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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
187 | Ubiquitination | NTSQSYAKVIKEHGT CCCHHHHHHHHHHCC | 22790023 | ||
210 | Phosphorylation | MKDIRAIYQVYNALQ HHHHHHHHHHHHHHH | 22817900 | ||
229 | Acetylation | AVCADVEKSERVVES HHHCCCHHHHHHHHH | 22826441 | ||
229 | Ubiquitination | AVCADVEKSERVVES HHHCCCHHHHHHHHH | 22790023 | ||
237 | S-nitrosocysteine | SERVVESCQAEVNKL HHHHHHHHHHHHHHH | - | ||
272 | Phosphorylation | LLSRQMPSESLEPAF HHHCCCCCCCCCCCC | 25777480 | ||
274 | Phosphorylation | SRQMPSESLEPAFSP HCCCCCCCCCCCCCC | 25777480 | ||
280 | Phosphorylation | ESLEPAFSPRMSYSG CCCCCCCCCCCCCCC | 26824392 | ||
284 | Phosphorylation | PAFSPRMSYSGFSAE CCCCCCCCCCCCCCC | 22942356 | ||
285 | Phosphorylation | AFSPRMSYSGFSAEG CCCCCCCCCCCCCCC | 28833060 | ||
286 | Phosphorylation | FSPRMSYSGFSAEGR CCCCCCCCCCCCCCC | 28833060 | ||
289 | Phosphorylation | RMSYSGFSAEGRSTL CCCCCCCCCCCCCCC | 28833060 | ||
339 | Phosphorylation | PRPQAVGSSSYASTS CCCCCCCCCCCEECC | 29472430 | ||
340 | Phosphorylation | RPQAVGSSSYASTSG CCCCCCCCCCEECCC | 29472430 | ||
341 | Phosphorylation | PQAVGSSSYASTSGG CCCCCCCCCEECCCC | 30352176 | ||
342 | Phosphorylation | QAVGSSSYASTSGGL CCCCCCCCEECCCCC | 22817900 | ||
344 | Phosphorylation | VGSSSYASTSGGLKF CCCCCCEECCCCCEE | 29472430 | ||
345 | Phosphorylation | GSSSYASTSGGLKFT CCCCCEECCCCCEEE | 29472430 | ||
346 | Phosphorylation | SSSYASTSGGLKFTG CCCCEECCCCCEEEC | 29472430 | ||
352 | Phosphorylation | TSGGLKFTGSGADLL CCCCCEEECCCCCCC | 25293948 | ||
354 | Phosphorylation | GGLKFTGSGADLLPS CCCEEECCCCCCCCC | 25293948 | ||
361 | Phosphorylation | SGADLLPSQSAAGDS CCCCCCCCCCCCCCC | 25367039 | ||
363 | Phosphorylation | ADLLPSQSAAGDSGE CCCCCCCCCCCCCCC | 21659605 | ||
368 | Phosphorylation | SQSAAGDSGEESDDS CCCCCCCCCCCCCCC | 21659605 | ||
372 | Phosphorylation | AGDSGEESDDSDYEN CCCCCCCCCCCCHHC | 22817900 | ||
375 | Phosphorylation | SGEESDDSDYENLID CCCCCCCCCHHCCCC | 21659605 | ||
377 | Phosphorylation | EESDDSDYENLIDPA CCCCCCCHHCCCCCC | 22817900 | ||
386 | Phosphorylation | NLIDPAESPHSEYSH CCCCCCCCCCCCCCC | 25293948 | ||
389 | Phosphorylation | DPAESPHSEYSHSKN CCCCCCCCCCCCCCC | 25293948 | ||
391 | Phosphorylation | AESPHSEYSHSKNSR CCCCCCCCCCCCCCC | 25293948 | ||
392 | Phosphorylation | ESPHSEYSHSKNSRP CCCCCCCCCCCCCCC | 25293948 | ||
394 | Phosphorylation | PHSEYSHSKNSRPST CCCCCCCCCCCCCCC | 25293948 | ||
400 | Phosphorylation | HSKNSRPSTHPDEDP CCCCCCCCCCCCCCC | 23375375 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ABRX2_MOUSE !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ATF4_MOUSE | Atf4 | physical | 22974638 | |
JUND_MOUSE | Jund | physical | 22974638 | |
BRCC3_MOUSE | Brcc3 | physical | 22974638 | |
ATF5_MOUSE | Atf5 | physical | 22974638 | |
UBC_MOUSE | Ubc | physical | 22974638 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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