| UniProt ID | TRPV6_HUMAN | |
|---|---|---|
| UniProt AC | Q9H1D0 | |
| Protein Name | Transient receptor potential cation channel subfamily V member 6 | |
| Gene Name | TRPV6 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 765 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein . |
|
| Protein Description | Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine. [PubMed: 11097838] | |
| Protein Sequence | MGPLQGDGGPALGGADVAPRLSPVRVWPRPQAPKEPALHPMGLSLPKEKGLILCLWSKFCRWFQRRESWAQSRDEQNLLQQKRIWESPLLLAAKDNDVQALNKLLKYEDCKVHQRGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTSELYEGQTALHIAVVNQNMNLVRALLARRASVSARATGTAFRRSPCNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDRHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHTQWTYGPLTSTLYDLTEIDSSGDEQSLLELIITTKKREARQILDQTPVKELVSLKWKRYGRPYFCMLGAIYLLYIICFTMCCIYRPLKPRTNNRTSPRDNTLLQQKLLQEAYMTPKDDIRLVGELVTVIGAIIILLVEVPDIFRMGVTRFFGQTILGGPFHVLIITYAFMVLVTMVMRLISASGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPEELGHFYDYPMALFSTFELFLTIIDGPANYNVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQIVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQDLNRQRIQRYAQAFHTRGSEDLDKDSVEKLELGCPFSPHLSLPMPSVSRSTSRSSANWERLRQGTLRRDLRGIINRGLEDGESWEYQI | |
| 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 |
|---|---|---|---|---|---|
| 107 | Phosphorylation | ALNKLLKYEDCKVHQ HHHHHHCCCCCCCCC | 15.86 | - | |
| 144 | Phosphorylation | VLMEAAPELVFEPMT HHHHHCHHHHEECCC | 15.00 | - | |
| 182 | Phosphorylation | ALLARRASVSARATG HHHHHHHHHHHHHCC | 2.79 | - | |
| 184 | Phosphorylation | LARRASVSARATGTA HHHHHHHHHHHCCCC | 35.92 | - | |
| 188 | Phosphorylation | ASVSARATGTAFRRS HHHHHHHCCCCCCCC | 35.18 | 22210691 | |
| 190 | Phosphorylation | VSARATGTAFRRSPC HHHHHCCCCCCCCCC | 27.09 | 22210691 | |
| 201 | Phosphorylation | RSPCNLIYFGEHPLS CCCCEEEEEECCCCC | 14.42 | - | |
| 208 | N-linked_Glycosylation | YFGEHPLSFAACVNS EEECCCCCEEECCCH | 42.93 | - | |
| 248 | N-linked_Glycosylation | HILILQPNKTFACQM EEEEECCCCCCHHHH | 28.57 | 12765696 | |
| 318 | Phosphorylation | GPLTSTLYDLTEIDS CCCHHCEEECCCCCC | 36.53 | - | |
| 358 | N-linked_Glycosylation | TPVKELVSLKWKRYG CCHHHHHHHCCHHHC | 48.25 | - | |
| 396 | Phosphorylation | YRPLKPRTNNRTSPR HCCCCCCCCCCCCCC | 4.43 | 29052541 | |
| 398 | N-linked_Glycosylation | PLKPRTNNRTSPRDN CCCCCCCCCCCCCCC | 1.47 | 12765696 | |
| 398 | N-linked_Glycosylation | PLKPRTNNRTSPRDN CCCCCCCCCCCCCCC | 1.47 | UniProtKB CARBOHYD | |
| 400 | Phosphorylation | KPRTNNRTSPRDNTL CCCCCCCCCCCCCHH | 2.86 | 23090842 | |
| 401 | Phosphorylation | PRTNNRTSPRDNTLL CCCCCCCCCCCCHHH | 1.86 | 23090842 | |
| 406 | Phosphorylation | RTSPRDNTLLQQKLL CCCCCCCHHHHHHHH | 58.81 | 23090842 | |
| 417 | Phosphorylation | QKLLQEAYMTPKDDI HHHHHHHHCCCHHHH | 22.47 | 23090842 | |
| 419 | Phosphorylation | LLQEAYMTPKDDIRL HHHHHHCCCHHHHHH | 20.67 | 23090842 | |
| 601 | Phosphorylation | MYSITYAAFAIIATL HHHHHHHHHHHHHHH | 8.32 | 18669648 | |
| 641 | Phosphorylation | RAQIVATTVMLERKL HHHHHHHHHHHHCCC | 34.16 | 18669648 | |
| 688 | Phosphorylation | RQRIQRYAQAFHTRG HHHHHHHHHHHHHCC | 27.35 | - | |
| 696 | Phosphorylation | QAFHTRGSEDLDKDS HHHHHCCCCCCCHHH | 41.46 | 28102081 | |
| 702 | Phosphorylation | GSEDLDKDSVEKLEL CCCCCCHHHHHHHCC | 14.57 | 11248124 | |
| 703 | Phosphorylation | SEDLDKDSVEKLELG CCCCCHHHHHHHCCC | 5.59 | 28102081 | |
| 714 | Phosphorylation | LELGCPFSPHLSLPM HCCCCCCCCCCCCCC | 29.00 | 28270605 | |
| 718 | Phosphorylation | CPFSPHLSLPMPSVS CCCCCCCCCCCCCCC | 22.82 | 28270605 | |
| 723 | Phosphorylation | HLSLPMPSVSRSTSR CCCCCCCCCCCCCCC | 12.78 | 28270605 | |
| 727 | Phosphorylation | PMPSVSRSTSRSSAN CCCCCCCCCCCCCCC | - | ||
| 728 | Phosphorylation | MPSVSRSTSRSSANW CCCCCCCCCCCCCCH | 22817900 | ||
| 731 | Phosphorylation | VSRSTSRSSANWERL CCCCCCCCCCCHHHH | - | ||
| 732 | Phosphorylation | SRSTSRSSANWERLR CCCCCCCCCCHHHHH | - | ||
| 742 | Phosphorylation | WERLRQGTLRRDLRG HHHHHHCCHHHHHHH | 11278579 | ||
| 760 | Phosphorylation | RGLEDGESWEYQI-- CCCCCCCCCCCCC-- | 25159151 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 184 | S | Phosphorylation | Kinase | PRKCB | P05771-2 | GPS |
| 201 | Y | Phosphorylation | Kinase | SRC | P12931 | Uniprot |
| 702 | T | Phosphorylation | Kinase | KPCA | P17252 | PhosphoELM |
| 728 | T | Phosphorylation | Kinase | PRKCB | P05771-2 | GPS |
| 742 | T | Phosphorylation | Kinase | PKCA | P17252 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | NEDD4L | Q96PU5 | PMID:20843805 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRPV6_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 TRPV6_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| NEDD4_HUMAN | NEDD4 | physical | 20843805 | |
| K1C40_HUMAN | KRT40 | physical | 25416956 | |
| KR108_HUMAN | KRTAP10-8 | physical | 25416956 | |
| KR103_HUMAN | KRTAP10-3 | physical | 25416956 | |
| NT2NL_HUMAN | NOTCH2NL | physical | 25416956 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Competitive regulation of CaT-like-mediated Ca2+ entry by proteinkinase C and calmodulin."; Niemeyer B.A., Bergs C., Wissenbach U., Flockerzi V., Trost C.; Proc. Natl. Acad. Sci. U.S.A. 98:3600-3605(2001). Cited for: FUNCTION, INTERACTION WITH CALMODULIN, PHOSPHORYLATION AT THR-702, ANDMUTAGENESIS OF THR-702. | |