APBB2_HUMAN - dbPTM
APBB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APBB2_HUMAN
UniProt AC Q92870
Protein Name Amyloid-beta A4 precursor protein-binding family B member 2
Gene Name APBB2
Organism Homo sapiens (Human).
Sequence Length 758
Subcellular Localization
Protein Description May modulate the internalization of amyloid-beta precursor protein..
Protein Sequence MSEVLPADSGVDTLAVFMASSGTTDVTNRNSPATPPNTLNLRSSHNELLNAEIKHTETKNSTPPKCRKKYALTNIQAAMGLSDPAAQPLLGNGSANIKLVKNGENQLRKAAEQGQQDPNKNLSPTAVINITSEKLEGKEPHPQDSSSCEILPSQPRRTKSFLNYYADLETSARELEQNRGNHHGTAEEKSQPVQGQASTIIGNGDLLLQKPNRPQSSPEDGQVATVSSSPETKKDHPKTGAKTDCALHRIQNLAPSDEESSWTTLSQDSASPSSPDETDIWSDHSFQTDPDLPPGWKRVSDIAGTYYWHIPTGTTQWERPVSIPADLQGSRKGSLSSVTPSPTPENEKQPWSDFAVLNGGKINSDIWKDLHAATVNPDPSLKEFEGATLRYASLKLRNAPHPDDDDSCSINSDPEAKCFAVRSLGWVEMAEEDLAPGKSSVAVNNCIRQLSYCKNDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPIVSIRVWGVGRDNGRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERKNAKALACSSLQERANVNLDVPLQVDFPTPKTELVQKFHVQYLGMLPVDKPVGMDILNSAIENLMTSSNKEDWLSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMGVGKDVHTFAFIMDTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQKCLVARPPSQKVRPPPPPADSVTRRVTTNVKRGVLSLIDTLKQKRPVTEMP
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
24PhosphorylationFMASSGTTDVTNRNS
HEECCCCCCCCCCCC		31.8125627689
27PhosphorylationSSGTTDVTNRNSPAT
CCCCCCCCCCCCCCC		31.1326425664
31PhosphorylationTDVTNRNSPATPPNT
CCCCCCCCCCCCCCC		16.8130266825
34PhosphorylationTNRNSPATPPNTLNL
CCCCCCCCCCCCEEC		42.5430266825
34 (in isoform 4)Phosphorylation-42.5424719451
38PhosphorylationSPATPPNTLNLRSSH
CCCCCCCCEECCCHH		23.8530266825
43 (in isoform 4)Phosphorylation-38.8327251275
43PhosphorylationPNTLNLRSSHNELLN
CCCEECCCHHHHHHH		38.8325849741
44 (in isoform 4)Phosphorylation-24.7324719451
44PhosphorylationNTLNLRSSHNELLNA
CCEECCCHHHHHHHH		24.7325849741
54UbiquitinationELLNAEIKHTETKNS
HHHHHHEECCCCCCC		35.66-
56PhosphorylationLNAEIKHTETKNSTP
HHHHEECCCCCCCCC		40.1123312004
58PhosphorylationAEIKHTETKNSTPPK
HHEECCCCCCCCCCC		36.3630576142
61PhosphorylationKHTETKNSTPPKCRK
ECCCCCCCCCCCHHH		43.7921406692
62PhosphorylationHTETKNSTPPKCRKK
CCCCCCCCCCCHHHH		53.6721406692
70PhosphorylationPPKCRKKYALTNIQA
CCCHHHHHHHHHHHH		15.1822210691
73PhosphorylationCRKKYALTNIQAAMG
HHHHHHHHHHHHHCC		23.3122210691
82PhosphorylationIQAAMGLSDPAAQPL
HHHHCCCCCCCCCCC		35.5022210691
123PhosphorylationQDPNKNLSPTAVINI
CCCCCCCCCCEEEEE		29.6025159151
123 (in isoform 4)Phosphorylation-29.6027251275
125 (in isoform 4)Phosphorylation-30.1324719451
125PhosphorylationPNKNLSPTAVINITS
CCCCCCCCEEEEECH		30.1330266825
131PhosphorylationPTAVINITSEKLEGK
CCEEEEECHHHHCCC		26.7523312004
132PhosphorylationTAVINITSEKLEGKE
CEEEEECHHHHCCCC		29.0123312004
145PhosphorylationKEPHPQDSSSCEILP
CCCCCCCCCCCEECC		20.9228985074
146PhosphorylationEPHPQDSSSCEILPS
CCCCCCCCCCEECCC		47.5028555341
147PhosphorylationPHPQDSSSCEILPSQ
CCCCCCCCCEECCCC		21.5228555341
158 (in isoform 4)Phosphorylation-32.1127642862
158PhosphorylationLPSQPRRTKSFLNYY
CCCCCCCCHHHHHHH		32.1127080861
159UbiquitinationPSQPRRTKSFLNYYA
CCCCCCCHHHHHHHH		37.082189047
159 (in isoform 1)Ubiquitination-37.0821890473
159 (in isoform 2)Ubiquitination-37.0821890473
160PhosphorylationSQPRRTKSFLNYYAD
CCCCCCHHHHHHHHH		34.0625159151
160 (in isoform 4)Phosphorylation-34.0624719451
164PhosphorylationRTKSFLNYYADLETS
CCHHHHHHHHHHHHH		11.3725884760
164 (in isoform 4)Phosphorylation-11.3727642862
165 (in isoform 4)Phosphorylation-7.8027642862
165PhosphorylationTKSFLNYYADLETSA
CHHHHHHHHHHHHHH		7.8023403867
198PhosphorylationQPVQGQASTIIGNGD
CCCCCCCCEEECCCC		16.5528348404
199PhosphorylationPVQGQASTIIGNGDL
CCCCCCCEEECCCCE		21.4528348404
216PhosphorylationQKPNRPQSSPEDGQV
CCCCCCCCCCCCCCE		51.0125849741
217PhosphorylationKPNRPQSSPEDGQVA
CCCCCCCCCCCCCEE		27.3625849741
217 (in isoform 4)Phosphorylation-27.3627251275
225PhosphorylationPEDGQVATVSSSPET
CCCCCEEEECCCCCC		23.2822199227
227PhosphorylationDGQVATVSSSPETKK
CCCEEEECCCCCCCC		22.2730576142
228PhosphorylationGQVATVSSSPETKKD
CCEEEECCCCCCCCC		45.6430576142
229PhosphorylationQVATVSSSPETKKDH
CEEEECCCCCCCCCC		21.1725159151
229 (in isoform 4)Phosphorylation-21.1727251275
232PhosphorylationTVSSSPETKKDHPKT
EECCCCCCCCCCCCC		46.9430576142
238AcetylationETKKDHPKTGAKTDC
CCCCCCCCCCCHHHH		57.0519815687
242UbiquitinationDHPKTGAKTDCALHR
CCCCCCCHHHHHHHH		46.36-
300PhosphorylationPPGWKRVSDIAGTYY
CCCCEEHHHCCCEEE		27.6024501219
312PhosphorylationTYYWHIPTGTTQWER
EEEEECCCCCCCCCC		46.7022210691
322PhosphorylationTQWERPVSIPADLQG
CCCCCCEECCCCCCC		26.0723312004
330PhosphorylationIPADLQGSRKGSLSS
CCCCCCCCCCCCCCC		20.1919664994
331 (in isoform 4)Phosphorylation-54.9324719451
332UbiquitinationADLQGSRKGSLSSVT
CCCCCCCCCCCCCCC		55.32-
334PhosphorylationLQGSRKGSLSSVTPS
CCCCCCCCCCCCCCC		28.2830266825
334 (in isoform 2)Phosphorylation-28.2825849741
335 (in isoform 4)Phosphorylation-6.3624719451
336PhosphorylationGSRKGSLSSVTPSPT
CCCCCCCCCCCCCCC		25.1830266825
336 (in isoform 2)Phosphorylation-25.1825849741
337PhosphorylationSRKGSLSSVTPSPTP
CCCCCCCCCCCCCCC		34.9930266825
337 (in isoform 4)Phosphorylation-34.9927251275
337 (in isoform 2)Phosphorylation-34.9928450419
338 (in isoform 4)Phosphorylation-9.0724719451
339PhosphorylationKGSLSSVTPSPTPEN
CCCCCCCCCCCCCCC		21.7230266825
339 (in isoform 2)Phosphorylation-21.7228450419
340 (in isoform 4)Phosphorylation-35.8327251275
341PhosphorylationSLSSVTPSPTPENEK
CCCCCCCCCCCCCCC		31.8530266825
341 (in isoform 2)Phosphorylation-31.8528450419
342 (in isoform 4)Phosphorylation-53.8524719451
343PhosphorylationSSVTPSPTPENEKQP
CCCCCCCCCCCCCCC		47.8029255136
343 (in isoform 2)Phosphorylation-47.8029978859
352PhosphorylationENEKQPWSDFAVLNG
CCCCCCCCCEEEECC		29.5422468782
353 (in isoform 2)Phosphorylation-31.4929978859
364PhosphorylationLNGGKINSDIWKDLH
ECCCCCCHHHHHHHH		33.6728857561
365 (in isoform 4)Phosphorylation-46.4027251275
380PhosphorylationATVNPDPSLKEFEGA
CCCCCCCCHHHCCCC		60.5029514088
381 (in isoform 4)Phosphorylation-8.1927251275
382UbiquitinationVNPDPSLKEFEGATL
CCCCCCHHHCCCCCC		65.77-
388PhosphorylationLKEFEGATLRYASLK
HHHCCCCCCEEEEEE		23.7124719451
389 (in isoform 4)Phosphorylation-3.8024719451
391PhosphorylationFEGATLRYASLKLRN
CCCCCCEEEEEECCC		12.0324719451
392 (in isoform 4)Phosphorylation-11.2724719451
393PhosphorylationGATLRYASLKLRNAP
CCCCEEEEEECCCCC		19.6622617229
394 (in isoform 4)Phosphorylation-4.6324719451
407PhosphorylationPHPDDDDSCSINSDP
CCCCCCCCCCCCCCH		19.4322167270
409PhosphorylationPDDDDSCSINSDPEA
CCCCCCCCCCCCHHH		28.8522167270
410 (in isoform 4)Phosphorylation-7.2124719451
412PhosphorylationDDSCSINSDPEAKCF
CCCCCCCCCHHHCEE		53.5222167270
413 (in isoform 4)Phosphorylation-40.3424719451
438UbiquitinationEEDLAPGKSSVAVNN
HHHCCCCCCHHHHHH		38.20-
454UbiquitinationIRQLSYCKNDIRDTV
HHHHHHCCCCHHHCC		49.80-
541 (in isoform 2)Phosphorylation-3.5029116813
556UbiquitinationMAERKNAKALACSSL
HHHHHCHHHHHCCCH		54.01-
559 (in isoform 2)Phosphorylation-8.94-
561PhosphorylationNAKALACSSLQERAN
CHHHHHCCCHHHHHC		28.6029116813
562PhosphorylationAKALACSSLQERANV
HHHHHCCCHHHHHCC		33.6827251275
563 (in isoform 4)Phosphorylation-3.3527251275
594PhosphorylationVQKFHVQYLGMLPVD
HHHHCCEECCCCCCC		12.2523663014
611PhosphorylationVGMDILNSAIENLMT
CCHHHHHHHHHHHHH		27.4623663014
618PhosphorylationSAIENLMTSSNKEDW
HHHHHHHHCCCCCCE		31.9723663014
619PhosphorylationAIENLMTSSNKEDWL
HHHHHHHCCCCCCEE		20.2523663014
620PhosphorylationIENLMTSSNKEDWLS
HHHHHHCCCCCCEEE		42.6323663014
658PhosphorylationECRVRFLSFMGVGKD
EEEEHHHHHCCCCCC		15.5221406692
716PhosphorylationCLVARPPSQKVRPPP
HEEECCCCCCCCCCC		45.3725159151
717 (in isoform 4)Phosphorylation-54.7824719451
728PhosphorylationPPPPPADSVTRRVTT
CCCCCCCCCCCCHHH		27.7428555341
743PhosphorylationNVKRGVLSLIDTLKQ
HHHHHHHHHHHHHHH		22.3727251275
744 (in isoform 4)Phosphorylation-3.4327251275
747PhosphorylationGVLSLIDTLKQKRPV
HHHHHHHHHHHHCCC		28.94-
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 APBB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APBB2_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 APBB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
14527950
HSP7C_HUMANHSPA8physical
26186194
TBCD4_HUMANTBC1D4physical
26186194
OSBL2_HUMANOSBPL2physical
26186194
A4_HUMANAPPphysical
26186194
APLP2_HUMANAPLP2physical
26186194
APBB1_HUMANAPBB1physical
26186194
AKAP1_HUMANAKAP1physical
26186194
GOPC_HUMANGOPCphysical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
APLP1_HUMANAPLP1physical
26186194
CBWD1_HUMANCBWD1physical
26186194
APOL2_HUMANAPOL2physical
26186194
GDS1_HUMANRAP1GDS1physical
26186194
SYDE2_HUMANSYDE2physical
26186194
ATP7A_HUMANATP7Aphysical
26186194
WDR41_HUMANWDR41physical
26186194
TBD2B_HUMANTBC1D2Bphysical
26186194
FMN2_HUMANFMN2physical
26186194
APLP1_HUMANAPLP1physical
28514442
SYDE2_HUMANSYDE2physical
28514442
APLP2_HUMANAPLP2physical
28514442
A4_HUMANAPPphysical
28514442
ATP7A_HUMANATP7Aphysical
28514442
AKAP1_HUMANAKAP1physical
28514442
OSBL2_HUMANOSBPL2physical
28514442
WDR41_HUMANWDR41physical
28514442
APBB1_HUMANAPBB1physical
28514442
GOPC_HUMANGOPCphysical
28514442
APOL2_HUMANAPOL2physical
28514442
TBD2B_HUMANTBC1D2Bphysical
28514442
FMN2_HUMANFMN2physical
28514442
TBCD4_HUMANTBC1D4physical
28514442
HGFA_HUMANHGFACphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
GDS1_HUMANRAP1GDS1physical
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 APBB2_HUMAN

loading...

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-336; THR-339 ANDTHR-343, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory