APBA2_HUMAN - dbPTM
APBA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APBA2_HUMAN
UniProt AC Q99767
Protein Name Amyloid-beta A4 precursor protein-binding family A member 2
Gene Name APBA2
Organism Homo sapiens (Human).
Sequence Length 749
Subcellular Localization
Protein Description Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta..
Protein Sequence MAHRKLESVGSGMLDHRVRPGPVPHSQEPESEDMELPLEGYVPEGLELAALRPESPAPEEQECHNHSPDGDSSSDYVNNTSEEEDYDEGLPEEEEGITYYIRYCPEDDSYLEGMDCNGEEYLAHSAHPVDTDECQEAVEEWTDSAGPHPHGHEAEGSQDYPDGQLPIPEDEPSVLEAHDQEEDGHYCASKEGYQDYYPEEANGNTGASPYRLRRGDGDLEDQEEDIDQIVAEIKMSLSMTSITSASEASPEHGPEPGPEDSVEACPPIKASCSPSRHEARPKSLNLLPEAKHPGDPQRGFKPKTRTPEERLKWPHEQVCNGLEQPRKQQRSDLNGPVDNNNIPETKKVASFPSFVAVPGPCEPEDLIDGIIFAANYLGSTQLLSERNPSKNIRMMQAQEAVSRVKRMQKAAKIKKKANSEGDAQTLTEVDLFISTQRIKVLNADTQETMMDHALRTISYIADIGNIVVLMARRRMPRSASQDCIETTPGAQEGKKQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDIINTQEMYNDDLIHFSNSENCKELQLEKHKGEILGVVVVESGWGSILPTVILANMMNGGPAARSGKLSIGDQIMSINGTSLVGLPLATCQGIIKGLKNQTQVKLNIVSCPPVTTVLIKRPDLKYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATAHEKIVQALSNSVGEIHMKTMPAAMFRLLTGQETPLYI
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
8PhosphorylationMAHRKLESVGSGMLD
CCCCCCCCCCCCCCC		42.0629255136
11PhosphorylationRKLESVGSGMLDHRV
CCCCCCCCCCCCCCC		20.9029255136
55PhosphorylationLAALRPESPAPEEQE
EEEECCCCCCCCCHH		29.1026074081
74PhosphorylationSPDGDSSSDYVNNTS
CCCCCCCCCCCCCCC		36.5922468782
186PhosphorylationDQEEDGHYCASKEGY
CCCCCCCCCCCCCCC		8.67-
193PhosphorylationYCASKEGYQDYYPEE
CCCCCCCCCCCCCHH		10.17-
196PhosphorylationSKEGYQDYYPEEANG
CCCCCCCCCCHHHCC		12.85-
197PhosphorylationKEGYQDYYPEEANGN
CCCCCCCCCHHHCCC		16.68-
205PhosphorylationPEEANGNTGASPYRL
CHHHCCCCCCCCCCC		35.2127732954
208PhosphorylationANGNTGASPYRLRRG
HCCCCCCCCCCCCCC		24.6515345747
210PhosphorylationGNTGASPYRLRRGDG
CCCCCCCCCCCCCCC		21.5627732954
236PhosphorylationIVAEIKMSLSMTSIT
HHHHHHHHHHCCCCC		16.5829978859
238PhosphorylationAEIKMSLSMTSITSA
HHHHHHHHCCCCCCC		16.8329978859
240PhosphorylationIKMSLSMTSITSASE
HHHHHHCCCCCCCHH		17.3829978859
241PhosphorylationKMSLSMTSITSASEA
HHHHHCCCCCCCHHC		18.4128348404
243PhosphorylationSLSMTSITSASEASP
HHHCCCCCCCHHCCC		20.2928348404
244PhosphorylationLSMTSITSASEASPE
HHCCCCCCCHHCCCC		28.2928348404
246PhosphorylationMTSITSASEASPEHG
CCCCCCCHHCCCCCC		33.2024076635
249PhosphorylationITSASEASPEHGPEP
CCCCHHCCCCCCCCC		27.1128348404
261PhosphorylationPEPGPEDSVEACPPI
CCCCCHHCCCCCCCC		21.8626074081
271PhosphorylationACPPIKASCSPSRHE
CCCCCCCCCCCCHHH		15.3226074081
273PhosphorylationPPIKASCSPSRHEAR
CCCCCCCCCCHHHCC		24.3423403867
275PhosphorylationIKASCSPSRHEARPK
CCCCCCCCHHHCCCC		29.9426074081
283PhosphorylationRHEARPKSLNLLPEA
HHHCCCCHHCCCCCC		25.7729978859
306PhosphorylationGFKPKTRTPEERLKW
CCCCCCCCHHHHHCC		40.04-
346UbiquitinationNNNIPETKKVASFPS
CCCCCCCCCCCCCCC		43.52-
347UbiquitinationNNIPETKKVASFPSF
CCCCCCCCCCCCCCE		50.91-
419PhosphorylationKIKKKANSEGDAQTL
HHHHHHCCCCCCCHH		48.0622210691
425PhosphorylationNSEGDAQTLTEVDLF
CCCCCCCHHHHHEEE		37.0522210691
427PhosphorylationEGDAQTLTEVDLFIS
CCCCCHHHHHEEEEE		37.0322210691
478PhosphorylationARRRMPRSASQDCIE
CCCCCCCCCCCCCHH		26.8030631047
480PhosphorylationRRMPRSASQDCIETT
CCCCCCCCCCCHHCC		28.0023401153
486PhosphorylationASQDCIETTPGAQEG
CCCCCHHCCCCCCHH		20.5523403867
487PhosphorylationSQDCIETTPGAQEGK
CCCCHHCCCCCCHHH		13.6123403867
609PhosphorylationNGGPAARSGKLSIGD
CCCCCHHCCCCCCCC		35.2430576142
613PhosphorylationAARSGKLSIGDQIMS
CHHCCCCCCCCEEEE		28.1930576142
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 APBA2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APBA2_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 APBA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSTN1_HUMANCLSTN1physical
12972431
A4_HUMANAPPphysical
12972431
NECA3_HUMANNECAB3physical
10833507
TF65_HUMANRELAphysical
10777610
A4_HUMANAPPphysical
9890987
STXB1_HUMANSTXBP1physical
15563604
APBA1_HUMANAPBA1physical
28514442
UBP20_HUMANUSP20physical
28514442
IQEC2_HUMANIQSEC2physical
28514442
TJAP1_HUMANTJAP1physical
28514442
IQEC1_HUMANIQSEC1physical
28514442
AAGAB_HUMANAAGABphysical
28514442
FBW1A_HUMANBTRCphysical
28514442
UBP33_HUMANUSP33physical
28514442
PLD1_HUMANPLD1physical
28514442
FBW1B_HUMANFBXW11physical
28514442
DMWD_HUMANDMWDphysical
28514442
NECA3_HUMANNECAB3physical
28514442
Z518A_HUMANZNF518Aphysical
28514442
DDX24_HUMANDDX24physical
28514442
HERC2_HUMANHERC2physical
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 APBA2_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-478 AND SER-480, ANDMASS SPECTROMETRY.

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