ABRX2_HUMAN - dbPTM
ABRX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABRX2_HUMAN
UniProt AC Q15018
Protein Name BRISC complex subunit Abraxas 2 {ECO:0000312|HGNC:HGNC:28975}
Gene Name ABRAXAS2 {ECO:0000312|HGNC:HGNC:28975}
Organism Homo sapiens (Human).
Sequence Length 415
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton . A minor proportion is detected in the nucleus (PubMed:21282113, PubMed:22974638). Translocates into the nucleus in response to DNA damage (PubMed:25283148). Direc
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. [PubMed: 19214193]
Protein Sequence MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSISDSQISNTEFLQVIEIHNHQPCSKLFSFYDYASKVNEESLDRILKDRRKKVIGWYRFRRNTQQQMSYREQVLHKQLTRILGVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISLAIPNLGNTSQQEYKVSSVPNTSQSYAKVIKEHGTDFFDKDGVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAEVNKLRRQITQRKNEKEQERRLQQAVLSRQMPSESLDPAFSPRMPSSGFAAEGRSTLGDAEASDPPPPYSDFHPNNQESTLSHSRMERSVFMPRPQAVGSSNYASTSAGLKYPGSGADLPPPQRAAGDSGEDSDDSDYENLIDPTEPSNSEYSHSKDSRPMAHPDEDPRNTQTSQI
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
10UbiquitinationASISGYTFSAVCFHS
CCCCCEEEEEEEEEC
22817900
70UbiquitinationSKLFSFYDYASKVNE
HHHHHHHHHHHHCCH
21963094
74UbiquitinationSFYDYASKVNEESLD
HHHHHHHHCCHHHHH
21906983
79PhosphorylationASKVNEESLDRILKD
HHHCCHHHHHHHHHH
25159151
83UbiquitinationNEESLDRILKDRRKK
CHHHHHHHHHHHHHH
21890473
86UbiquitinationSLDRILKDRRKKVIG
HHHHHHHHHHHHHHH
22817900
95UbiquitinationRKKVIGWYRFRRNTQ
HHHHHHHHHCCCCCH
22817900
100UbiquitinationGWYRFRRNTQQQMSY
HHHHCCCCCHHHHHH
22817900
101PhosphorylationWYRFRRNTQQQMSYR
HHHCCCCCHHHHHHH
-
114AcetylationYREQVLHKQLTRILG
HHHHHHHHHHHHHHC
26051181
114UbiquitinationYREQVLHKQLTRILG
HHHHHHHHHHHHHHC
21906983
115UbiquitinationREQVLHKQLTRILGV
HHHHHHHHHHHHHCC
21963094
139UbiquitinationFISTANNSTHALEYV
HHHCCCCCCHHHHEE
24816145
159PhosphorylationRRYNQRISLAIPNLG
CCCCCCEEEEECCCC
27050516
168PhosphorylationAIPNLGNTSQQEYKV
EECCCCCCCCCEEEC
20068231
169PhosphorylationIPNLGNTSQQEYKVS
ECCCCCCCCCEEECC
20068231
173PhosphorylationGNTSQQEYKVSSVPN
CCCCCCEEECCCCCC
20068231
174UbiquitinationNTSQQEYKVSSVPNT
CCCCCEEECCCCCCC
21906983
187UbiquitinationNTSQSYAKVIKEHGT
CCCHHHHHHHHHHCC
21906983
190UbiquitinationQSYAKVIKEHGTDFF
HHHHHHHHHHCCCCC
22817900
199UbiquitinationHGTDFFDKDGVMKDI
HCCCCCCCCCHHHHH
21906983
204UbiquitinationFDKDGVMKDIRAIYQ
CCCCCHHHHHHHHHH
22817900
210PhosphorylationMKDIRAIYQVYNALQ
HHHHHHHHHHHHHHH
28152594
213PhosphorylationIRAIYQVYNALQEKV
HHHHHHHHHHHHHHH
18785766
219UbiquitinationVYNALQEKVQAVCAD
HHHHHHHHHHHHHCC
21963094
229AcetylationAVCADVEKSERVVES
HHHCCCHHHHHHHHH
26051181
229UbiquitinationAVCADVEKSERVVES
HHHCCCHHHHHHHHH
32015554
230PhosphorylationVCADVEKSERVVESC
HHCCCHHHHHHHHHH
27732954
243UbiquitinationSCQAEVNKLRRQITQ
HHHHHHHHHHHHHHH
24816145
249PhosphorylationNKLRRQITQRKNEKE
HHHHHHHHHHHCHHH
-
255AcetylationITQRKNEKEQERRLQ
HHHHHCHHHHHHHHH
19823645
272PhosphorylationVLSRQMPSESLDPAF
HHHCCCCHHHCCCCC
23403867
274PhosphorylationSRQMPSESLDPAFSP
HCCCCHHHCCCCCCC
29255136
280PhosphorylationESLDPAFSPRMPSSG
HHCCCCCCCCCCCCC
23401153
285PhosphorylationAFSPRMPSSGFAAEG
CCCCCCCCCCCCCCC
28857561
286PhosphorylationFSPRMPSSGFAAEGR
CCCCCCCCCCCCCCC
28348404
294PhosphorylationGFAAEGRSTLGDAEA
CCCCCCCCCCCCCCC
24248375
295PhosphorylationFAAEGRSTLGDAEAS
CCCCCCCCCCCCCCC
24248375
302PhosphorylationTLGDAEASDPPPPYS
CCCCCCCCCCCCCCC
25394399
308PhosphorylationASDPPPPYSDFHPNN
CCCCCCCCCCCCCCC
28796482
309PhosphorylationSDPPPPYSDFHPNNQ
CCCCCCCCCCCCCCC
28796482
318PhosphorylationFHPNNQESTLSHSRM
CCCCCCCCCCCCCHH
28796482
319PhosphorylationHPNNQESTLSHSRME
CCCCCCCCCCCCHHC
28796482
321PhosphorylationNNQESTLSHSRMERS
CCCCCCCCCCHHCCC
28796482
323PhosphorylationQESTLSHSRMERSVF
CCCCCCCCHHCCCEE
28796482
328PhosphorylationSHSRMERSVFMPRPQ
CCCHHCCCEEECCCC
21945579
339PhosphorylationPRPQAVGSSNYASTS
CCCCCCCCCCCCCCC
21945579
340PhosphorylationRPQAVGSSNYASTSA
CCCCCCCCCCCCCCC
21945579
342PhosphorylationQAVGSSNYASTSAGL
CCCCCCCCCCCCCCC
21945579
344PhosphorylationVGSSNYASTSAGLKY
CCCCCCCCCCCCCCC
21945579
345PhosphorylationGSSNYASTSAGLKYP
CCCCCCCCCCCCCCC
21945579
346PhosphorylationSSNYASTSAGLKYPG
CCCCCCCCCCCCCCC
21945579
354PhosphorylationAGLKYPGSGADLPPP
CCCCCCCCCCCCCCC
25159151
368PhosphorylationPQRAAGDSGEDSDDS
CCCCCCCCCCCCCCC
26055452
372PhosphorylationAGDSGEDSDDSDYEN
CCCCCCCCCCCCCCC
26055452
375PhosphorylationSGEDSDDSDYENLID
CCCCCCCCCCCCCCC
26055452
377PhosphorylationEDSDDSDYENLIDPT
CCCCCCCCCCCCCCC
22617229
384PhosphorylationYENLIDPTEPSNSEY
CCCCCCCCCCCCCCC
28796482
387PhosphorylationLIDPTEPSNSEYSHS
CCCCCCCCCCCCCCC
28796482
389PhosphorylationDPTEPSNSEYSHSKD
CCCCCCCCCCCCCCC
28796482
391PhosphorylationTEPSNSEYSHSKDSR
CCCCCCCCCCCCCCC
28796482
392PhosphorylationEPSNSEYSHSKDSRP
CCCCCCCCCCCCCCC
28796482
394PhosphorylationSNSEYSHSKDSRPMA
CCCCCCCCCCCCCCC
28796482
410PhosphorylationPDEDPRNTQTSQI--
CCCCCCCCCCCCC--
29214152
412PhosphorylationEDPRNTQTSQI----
CCCCCCCCCCC----
23312004
413PhosphorylationDPRNTQTSQI-----
CCCCCCCCCC-----
20068231

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABRX2_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 ABRX2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THAP5_HUMANTHAP5physical
21195082
BRCC3_HUMANBRCC3physical
21282113
BABA2_HUMANBREphysical
21282113
BABA1_HUMANBABAM1physical
21282113
BRCC3_HUMANBRCC3physical
20656690
BABA2_HUMANBREphysical
22863883
JIP4_HUMANSPAG9physical
22863883
ROA2_HUMANHNRNPA2B1physical
22863883
UBP7_HUMANUSP7physical
25283148
P53_HUMANTP53physical
25283148
BABA1_HUMANBABAM1physical
25283148
BABA2_HUMANBREphysical
25283148
BRCC3_HUMANBRCC3physical
25283148
LAMC1_HUMANLAMC1physical
26186194
THA11_HUMANTHAP11physical
26186194
TRAF7_HUMANTRAF7physical
26186194
BRCC3_HUMANBRCC3physical
26186194
BIRC6_HUMANBIRC6physical
26186194
NUMA1_HUMANNUMA1physical
26195665
BRCC3_HUMANBRCC3physical
26195665
BABA1_HUMANBABAM1physical
26195665
BABA2_HUMANBREphysical
26195665
GLYM_HUMANSHMT2physical
28514442
BRCC3_HUMANBRCC3physical
28514442
THA11_HUMANTHAP11physical
28514442
LAMC1_HUMANLAMC1physical
28514442
PRS8_HUMANPSMC5physical
28514442
TRAF7_HUMANTRAF7physical
28514442
BRCC3_HUMANBRCC3physical
24075985
BABA1_HUMANBABAM1physical
24075985
BABA2_HUMANBREphysical
24075985
GLYM_HUMANSHMT2physical
24075985
GLYC_HUMANSHMT1physical
24075985
INAR1_HUMANIFNAR1physical
24075985

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABRX2_HUMAN

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Related Literatures of Post-Translational Modification

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