AP2B1_HUMAN - dbPTM
AP2B1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP2B1_HUMAN
UniProt AC P63010
Protein Name AP-2 complex subunit beta
Gene Name AP2B1
Organism Homo sapiens (Human).
Sequence Length 937
Subcellular Localization Cell membrane . Membrane, coated pit
Peripheral membrane protein
Cytoplasmic side . AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV.
Protein Description Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly..
Protein Sequence MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANAVAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQYVALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRKYPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEVVLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRKHLPIHHGSTDAGDSPVGTTTATNLEQPQVIPSQGDLLGDLLNLDLGPPVNVPQVSSMQMGAVDLLGGGLDSLVGQSFIPSSVPATFAPSPTPAVVSSGLNDLFELSTGIGMAPGGYVAPKAVWLPAVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIHTPLMPNQSIDVSLPLNTLGPVMKMEPLNNLQVAVKNNIDVFYFSCLIPLNVLFVEDGKMERQVFLATWKDIPNENELQFQIKECHLNADTVSSKLQNNNVYTIAKRNVEGQDMLYQSLKLTNGIWILAELRIQPGNPNYTLSLKCRAPEVSQYIYQVYDSILKN
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
2Acetylation------MTDSKYFTT
------CCCCCCCCC		49.3222814378
2Phosphorylation------MTDSKYFTT
------CCCCCCCCC		49.3223401153
2 (in isoform 2)Phosphorylation-49.3224719451
4Phosphorylation----MTDSKYFTTNK
----CCCCCCCCCCC		21.7923401153
4 (in isoform 2)Phosphorylation-21.7924719451
5Malonylation---MTDSKYFTTNKK
---CCCCCCCCCCCC		47.3926320211
5Ubiquitination---MTDSKYFTTNKK
---CCCCCCCCCCCC		47.39-
5 (in isoform 2)Ubiquitination-47.39-
6Phosphorylation--MTDSKYFTTNKKG
--CCCCCCCCCCCCC		15.3123401153
6 (in isoform 2)Phosphorylation-15.31-
8PhosphorylationMTDSKYFTTNKKGEI
CCCCCCCCCCCCCCE		26.7723401153
9PhosphorylationTDSKYFTTNKKGEIF
CCCCCCCCCCCCCEE		34.8323401153
11AcetylationSKYFTTNKKGEIFEL
CCCCCCCCCCCEEEH		61.1225953088
11MalonylationSKYFTTNKKGEIFEL
CCCCCCCCCCCEEEH		61.1226320211
11UbiquitinationSKYFTTNKKGEIFEL
CCCCCCCCCCCEEEH		61.12-
12MalonylationKYFTTNKKGEIFELK
CCCCCCCCCCEEEHH		64.9426320211
12UbiquitinationKYFTTNKKGEIFELK
CCCCCCCCCCEEEHH		64.94-
19AcetylationKGEIFELKAELNNEK
CCCEEEHHHHHCCHH		32.3920167786
19UbiquitinationKGEIFELKAELNNEK
CCCEEEHHHHHCCHH		32.39-
26AcetylationKAELNNEKKEKRKEA
HHHHCCHHHHHHHHH		69.2520167786
36MalonylationKRKEAVKKVIAAMTV
HHHHHHHHHHHHHHC		32.0726320211
41SulfoxidationVKKVIAAMTVGKDVS
HHHHHHHHHCCCCHH		2.0021406390
60UbiquitinationDVVNCMQTDNLELKK
HHHHHHCCCCHHHHH		10.4421890473
70PhosphorylationLELKKLVYLYLMNYA
HHHHHHHHHHHHHHH		10.4824260401
76PhosphorylationVYLYLMNYAKSQPDM
HHHHHHHHHHCCCCH		11.0524260401
79PhosphorylationYLMNYAKSQPDMAIM
HHHHHHHCCCCHHHH		38.4820068231
79 (in isoform 2)Phosphorylation-38.48-
90PhosphorylationMAIMAVNSFVKDCED
HHHHHHHHHHHCCCC		25.4720068231
117AcetylationMGCIRVDKITEYLCE
CCCEEHHHHHHHHHH		48.9825953088
117MalonylationMGCIRVDKITEYLCE
CCCEEHHHHHHHHHH		48.9826320211
117UbiquitinationMGCIRVDKITEYLCE
CCCEEHHHHHHHHHH		48.98-
117 (in isoform 1)Ubiquitination-48.9821890473
117 (in isoform 2)Ubiquitination-48.9821890473
119PhosphorylationCIRVDKITEYLCEPL
CEEHHHHHHHHHHHH		25.0728152594
121PhosphorylationRVDKITEYLCEPLRK
EHHHHHHHHHHHHHH		14.1728152594
123GlutathionylationDKITEYLCEPLRKCL
HHHHHHHHHHHHHHC		5.0422555962
128UbiquitinationYLCEPLRKCLKDEDP
HHHHHHHHHCCCCCH		52.15-
129GlutathionylationLCEPLRKCLKDEDPY
HHHHHHHHCCCCCHH		4.6422555962
131AcetylationEPLRKCLKDEDPYVR
HHHHHHCCCCCHHHH		69.4226051181
131UbiquitinationEPLRKCLKDEDPYVR
HHHHHHCCCCCHHHH		69.42-
131 (in isoform 2)Ubiquitination-69.42-
136PhosphorylationCLKDEDPYVRKTAAV
HCCCCCHHHHHHHHH		25.8082609
138MethylationKDEDPYVRKTAAVCV
CCCCHHHHHHHHHHH		25.43-
139UbiquitinationDEDPYVRKTAAVCVA
CCCHHHHHHHHHHHH		32.26-
147AcetylationTAAVCVAKLHDINAQ
HHHHHHHHHHHCCHH		26.4226051181
147UbiquitinationTAAVCVAKLHDINAQ
HHHHHHHHHHHCCHH		26.42-
155SulfoxidationLHDINAQMVEDQGFL
HHHCCHHHHCCCCHH		3.1130846556
215UbiquitinationLTALNECTEWGQIFI
HHHHHHCCCCCCEEH		28.7021890473
245PhosphorylationQSICERVTPRLSHAN
HHHHHHHCCCCCCCC		14.6515994057
249PhosphorylationERVTPRLSHANSAVV
HHHCCCCCCCCHHHH		23.1025332170
258PhosphorylationANSAVVLSAVKVLMK
CCHHHHHHHHHHHHH		21.2925332170
265AcetylationSAVKVLMKFLELLPK
HHHHHHHHHHHHCCC		42.5119608861
265 (in isoform 2)Acetylation-42.51-
272UbiquitinationKFLELLPKDSDYYNM
HHHHHCCCCCHHHHH		70.5921906983
272 (in isoform 1)Ubiquitination-70.5921890473
272 (in isoform 2)Ubiquitination-70.5921890473
274PhosphorylationLELLPKDSDYYNMLL
HHHCCCCCHHHHHHH		33.3726356563
276PhosphorylationLLPKDSDYYNMLLKK
HCCCCCHHHHHHHHH		10.7427273156
276 (in isoform 2)Phosphorylation-10.7427642862
277PhosphorylationLPKDSDYYNMLLKKL
CCCCCHHHHHHHHHH		10.0926356563
277 (in isoform 2)Phosphorylation-10.0925147952
278UbiquitinationPKDSDYYNMLLKKLA
CCCCHHHHHHHHHHC		14.3821890473
279SulfoxidationKDSDYYNMLLKKLAP
CCCHHHHHHHHHHCC		2.4030846556
282AcetylationDYYNMLLKKLAPPLV
HHHHHHHHHHCCCCC		41.6026051181
282UbiquitinationDYYNMLLKKLAPPLV
HHHHHHHHHHCCCCC		41.60-
300PhosphorylationSGEPEVQYVALRNIN
CCCCCHHEEEEECCE		7.89110747683
318AcetylationQKRPEILKQEIKVFF
ECCHHHHHHHEEEEE		52.0919608861
318MalonylationQKRPEILKQEIKVFF
ECCHHHHHHHEEEEE		52.0926320211
318UbiquitinationQKRPEILKQEIKVFF
ECCHHHHHHHEEEEE		52.09-
318 (in isoform 2)Acetylation-52.09-
327AcetylationEIKVFFVKYNDPIYV
HEEEEEEECCCCEEE		32.9326051181
328PhosphorylationIKVFFVKYNDPIYVK
EEEEEEECCCCEEEE		21.3528152594
333PhosphorylationVKYNDPIYVKLEKLD
EECCCCEEEEHHHHH		9.27110749209
335AcetylationYNDPIYVKLEKLDIM
CCCCEEEEHHHHHHH		33.6826051181
335UbiquitinationYNDPIYVKLEKLDIM
CCCCEEEEHHHHHHH		33.68-
335 (in isoform 1)Ubiquitination-33.6821890473
335 (in isoform 2)Ubiquitination-33.6821890473
361PhosphorylationVLAELKEYATEVDVD
HHHHHHHHHCCCCHH		19.7520068231
361 (in isoform 2)Phosphorylation-19.75-
363PhosphorylationAELKEYATEVDVDFV
HHHHHHHCCCCHHHH		35.3220068231
383AcetylationAIGRCAIKVEQSAER
HHHHHEEEHHHHHHH		22.6126051181
383UbiquitinationAIGRCAIKVEQSAER
HHHHHEEEHHHHHHH		22.61-
393PhosphorylationQSAERCVSTLLDLIQ
HHHHHHHHHHHHHHH		19.5728857561
394PhosphorylationSAERCVSTLLDLIQT
HHHHHHHHHHHHHHH		15.7929083192
401PhosphorylationTLLDLIQTKVNYVVQ
HHHHHHHHHHHHHHH		29.9329083192
481UbiquitinationHDESTQVQLTLLTAI
CCCCHHHHHHHHHHH		20.9321890473
497PhosphorylationKLFLKKPSETQELVQ
HHHCCCCHHHHHHHH		63.2518691976
497 (in isoform 2)Phosphorylation-63.25-
524PhosphorylationPDLRDRGYIYWRLLS
CCHHHHCEEEEEEEC		7.547458789
531PhosphorylationYIYWRLLSTDPVTAK
EEEEEEECCCCCCHH		35.0430087585
532PhosphorylationIYWRLLSTDPVTAKE
EEEEEECCCCCCHHH		44.2730087585
536PhosphorylationLLSTDPVTAKEVVLS
EECCCCCCHHHHHHC		37.0830087585
538UbiquitinationSTDPVTAKEVVLSEK
CCCCCCHHHHHHCCC		41.5021890473
538 (in isoform 1)Ubiquitination-41.5021890473
538 (in isoform 2)Ubiquitination-41.5021890473
574PhosphorylationIGSLASVYHKPPNAF
HHHHHHHCCCCCCCC		11.13138777
599PhosphorylationHLPIHHGSTDAGDSP
CCCCCCCCCCCCCCC		20.8224275569
605PhosphorylationGSTDAGDSPVGTTTA
CCCCCCCCCCCCCCC		22.1426074081
609PhosphorylationAGDSPVGTTTATNLE
CCCCCCCCCCCCCCC		22.6226074081
610PhosphorylationGDSPVGTTTATNLEQ
CCCCCCCCCCCCCCC		14.4326074081
662UbiquitinationLLGGGLDSLVGQSFI
HHCCCHHHHCCCCCC		29.9621890473
671O-linked_GlycosylationVGQSFIPSSVPATFA
CCCCCCCCCCCCCCC		38.8723301498
672O-linked_GlycosylationGQSFIPSSVPATFAP
CCCCCCCCCCCCCCC		27.1123301498
680PhosphorylationVPATFAPSPTPAVVS
CCCCCCCCCCCCHHC		37.6726074081
682PhosphorylationATFAPSPTPAVVSSG
CCCCCCCCCCHHCCC		28.3726074081
694 (in isoform 2)Phosphorylation-11.21-
698PhosphorylationNDLFELSTGIGMAPG
HHHHHHCCCCCCCCC		45.5024275569
719AcetylationAVWLPAVKAKGLEIS
EEEECCCCCCCEEEE		46.6225953088
719UbiquitinationAVWLPAVKAKGLEIS
EEEECCCCCCCEEEE		46.62-
719 (in isoform 1)Ubiquitination-46.6221890473
721UbiquitinationWLPAVKAKGLEISGT
EECCCCCCCEEEEEE		59.31-
733 (in isoform 2)Ubiquitination-39.9621890473
735 (in isoform 2)Ubiquitination-10.32-
737PhosphorylationTHRQGHIYMEMNFTN
EECCCEEEEEEECCH		4.9518938240
738SulfoxidationHRQGHIYMEMNFTNK
ECCCEEEEEEECCHH		3.7830846556
740SulfoxidationQGHIYMEMNFTNKAL
CCEEEEEEECCHHHH		2.5930846556
751 (in isoform 2)Phosphorylation-26.32-
767PhosphorylationNSFGVIPSTPLAIHT
CCCCCCCCCCEEECC		31.3725627689
768PhosphorylationSFGVIPSTPLAIHTP
CCCCCCCCCEEECCC		19.5725159151
774PhosphorylationSTPLAIHTPLMPNQS
CCCEEECCCCCCCCC		16.4125159151
797SulfoxidationTLGPVMKMEPLNNLQ
CCCCCEECEECCCCC		3.2821406390
821UbiquitinationFYFSCLIPLNVLFVE
EEEECCCEECEEEEE		12.6321890473
834MethylationVEDGKMERQVFLATW
EECCCEEEEEEEEEC		34.17-
840PhosphorylationERQVFLATWKDIPNE
EEEEEEEECCCCCCC		34.8846164997
855UbiquitinationNELQFQIKECHLNAD
CCEEEEEEEEECCCH		43.43-
860UbiquitinationQIKECHLNADTVSSK
EEEEEECCCHHHHHH		16.4721890473
867AcetylationNADTVSSKLQNNNVY
CCHHHHHHHHCCCEE		46.7326051181
867UbiquitinationNADTVSSKLQNNNVY
CCHHHHHHHHCCCEE		46.73-
869 (in isoform 2)Ubiquitination-55.10-
874PhosphorylationKLQNNNVYTIAKRNV
HHHCCCEEEEEECCC		8.4428152594
875PhosphorylationLQNNNVYTIAKRNVE
HHCCCEEEEEECCCC		15.3528152594
878AcetylationNNVYTIAKRNVEGQD
CCEEEEEECCCCCHH		40.4326051181
878UbiquitinationNNVYTIAKRNVEGQD
CCEEEEEECCCCCHH		40.4321906983
878 (in isoform 1)Ubiquitination-40.4321890473
881 (in isoform 2)Ubiquitination-11.53-
888PhosphorylationVEGQDMLYQSLKLTN
CCCHHHHHHHHHCCC		6.8727259358
888 (in isoform 2)Phosphorylation-6.8727642862
890PhosphorylationGQDMLYQSLKLTNGI
CHHHHHHHHHCCCCE		17.57-
892 (in isoform 2)Ubiquitination-59.5221890473
912PhosphorylationIQPGNPNYTLSLKCR
ECCCCCCEEEEEEEC		15.4328152594
913PhosphorylationQPGNPNYTLSLKCRA
CCCCCCEEEEEEECC		19.2628152594
915PhosphorylationGNPNYTLSLKCRAPE
CCCCEEEEEEECCHH		20.2728152594
917UbiquitinationPNYTLSLKCRAPEVS
CCEEEEEEECCHHHH		20.492189047
917 (in isoform 1)Ubiquitination-20.4921890473
926PhosphorylationRAPEVSQYIYQVYDS
CCHHHHHHHHHHHHH		8.2931137097
928PhosphorylationPEVSQYIYQVYDSIL
HHHHHHHHHHHHHHH		6.2375179
931 (in isoform 2)Ubiquitination-6.6121890473
933PhosphorylationYIYQVYDSILKN---
HHHHHHHHHHCC---		16.4824719451
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
737YPhosphorylationKinaseSRCP12931
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP2B1_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 AP2B1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K0408_HUMANKIAA0408physical
16189514
DHX58_HUMANDHX58physical
16189514
MLH1_HUMANMLH1physical
16189514
AP1M1_HUMANAP1M1physical
16189514
MEA1_HUMANMEA1physical
16189514
GCP4_HUMANTUBGCP4physical
16189514
ARH_HUMANLDLRAP1physical
16189514
THAP1_HUMANTHAP1physical
16189514
P121A_HUMANPOM121physical
16189514
NECP2_HUMANNECAP2physical
16189514
VATG1_HUMANATP6V1G1physical
16189514
NUP54_HUMANNUP54physical
16189514
TE2IP_HUMANTERF2IPphysical
16189514
FA46C_HUMANFAM46Cphysical
16189514
RIBC2_HUMANRIBC2physical
16189514
AP1M2_HUMANAP1M2physical
16189514
AP2M1_HUMANAP2M1physical
16189514
BUB1B_HUMANBUB1Bphysical
12419313
ARRB2_HUMANARRB2physical
12070169
CLH1_HUMANCLTCphysical
17052248
EPN1_HUMANEPN1physical
22863883
LCAP_HUMANLNPEPphysical
22863883
NUSAP_HUMANNUSAP1physical
22863883
SC24C_HUMANSEC24Cphysical
22863883
XPO7_HUMANXPO7physical
22863883
PI51C_HUMANPIP5K1Cphysical
20435073
ADT3_HUMANSLC25A6physical
25416956
IMA1_HUMANKPNA2physical
25416956
U2AF1_HUMANU2AF1physical
25416956
AP1M2_HUMANAP1M2physical
25416956
RPGF3_HUMANRAPGEF3physical
25416956
THIOM_HUMANTXN2physical
25416956
AFF4_HUMANAFF4physical
25416956
THAP1_HUMANTHAP1physical
25416956
ATP23_HUMANXRCC6BP1physical
25416956
NEUR4_HUMANNEU4physical
25416956
AP1S1_HUMANAP1S1physical
26344197
AP1S2_HUMANAP1S2physical
26344197
AP2S1_HUMANAP2S1physical
26344197
COX5B_HUMANCOX5Bphysical
26344197
NUP50_HUMANNUP50physical
26344197
TOM40_HUMANTOMM40physical
26344197
VAPA_HUMANVAPAphysical
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 AP2B1_HUMAN

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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-265 AND LYS-318, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2 AND SER-4, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-276, AND MASSSPECTROMETRY.
"c-Src-mediated phosphorylation of AP-2 reveals a general mechanismfor receptors internalizing through the clathrin pathway.";
Zimmerman B., Simaan M., Lee M.-H., Luttrell L.M., Laporte S.A.;
Cell. Signal. 21:103-110(2009).
Cited for: PHOSPHORYLATION AT TYR-737.
"Src-dependent phosphorylation of beta2-adaptin dissociates the beta-arrestin-AP-2 complex.";
Fessart D., Simaan M., Zimmerman B., Comeau J., Hamdan F.F.,Wiseman P.W., Bouvier M., Laporte S.A.;
J. Cell Sci. 120:1723-1732(2007).
Cited for: PHOSPHORYLATION AT TYR-737, AND INTERACTION WITH ARRB1.
"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-737 AND TYR-888, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-737, AND MASSSPECTROMETRY.

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