BRCC3_HUMAN - dbPTM
BRCC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRCC3_HUMAN
UniProt AC P46736
Protein Name Lys-63-specific deubiquitinase BRCC36
Gene Name BRCC3
Organism Homo sapiens (Human).
Sequence Length 316
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, cytoskeleton, spindle pole . Localizes at sites of DNA damage at double-strand breaks (DSBs) (PubMed:20656690, PubMed:26344097). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm (PubMed:20656690).
Protein Description Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. [PubMed: 19214193]
Protein Sequence MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDTRSDSKFAYTGTEMRTVAEKVDAVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSESLHGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLQELQQEKEELMQELSSLE
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
2Acetylation------MAVQVVQAV
------CHHHHHHHH
10.64-
28PhosphorylationVCLNHALSTEKEEVM
HHHHHHCCCCCHHHH
34.9920068231
51UbiquitinationDDTRSDSKFAYTGTE
CCCCCCCCCCCCCCH
38.7227667366
51 (in isoform 5)Ubiquitination-38.7221890473
51 (in isoform 1)Ubiquitination-38.7221890473
51 (in isoform 2)Ubiquitination-38.7221890473
52 (in isoform 3)Ubiquitination-7.9121890473
52UbiquitinationDTRSDSKFAYTGTEM
CCCCCCCCCCCCCHH
7.9123000965
54PhosphorylationRSDSKFAYTGTEMRT
CCCCCCCCCCCHHHH
14.6121945579
55PhosphorylationSDSKFAYTGTEMRTV
CCCCCCCCCCHHHHH
33.9121945579
55 (in isoform 3)Phosphorylation-33.9125627689
61PhosphorylationYTGTEMRTVAEKVDA
CCCCHHHHHHHHCCE
23.8220068231
65 (in isoform 5)Ubiquitination-35.3621890473
65 (in isoform 1)Ubiquitination-35.3621890473
65 (in isoform 2)Ubiquitination-35.3621890473
65UbiquitinationEMRTVAEKVDAVRIV
HHHHHHHHCCEEEEE
35.3621906983
66 (in isoform 3)Ubiquitination-4.2621890473
66UbiquitinationMRTVAEKVDAVRIVH
HHHHHHHCCEEEEEE
4.2627667366
142PhosphorylationDVRTQAMYQMMDQGF
HHHHHHHHHHHHCCC
9.0324043423
155PhosphorylationGFVGLIFSCFIEDKN
CCHHEEEEEEEECCC
10.9224043423
156 (in isoform 4)Ubiquitination-2.5121890473
180UbiquitinationFQSIQAQKSSESLHG
HHHHHHHHCCCCCCC
59.9923000965
180 (in isoform 1)Ubiquitination-59.9921890473
180 (in isoform 2)Ubiquitination-59.9921890473
181UbiquitinationQSIQAQKSSESLHGP
HHHHHHHCCCCCCCC
27.5323000965
181 (in isoform 3)Ubiquitination-27.5321890473
199PhosphorylationWSSSQHISIEGQKEE
CCCCCCEEECCCCHH
16.6827251275
201UbiquitinationSSQHISIEGQKEEER
CCCCEEECCCCHHHH
49.1021963094
202UbiquitinationSQHISIEGQKEEERY
CCCEEECCCCHHHHH
42.0421963094
204UbiquitinationHISIEGQKEEERYER
CEEECCCCHHHHHHH
77.33-
212UbiquitinationEEERYERIEIPIHIV
HHHHHHHEECCEEEC
3.6329967540
213UbiquitinationEERYERIEIPIHIVP
HHHHHHEECCEEECC
49.2729967540
223PhosphorylationIHIVPHVTIGKVCLE
EEECCCCCCCHHHHH
22.4520068231
226UbiquitinationVPHVTIGKVCLESAV
CCCCCCCHHHHHHHH
26.4021963094
227UbiquitinationPHVTIGKVCLESAVE
CCCCCCHHHHHHHHH
3.6721963094
231PhosphorylationIGKVCLESAVELPKI
CCHHHHHHHHHHCHH
25.3520068231
236UbiquitinationLESAVELPKILCQEE
HHHHHHHCHHHCHHH
14.2421963094
237UbiquitinationESAVELPKILCQEEQ
HHHHHHCHHHCHHHH
62.0221963094
247PhosphorylationCQEEQDAYRRIHSLT
CHHHHHHHHHHHHHH
14.55-
252PhosphorylationDAYRRIHSLTHLDSV
HHHHHHHHHHCHHHC
32.3723312004
254PhosphorylationYRRIHSLTHLDSVTK
HHHHHHHHCHHHCEE
24.3323312004
258PhosphorylationHSLTHLDSVTKIHNG
HHHHCHHHCEEEECC
37.7417525341
260PhosphorylationLTHLDSVTKIHNGSV
HHCHHHCEEEECCCE
28.3825627689
261UbiquitinationTHLDSVTKIHNGSVF
HCHHHCEEEECCCEE
39.5521963094
262UbiquitinationHLDSVTKIHNGSVFT
CHHHCEEEECCCEEC
1.9221963094
280UbiquitinationCSQMSAVSGPLLQWL
HHHHHHHHHHHHHHH
34.1221963094
281UbiquitinationSQMSAVSGPLLQWLE
HHHHHHHHHHHHHHH
15.4121963094
305AcetylationLQELQQEKEELMQEL
HHHHHHHHHHHHHHH
52.7526051181
305UbiquitinationLQELQQEKEELMQEL
HHHHHHHHHHHHHHH
52.7521963094
306UbiquitinationQELQQEKEELMQELS
HHHHHHHHHHHHHHH
56.4621963094
313PhosphorylationEELMQELSSLE----
HHHHHHHHCCC----
31.9329514088
314PhosphorylationELMQELSSLE-----
HHHHHHHCCC-----
49.4929514088

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

Oops, there are no upstream regulatory protein records of BRCC3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRCC3_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 BRCC3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BARD1_HUMANBARD1physical
14636569
BRCA1_HUMANBRCA1physical
14636569
BABA2_HUMANBREphysical
14636569
RAD51_HUMANRAD51physical
14636569
P53_HUMANTP53physical
14636569
UB2D1_HUMANUBE2D1physical
14636569
ATPO_HUMANATP5Ophysical
19615732
OST48_HUMANDDOSTphysical
19615732
E2F5_HUMANE2F5physical
19615732
MCM2_HUMANMCM2physical
19615732
NDUAA_HUMANNDUFA10physical
19615732
GLYM_HUMANSHMT2physical
19615732
BABA2_HUMANBREphysical
19615732
SP16H_HUMANSUPT16Hphysical
19615732
ABRX2_HUMANFAM175Bphysical
19615732
BABA1_HUMANBABAM1physical
19615732
UIMC1_HUMANUIMC1physical
19615732
CAND1_HUMANCAND1physical
19615732
ABRX1_HUMANFAM175Aphysical
19615732
EXOC8_HUMANEXOC8physical
19615732
UIMC1_HUMANUIMC1physical
18077395
ABRX1_HUMANFAM175Aphysical
18077395
BRCA1_HUMANBRCA1physical
17664283
BRCA2_HUMANBRCA2physical
17664283
BARD1_HUMANBARD1physical
17664283
BACH1_HUMANBACH1physical
17664283
BABA1_HUMANBABAM1physical
19261749
BABA2_HUMANBREphysical
19261749
ABRX1_HUMANFAM175Aphysical
19261749
ABRX2_HUMANFAM175Bphysical
20032457
BABA2_HUMANBREphysical
20032457
BABA1_HUMANBABAM1physical
20032457
UIMC1_HUMANUIMC1physical
21282113
ABRX1_HUMANFAM175Aphysical
21282113
ABRX2_HUMANFAM175Bphysical
21282113
BABA2_HUMANBREphysical
21282113
BRCC3_HUMANBRCC3physical
21282113
BABA1_HUMANBABAM1physical
21282113
ABRX1_HUMANFAM175Aphysical
20656689
BABA2_HUMANBREphysical
20656689
UIMC1_HUMANUIMC1physical
20656689
UIMC1_HUMANUIMC1physical
19261748
BABA2_HUMANBREphysical
19261748
ABRX1_HUMANFAM175Aphysical
19261748
BABA1_HUMANBABAM1physical
19261748
ABRX2_HUMANFAM175Bphysical
22863883
JIP4_HUMANSPAG9physical
22863883
HUWE1_HUMANHUWE1physical
22863883
LARP7_HUMANLARP7physical
22863883
WDHD1_HUMANWDHD1physical
22863883
UBC_HUMANUBCphysical
19202061
UIMC1_HUMANUIMC1physical
19202061
FANCG_HUMANFANCGphysical
25132264
NUMA1_HUMANNUMA1physical
26195665
FANCA_HUMANFANCAphysical
28215707
INAR1_HUMANIFNAR1physical
24075985

Drug and Disease Associations
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.
Regulatory Network of BRCC3_HUMAN

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Related Literatures of Post-Translational Modification

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