BRAP_HUMAN - dbPTM
BRAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRAP_HUMAN
UniProt AC Q7Z569
Protein Name BRCA1-associated protein
Gene Name BRAP {ECO:0000312|HGNC:HGNC:1099}
Organism Homo sapiens (Human).
Sequence Length 592
Subcellular Localization Cytoplasm .
Protein Description Negatively regulates MAP kinase activation by limiting the formation of Raf/MEK complexes probably by inactivation of the KSR1 scaffold protein. Also acts as a Ras responsive E3 ubiquitin ligase that, on activation of Ras, is modified by auto-polyubiquitination resulting in the release of inhibition of Raf/MEK complex formation. May also act as a cytoplasmic retention protein with a role in regulating nuclear transport..
Protein Sequence MSVSLVVIRLELAEHSPVPAGFGFSAAAGEMSDEEIKKTTLASAVACLEGKSPGEKVAIIHQHLGRREMTDVIIETMKSNPDELKTTVEERKSSEASPTAQRSKDHSKECINAAPDSPSKQLPDQISFFSGNPSVEIVHGIMHLYKTNKMTSLKEDVRRSAMLCILTVPAAMTSHDLMKFVAPFNEVIEQMKIIRDSTPNQYMVLIKFRAQADADSFYMTCNGRQFNSIEDDVCQLVYVERAEVLKSEDGASLPVMDLTELPKCTVCLERMDESVNGILTTLCNHSFHSQCLQRWDDTTCPVCRYCQTPEPVEENKCFECGVQENLWICLICGHIGCGRYVSRHAYKHFEETQHTYAMQLTNHRVWDYAGDNYVHRLVASKTDGKIVQYECEGDTCQEEKIDALQLEYSYLLTSQLESQRIYWENKIVRIEKDTAEEINNMKTKFKETIEKCDNLEHKLNDLLKEKQSVERKCTQLNTKVAKLTNELKEEQEMNKCLRANQVLLQNKLKEEERVLKETCDQKDLQITEIQEQLRDVMFYLETQQKINHLPAETRQEIQEGQINIAMASASSPASSGGSGKLPSRKGRSKRGK
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
32PhosphorylationSAAAGEMSDEEIKKT
CCCCCCCCHHHHHHH		37.2527499020
38UbiquitinationMSDEEIKKTTLASAV
CCHHHHHHHHHHHHH		53.02-
39PhosphorylationSDEEIKKTTLASAVA
CHHHHHHHHHHHHHH		23.2623186163
40PhosphorylationDEEIKKTTLASAVAC
HHHHHHHHHHHHHHH		29.2523186163
43PhosphorylationIKKTTLASAVACLEG
HHHHHHHHHHHHHCC		26.7929214152
51UbiquitinationAVACLEGKSPGEKVA
HHHHHCCCCCCCEEE		44.07-
52PhosphorylationVACLEGKSPGEKVAI
HHHHCCCCCCCEEEE		49.3325159151
70PhosphorylationHLGRREMTDVIIETM
CCCCHHHHHHHHHHH		23.5128102081
76PhosphorylationMTDVIIETMKSNPDE
HHHHHHHHHHCCHHH		21.3528102081
79PhosphorylationVIIETMKSNPDELKT
HHHHHHHCCHHHHHH		42.6522496350
85AcetylationKSNPDELKTTVEERK
HCCHHHHHHHHHHHH		39.85130463
85UbiquitinationKSNPDELKTTVEERK
HCCHHHHHHHHHHHH		39.85-
86PhosphorylationSNPDELKTTVEERKS
CCHHHHHHHHHHHHC		49.0128450419
87PhosphorylationNPDELKTTVEERKSS
CHHHHHHHHHHHHCC		25.0828450419
93PhosphorylationTTVEERKSSEASPTA
HHHHHHHCCCCCCCH		39.3628176443
94PhosphorylationTVEERKSSEASPTAQ
HHHHHHCCCCCCCHH		39.9728176443
97PhosphorylationERKSSEASPTAQRSK
HHHCCCCCCCHHHCH		20.8023401153
99PhosphorylationKSSEASPTAQRSKDH
HCCCCCCCHHHCHHC		32.6929255136
103PhosphorylationASPTAQRSKDHSKEC
CCCCHHHCHHCCHHH		30.2926074081
107PhosphorylationAQRSKDHSKECINAA
HHHCHHCCHHHHHCC		40.0424505115
117PhosphorylationCINAAPDSPSKQLPD
HHHCCCCCCCCCCCC		29.9829255136
119PhosphorylationNAAPDSPSKQLPDQI
HCCCCCCCCCCCCCC		36.6729255136
127PhosphorylationKQLPDQISFFSGNPS
CCCCCCCEECCCCCC		18.0126074081
154UbiquitinationTNKMTSLKEDVRRSA
HCCCCCCCHHHHHHH		52.19-
173PhosphorylationLTVPAAMTSHDLMKF
HHHCCCCCCHHHHHH		20.4129116813
174PhosphorylationTVPAAMTSHDLMKFV
HHCCCCCCHHHHHHH		11.2629116813
202UbiquitinationRDSTPNQYMVLIKFR
HCCCCCEEEEEEEEE		8.8821890473
206UbiquitinationPNQYMVLIKFRAQAD
CCEEEEEEEEEEECC		2.4221890473
221UbiquitinationADSFYMTCNGRQFNS
CCEEEEEECCEECCC		2.64-
247UbiquitinationERAEVLKSEDGASLP
EEHHHEECCCCCCCC		36.44-
263UbiquitinationMDLTELPKCTVCLER
CCCCCCCCCEEEHHC		55.98-
265UbiquitinationLTELPKCTVCLERMD
CCCCCCCEEEHHCCC		22.00-
267UbiquitinationELPKCTVCLERMDES
CCCCCEEEHHCCCHH		1.43-
286PhosphorylationLTTLCNHSFHSQCLQ
HHHHHCCCHHHHHHH		15.6325159151
289PhosphorylationLCNHSFHSQCLQRWD
HHCCCHHHHHHHHCC		22.1521712546
305PhosphorylationTTCPVCRYCQTPEPV
CCCCCCCCCCCCCCC		5.4728985074
308PhosphorylationPVCRYCQTPEPVEEN
CCCCCCCCCCCCCCC		26.5125850435
328UbiquitinationGVQENLWICLICGHI
CCCCCCEEHHHCCCC		1.22-
352PhosphorylationAYKHFEETQHTYAMQ
HHHHHHHCCCEEEEH		20.60-
361PhosphorylationHTYAMQLTNHRVWDY
CEEEEHHHCCCHHHC		16.46-
381UbiquitinationVHRLVASKTDGKIVQ
CEEEEEECCCCCEEE		40.6821906983
381UbiquitinationVHRLVASKTDGKIVQ
CEEEEEECCCCCEEE		40.6821890473
385UbiquitinationVASKTDGKIVQYECE
EEECCCCCEEEEEEE		42.3821906983
385UbiquitinationVASKTDGKIVQYECE
EEECCCCCEEEEEEE		42.3821890473
389PhosphorylationTDGKIVQYECEGDTC
CCCCEEEEEEECCCC		16.2028796482
400UbiquitinationGDTCQEEKIDALQLE
CCCCCHHHCCHHHHH		45.1721906983
401UbiquitinationDTCQEEKIDALQLEY
CCCCHHHCCHHHHHH		4.1921890473
422PhosphorylationQLESQRIYWENKIVR
HHHHCCEEEECCEEE		14.62-
426UbiquitinationQRIYWENKIVRIEKD
CCEEEECCEEEEECC		30.94-
432NeddylationNKIVRIEKDTAEEIN
CCEEEEECCCHHHHH		58.99-
442UbiquitinationAEEINNMKTKFKETI
HHHHHHHHHHHHHHH		51.16-
444UbiquitinationEINNMKTKFKETIEK
HHHHHHHHHHHHHHH		49.25-
446UbiquitinationNNMKTKFKETIEKCD
HHHHHHHHHHHHHHH		56.34-
458UbiquitinationKCDNLEHKLNDLLKE
HHHCHHHHHHHHHHH		39.34-
458AcetylationKCDNLEHKLNDLLKE
HHHCHHHHHHHHHHH		39.3422369019
464UbiquitinationHKLNDLLKEKQSVER
HHHHHHHHHHHHHHH		70.89-
482UbiquitinationQLNTKVAKLTNELKE
HHHHHHHHHHHHHHH		59.85-
493SulfoxidationELKEEQEMNKCLRAN
HHHHHHHHHHHHHHH		6.0821406390
507UbiquitinationNQVLLQNKLKEEERV
HHHHHHHHHHHHHHH		48.23-
522UbiquitinationLKETCDQKDLQITEI
HHHHCCHHHCCHHHH		47.34-
527PhosphorylationDQKDLQITEIQEQLR
CHHHCCHHHHHHHHH		17.6723403867
568PhosphorylationQINIAMASASSPASS
CCEEEEEECCCCCCC		18.6529978859
570PhosphorylationNIAMASASSPASSGG
EEEEEECCCCCCCCC		34.0729978859
571PhosphorylationIAMASASSPASSGGS
EEEEECCCCCCCCCC		24.9721815630
574PhosphorylationASASSPASSGGSGKL
EECCCCCCCCCCCCC		32.6628348404
575PhosphorylationSASSPASSGGSGKLP
ECCCCCCCCCCCCCC		49.6428348404
578PhosphorylationSPASSGGSGKLPSRK
CCCCCCCCCCCCCCC		35.9628348404
580UbiquitinationASSGGSGKLPSRKGR
CCCCCCCCCCCCCCC		59.9421906983
580UbiquitinationASSGGSGKLPSRKGR
CCCCCCCCCCCCCCC		59.9421890473
583PhosphorylationGGSGKLPSRKGRSKR
CCCCCCCCCCCCCCC		58.0024719451
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
-KUbiquitinationE3 ubiquitin ligaseBRAPQ7Z569
PMID:23105109
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRAP_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 BRAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRCA1_HUMANBRCA1physical
9497340
CC14A_HUMANCDC14Aphysical
19152073
IKKB_HUMANIKBKBphysical
21670849
IKBB_HUMANNFKBIBphysical
21670849
MP2K1_HUMANMAP2K1physical
18332145
BRAF_HUMANBRAFphysical
18332145
KSR1_HUMANKSR1physical
18332145
UBP4_HUMANUSP4physical
23105109
UBP15_HUMANUSP15physical
23105109
NEDD8_HUMANNEDD8physical
23554956
BRAP_HUMANBRAPphysical
23554956
CUL1_HUMANCUL1physical
23554956
TRI55_HUMANTRIM55physical
22493164
TRI41_HUMANTRIM41physical
22493164
TRIM8_HUMANTRIM8physical
22493164
HM20A_HUMANHMG20Aphysical
23707952
NUMA1_HUMANNUMA1physical
23707952
SYNE2_HUMANSYNE2physical
23707952
EFHC1_HUMANEFHC1physical
25820252
UBB_HUMANUBBphysical
25820252
UBC_HUMANUBCphysical
25820252
APOA1_HUMANAPOA1physical
25820252
NUMA1_HUMANNUMA1physical
25820252
SYNE2_HUMANSYNE2physical
25820252
BRK1_HUMANBRK1physical
25820252
CC105_HUMANCCDC105physical
25820252
SHP1L_HUMANSHCBP1Lphysical
25820252
TEX35_HUMANTEX35physical
25820252
DNMT1_HUMANDNMT1physical
25820252
PHLP1_HUMANPHLPP1physical
25820252
F184A_HUMANFAM184Aphysical
25820252
FBX2_HUMANFBXO2physical
25820252
ZN382_HUMANZNF382physical
25820252
ZN479_HUMANZNF479physical
25820252
AKAP3_HUMANAKAP3physical
25820252
BRAP_HUMANBRAPphysical
25820252
TANC2_HUMANTANC2physical
25820252
RBM12_HUMANRBM12physical
25820252
ATMIN_HUMANATMINphysical
25820252
CCD30_HUMANCCDC30physical
25820252
SMCE1_HUMANSMARCE1physical
25820252
ZN521_HUMANZNF521physical
25820252
HM20A_HUMANHMG20Aphysical
25820252
UBC_HUMANUBCphysical
28768733
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 BRAP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-119, ANDMASS 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-52, AND MASSSPECTROMETRY.

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