BABA2_HUMAN - dbPTM
BABA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BABA2_HUMAN
UniProt AC Q9NXR7
Protein Name BRISC and BRCA1-A complex member 2 {ECO:0000312|HGNC:HGNC:1106}
Gene Name BABAM2 {ECO:0000312|HGNC:HGNC:1106}
Organism Homo sapiens (Human).
Sequence Length 383
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. [PubMed: 17525341]
Protein Sequence MSPEVALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFGEDAEFLPDPSALQNLASWNPSNPECLLLVVKELVQQYHQFQCSRLRESSRLMFEYQTLLEEPQYGENMEIYAGKKNNWTGEFSARFLLKLPVDFSNIPTYLLKDVNEDPGEDVALLSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSHFGTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNSGQLYSQAQKNYPYSPRWDGNEMAKRAKAYFKTFVPQFQEAAFANGKL
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-------MSPEVALN
-------CCHHHHHH
22223895
2Phosphorylation------MSPEVALNR
------CCHHHHHHH
23401153
11PhosphorylationEVALNRISPMLSPFI
HHHHHHHHHHHHHHH
28348404
15PhosphorylationNRISPMLSPFISSVV
HHHHHHHHHHHHHHH
21815630
19PhosphorylationPMLSPFISSVVRNGK
HHHHHHHHHHHHCCC
26270265
20PhosphorylationMLSPFISSVVRNGKV
HHHHHHHHHHHCCCC
28857561
26AcetylationSSVVRNGKVGLDATN
HHHHHCCCCCCCCCC
25953088
26UbiquitinationSSVVRNGKVGLDATN
HHHHHCCCCCCCCCC
29967540
41UbiquitinationCLRITDLKSGCTSLT
CEEEEECCCCCCCCC
21963094
42PhosphorylationLRITDLKSGCTSLTP
EEEEECCCCCCCCCC
23312004
45PhosphorylationTDLKSGCTSLTPGPN
EECCCCCCCCCCCCC
23312004
46PhosphorylationDLKSGCTSLTPGPNC
ECCCCCCCCCCCCCC
23312004
48PhosphorylationKSGCTSLTPGPNCDR
CCCCCCCCCCCCCCC
21815630
57UbiquitinationGPNCDRFKLHIPYAG
CCCCCCEEEECCCCC
29967540
135PhosphorylationQCSRLRESSRLMFEY
HHHHHHHHHHHHHHH
27273156
161UbiquitinationNMEIYAGKKNNWTGE
CEEEEEECCCCCCCE
-
162 (in isoform 4)Ubiquitination-21890473
162 (in isoform 3)Ubiquitination-21890473
162 (in isoform 2)Ubiquitination-21890473
162 (in isoform 1)Ubiquitination-21890473
162UbiquitinationMEIYAGKKNNWTGEF
EEEEEECCCCCCCEE
21890473
176UbiquitinationFSARFLLKLPVDFSN
EEEEEEECCCCCHHH
-
263PhosphorylationLLTNKVQYVIQGYHK
HHHCHHHHHHCCHHH
27174698
270AcetylationYVIQGYHKRREYIAA
HHHCCHHHHHHHHHH
19608861
347PhosphorylationYSQAQKNYPYSPRWD
HCHHHHHCCCCCCCC
20068231
349PhosphorylationQAQKNYPYSPRWDGN
HHHHHCCCCCCCCHH
20068231
350PhosphorylationAQKNYPYSPRWDGNE
HHHHCCCCCCCCHHH
20068231
360UbiquitinationWDGNEMAKRAKAYFK
CCHHHHHHHHHHHHH
-
366 (in isoform 4)Phosphorylation--
367 (in isoform 2)Ubiquitination-21890473
367UbiquitinationKRAKAYFKTFVPQFQ
HHHHHHHHHHHHHHH
21890473
373 (in isoform 4)Phosphorylation--
374 (in isoform 3)Phosphorylation--
374 (in isoform 4)Phosphorylation--
375 (in isoform 4)Phosphorylation--
382AcetylationEAAFANGKL------
HHHHHCCCC------
24431675
382UbiquitinationEAAFANGKL------
HHHHHCCCC------
21906983
382 (in isoform 2)Ubiquitination-21890473
389UbiquitinationKL-------------
CC-------------
29967540
424Ubiquitination------------------------------------------------
------------------------------------------------
21890473
439Ubiquitination---------------------------------------------------------------
---------------------------------------------------------------
27667366
446Ubiquitination----------------------------------------------------------------------
----------------------------------------------------------------------
29967540

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 BABA2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BABA2_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 BABA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BABA1_HUMANBABAM1physical
16189514
BABA1_HUMANBABAM1physical
17353931
BRCC3_HUMANBRCC3physical
17353931
ABRX2_HUMANFAM175Bphysical
17353931
BARD1_HUMANBARD1physical
14636569
BRCA1_HUMANBRCA1physical
14636569
RAD51_HUMANRAD51physical
14636569
P53_HUMANTP53physical
14636569
UB2D1_HUMANUBE2D1physical
14636569
PHB_HUMANPHBphysical
19615732
RPN2_HUMANRPN2physical
19615732
GLYM_HUMANSHMT2physical
19615732
SSRG_HUMANSSR3physical
19615732
LPPRC_HUMANLRPPRCphysical
19615732
CMC2_HUMANSLC25A13physical
19615732
ATG2A_HUMANATG2Aphysical
19615732
ABRX2_HUMANFAM175Bphysical
19615732
TTC28_HUMANTTC28physical
19615732
FKBP8_HUMANFKBP8physical
19615732
DRS7B_HUMANDHRS7Bphysical
19615732
BABA1_HUMANBABAM1physical
19615732
UIMC1_HUMANUIMC1physical
19615732
TMX3_HUMANTMX3physical
19615732
UGGG2_HUMANUGGT2physical
19615732
MMS19_HUMANMMS19physical
19615732
BRCC3_HUMANBRCC3physical
19615732
ABRX1_HUMANFAM175Aphysical
19615732
TNR1A_HUMANTNFRSF1Aphysical
15465831
TNR6_HUMANFASphysical
15465831
UIMC1_HUMANUIMC1physical
19261749
ABRX1_HUMANFAM175Aphysical
19261749
BRCC3_HUMANBRCC3physical
19261749
BABA1_HUMANBABAM1physical
19261749
UIMC1_HUMANUIMC1physical
19261746
BABA1_HUMANBABAM1physical
19261746
BRCC3_HUMANBRCC3physical
19261746
UIMC1_HUMANUIMC1physical
21282113
ABRX1_HUMANFAM175Aphysical
21282113
ABRX2_HUMANFAM175Bphysical
21282113
BRCC3_HUMANBRCC3physical
21282113
BABA1_HUMANBABAM1physical
21282113
BRCC3_HUMANBRCC3physical
20656689
UIMC1_HUMANUIMC1physical
20656689
ABRX1_HUMANFAM175Aphysical
20656689
BABA1_HUMANBABAM1physical
20656689
UIMC1_HUMANUIMC1physical
19261748
ABRX1_HUMANFAM175Aphysical
19261748
BABA1_HUMANBABAM1physical
19261748
BRCC3_HUMANBRCC3physical
19261748
ROA2_HUMANHNRNPA2B1physical
22863883
OPTN_HUMANOPTNphysical
22863883
TFG_HUMANTFGphysical
22863883
CH3L1_HUMANCHI3L1physical
26186194
GLYM_HUMANSHMT2physical
28514442
CH3L1_HUMANCHI3L1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BABA2_HUMAN

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Related Literatures of Post-Translational Modification

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