AP1B1_HUMAN - dbPTM
AP1B1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP1B1_HUMAN
UniProt AC Q10567
Protein Name AP-1 complex subunit beta-1
Gene Name AP1B1
Organism Homo sapiens (Human).
Sequence Length 949
Subcellular Localization Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side. 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 MTDSKYFTTTKKGEIFELKAELNSDKKEKKKEAVKKVIASMTVGKDVSALFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNTFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQLVEDQGFLDTLKDLISDSNPMVVANAVAALSEIAESHPSSNLLDLNPQSINKLLTALNECTEWGQIFILDCLANYMPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFMEMLSKDLDYYGTLLKKLAPPLVTLLSAEPELQYVALRNINLIVQKRPEILKHEMKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIKDIFRKYPNKYESVIATLCENLDSLDEPEARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLQLLTAIVKLFLKKPTETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVAAKEVVLAEKPLISEETDLIEPTLLDELICYIGTLASVYHKPPSAFVEGGRGVVHKSLPPRTASSESAESPETAPTGAPPGEQPDVIPAQGDLLGDLLNLDLGPPVSGPPLATSSVQMGAVDLLGGGLDSLMGDEPEGIGGTNFVAPPTAAVPANLGAPIGSGLSDLFDLTSGVGTLSGSYVAPKAVWLPAMKAKGLEISGTFTRQVGSISMDLQLTNKALQVMTDFAIQFNRNSFGLAPATPLQVHAPLSPNQTVEISLPLSTVGSVMKMEPLNNLQVAVKNNIDVFYFSTLYPLHILFVEDGKMDRQMFLATWKDIPNENEAQFQIRDCPLNAEAASSKLQSSNIFTVAKRNVEGQDMLYQSLKLTNGIWVLAELRIQPGNPSCTDLELSLKCRAPEVSQHVYQAYETILKN
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
49.3217192257
4Phosphorylation----MTDSKYFTTTK
----CCCCCCEECCC
21.7925002506
5Ubiquitination---MTDSKYFTTTKK
---CCCCCCEECCCC
47.3923000965
5 (in isoform 3)Ubiquitination-47.39-
6Phosphorylation--MTDSKYFTTTKKG
--CCCCCCEECCCCC
15.3129759185
8PhosphorylationMTDSKYFTTTKKGEI
CCCCCCEECCCCCEE
30.3928060719
9PhosphorylationTDSKYFTTTKKGEIF
CCCCCEECCCCCEEE
27.0728857561
10PhosphorylationDSKYFTTTKKGEIFE
CCCCEECCCCCEEEE
27.9228857561
112-HydroxyisobutyrylationSKYFTTTKKGEIFEL
CCCEECCCCCEEEEE
57.60-
11UbiquitinationSKYFTTTKKGEIFEL
CCCEECCCCCEEEEE
57.6023000965
12UbiquitinationKYFTTTKKGEIFELK
CCEECCCCCEEEEEE
60.7333845483
12 (in isoform 3)Malonylation-60.7326320211
12 (in isoform 3)Ubiquitination-60.73-
24PhosphorylationELKAELNSDKKEKKK
EEECHHCCCHHHHHH
64.5350565767
31UbiquitinationSDKKEKKKEAVKKVI
CCHHHHHHHHHHHHH
63.07-
35UbiquitinationEKKKEAVKKVIASMT
HHHHHHHHHHHHHHC
48.66-
40PhosphorylationAVKKVIASMTVGKDV
HHHHHHHHHCCCCCH
12.1225954137
42PhosphorylationKKVIASMTVGKDVSA
HHHHHHHCCCCCHHH
24.5025954137
60UbiquitinationDVVNCMQTDNLELKK
HHHHHHCCCCHHHHH
10.4429901268
70PhosphorylationLELKKLVYLYLMNYA
HHHHHHHHHHHHHHH
10.4824260401
74UbiquitinationKLVYLYLMNYAKSQP
HHHHHHHHHHHHHCC
1.9733845483
76PhosphorylationVYLYLMNYAKSQPDM
HHHHHHHHHHHCCCC
11.0524260401
79PhosphorylationYLMNYAKSQPDMAIM
HHHHHHHHCCCCEEH
38.4820068231
90PhosphorylationMAIMAVNTFVKDCED
CEEHHHHHHHHHCCC
24.1746164897
90UbiquitinationMAIMAVNTFVKDCED
CEEHHHHHHHHHCCC
24.1732015554
95GlutathionylationVNTFVKDCEDPNPLI
HHHHHHHCCCCCHHH
5.4622555962
95S-palmitoylationVNTFVKDCEDPNPLI
HHHHHHHCCCCCHHH
5.4626865113
117UbiquitinationMGCIRVDKITEYLCE
CCCEEHHHHHHHHHH
48.9821890473
117UbiquitinationMGCIRVDKITEYLCE
CCCEEHHHHHHHHHH
48.9822817900
117 (in isoform 1)Ubiquitination-48.9821890473
117 (in isoform 2)Ubiquitination-48.9821890473
117 (in isoform 3)Ubiquitination-48.98-
117UbiquitinationMGCIRVDKITEYLCE
CCCEEHHHHHHHHHH
48.9821890473
117UbiquitinationMGCIRVDKITEYLCE
CCCEEHHHHHHHHHH
48.9821890473
119PhosphorylationCIRVDKITEYLCEPL
CEEHHHHHHHHHHHH
25.0728152594
121PhosphorylationRVDKITEYLCEPLRK
EHHHHHHHHHHHHHH
14.1728152594
123GlutathionylationDKITEYLCEPLRKCL
HHHHHHHHHHHHHHC
5.0422555962
128UbiquitinationYLCEPLRKCLKDEDP
HHHHHHHHHCCCCCH
52.1523503661
129GlutathionylationLCEPLRKCLKDEDPY
HHHHHHHHCCCCCHH
4.6422555962
131UbiquitinationEPLRKCLKDEDPYVR
HHHHHHCCCCCHHHH
69.4233845483
131 (in isoform 3)Ubiquitination-69.42-
136PhosphorylationCLKDEDPYVRKTAAV
HCCCCCHHHHHHHHH
25.8082609
138MethylationKDEDPYVRKTAAVCV
CCCCHHHHHHHHHHH
25.43-
139UbiquitinationDEDPYVRKTAAVCVA
CCCHHHHHHHHHHHH
32.2627667366
147UbiquitinationTAAVCVAKLHDINAQ
HHHHHHHHHHHHCHH
26.4232015554
245PhosphorylationQSICERVTPRLSHAN
HHHHHHHCCCCCCCC
14.6515994073
249PhosphorylationERVTPRLSHANSAVV
HHHCCCCCCCCHHHH
23.1025332170
258PhosphorylationANSAVVLSAVKVLMK
CCHHHHHHHHHHHHH
21.2925332170
272UbiquitinationKFMEMLSKDLDYYGT
HHHHHHHCCCCHHHH
59.3522817900
272 (in isoform 1)Ubiquitination-59.3521890473
272 (in isoform 2)Ubiquitination-59.3521890473
276PhosphorylationMLSKDLDYYGTLLKK
HHHCCCCHHHHHHHH
15.8726074081
277PhosphorylationLSKDLDYYGTLLKKL
HHCCCCHHHHHHHHH
11.8726074081
279PhosphorylationKDLDYYGTLLKKLAP
CCCCHHHHHHHHHHC
16.8830815383
282UbiquitinationDYYGTLLKKLAPPLV
CHHHHHHHHHHCCHH
49.1821890473
2822-HydroxyisobutyrylationDYYGTLLKKLAPPLV
CHHHHHHHHHHCCHH
49.18-
282UbiquitinationDYYGTLLKKLAPPLV
CHHHHHHHHHHCCHH
49.1821890473
282 (in isoform 1)Ubiquitination-49.1821890473
282 (in isoform 2)Ubiquitination-49.1821890473
282UbiquitinationDYYGTLLKKLAPPLV
CHHHHHHHHHHCCHH
49.1821890473
282UbiquitinationDYYGTLLKKLAPPLV
CHHHHHHHHHHCCHH
49.1821890473
300PhosphorylationSAEPELQYVALRNIN
CCCHHHHHHHHHCCC
10.58110749201
318AcetylationQKRPEILKHEMKVFF
ECCHHHHCCCEEEEE
43.0819608861
322AcetylationEILKHEMKVFFVKYN
HHHCCCEEEEEEECC
32.6722424773
328PhosphorylationMKVFFVKYNDPIYVK
EEEEEEECCCCEEEE
21.3528152594
333PhosphorylationVKYNDPIYVKLEKLD
EECCCCEEEEHHHHH
9.27110749209
335UbiquitinationYNDPIYVKLEKLDIM
CCCCEEEEHHHHHHH
33.6821906983
335 (in isoform 1)Ubiquitination-33.6821890473
335 (in isoform 2)Ubiquitination-33.6821890473
359UbiquitinationAQVLAELKEYATEVD
HHHHHHHHHHHCCCC
39.9416196087
361PhosphorylationVLAELKEYATEVDVD
HHHHHHHHHCCCCHH
19.7520068231
363PhosphorylationAELKEYATEVDVDFV
HHHHHHHCCCCHHHH
35.3220068231
383UbiquitinationAIGRCAIKVEQSAER
HHHHHEEEHHHHHHH
22.6124816145
383 (in isoform 3)Ubiquitination-22.61-
393PhosphorylationQSAERCVSTLLDLIQ
HHHHHHHHHHHHHHH
19.5728857561
394PhosphorylationSAERCVSTLLDLIQT
HHHHHHHHHHHHHHH
15.7929083192
401PhosphorylationTLLDLIQTKVNYVVQ
HHHHHHHHHHHHHHH
29.9329083192
481UbiquitinationHDESTQVQLQLLTAI
CCCCHHHHHHHHHHH
17.4233845483
497PhosphorylationKLFLKKPTETQELVQ
HHHCCCCCHHHHHHH
61.6229978859
499PhosphorylationFLKKPTETQELVQQV
HCCCCCHHHHHHHHH
29.8029978859
508PhosphorylationELVQQVLSLATQDSD
HHHHHHHHHHHCCCC
19.6629978859
511PhosphorylationQQVLSLATQDSDNPD
HHHHHHHHCCCCCCC
37.9029978859
514PhosphorylationLSLATQDSDNPDLRD
HHHHHCCCCCCCHHH
29.4829978859
524PhosphorylationPDLRDRGYIYWRLLS
CCHHHHCEEEEEECC
7.547458789
531PhosphorylationYIYWRLLSTDPVAAK
EEEEEECCCCCCCHH
35.0428450419
532PhosphorylationIYWRLLSTDPVAAKE
EEEEECCCCCCCHHH
44.2728450419
534UbiquitinationWRLLSTDPVAAKEVV
EEECCCCCCCHHHHH
20.1029901268
538UbiquitinationSTDPVAAKEVVLAEK
CCCCCCHHHHHHCCC
41.1033845483
574Nitrated tyrosineIGTLASVYHKPPSAF
HHHHHHHHCCCCHHH
11.13-
574NitrationIGTLASVYHKPPSAF
HHHHHHHHCCCCHHH
11.13-
591UbiquitinationGGRGVVHKSLPPRTA
CCCCCEECCCCCCCC
41.9223000965
592PhosphorylationGRGVVHKSLPPRTAS
CCCCEECCCCCCCCC
31.0924719451
597PhosphorylationHKSLPPRTASSESAE
ECCCCCCCCCCCCCC
36.3418423515
599PhosphorylationSLPPRTASSESAESP
CCCCCCCCCCCCCCC
33.7424275569
600PhosphorylationLPPRTASSESAESPE
CCCCCCCCCCCCCCC
32.8618423525
602PhosphorylationPRTASSESAESPETA
CCCCCCCCCCCCCCC
39.0118423535
605PhosphorylationASSESAESPETAPTG
CCCCCCCCCCCCCCC
27.9669013251
661UbiquitinationGAVDLLGGGLDSLMG
CCHHHHCCCHHHHCC
33.2033845483
666UbiquitinationLGGGLDSLMGDEPEG
HCCCHHHHCCCCCCC
4.4333845483
673UbiquitinationLMGDEPEGIGGTNFV
HCCCCCCCCCCCCCC
34.2633845483
723UbiquitinationYVAPKAVWLPAMKAK
EECCCEEEHHHHHCC
11.0733845483
727SulfoxidationKAVWLPAMKAKGLEI
CEEEHHHHHCCCCEE
4.0230846556
728AcetylationAVWLPAMKAKGLEIS
EEEHHHHHCCCCEEE
49.4025953088
730UbiquitinationWLPAMKAKGLEISGT
EHHHHHCCCCEEEEE
59.5233845483
735PhosphorylationKAKGLEISGTFTRQV
HCCCCEEEEEEECCC
23.5422210691
739PhosphorylationLEISGTFTRQVGSIS
CEEEEEEECCCCCEE
21.7469213769
786PhosphorylationLQVHAPLSPNQTVEI
EEEECCCCCCCEEEE
22.277968539
790PhosphorylationAPLSPNQTVEISLPL
CCCCCCCEEEEEEEC
27.0945741499
849UbiquitinationDRQMFLATWKDIPNE
CHHHEEEECCCCCCC
34.8829967540
860UbiquitinationIPNENEAQFQIRDCP
CCCCCCHHHEEECCC
25.3021890473
860UbiquitinationIPNENEAQFQIRDCP
CCCCCCHHHEEECCC
25.3021890473
869UbiquitinationQIRDCPLNAEAASSK
EEECCCCCHHHHHHH
22.3729967540
869 (in isoform 3)Ubiquitination-22.37-
876UbiquitinationNAEAASSKLQSSNIF
CHHHHHHHCHHCCCE
48.3129967540
879PhosphorylationAASSKLQSSNIFTVA
HHHHHCHHCCCEEEE
35.4746164879
880UbiquitinationASSKLQSSNIFTVAK
HHHHCHHCCCEEEEE
22.4521890473
880PhosphorylationASSKLQSSNIFTVAK
HHHHCHHCCCEEEEE
22.4546164885
880UbiquitinationASSKLQSSNIFTVAK
HHHHCHHCCCEEEEE
22.4521890473
880 (in isoform 2)Ubiquitination-22.4521890473
880 (in isoform 3)Malonylation-22.4526320211
880 (in isoform 3)Ubiquitination-22.45-
880UbiquitinationASSKLQSSNIFTVAK
HHHHCHHCCCEEEEE
22.4521890473
8872-HydroxyisobutyrylationSNIFTVAKRNVEGQD
CCCEEEEECCCCCHH
39.92-
887UbiquitinationSNIFTVAKRNVEGQD
CCCEEEEECCCCCHH
39.9227667366
887 (in isoform 1)Ubiquitination-39.9221890473
897PhosphorylationVEGQDMLYQSLKLTN
CCCHHHHHHHHCCCC
6.8727259358
899PhosphorylationGQDMLYQSLKLTNGI
CHHHHHHHHCCCCCE
17.57-
919 (in isoform 3)Ubiquitination-36.37-

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP1B1_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 AP1B1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP1G1_HUMANAP1G1physical
9733768
ARF1_HUMANARF1physical
11926829
AMPH_HUMANAMPHphysical
9280305
KI13A_HUMANKIF13Aphysical
11106728
AP2M1_HUMANAP2M1physical
7593184
AP1M1_HUMANAP1M1physical
7593184
AP1G1_HUMANAP1G1physical
22939629
AP1M1_HUMANAP1M1physical
22939629
AP1S2_HUMANAP1S2physical
22939629
AP1S1_HUMANAP1S1physical
22939629
NTRK2_HUMANNTRK2physical
21988832
INT9_HUMANINTS9physical
22863883
TBD2A_HUMANTBC1D2physical
22863883
CIP4_HUMANTRIP10physical
22863883
TRM61_HUMANTRMT61Aphysical
22863883
AP1S1_HUMANAP1S1physical
26344197
AP1S2_HUMANAP1S2physical
26344197
RHG01_HUMANARHGAP1physical
26344197
FLNB_HUMANFLNBphysical
26344197
AAKB1_HUMANPRKAB1physical
26344197
TTC37_HUMANTTC37physical
26344197
UBA1_HUMANUBA1physical
26344197

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 AP1B1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-897, AND MASSSPECTROMETRY.

TOP