BMI1_MOUSE - dbPTM
BMI1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BMI1_MOUSE
UniProt AC P25916
Protein Name Polycomb complex protein BMI-1
Gene Name Bmi1
Organism Mus musculus (Mouse).
Sequence Length 324
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. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2 (By similarity)..
Protein Sequence MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEEKRIITDDEIISLSIEFFDQSRLDRKVNKEKPKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKMSHQRDGLTNAGELESDSGSDKANSPAGGVPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSANHQSSFASRPRKSSLNGSSATSSG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
110PhosphorylationSADAANGSNEDRGEV
CCCCCCCCCCCCCCC		36.5325338131
161PhosphorylationEEVNDKRYLRCPAAM
HHHCCCCHHCCHHHH		12.3019367708
249PhosphorylationTNAGELESDSGSDKA
CCCHHCCCCCCCCCC		50.1025521595
251PhosphorylationAGELESDSGSDKANS
CHHCCCCCCCCCCCC		49.8522324799
253PhosphorylationELESDSGSDKANSPA
HCCCCCCCCCCCCCC		39.6325521595
313PhosphorylationFASRPRKSSLNGSSA
CCCCCCCHHCCCCCC		41.1425266776
314PhosphorylationASRPRKSSLNGSSAT
CCCCCCHHCCCCCCC		28.9630352176
318PhosphorylationRKSSLNGSSATSSG-
CCHHCCCCCCCCCC-		18.7423984901
319PhosphorylationKSSLNGSSATSSG--
CHHCCCCCCCCCC--		36.6423984901
321PhosphorylationSLNGSSATSSG----
HCCCCCCCCCC----		25.9327717184
322PhosphorylationLNGSSATSSG-----
CCCCCCCCCC-----		32.5527717184
323PhosphorylationNGSSATSSG------
CCCCCCCCC------		44.1427717184
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseSpopQ6ZWS8
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BMI1_MOUSE !!
Disease-associated PTM Sites based on SAP

* 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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHC1_HUMANPHC1physical
12167701
RING1_HUMANRING1physical
12167701
CBX4_HUMANCBX4physical
12167701
CBX8_HUMANCBX8physical
12167701
PHC3_HUMANPHC3physical
12167701
SMCA5_HUMANSMARCA5physical
12167701
SCMH1_HUMANSCMH1physical
12167701
HSP74_HUMANHSPA4physical
12167701
PHC2_HUMANPHC2physical
12167701
DMAP1_MOUSEDmap1physical
17214966
CBX2_MOUSECbx2physical
9571155
PHC1_MOUSEPhc1physical
9571155
NRAM1_MOUSESlc11a1physical
17726103
CDN2A_MOUSECdkn2agenetic
22351929
ARF_MOUSECdkn2agenetic
22351929
RING2_MOUSERnf2physical
9627119
GATA6_MOUSEGata6physical
22713603
PHC2_MOUSEPhc2physical
19369945
RING1_HUMANRING1physical
12589020
RING2_HUMANRNF2physical
12589020
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BMI1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; SER-251 ANDSER-253, AND MASS SPECTROMETRY.

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