| UniProt ID | BMI1_HUMAN | |
|---|---|---|
| UniProt AC | P35226 | |
| Protein Name | Polycomb complex protein BMI-1 | |
| Gene Name | BMI1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 326 | |
| Subcellular Localization | Nucleus . Cytoplasm . | |
| Protein Description | Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. [PubMed: 15386022] | |
| Protein Sequence | MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEDKRIITDDEIISLSIEFFDQNRLDRKVNKDKEKSKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSGNHQSSFANRPRKSSVNGSSATSSG | |
| 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 |
|---|---|---|---|---|---|
| 51 | Acetylation | VRYLETSKYCPICDV HHHHHHCCCCCCCCE | 59.29 | 26051181 | |
| 51 | Ubiquitination | VRYLETSKYCPICDV HHHHHHCCCCCCCCE | 59.29 | 32015554 | |
| 62 | Ubiquitination | ICDVQVHKTRPLLNI CCCEEEEECCCCCCC | 47.58 | PubMed | |
| 73 | Ubiquitination | LLNIRSDKTLQDIVY CCCCCCCCCHHHHHH | 53.00 | 21890473 | |
| 81 | Ubiquitination | TLQDIVYKLVPGLFK CHHHHHHHHCCCCCH | 31.92 | 33845483 | |
| 88 | Sumoylation | KLVPGLFKNEMKRRR HHCCCCCHHHHHHHH | 57.97 | - | |
| 88 | Ubiquitination | KLVPGLFKNEMKRRR HHCCCCCHHHHHHHH | 57.97 | 32015554 | |
| 88 | Sumoylation | KLVPGLFKNEMKRRR HHCCCCCHHHHHHHH | 57.97 | - | |
| 103 | Phosphorylation | DFYAAHPSADAANGS CHHHHCCCCCCCCCC | 28.99 | 27732954 | |
| 110 | Phosphorylation | SADAANGSNEDRGEV CCCCCCCCCCCCCCC | 36.53 | 30624053 | |
| 114 | Methylation | ANGSNEDRGEVADED CCCCCCCCCCCCCCC | 36.67 | - | |
| 122 | Ubiquitination | GEVADEDKRIITDDE CCCCCCCCCCCCCHH | 43.37 | 24816145 | |
| 151 | Acetylation | DRKVNKDKEKSKEEV HHCCCCCHHHCHHHH | 69.52 | 7987715 | |
| 153 | Ubiquitination | KVNKDKEKSKEEVND CCCCCHHHCHHHHCC | 72.99 | 24816145 | |
| 203 | Phosphorylation | EEEPLKDYYTLMDIA ECCCCCCCEEHHHHH | 9.21 | 26657352 | |
| 204 | Phosphorylation | EEPLKDYYTLMDIAY CCCCCCCEEHHHHHH | 11.97 | - | |
| 216 | Ubiquitination | IAYIYTWRRNGPLPL HHHHHHCCCCCCCCC | 17.87 | - | |
| 224 | Ubiquitination | RNGPLPLKYRVRPTC CCCCCCCEEEECCCC | 29.13 | - | |
| 224 | Acetylation | RNGPLPLKYRVRPTC CCCCCCCEEEECCCC | 29.13 | 26051181 | |
| 231 | Sumoylation | KYRVRPTCKRMKISH EEEECCCCCCCCCCC | 2.66 | - | |
| 244 | Phosphorylation | SHQRDGLTNAGELES CCCCCCCCCCHHCCC | 28.66 | 23403867 | |
| 251 | Phosphorylation | TNAGELESDSGSDKA CCCHHCCCCCCCCCC | 50.10 | 30266825 | |
| 253 | Phosphorylation | AGELESDSGSDKANS CHHCCCCCCCCCCCC | 49.85 | 30266825 | |
| 255 | Phosphorylation | ELESDSGSDKANSPA HCCCCCCCCCCCCCC | 39.63 | 29255136 | |
| 255 | O-linked_Glycosylation | ELESDSGSDKANSPA HCCCCCCCCCCCCCC | 39.63 | 29485866 | |
| 257 | Methylation | ESDSGSDKANSPAGG CCCCCCCCCCCCCCC | 51.68 | - | |
| 260 | Phosphorylation | SGSDKANSPAGGIPS CCCCCCCCCCCCCCC | 22.46 | - | |
| 269 | Phosphorylation | AGGIPSTSSCLPSPS CCCCCCCCCCCCCCC | 24.32 | - | |
| 274 | Phosphorylation | STSSCLPSPSTPVQS CCCCCCCCCCCCCCC | 20.66 | - | |
| 276 | Phosphorylation | SSCLPSPSTPVQSPH CCCCCCCCCCCCCCC | 50.08 | - | |
| 277 | Phosphorylation | SCLPSPSTPVQSPHP CCCCCCCCCCCCCCC | 30.75 | - | |
| 281 | Phosphorylation | SPSTPVQSPHPQFPH CCCCCCCCCCCCCCC | 25.96 | - | |
| 290 | Phosphorylation | HPQFPHISSTMNGTS CCCCCCCCCCCCCCC | 19.40 | - | |
| 315 | Phosphorylation | FANRPRKSSVNGSSA CCCCCCCCCCCCCCC | 40.58 | 26329039 | |
| 316 | Phosphorylation | ANRPRKSSVNGSSAT CCCCCCCCCCCCCCC | 23.72 | 26329039 | |
| 320 | Phosphorylation | RKSSVNGSSATSSG- CCCCCCCCCCCCCC- | 16.17 | 28857561 | |
| 321 | Phosphorylation | KSSVNGSSATSSG-- CCCCCCCCCCCCC-- | 36.64 | 26329039 | |
| 323 | Phosphorylation | SVNGSSATSSG---- CCCCCCCCCCC---- | 25.93 | 26329039 | |
| 324 | Phosphorylation | VNGSSATSSG----- CCCCCCCCCC----- | 32.55 | 26329039 | |
| 325 | Phosphorylation | NGSSATSSG------ CCCCCCCCC------ | 44.14 | 26329039 | |
| 367 | Ubiquitination | ------------------------------------------------ ------------------------------------------------ | - | ||
| 387 | Phosphorylation | -------------------------------------------------------------------- -------------------------------------------------------------------- | - | ||
| 394 | Phosphorylation | --------------------------------------------------------------------------- --------------------------------------------------------------------------- | 27251275 | ||
| 396 | Phosphorylation | ----------------------------------------------------------------------------- ----------------------------------------------------------------------------- | 27251275 | ||
| 398 | Phosphorylation | ------------------------------------------------------------------------------- ------------------------------------------------------------------------------- | 27251275 | ||
| 458 | Phosphorylation | ------------------------------------------------------------------------------------------------------------------------------------------- ------------------------------------------------------------------------------------------------------------------------------------------- | - | ||
| 459 | Phosphorylation | -------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------- | 24719451 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 110 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 316 | S | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | BTRC | Q9Y297 | PMID:24658274 |
| - | K | Ubiquitination | E3 ubiquitin ligase | SPOP | O43791 | PMID:15897469 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BMI1_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 BMI1_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| 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. | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-253 ANDSER-255, AND MASS SPECTROMETRY. | |