APBA1_MOUSE - dbPTM
APBA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APBA1_MOUSE
UniProt AC B2RUJ5
Protein Name Amyloid-beta A4 precursor protein-binding family A member 1
Gene Name Apba1
Organism Mus musculus (Mouse).
Sequence Length 842
Subcellular Localization Cytoplasm. Cytoplasm, perinuclear region. Nucleus.
Isoform 3: Golgi apparatus.
Protein Description Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of AAP-beta (By similarity)..
Protein Sequence MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVVEGQQPSPSPPPPAGHEPEDHRGHPAPPPPPPPQEEEEEERGECLARSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHVEAAQRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGLPAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPVDGDSPSPGSSSPLGAESSSIPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI
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
82PhosphorylationRGECLARSASTESGF
HHCCCHHHCCCCCCC
22.4427742792
84PhosphorylationECLARSASTESGFHN
CCCHHHCCCCCCCCC
33.6725521595
85PhosphorylationCLARSASTESGFHNH
CCHHHCCCCCCCCCC
33.6127742792
87PhosphorylationARSASTESGFHNHTD
HHHCCCCCCCCCCCC
47.0125521595
93PhosphorylationESGFHNHTDTAEGDV
CCCCCCCCCCCCCCH
40.1230372032
95PhosphorylationGFHNHTDTAEGDVLA
CCCCCCCCCCCCHHH
27.9726160508
158PhosphorylationPNHLHFHSLEHEEAM
CCCCCCCCCCCHHHH
34.2122817900
187PhosphorylationHRAEDEPYAEPYADY
CCCCCCCCCCCCCCC
22.88-
191PhosphorylationDEPYAEPYADYGGLQ
CCCCCCCCCCCCCHH
12.01-
202PhosphorylationGGLQEHVYEEIGDAP
CCHHHHHHHHHCCCC
15.11-
242PhosphorylationLGARLHHYDERSDGE
HHHHHCCCCCCCCCC
14.5722324799
246PhosphorylationLHHYDERSDGESDSP
HCCCCCCCCCCCCCH
48.1725521595
250PhosphorylationDERSDGESDSPEKEA
CCCCCCCCCCHHHHH
49.2525521595
252PhosphorylationRSDGESDSPEKEAEF
CCCCCCCCHHHHHHC
44.2125521595
262PhosphorylationKEAEFAPYPRMDSYE
HHHHCCCCCCCCCCC
10.4720415495
267PhosphorylationAPYPRMDSYEQEEDI
CCCCCCCCCCCCCCH
22.6425521595
268PhosphorylationPYPRMDSYEQEEDID
CCCCCCCCCCCCCHH
19.8425521595
284PhosphorylationIVAEVKQSMSSQSLD
HHHHHHHHHCHHHHH
18.2123737553
286PhosphorylationAEVKQSMSSQSLDKA
HHHHHHHCHHHHHHH
30.3925521595
287PhosphorylationEVKQSMSSQSLDKAA
HHHHHHCHHHHHHHH
18.3625521595
289PhosphorylationKQSMSSQSLDKAAED
HHHHCHHHHHHHHHH
40.2525521595
309PhosphorylationQDLERAPTPGGGHPD
HHHHHCCCCCCCCCC
33.3125521595
317PhosphorylationPGGGHPDSPGLPAPA
CCCCCCCCCCCCCCC
25.8925521595
333PhosphorylationQQQRVVGTPGGSEVG
CCCCEEECCCCCHHH
13.7222324799
337PhosphorylationVVGTPGGSEVGQRYS
EEECCCCCHHHHHHC
34.7229899451
344PhosphorylationSEVGQRYSKEKRDAI
CHHHHHHCHHHHHHH
36.2125338131
366UbiquitinationKEAIEEVKTRTIRSP
HHHHHHHHHCCCCCC
35.2527667366
367PhosphorylationEAIEEVKTRTIRSPY
HHHHHHHHCCCCCCC
37.9222324799
369PhosphorylationIEEVKTRTIRSPYTP
HHHHHHCCCCCCCCC
26.4419060867
372PhosphorylationVKTRTIRSPYTPDEP
HHHCCCCCCCCCCCC
20.5722324799
374PhosphorylationTRTIRSPYTPDEPKE
HCCCCCCCCCCCCCC
31.9522324799
375PhosphorylationRTIRSPYTPDEPKEP
CCCCCCCCCCCCCCC
27.8725521595
393PhosphorylationMRQDISPTRDCDDQR
EECCCCCCCCCCCCC
32.14-
406PhosphorylationQRPVDGDSPSPGSSS
CCCCCCCCCCCCCCC
32.5722817900
408PhosphorylationPVDGDSPSPGSSSPL
CCCCCCCCCCCCCCC
45.9325521595
411PhosphorylationGDSPSPGSSSPLGAE
CCCCCCCCCCCCCCC
30.9025293948
412PhosphorylationDSPSPGSSSPLGAES
CCCCCCCCCCCCCCC
41.7225293948
413PhosphorylationSPSPGSSSPLGAESS
CCCCCCCCCCCCCCC
26.3322817900
419PhosphorylationSSPLGAESSSIPLHP
CCCCCCCCCCCCCCC
28.9325293948
420PhosphorylationSPLGAESSSIPLHPG
CCCCCCCCCCCCCCC
24.6425293948
421PhosphorylationPLGAESSSIPLHPGD
CCCCCCCCCCCCCCC
37.1925293948
571PhosphorylationARRRMPRSNSQENVE
CCCCCCCCCCCCCCC
34.6627742792
573PhosphorylationRRMPRSNSQENVEAS
CCCCCCCCCCCCCCC
39.8725521595
580PhosphorylationSQENVEASHPSQDGK
CCCCCCCCCCCCCHH
23.5627742792
599PhosphorylationMICHVFESEDAQLIA
EEEEEECCHHHHHHH
29.3420047950
617PhosphorylationGQAFSVAYQEFLRAN
HHHHHHHHHHHHHHC
13.35-

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
187YPhosphorylationKinaseSRCQ9WUD9
PSP
191YPhosphorylationKinaseSRCQ9WUD9
PSP
202YPhosphorylationKinaseSRCQ9WUD9
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APBA1_MOUSE !!

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 APBA1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LIPA2_MOUSEPpfia2physical
16186258
CSKP_MOUSECaskphysical
9822620

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APBA1_MOUSE

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Related Literatures of Post-Translational Modification

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