI CCCEEEEEEEEECCC | 34.59 | - | |
| 167 | N-linked_Glycosylation | LSEAFTLNCSHENGT HHHEEECCCCCCCCC | 23.37 | - | |
| 189 | N-linked_Glycosylation | KDGKPLLNDSRMLLS ECCCCCCCCCCCCCC | 53.55 | - | |
| 205 | Phosphorylation | DQKVLTITRVLMEDD CCEEEEEEEEEECCC | 14.97 | 28285833 | |
| 216 | Phosphorylation | MEDDDLYSCVVENPI ECCCCHHHCEEECCH | 14.03 | 28285833 | |
| 224 | Phosphorylation | CVVENPISQVRSLPV CEEECCHHHHHCCCE | 24.71 | 28285833 | |
| 280 | Phosphorylation | RKLEKQNSLEYMDQN HHHHHHCHHHHHHCC | 21.78 | 25521595 | |
| 283 | Phosphorylation | EKQNSLEYMDQNDDR HHHCHHHHHHCCCHH | 15.98 | 25521595 | |
| 292 | Ubiquitination | DQNDDRLKSEADTLP HCCCHHHHHHHHHCC | 47.33 | - | |
| 293 | Phosphorylation | QNDDRLKSEADTLPR CCCHHHHHHHHHCCC | 42.48 | 23527152 | |
| 297 | Phosphorylation | RLKSEADTLPRSGEQ HHHHHHHHCCCCCHH | 45.79 | 25521595 | |
| 301 | Phosphorylation | EADTLPRSGEQERKN HHHHCCCCCHHHHCC | 44.75 | 25521595 | |
| 307 | Ubiquitination | RSGEQERKNPMALYI CCCHHHHCCCEEEEE | 65.73 | - | |
| 313 | Phosphorylation | RKNPMALYILKDKDS HCCCEEEEEECCCCC | 8.48 | 29899451 | |
| 316 | Ubiquitination | PMALYILKDKDSSEP CEEEEEECCCCCCCC | 53.85 | - | |
| 318 | Ubiquitination | ALYILKDKDSSEPDE EEEEECCCCCCCCCC | 58.90 | - | |
| 320 | Phosphorylation | YILKDKDSSEPDENP EEECCCCCCCCCCCC | 42.20 | 25521595 | |
| 321 | Phosphorylation | ILKDKDSSEPDENPA EECCCCCCCCCCCCC | 64.38 | 25521595 | |
| 329 | Phosphorylation | EPDENPATEPRSTTE CCCCCCCCCCCCCCC | 48.02 | 29899451 | |
| 333 | Phosphorylation | NPATEPRSTTEPGPP CCCCCCCCCCCCCCC | 50.85 | 23527152 | |
| 334 | Phosphorylation | PATEPRSTTEPGPPG CCCCCCCCCCCCCCC | 36.14 | 29899451 | |
| 342 | Phosphorylation | TEPGPPGYSVSPPVP CCCCCCCCCCCCCCC | 16.21 | 29899451 | |
| 343 | Phosphorylation | EPGPPGYSVSPPVPG CCCCCCCCCCCCCCC | 23.25 | 29899451 | |
| 345 | Phosphorylation | GPPGYSVSPPVPGRS CCCCCCCCCCCCCCC | 19.97 | 24925903 | |
| 352 | Phosphorylation | SPPVPGRSPGLPIRS CCCCCCCCCCCCCHH | 29.27 | 25521595 | |
| 359 | Phosphorylation | SPGLPIRSARRYPRS CCCCCCHHCCCCCCC | 27.18 | 29899451 | |
| 366 | Phosphorylation | SARRYPRSPARSPAT HCCCCCCCCCCCCCC | 20.57 | 29899451 | |
| 370 | Phosphorylation | YPRSPARSPATGRTH CCCCCCCCCCCCCCC | 22.46 | 25521595 | |
| 376 | Phosphorylation | RSPATGRTHTSPPRA CCCCCCCCCCCCCCC | 30.74 | 25521595 | |
| 378 | Phosphorylation | PATGRTHTSPPRAPS CCCCCCCCCCCCCCC | 42.17 | 25521595 | |
| 379 | Phosphorylation | ATGRTHTSPPRAPSS CCCCCCCCCCCCCCC | 25.88 | 25521595 | |
| 385 | Phosphorylation | TSPPRAPSSPGRSRS CCCCCCCCCCCCCCC | 48.45 | 25521595 | |
| 386 | Phosphorylation | SPPRAPSSPGRSRSS CCCCCCCCCCCCCCC | 30.25 | 25521595 | |
| 390 | Phosphorylation | APSSPGRSRSSSRSL CCCCCCCCCCCCHHH | 42.29 | 29899451 | |
| 417 | Phosphorylation | ESGQVEISA------ CCCCEEECC------ | 17.89 | 22807455 |
| 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 HECAM_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HECAM_MOUSE !! | ||||||
* 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 HECAM_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of HECAM_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-320 ANDSER-352, AND MASS SPECTROMETRY. | |