| UniProt ID | CLP1L_HUMAN | |
|---|---|---|
| UniProt AC | Q96KA5 | |
| Protein Name | Cleft lip and palate transmembrane protein 1-like protein | |
| Gene Name | CLPTM1L | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 538 | |
| Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
| Protein Description | Enhances cisplatin-mediated apoptosis, when overexpressed.. | |
| Protein Sequence | MWSGRSSFTSLVVGVFVVYVVHTCWVMYGIVYTRPCSGDANCIQPYLARRPKLQLSVYTTTRSHLGAENNIDLVLNVEDFDVESKFERTVNVSVPKKTRNNGTLYAYIFLHHAGVLPWHDGKQVHLVSPLTTYMVPKPEEINLLTGESDTQQIEAEKKPTSALDEPVSHWRPRLALNVMADNFVFDGSSLPADVHRYMKMIQLGKTVHYLPILFIDQLSNRVKDLMVINRSTTELPLTVSYDKVSLGRLRFWIHMQDAVYSLQQFGFSEKDADEVKGIFVDTNLYFLALTFFVAAFHLLFDFLAFKNDISFWKKKKSMIGMSTKAVLWRCFSTVVIFLFLLDEQTSLLVLVPAGVGAAIELWKVKKALKMTIFWRGLMPEFQFGTYSESERKTEEYDTQAMKYLSYLLYPLCVGGAVYSLLNIKYKSWYSWLINSFVNGVYAFGFLFMLPQLFVNYKLKSVAHLPWKAFTYKAFNTFIDDVFAFIITMPTSHRLACFRDDVVFLVYLYQRWLYPVDKRRVNEFGESYEEKATRAPHTD | |
| 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 |
|---|---|---|---|---|---|
| 60 | Phosphorylation | LQLSVYTTTRSHLGA EEEEEEECCCHHCCC | 11.52 | 20068231 | |
| 84 | Phosphorylation | VEDFDVESKFERTVN ECCCCCHHCEEEEEE | 42.36 | 28450419 | |
| 85 (in isoform 2) | Ubiquitination | - | 37.43 | 21890473 | |
| 85 (in isoform 1) | Ubiquitination | - | 37.43 | 21890473 | |
| 85 | Ubiquitination | EDFDVESKFERTVNV CCCCCHHCEEEEEEE | 37.43 | 22817900 | |
| 89 | O-linked_Glycosylation | VESKFERTVNVSVPK CHHCEEEEEEEECCC | 14.83 | 30059200 | |
| 91 | N-linked_Glycosylation | SKFERTVNVSVPKKT HCEEEEEEEECCCCC | 21.52 | UniProtKB CARBOHYD | |
| 91 | N-linked_Glycosylation | SKFERTVNVSVPKKT HCEEEEEEEECCCCC | 21.52 | 20068230 | |
| 101 | N-linked_Glycosylation | VPKKTRNNGTLYAYI CCCCCCCCCCEEEEE | 41.35 | UniProtKB CARBOHYD | |
| 137 | Ubiquitination | LTTYMVPKPEEINLL CEEEECCCHHHCCEE | 54.36 | 29967540 | |
| 158 | Ubiquitination | QQIEAEKKPTSALDE HHHHHHHCCCCCCCC | 45.06 | 29967540 | |
| 198 | Ubiquitination | PADVHRYMKMIQLGK CHHHHHHHHHHHHCC | 2.10 | 21890473 | |
| 199 (in isoform 2) | Ubiquitination | - | 24.74 | 21890473 | |
| 199 (in isoform 1) | Ubiquitination | - | 24.74 | 21890473 | |
| 199 | Ubiquitination | ADVHRYMKMIQLGKT HHHHHHHHHHHHCCC | 24.74 | 21890473 | |
| 205 | Ubiquitination | MKMIQLGKTVHYLPI HHHHHHCCCEEHHHH | 56.84 | - | |
| 206 | Phosphorylation | KMIQLGKTVHYLPIL HHHHHCCCEEHHHHH | 15.66 | - | |
| 209 | Phosphorylation | QLGKTVHYLPILFID HHCCCEEHHHHHHHH | 15.16 | - | |
| 223 | Ubiquitination | DQLSNRVKDLMVINR HHHCHHCEEEEEECC | 41.74 | - | |
| 229 | N-linked_Glycosylation | VKDLMVINRSTTELP CEEEEEECCCCCCCE | 22.05 | 19159218 | |
| 231 | Phosphorylation | DLMVINRSTTELPLT EEEEECCCCCCCEEE | 34.88 | 20068231 | |
| 232 | Phosphorylation | LMVINRSTTELPLTV EEEECCCCCCCEEEE | 22.51 | 20068231 | |
| 233 | Phosphorylation | MVINRSTTELPLTVS EEECCCCCCCEEEEE | 36.45 | 20068231 | |
| 238 | Phosphorylation | STTELPLTVSYDKVS CCCCCEEEEEEEEEC | 12.88 | - | |
| 240 | Phosphorylation | TELPLTVSYDKVSLG CCCEEEEEEEEECCC | 23.52 | 20068231 | |
| 241 | Phosphorylation | ELPLTVSYDKVSLGR CCEEEEEEEEECCCE | 18.56 | 20068231 | |
| 242 | Ubiquitination | LPLTVSYDKVSLGRL CEEEEEEEEECCCEE | 37.06 | 27667366 | |
| 243 (in isoform 2) | Ubiquitination | - | 26.03 | 21890473 | |
| 243 | Ubiquitination | PLTVSYDKVSLGRLR EEEEEEEEECCCEEE | 26.03 | 27667366 | |
| 243 (in isoform 1) | Ubiquitination | - | 26.03 | 21890473 | |
| 312 | Ubiquitination | FKNDISFWKKKKSMI HHCCHHHHHHHHHHC | 12.55 | 22817900 | |
| 313 | Ubiquitination | KNDISFWKKKKSMIG HCCHHHHHHHHHHCC | 53.34 | 22817900 | |
| 314 | Ubiquitination | NDISFWKKKKSMIGM CCHHHHHHHHHHCCC | 56.90 | 22817900 | |
| 315 | Ubiquitination | DISFWKKKKSMIGMS CHHHHHHHHHHCCCC | 46.48 | 22817900 | |
| 316 (in isoform 1) | Ubiquitination | - | 54.88 | 21890473 | |
| 316 | Ubiquitination | ISFWKKKKSMIGMST HHHHHHHHHHCCCCH | 54.88 | 22817900 | |
| 316 (in isoform 2) | Ubiquitination | - | 54.88 | 21890473 | |
| 323 | Ubiquitination | KSMIGMSTKAVLWRC HHHCCCCHHHHHHHH | 17.71 | 21963094 | |
| 324 | Ubiquitination | SMIGMSTKAVLWRCF HHCCCCHHHHHHHHH | 29.23 | 21963094 | |
| 387 | Phosphorylation | EFQFGTYSESERKTE HHCCCCCCHHHHCCH | 34.19 | - | |
| 389 | Phosphorylation | QFGTYSESERKTEEY CCCCCCHHHHCCHHH | 36.44 | - | |
| 392 | Ubiquitination | TYSESERKTEEYDTQ CCCHHHHCCHHHHHH | 57.12 | - | |
| 396 | Phosphorylation | SERKTEEYDTQAMKY HHHCCHHHHHHHHHH | 20.32 | - | |
| 403 | Phosphorylation | YDTQAMKYLSYLLYP HHHHHHHHHHHHHHH | 6.44 | - | |
| 406 | Phosphorylation | QAMKYLSYLLYPLCV HHHHHHHHHHHHHHH | 9.72 | - | |
| 423 (in isoform 2) | Ubiquitination | - | 5.35 | 21890473 | |
| 431 (in isoform 2) | Ubiquitination | - | 5.88 | 21890473 | |
| 456 | Ubiquitination | LPQLFVNYKLKSVAH HHHHHHHCCCCCCCC | 16.64 | 22817900 | |
| 457 | Ubiquitination | PQLFVNYKLKSVAHL HHHHHHCCCCCCCCC | 44.21 | 22817900 | |
| 458 | Ubiquitination | QLFVNYKLKSVAHLP HHHHHCCCCCCCCCC | 3.36 | 21890473 | |
| 459 (in isoform 1) | Ubiquitination | - | 38.44 | 21890473 | |
| 459 | 2-Hydroxyisobutyrylation | LFVNYKLKSVAHLPW HHHHCCCCCCCCCCH | 38.44 | - | |
| 459 | Ubiquitination | LFVNYKLKSVAHLPW HHHHCCCCCCCCCCH | 38.44 | 21963094 | |
| 466 | Ubiquitination | KSVAHLPWKAFTYKA CCCCCCCHHHHHHHH | 15.80 | 21890473 | |
| 467 | Ubiquitination | SVAHLPWKAFTYKAF CCCCCCHHHHHHHHH | 31.51 | 23000965 | |
| 467 (in isoform 1) | Ubiquitination | - | 31.51 | 21890473 | |
| 471 | Ubiquitination | LPWKAFTYKAFNTFI CCHHHHHHHHHHHHH | 8.21 | 23000965 | |
| 472 | Ubiquitination | PWKAFTYKAFNTFID CHHHHHHHHHHHHHH | 43.36 | 23000965 | |
| 481 (in isoform 2) | Ubiquitination | - | 3.10 | 21890473 | |
| 488 | Sulfoxidation | VFAFIITMPTSHRLA HHHHHCCCCCCCCCH | 2.10 | 28183972 | |
| 494 (in isoform 2) | Ubiquitination | - | 3.99 | 21890473 | |
| 516 | Ubiquitination | QRWLYPVDKRRVNEF HHHHCCCCHHHHHHH | 33.95 | 21963094 | |
| 517 (in isoform 1) | Ubiquitination | - | 42.19 | 21890473 | |
| 517 | Ubiquitination | RWLYPVDKRRVNEFG HHHCCCCHHHHHHHH | 42.19 | 21906983 | |
| 526 | Phosphorylation | RVNEFGESYEEKATR HHHHHHHHHHHHHCC | 37.92 | 25159151 | |
| 527 | Phosphorylation | VNEFGESYEEKATRA HHHHHHHHHHHHCCC | 24.65 | 23663014 | |
| 529 | Ubiquitination | EFGESYEEKATRAPH HHHHHHHHHHCCCCC | 39.49 | 27667366 | |
| 530 (in isoform 1) | Ubiquitination | - | 43.02 | 21890473 | |
| 530 | Ubiquitination | FGESYEEKATRAPHT HHHHHHHHHCCCCCC | 43.02 | 27667366 | |
| 530 | 2-Hydroxyisobutyrylation | FGESYEEKATRAPHT HHHHHHHHHCCCCCC | 43.02 | - | |
| 532 | Phosphorylation | ESYEEKATRAPHTD- HHHHHHHCCCCCCC- | 38.13 | 23312004 |
| 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 CLP1L_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CLP1L_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 CLP1L_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SPTN1_HUMAN | SPTAN1 | physical | 22939629 | |
| RM47_HUMAN | MRPL47 | physical | 22939629 | |
| QCR8_HUMAN | UQCRQ | physical | 22939629 | |
| GLPK_HUMAN | GK | physical | 21988832 |
| 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 |
| "Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-229, AND MASSSPECTROMETRY. | |