ABRX2_MOUSE - dbPTM
ABRX2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABRX2_MOUSE
UniProt AC Q3TCJ1
Protein Name BRISC complex subunit Abraxas 2 {ECO:0000312|MGI:MGI:1926116}
Gene Name Abraxas2 {ECO:0000312|MGI:MGI:1926116}
Organism Mus musculus (Mouse).
Sequence Length 415
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton . A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minu
Protein Description Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (By similarity). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins. [PubMed: 21195082 Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activities by enhancing its stability and cell surface expression]
Protein Sequence MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSISDSQISNTEFLQVIEIHNHQPCSQLFSFYDYASKVNEESLDRILKDRRKKVIGWYRFRRNTQQQMSYREQVIHKQLTRILGVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISLAIPNLGNTSQQEYKVSSVPNTSQSYAKVIKEHGTDFFDKDGVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAEVNKLRRQITQKKNEKEQERRLQQALLSRQMPSESLEPAFSPRMSYSGFSAEGRSTLAETEPSDPPPPYSDFHPNNQESTLSHSRMERSVFMPRPQAVGSSSYASTSGGLKFTGSGADLLPSQSAAGDSGEESDDSDYENLIDPAESPHSEYSHSKNSRPSTHPDEDPRNTQTSQI
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
187UbiquitinationNTSQSYAKVIKEHGT
CCCHHHHHHHHHHCC
22790023
210PhosphorylationMKDIRAIYQVYNALQ
HHHHHHHHHHHHHHH
22817900
229AcetylationAVCADVEKSERVVES
HHHCCCHHHHHHHHH
22826441
229UbiquitinationAVCADVEKSERVVES
HHHCCCHHHHHHHHH
22790023
237S-nitrosocysteineSERVVESCQAEVNKL
HHHHHHHHHHHHHHH
-
272PhosphorylationLLSRQMPSESLEPAF
HHHCCCCCCCCCCCC
25777480
274PhosphorylationSRQMPSESLEPAFSP
HCCCCCCCCCCCCCC
25777480
280PhosphorylationESLEPAFSPRMSYSG
CCCCCCCCCCCCCCC
26824392
284PhosphorylationPAFSPRMSYSGFSAE
CCCCCCCCCCCCCCC
22942356
285PhosphorylationAFSPRMSYSGFSAEG
CCCCCCCCCCCCCCC
28833060
286PhosphorylationFSPRMSYSGFSAEGR
CCCCCCCCCCCCCCC
28833060
289PhosphorylationRMSYSGFSAEGRSTL
CCCCCCCCCCCCCCC
28833060
339PhosphorylationPRPQAVGSSSYASTS
CCCCCCCCCCCEECC
29472430
340PhosphorylationRPQAVGSSSYASTSG
CCCCCCCCCCEECCC
29472430
341PhosphorylationPQAVGSSSYASTSGG
CCCCCCCCCEECCCC
30352176
342PhosphorylationQAVGSSSYASTSGGL
CCCCCCCCEECCCCC
22817900
344PhosphorylationVGSSSYASTSGGLKF
CCCCCCEECCCCCEE
29472430
345PhosphorylationGSSSYASTSGGLKFT
CCCCCEECCCCCEEE
29472430
346PhosphorylationSSSYASTSGGLKFTG
CCCCEECCCCCEEEC
29472430
352PhosphorylationTSGGLKFTGSGADLL
CCCCCEEECCCCCCC
25293948
354PhosphorylationGGLKFTGSGADLLPS
CCCEEECCCCCCCCC
25293948
361PhosphorylationSGADLLPSQSAAGDS
CCCCCCCCCCCCCCC
25367039
363PhosphorylationADLLPSQSAAGDSGE
CCCCCCCCCCCCCCC
21659605
368PhosphorylationSQSAAGDSGEESDDS
CCCCCCCCCCCCCCC
21659605
372PhosphorylationAGDSGEESDDSDYEN
CCCCCCCCCCCCHHC
22817900
375PhosphorylationSGEESDDSDYENLID
CCCCCCCCCHHCCCC
21659605
377PhosphorylationEESDDSDYENLIDPA
CCCCCCCHHCCCCCC
22817900
386PhosphorylationNLIDPAESPHSEYSH
CCCCCCCCCCCCCCC
25293948
389PhosphorylationDPAESPHSEYSHSKN
CCCCCCCCCCCCCCC
25293948
391PhosphorylationAESPHSEYSHSKNSR
CCCCCCCCCCCCCCC
25293948
392PhosphorylationESPHSEYSHSKNSRP
CCCCCCCCCCCCCCC
25293948
394PhosphorylationPHSEYSHSKNSRPST
CCCCCCCCCCCCCCC
25293948
400PhosphorylationHSKNSRPSTHPDEDP
CCCCCCCCCCCCCCC
23375375

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 ABRX2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABRX2_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 ABRX2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATF4_MOUSEAtf4physical
22974638
JUND_MOUSEJundphysical
22974638
BRCC3_MOUSEBrcc3physical
22974638
ATF5_MOUSEAtf5physical
22974638
UBC_MOUSEUbcphysical
22974638

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABRX2_MOUSE

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Related Literatures of Post-Translational Modification

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