BABA1_HUMAN - dbPTM
BABA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BABA1_HUMAN
UniProt AC Q9NWV8
Protein Name BRISC and BRCA1-A complex member 1
Gene Name BABAM1
Organism Homo sapiens (Human).
Sequence Length 329
Subcellular Localization Cytoplasm . Nucleus . Localizes at sites of DNA damage at double-strand breaks (DSBs).
Protein Description Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. [PubMed: 24075985]
Protein Sequence MEVAEPSSPTEEEEEEEEHSAEPRPRTRSNPEGAEDRAVGAQASVGSRSEGEGEAASADDGSLNTSGAGPKSWQVPPPAPEVQIRTPRVNCPEKVIICLDLSEEMSLPKLESFNGSKTNALNVSQKMIEMFVRTKHKIDKSHEFALVVVNDDTAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDVVYIHNGTEEKEEEMSWKDMFAFMGSLDTKGTSYKYEVALAGPALELHNCMAKLLAHPLQRPCQSHASYSLLEEEDEAIEVEATV
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-------MEVAEPSS
-------CCCCCCCC		9.3719413330
7Phosphorylation-MEVAEPSSPTEEEE
-CCCCCCCCCCHHHH		40.2229255136
8PhosphorylationMEVAEPSSPTEEEEE
CCCCCCCCCCHHHHH		46.7029255136
10PhosphorylationVAEPSSPTEEEEEEE
CCCCCCCCHHHHHHH		58.9629255136
20PhosphorylationEEEEEEHSAEPRPRT
HHHHHHHCCCCCCCC		37.2922617229
27PhosphorylationSAEPRPRTRSNPEGA
CCCCCCCCCCCCCCH		40.9223401153
29PhosphorylationEPRPRTRSNPEGAED
CCCCCCCCCCCCHHH		57.0029255136
37MethylationNPEGAEDRAVGAQAS
CCCCHHHHHHCCCCC		23.76115484531
44PhosphorylationRAVGAQASVGSRSEG
HHHCCCCCCCCCCCC		18.2229255136
46 (in isoform 2)Phosphorylation-18.17-
47PhosphorylationGAQASVGSRSEGEGE
CCCCCCCCCCCCCCC		30.4023401153
48 (in isoform 2)Ubiquitination-32.5721890473
49PhosphorylationQASVGSRSEGEGEAA
CCCCCCCCCCCCCCC		52.2119664994
57PhosphorylationEGEGEAASADDGSLN
CCCCCCCCCCCCCCC		39.0023927012
62PhosphorylationAASADDGSLNTSGAG
CCCCCCCCCCCCCCC		25.9925159151
65PhosphorylationADDGSLNTSGAGPKS
CCCCCCCCCCCCCCC		33.5530278072
66PhosphorylationDDGSLNTSGAGPKSW
CCCCCCCCCCCCCCC		26.1023927012
71UbiquitinationNTSGAGPKSWQVPPP
CCCCCCCCCCCCCCC		64.51-
72PhosphorylationTSGAGPKSWQVPPPA
CCCCCCCCCCCCCCC		26.3527251275
86PhosphorylationAPEVQIRTPRVNCPE
CCCCEEECCCCCCCC		19.64-
112PhosphorylationMSLPKLESFNGSKTN
CCCCCHHHCCCCCCC		34.1523312004
116PhosphorylationKLESFNGSKTNALNV
CHHHCCCCCCCCCHH		37.0923312004
117UbiquitinationLESFNGSKTNALNVS
HHHCCCCCCCCCHHH		47.3921890473
117 (in isoform 1)Ubiquitination-47.3921890473
118PhosphorylationESFNGSKTNALNVSQ
HHCCCCCCCCCHHHH		27.6723312004
124PhosphorylationKTNALNVSQKMIEMF
CCCCCHHHHHHHHHH		24.0221406692
126UbiquitinationNALNVSQKMIEMFVR
CCCHHHHHHHHHHHH		34.0521890473
126 (in isoform 1)Ubiquitination-34.0521890473
194PhosphorylationFSLIQQKTELPVTEN
HHHHHHCCCCCCCCC		38.1222468782
213PhosphorylationPPPYVVRTILVYSRP
CCCEEEEEEEEECCC		13.6722468782
234UbiquitinationSLTEPMKKMFQCPYF
CCCHHHHHHHCCCCE		38.40-
252PhosphorylationVVYIHNGTEEKEEEM
EEEEECCCHHHCHHC		46.41-
276PhosphorylationGSLDTKGTSYKYEVA
HCCCCCCCCCEEEEE		30.3630387612
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
29SPhosphorylationKinaseAKT1P31749
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BABA1_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 BABA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARF4_HUMANARF4physical
19615732
GNAL_HUMANGNALphysical
19615732
NDUA5_HUMANNDUFA5physical
19615732
NSF_HUMANNSFphysical
19615732
ODPA_HUMANPDHA1physical
19615732
PLK1_HUMANPLK1physical
19615732
AAKG1_HUMANPRKAG1physical
19615732
PSA4_HUMANPSMA4physical
19615732
RAGP1_HUMANRANGAP1physical
19615732
GLYM_HUMANSHMT2physical
19615732
M2OM_HUMANSLC25A11physical
19615732
TNKS1_HUMANTNKSphysical
19615732
GUAA_HUMANGMPSphysical
19615732
VPS4B_HUMANVPS4Bphysical
19615732
BABA2_HUMANBREphysical
19615732
MELK_HUMANMELKphysical
19615732
CMC2_HUMANSLC25A13physical
19615732
DX39A_HUMANDDX39Aphysical
19615732
MICU1_HUMANMICU1physical
19615732
CLPX_HUMANCLPXphysical
19615732
PARK7_HUMANPARK7physical
19615732
RRP44_HUMANDIS3physical
19615732
ABRX2_HUMANFAM175Bphysical
19615732
PRDX5_HUMANPRDX5physical
19615732
VPS4A_HUMANVPS4Aphysical
19615732
UBXN1_HUMANUBXN1physical
19615732
PBDC1_HUMANPBDC1physical
19615732
UIMC1_HUMANUIMC1physical
19615732
UGGG2_HUMANUGGT2physical
19615732
LRC47_HUMANLRRC47physical
19615732
ADPPT_HUMANAASDHPPTphysical
19615732
P5CR3_HUMANPYCRLphysical
19615732
BRCC3_HUMANBRCC3physical
19615732
SLIRP_HUMANSLIRPphysical
19615732
ABRX1_HUMANFAM175Aphysical
19615732
ALAT2_HUMANGPT2physical
19615732
ATAD1_HUMANATAD1physical
19615732
RM53_HUMANMRPL53physical
19615732
SFXN4_HUMANSFXN4physical
19615732
F210A_HUMANFAM210Aphysical
19615732
BRCA1_HUMANBRCA1physical
19261749
BABA2_HUMANBREphysical
19261749
UIMC1_HUMANUIMC1physical
19261749
ABRX1_HUMANFAM175Aphysical
19261749
BRCC3_HUMANBRCC3physical
19261749
ABRX1_HUMANFAM175Aphysical
19261746
BABA2_HUMANBREphysical
19261746
BRCC3_HUMANBRCC3physical
19261746
BRCA1_HUMANBRCA1physical
19261746
UIMC1_HUMANUIMC1physical
19261746
UIMC1_HUMANUIMC1physical
21282113
BABA2_HUMANBREphysical
21282113
BRCC3_HUMANBRCC3physical
21282113
ABRX2_HUMANFAM175Bphysical
21282113
ABRX1_HUMANFAM175Aphysical
21282113
UIMC1_HUMANUIMC1physical
19261748
BABA2_HUMANBREphysical
19261748
ABRX1_HUMANFAM175Aphysical
19261748
BRCC3_HUMANBRCC3physical
19261748
PCNA_HUMANPCNAphysical
22939629
BABA2_HUMANBREphysical
22863883
TFG_HUMANTFGphysical
22863883
BABA2_HUMANBREphysical
26186194
GLYM_HUMANSHMT2physical
26186194
TNKS2_HUMANTNKS2physical
26186194
TNKS1_HUMANTNKSphysical
26186194
ABRX1_HUMANFAM175Aphysical
26186194
UIMC1_HUMANUIMC1physical
26186194
BRCC3_HUMANBRCC3physical
26186194
ABRX2_HUMANFAM175Bphysical
26186194
BABA2_HUMANBREphysical
26344197
ABRX1_HUMANFAM175Aphysical
28514442
UIMC1_HUMANUIMC1physical
28514442
TNKS2_HUMANTNKS2physical
28514442
TNKS1_HUMANTNKSphysical
28514442
BABA2_HUMANBREphysical
28514442
ABRX2_HUMANFAM175Bphysical
28514442
BRCC3_HUMANBRCC3physical
28514442
GLYM_HUMANSHMT2physical
28514442
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 BABA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-49; SER-62;THR-65 AND SER-66, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-66, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-62, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.

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