AP1B1_MOUSE - dbPTM
AP1B1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP1B1_MOUSE
UniProt AC O35643
Protein Name AP-1 complex subunit beta-1
Gene Name Ap1b1
Organism Mus musculus (Mouse).
Sequence Length 943
Subcellular Localization Cytoplasmic vesicle, clathrin-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Golgi apparatus. Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex..
Protein Description Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules..
Protein Sequence MTDSKYFTTTKKGEIFELKAELNSDKKEKKKEAVKKVIASMTVGKDVSALFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNTFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQLVEDQGFLDTLKDLISDSNPMVVANAVAALSEIAESHPSSNLLDLNPQSINKLLTALNECTEWGQIFILDCLANYMPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFMEMLSKDLDYYATLLKKLAPPLVTLLSAEPELQYVALRNINLIVQKRPEILKHEMKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIKDIFRKYPNKYESVIATLCENLDSLDEPEARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLQLLTAIVKLFLKKPTETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVAAKEVVLAEKPLISEETDLIEPTLLDELICYIGTLASVYHKPPNAFVEGGRGVVHKSLPPRTASSESTESPETAPAGAPAGDQPDVIPAQGDLLGDLLNLDLGPPVSGPPLAASSVQMGAVDLLGGGLDSLIGDSNFGAPSASVAAAPAPARLGAPISSGLSDLFDLTSGVGTLSGSYVAPKAVWLPAMKAKGLEISGTFTRQAGSISMDLQLTNKALQVMTDFAIQFNRNSFGLAPAAPLQVHVPLSPNQTVEISLPLNTVGSVLKMEPLNNLQVAVKNNIDVFYFSTLYPLHVLFVEDGKMDRQMFLATWKDIANENEAQFQIRDCPLNTEAASNKLQSSNIFTVAKRNVEGQDMLYQSLKLTNGIWVLAELRIQPGNPSFTLSLKCRAPEVSQHVYQAYETILKN
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
2Phosphorylation------MTDSKYFTT
------CCCCCCEEC		49.3229176673
4Phosphorylation----MTDSKYFTTTK
----CCCCCCEECCC		21.7929176673
5Acetylation---MTDSKYFTTTKK
---CCCCCCEECCCC		47.3923954790
12UbiquitinationKYFTTTKKGEIFELK
CCEECCCCCEEEEEE		60.73-
12MalonylationKYFTTTKKGEIFELK
CCEECCCCCEEEEEE		60.7326320211
117UbiquitinationMGCIRVDKITEYLCE
CCCEEHHHHHHHHHH		48.98-
117AcetylationMGCIRVDKITEYLCE
CCCEEHHHHHHHHHH		48.9822826441
131UbiquitinationEPLRKCLKDEDPYVR
HHHHHHCCCCCHHHH		69.42-
136PhosphorylationCLKDEDPYVRKTAAV
HCCCCCHHHHHHHHH		25.8075165
144GlutathionylationVRKTAAVCVAKLHDI
HHHHHHHHHHHHHHH		1.8024333276
239PhosphorylationKDDREAQSICERVTP
CCHHHHHHHHHHHCC		35.9329899451
249PhosphorylationERVTPRLSHANSAVV
HHHCCCCCCCCHHHH		23.1015994067
253PhosphorylationPRLSHANSAVVLSAV
CCCCCCCHHHHHHHH		24.1922807455
258PhosphorylationANSAVVLSAVKVLMK
CCHHHHHHHHHHHHH		21.29-
265AcetylationSAVKVLMKFMEMLSK
HHHHHHHHHHHHHHC		37.0822826441
277PhosphorylationLSKDLDYYATLLKKL
HHCCHHHHHHHHHHH		7.87138775
282AcetylationDYYATLLKKLAPPLV
HHHHHHHHHHCHHHH		49.1823954790
282UbiquitinationDYYATLLKKLAPPLV
HHHHHHHHHHCHHHH		49.18-
282SuccinylationDYYATLLKKLAPPLV
HHHHHHHHHHCHHHH		49.1823954790
318MalonylationQKRPEILKHEMKVFF
ECCHHHHCCCEEEEE		43.0826320211
318AcetylationQKRPEILKHEMKVFF
ECCHHHHCCCEEEEE		43.08-
322AcetylationEILKHEMKVFFVKYN
HHHCCCEEEEEEECC		32.6723954790
327AcetylationEMKVFFVKYNDPIYV
CEEEEEEECCCCEEE		32.9366700615
335AcetylationYNDPIYVKLEKLDIM
CCCCEEEEHHHHHHH		33.6822826441
347PhosphorylationDIMIRLASQANIAQV
HHHHHHHCCCCHHHH		34.1220415495
380S-palmitoylationAVRAIGRCAIKVEQS
HHHHHHHHEEEHHHH		3.7526165157
393PhosphorylationQSAERCVSTLLDLIQ
HHHHHHHHHHHHHHH		19.5730993257
394PhosphorylationSAERCVSTLLDLIQT
HHHHHHHHHHHHHHH		15.7929899451
538UbiquitinationSTDPVAAKEVVLAEK
CCCCCCHHHHHHCCC		41.10-
574Nitrated tyrosineIGTLASVYHKPPNAF
HHHHHHHHCCCCCCE		11.13-
574NitrationIGTLASVYHKPPNAF
HHHHHHHHCCCCCCE		11.1316800626
574NitrationIGTLASVYHKPPNAF
HHHHHHHHCCCCCCE		11.1316800626
591UbiquitinationGGRGVVHKSLPPRTA
CCCCCCCCCCCCCCC		41.92-
693PhosphorylationARLGAPISSGLSDLF
HHCCCCCCCCCHHHH		19.7923984901
694PhosphorylationRLGAPISSGLSDLFD
HCCCCCCCCCHHHHH		44.4623984901
697PhosphorylationAPISSGLSDLFDLTS
CCCCCCCHHHHHCCC		35.4723984901
703PhosphorylationLSDLFDLTSGVGTLS
CHHHHHCCCCCCCCC		25.8623984901
704PhosphorylationSDLFDLTSGVGTLSG
HHHHHCCCCCCCCCC		38.4926643407
710PhosphorylationTSGVGTLSGSYVAPK
CCCCCCCCCCEECCC		26.0730352176
712PhosphorylationGVGTLSGSYVAPKAV
CCCCCCCCEECCCEE		17.0422871156
725UbiquitinationAVWLPAMKAKGLEIS
EEEHHHHHCCCCEEE		49.40-
767PhosphorylationAIQFNRNSFGLAPAA
HHHCCCCCCCCCCCC		19.9020415495
783PhosphorylationLQVHVPLSPNQTVEI
EEEECCCCCCCEEEE		18.7420415495
787PhosphorylationVPLSPNQTVEISLPL
CCCCCCCEEEEEEEC		27.0923984901
791PhosphorylationPNQTVEISLPLNTVG
CCCEEEEEEECCCCC		15.4923984901
796PhosphorylationEISLPLNTVGSVLKM
EEEEECCCCCCEEEE		33.6520415495
799PhosphorylationLPLNTVGSVLKMEPL
EECCCCCCEEEEEEC		21.6820415495
863S-nitrosylationAQFQIRDCPLNTEAA
HHHEEECCCCCHHHH		2.7221278135
863S-nitrosocysteineAQFQIRDCPLNTEAA
HHHEEECCCCCHHHH		2.72-
884UbiquitinationSNIFTVAKRNVEGQD
CCCEEEEECCCCCHH		39.92-
894PhosphorylationVEGQDMLYQSLKLTN
CCCHHHHHHHHCCCC		6.8775177
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 AP1B1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP1B1_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 AP1B1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AP1B1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP1B1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Nitration
ReferencePubMed
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease.";
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.;
Biochemistry 45:8009-8022(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-574, AND MASS SPECTROMETRY.

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