BIN1_HUMAN - dbPTM
BIN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BIN1_HUMAN
UniProt AC O00499
Protein Name Myc box-dependent-interacting protein 1
Gene Name BIN1
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Isoform BIN1: Nucleus.
Isoform IIA: Cytoplasm.
Protein Description May be involved in regulation of synaptic vesicle endocytosis. May act as a tumor suppressor and inhibits malignant cell transformation..
Protein Sequence MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQLRKGPPVPPPPKHTPSKEVKQEQILSLFEDTFVPEISVTTPSQFEAPGPFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVP
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------MAEMGSKGV
------CCCCCCCCC		18.5822814378
13MalonylationSKGVTAGKIASNVQK
CCCCCHHHHHHHHHH		32.4126320211
16PhosphorylationVTAGKIASNVQKKLT
CCHHHHHHHHHHHHH		40.7921955146
28AcetylationKLTRAQEKVLQKLGK
HHHHHHHHHHHHHCC		35.8425953088
40UbiquitinationLGKADETKDEQFEQC
HCCCCCCCHHHHHHH		58.16-
53UbiquitinationQCVQNFNKQLTEGTR
HHHHHHHHHCCCCCH		42.41-
56PhosphorylationQNFNKQLTEGTRLQK
HHHHHHCCCCCHHHH		29.8520068231
59PhosphorylationNKQLTEGTRLQKDLR
HHHCCCCCHHHHHHH		23.2120068231
66MethylationTRLQKDLRTYLASVK
CHHHHHHHHHHHHHH		31.30-
67PhosphorylationRLQKDLRTYLASVKA
HHHHHHHHHHHHHHH		30.1320068231
68PhosphorylationLQKDLRTYLASVKAM
HHHHHHHHHHHHHHH		8.2020068231
71PhosphorylationDLRTYLASVKAMHEA
HHHHHHHHHHHHHHH		22.8920068231
75SulfoxidationYLASVKAMHEASKKL
HHHHHHHHHHHHHHH		2.1330846556
79PhosphorylationVKAMHEASKKLNECL
HHHHHHHHHHHHHHH		27.60-
146MalonylationRIAKRGRKLVDYDSA
HHHHHCCCCCCHHHH		56.5426320211
146UbiquitinationRIAKRGRKLVDYDSA
HHHHHCCCCCCHHHH		56.54-
150PhosphorylationRGRKLVDYDSARHHY
HCCCCCCHHHHHHHH		12.34-
152PhosphorylationRKLVDYDSARHHYES
CCCCCHHHHHHHHHH		22.45-
1642-HydroxyisobutyrylationYESLQTAKKKDEAKI
HHHHHHHCHHCHHHC		64.84-
164UbiquitinationYESLQTAKKKDEAKI
HHHHHHHCHHCHHHC		64.84-
173 (in isoform 10)Acetylation-49.80-
176PhosphorylationAKIAKPVSLLEKAAP
HHCCCCHHHHHHHCC		35.4524719451
219SulfoxidationAQKVFEEMNVDLQEE
HHHHHHHHCCCHHHH		4.6930846556
258UbiquitinationNFHKEMSKLNQNLND
HHHHHHHHHHHHHHH		50.58-
270 (in isoform 10)Phosphorylation-6.0719764811
270 (in isoform 8)Phosphorylation-6.0719764811
270 (in isoform 11)Phosphorylation-6.0719764811
272UbiquitinationDVLVGLEKQHGSNTF
HHHHHHHHCCCCCEE		53.27-
276PhosphorylationGLEKQHGSNTFTVKA
HHHHCCCCCEEEEEE		30.4926437602
278PhosphorylationEKQHGSNTFTVKAQP
HHCCCCCEEEEEEEC		23.5226437602
280 (in isoform 10)Phosphorylation-21.0419764811
280PhosphorylationQHGSNTFTVKAQPSD
CCCCCEEEEEEECCC		21.0426437602
280 (in isoform 8)Phosphorylation-21.0419764811
280 (in isoform 11)Phosphorylation-21.0419764811
282 (in isoform 8)Phosphorylation-37.9419764811
282 (in isoform 10)Phosphorylation-37.9419764811
282 (in isoform 11)Phosphorylation-37.9419764811
282UbiquitinationGSNTFTVKAQPSDNA
CCCEEEEEEECCCCC		37.94-
286PhosphorylationFTVKAQPSDNAPAKG
EEEEEECCCCCCCCC		31.2723401153
287 (in isoform 8)Phosphorylation-63.0919764811
287 (in isoform 10)Phosphorylation-63.0919764811
287 (in isoform 11)Phosphorylation-63.0919764811
291 (in isoform 10)Phosphorylation-29.9418669648
292 (in isoform 9)Phosphorylation-63.0622673903
296 (in isoform 9)Phosphorylation-34.3122673903
296PhosphorylationAPAKGNKSPSPPDGS
CCCCCCCCCCCCCCC		34.3119664994
298PhosphorylationAKGNKSPSPPDGSPA
CCCCCCCCCCCCCCC		57.0419664994
300 (in isoform 7)Phosphorylation-64.0322468782
300 (in isoform 9)Phosphorylation-64.0326657352
302 (in isoform 7)Phosphorylation-41.1022468782
302 (in isoform 9)Phosphorylation-41.1028450419
303PhosphorylationSPSPPDGSPAATPEI
CCCCCCCCCCCCCCE		20.8129255136
304 (in isoform 9)Phosphorylation-31.2926657352
305 (in isoform 9)Phosphorylation-26.1826657352
307PhosphorylationPDGSPAATPEIRVNH
CCCCCCCCCCEEECC		24.4622167270
307 (in isoform 10)Phosphorylation-24.4622673903
311 (in isoform 10)Phosphorylation-22.8622673903
313 (in isoform 9)Phosphorylation-24.7722673903
315 (in isoform 8)Phosphorylation-46.2722468782
315 (in isoform 10)Phosphorylation-46.2726657352
317 (in isoform 8)Phosphorylation-44.8122468782
317 (in isoform 10)Phosphorylation-44.8128450419
319 (in isoform 10)Phosphorylation-27.6526657352
320 (in isoform 10)Phosphorylation-36.6626657352
321 (in isoform 9)Phosphorylation-28.5122210691
323PhosphorylationPEPAGGATPGATLPK
CCCCCCCCCCCCCCC		26.0630266825
327PhosphorylationGGATPGATLPKSPSQ
CCCCCCCCCCCCHHH		49.8930266825
328 (in isoform 10)Phosphorylation-5.0822673903
331PhosphorylationPGATLPKSPSQLRKG
CCCCCCCCHHHHCCC		28.0429255136
333PhosphorylationATLPKSPSQLRKGPP
CCCCCCHHHHCCCCC		49.2729255136
336 (in isoform 10)Phosphorylation-33.9622210691
343 (in isoform 2)Phosphorylation-59.04-
348O-linked_GlycosylationVPPPPKHTPSKEVKQ
CCCCCCCCCCHHHCH		35.0728510447
348PhosphorylationVPPPPKHTPSKEVKQ
CCCCCCCCCCHHHCH		35.0725159151
350O-linked_GlycosylationPPPKHTPSKEVKQEQ
CCCCCCCCHHHCHHH		42.4728510447
350PhosphorylationPPPKHTPSKEVKQEQ
CCCCCCCCHHHCHHH		42.4728152594
350 (in isoform 2)Phosphorylation-42.47-
365PhosphorylationILSLFEDTFVPEISV
HHHHHCCCCCCEEEE		21.23-
488PhosphorylationAASEAASSSLPAVVV
HHHHHHHHCCCEEEE		31.0318669648
489PhosphorylationASEAASSSLPAVVVE
HHHHHHHCCCEEEEE		35.5618669648
510PhosphorylationNGTVEGGSGAGRLDL
CCEEECCCCCCCCCC		36.00-
534PhosphorylationAQHDYTATDTDELQL
ECCCCCCCCCCCCEE		31.47-
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
348TPhosphorylationKinaseCDK2P24941
PSP
348TPhosphorylationKinaseCDK5Q00535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BIN1_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 BIN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNX4_HUMANSNX4physical
12668730
RIN3_HUMANRIN3physical
12972505
PLD1_HUMANPLD1physical
10764771
PLD2_HUMANPLD2physical
10764771
BIN1_HUMANBIN1physical
10391921
XRCC6_MOUSEXrcc6physical
17671430
XRCC5_MOUSEXrcc5physical
17671430
XRCC6_HUMANXRCC6physical
17671430
XRCC5_HUMANXRCC5physical
17671430
RFX3_HUMANRFX3physical
20211142
ZBTB3_HUMANZBTB3physical
20211142
MYC_HUMANMYCphysical
10380878
CLH1_HUMANCLTCphysical
9195986
AP2A2_HUMANAP2A2physical
9195986
MYC_HUMANMYCphysical
15992821
CLIP1_HUMANCLIP1physical
19004523
BIN2_HUMANBIN2physical
10903846
A4_HUMANAPPphysical
21832049
SOS1_HUMANSOS1physical
9182529
SOS2_HUMANSOS2physical
9182529
AP2A1_HUMANAP2A1physical
9182529
DYN1_RATDnm1physical
9182529
DLGP4_HUMANDLGAP4physical
16275660
XRCC4_HUMANXRCC4physical
16275660
F16P1_HUMANFBP1physical
16275660
MTM1_HUMANMTM1physical
23917616
WASL_MOUSEWaslphysical
25262827
WASL_HUMANWASLphysical
25262827
DYN2_HUMANDNM2physical
25350771
DYN1_RATDnm1physical
9736607
E2F1_HUMANE2F1physical
25257171
SYNE2_HUMANSYNE2physical
26506308
CLIP1_HUMANCLIP1physical
26506308
ACTS_HUMANACTA1physical
26506308
EH1L1_HUMANEHBP1L1physical
26833786
RAB8A_HUMANRAB8Aphysical
26833786
RAB8B_HUMANRAB8Bphysical
26833786
CHM4B_HUMANCHMP4Bphysical
28806752
TAU_HUMANMAPTphysical
28755476
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
255200Myopathy, centronuclear, 2 (CNM2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BIN1_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-296; SER-298 ANDSER-303, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298; SER-303;THR-307; THR-323 AND SER-331, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298; SER-303AND SER-331, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298 ANDSER-303, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, AND MASSSPECTROMETRY.

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