BCL10_HUMAN - dbPTM
BCL10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCL10_HUMAN
UniProt AC O95999
Protein Name B-cell lymphoma/leukemia 10
Gene Name BCL10
Organism Homo sapiens (Human).
Sequence Length 233
Subcellular Localization Cytoplasm, perinuclear region . Membrane raft . Appears to have a perinuclear, compact and filamentous pattern of expression. Also found in the nucleus of several types of tumor cells. Colocalized with DPP4 in membrane rafts.
Protein Description Involved in adaptive immune response. [PubMed: 25365219 Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK. May be an adapter protein between upstream TNFR1-TRADD-RIP complex and the downstream NIK-IKK-IKAP complex. Is a substrate for MALT1]
Protein Sequence MEPTAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLDTLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFPDGATNNLSRSNSDESNFSEKLRASTVMYHPEGESSTTPFFSTNSSLNLPVLEVGRTENTIFSSTTLPRPGDPGAPPLPPDLQLEEEGTCANSSEMFLPLRSRTVSRQ
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
1Acetylation-------MEPTAPSL
-------CCCCCCCC
14.5419413330
4Phosphorylation----MEPTAPSLTEE
----CCCCCCCCCHH
37.5823663014
7Phosphorylation-MEPTAPSLTEEDLT
-CCCCCCCCCHHHHH
45.5223663014
9PhosphorylationEPTAPSLTEEDLTEV
CCCCCCCCHHHHHHH
41.4823663014
14PhosphorylationSLTEEDLTEVKKDAL
CCCHHHHHHHHHHHH
51.5623663014
17UbiquitinationEEDLTEVKKDALENL
HHHHHHHHHHHHHHH
38.41-
18UbiquitinationEDLTEVKKDALENLR
HHHHHHHHHHHHHHH
54.10-
29S-palmitoylationENLRVYLCEKIIAER
HHHHHHHHHHHHHHH
2.4729575903
31UbiquitinationLRVYLCEKIIAERHF
HHHHHHHHHHHHHHH
38.1118287044
52PhosphorylationKILSREDTEEISCRT
HHCCCCCCCCCCCCH
30.6627273156
59PhosphorylationTEEISCRTSSRKRAG
CCCCCCCHHHHHHHH
35.0725627689
63UbiquitinationSCRTSSRKRAGKLLD
CCCHHHHHHHHHHHH
48.851828704
67AcetylationSSRKRAGKLLDYLQE
HHHHHHHHHHHHHHH
44.9125953088
67UbiquitinationSSRKRAGKLLDYLQE
HHHHHHHHHHHHHHH
44.91-
77UbiquitinationDYLQENPKGLDTLVE
HHHHHCCCCHHHHHH
81.39-
81PhosphorylationENPKGLDTLVESIRR
HCCCCHHHHHHHHHH
37.4321406692
85PhosphorylationGLDTLVESIRREKTQ
CHHHHHHHHHHHHHH
17.5721406692
90UbiquitinationVESIRREKTQNFLIQ
HHHHHHHHHHCHHHH
54.31-
98UbiquitinationTQNFLIQKITDEVLK
HHCHHHHHHHHHHHH
40.35-
100PhosphorylationNFLIQKITDEVLKLR
CHHHHHHHHHHHHHC
32.89-
105UbiquitinationKITDEVLKLRNIKLE
HHHHHHHHHCCCCHH
51.05-
110UbiquitinationVLKLRNIKLEHLKGL
HHHHCCCCHHHCCCC
51.91-
115UbiquitinationNIKLEHLKGLKCSSC
CCCHHHCCCCCCCCC
65.19-
118UbiquitinationLEHLKGLKCSSCEPF
HHHCCCCCCCCCCCC
40.51-
120PhosphorylationHLKGLKCSSCEPFPD
HCCCCCCCCCCCCCC
36.1129255136
121PhosphorylationLKGLKCSSCEPFPDG
CCCCCCCCCCCCCCC
31.7829255136
130PhosphorylationEPFPDGATNNLSRSN
CCCCCCCCCCCCCCC
30.1229255136
134PhosphorylationDGATNNLSRSNSDES
CCCCCCCCCCCCCCC
35.4729255136
136PhosphorylationATNNLSRSNSDESNF
CCCCCCCCCCCCCCH
36.9925159151
138PhosphorylationNNLSRSNSDESNFSE
CCCCCCCCCCCCHHH
43.9623927012
141PhosphorylationSRSNSDESNFSEKLR
CCCCCCCCCHHHHHH
48.4423927012
144PhosphorylationNSDESNFSEKLRAST
CCCCCCHHHHHHHHE
37.7628450419
146UbiquitinationDESNFSEKLRASTVM
CCCCHHHHHHHHEEE
41.91-
163PhosphorylationPEGESSTTPFFSTNS
CCCCCCCCCCEECCC
21.75-
167PhosphorylationSSTTPFFSTNSSLNL
CCCCCCEECCCCCCC
27.3628348404
168PhosphorylationSTTPFFSTNSSLNLP
CCCCCEECCCCCCCC
33.6822468782
170PhosphorylationTPFFSTNSSLNLPVL
CCCEECCCCCCCCEE
35.9717371994
171PhosphorylationPFFSTNSSLNLPVLE
CCEECCCCCCCCEEE
24.2817371994
218PhosphorylationEEGTCANSSEMFLPL
CCCCCCCCCCCEEEE
14.7820466000
227PhosphorylationEMFLPLRSRTVSRQ-
CCEEEECCCCCCCC-
39.73-
229PhosphorylationFLPLRSRTVSRQ---
EEEECCCCCCCC---
24.87-
231PhosphorylationPLRSRTVSRQ-----
EECCCCCCCC-----
25.0916280327

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
134SPhosphorylationKinaseIKBKBO14920
GPS
136SPhosphorylationKinaseIKBKBO14920
GPS
138SPhosphorylationKinaseIKBKBO14920
GPS
138SPhosphorylationKinaseCAMK2BQ13554
GPS
141SPhosphorylationKinaseIKBKBO14920
GPS
144SPhosphorylationKinaseIKBKBO14920
GPS
218SPhosphorylationKinaseAKT1P31749
PSP
231SPhosphorylationKinaseAKT1P31749
PSP
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseBIRC3Q13489
PMID:16775419
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:15082780
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:15082780

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCL10_HUMAN !!

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 BCL10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KT33B_HUMANKRT33Bphysical
17353931
MALT1_HUMANMALT1physical
11090634
TRADD_HUMANTRADDphysical
10400625
CAR10_HUMANCARD10physical
11259443
CARD9_HUMANCARD9physical
11053425
CAR11_HUMANCARD11physical
11278692
CAR14_HUMANCARD14physical
11278692
TRAF2_HUMANTRAF2physical
10753917
BCL10_HUMANBCL10physical
16775419
IKBA_HUMANNFKBIAphysical
20551178
MALT1_HUMANMALT1physical
20551178
MIB2_MOUSEMib2physical
21896478
BCL10_HUMANBCL10physical
21896478
MALT1_MOUSEMalt1physical
21896478
MIB2_HUMANMIB2physical
21896478
CAR11_HUMANCARD11physical
19815501
MALT1_HUMANMALT1physical
19444310
CAR11_HUMANCARD11physical
19444310
KCC2G_HUMANCAMK2Gphysical
21513986
CAR11_HUMANCARD11physical
21513986
IKKB_HUMANIKBKBphysical
17213322
FBW1A_HUMANBTRCphysical
17213322
MALT1_HUMANMALT1physical
11262391
IKKA_HUMANCHUKphysical
11113112
IKKB_HUMANIKBKBphysical
11113112
NEMO_HUMANIKBKGphysical
11113112
TRAF2_HUMANTRAF2physical
11466612
BIRC3_HUMANBIRC3physical
11466612
CAR11_HUMANCARD11physical
18625728
MK09_HUMANMAPK9physical
17189706
MALT1_HUMANMALT1physical
17948050
AKT1_HUMANAKT1physical
16280327
BCL3_HUMANBCL3physical
16280327
USP9X_HUMANUSP9Xphysical
23690623
NEMO_HUMANIKBKGphysical
23690623
MALT1_HUMANMALT1physical
23690623
CAR11_HUMANCARD11physical
23690623
I15RA_HUMANIL15RAphysical
21988832
CDK9_HUMANCDK9physical
21988832
SRSF1_HUMANSRSF1physical
21988832
S20A1_HUMANSLC20A1physical
21988832
NHRF1_HUMANSLC9A3R1physical
21988832
TMG4_HUMANPRRG4physical
21988832
USBP1_HUMANUSHBP1physical
21988832
MALT1_HUMANMALT1physical
24130731
BIRC3_HUMANBIRC3physical
16395405
MALT1_HUMANMALT1physical
14695475
UB2V2_HUMANUBE2V2physical
14695475
NEMO_HUMANIKBKGphysical
14695475
IKKA_HUMANCHUKphysical
14695475
IKKB_HUMANIKBKBphysical
14695475
UBE2N_HUMANUBE2Nphysical
14695475
BCL10_HUMANBCL10physical
25416956
CAR11_HUMANCARD11physical
25548215
MALT1_HUMANMALT1physical
25548215
BCL10_HUMANBCL10physical
24074955
CAR11_HUMANCARD11physical
21157432
2AAA_HUMANPPP2R1Aphysical
21157432
MALT1_HUMANMALT1physical
21157432
PP2AA_HUMANPPP2CAphysical
21157432
SQSTM_HUMANSQSTM1physical
22658522
MALT1_HUMANMALT1physical
22658522
ATG5_HUMANATG5physical
22658522
MLP3A_HUMANMAP1LC3Aphysical
22658522
RNF31_HUMANRNF31physical
27777308
CAR11_HUMANCARD11physical
27777308
MALT1_HUMANMALT1physical
27777308
MALT1_HUMANMALT1physical
22528498
MALT1_HUMANMALT1physical
19118383
CAR11_HUMANCARD11physical
19118383
IKKB_HUMANIKBKBphysical
19118383
CAR14_HUMANCARD14physical
27071417

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=A chromosomal aberration involving BCL10 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(1
14)(p22
q32). Although the BCL10/IgH translocation leaves the coding region of BCL10 intact, frequent BCL10 mutations could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions.
616098
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BCL10_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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