BIN2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BIN2_RAT
• UniProt AC: Q68FR2
• Protein Name: Bridging integrator 2
• Gene Name: Bin2
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 507
• Subcellular Localization: Cytoplasm . Cell projection, podosome membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasm, cell cortex . Cell projection, phagocytic cup . Associates with membranes enriched in phosphoinositides. Detected in the actin-rich cell cort
• Protein Description: Promotes cell motility and migration, probably via its interaction with the cell membrane and with podosome proteins that mediate interaction with the cytoskeleton. Modulates membrane curvature and mediates membrane tubulation (By similarity). Plays a role in podosome formation. Inhibits phagocytosis..
• Protein Sequence: MAEGKAGGAAGLFAKQMQKKFSRAQEKVLQKLGKTVETKDERFEQSASNFYQQQAEGHRLYKDLKNFLSAVKVMRESSKRVSETLQEIYNSDWDGHEDLKAIVGNNDLLWEDYEEKLADQALRTMENYVSQFSEVKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKMAKAEEDFSKAQVVFEDLNQELLEELPVLYNSRIGCYVTVFQNISNLRDVFYREMSKLNHSLYEVMSKLEKQHSNKVFVVKGLSSSSRRSLVISPPVQTCTAFSPVSPVTSPTSPNALSVTSESESVSATAEELTSEAVGEDSCESEESLKDEEADEDQSETSSSEEEEDEDEDEDEEESLAACNGPTPTPAPTPAPASPAAEVKSQEEAAPCSPTSSLGRGQTGKEHSPPGEVVLRARASSEGAEQSKRTASVQRTSAPPSRPPPPKASGGGLSSPPGSAEASKACHPRASSDASSDPEPPETGEKEGTGSSGPKEPHASSTKSATQVVSNDENTEL

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
65	Acetylation	HRLYKDLKNFLSAVK HHHHHHHHHHHHHHH	56.65	22902405
136	Acetylation	VSQFSEVKERIAKRG HHHHHHHHHHHHHHC	36.90	22902405
145	Acetylation	RIAKRGRKLVDYDSA HHHHHCCCCCCHHHH	56.54	72588179
214	Phosphorylation	VTVFQNISNLRDVFY EEEECCHHHHHHHHH	37.04	29779826
273	Phosphorylation	VQTCTAFSPVSPVTS CCCCCCCCCCCCCCC	23.17	-
375	Phosphorylation	SPAAEVKSQEEAAPC CCCHHCCCHHHHCCC	48.26	30181290
383	Phosphorylation	QEEAAPCSPTSSLGR HHHHCCCCCCCCCCC	30.10	29779826
385	Phosphorylation	EAAPCSPTSSLGRGQ HHCCCCCCCCCCCCC	18.04	22673903
386	Phosphorylation	AAPCSPTSSLGRGQT HCCCCCCCCCCCCCC	27.27	22673903
387	Phosphorylation	APCSPTSSLGRGQTG CCCCCCCCCCCCCCC	37.00	25532521
393	Phosphorylation	SSLGRGQTGKEHSPP CCCCCCCCCCCCCCC	53.71	23298284
398	Phosphorylation	GQTGKEHSPPGEVVL CCCCCCCCCCCCEEE	33.60	29779826
411	Phosphorylation	VLRARASSEGAEQSK EEEEECCCCCHHHHH	38.78	25403869
426	Phosphorylation	RTASVQRTSAPPSRP HCCCCCCCCCCCCCC	16.49	23298284
427	Phosphorylation	TASVQRTSAPPSRPP CCCCCCCCCCCCCCC	40.75	23298284
431	Phosphorylation	QRTSAPPSRPPPPKA CCCCCCCCCCCCCCC	57.25	25575281
439	Phosphorylation	RPPPPKASGGGLSSP CCCCCCCCCCCCCCC	44.06	22673903
444	Phosphorylation	KASGGGLSSPPGSAE CCCCCCCCCCCCCHH	44.04	23298284
445	Phosphorylation	ASGGGLSSPPGSAEA CCCCCCCCCCCCHHH	39.91	23298284
449	Phosphorylation	GLSSPPGSAEASKAC CCCCCCCCHHHHHHC	28.80	-
461	Phosphorylation	KACHPRASSDASSDP HHCCCCCCCCCCCCC	29.99	22108457
462	Phosphorylation	ACHPRASSDASSDPE HCCCCCCCCCCCCCC	35.89	28551015
465	Phosphorylation	PRASSDASSDPEPPE CCCCCCCCCCCCCCC	40.02	28551015
466	Phosphorylation	RASSDASSDPEPPET CCCCCCCCCCCCCCC	59.93	29779826
473	Phosphorylation	SDPEPPETGEKEGTG CCCCCCCCCCCCCCC	57.31	28551015
494	Phosphorylation	PHASSTKSATQVVSN CCCCCCCCCCEEECC	36.32	22673903
496	Phosphorylation	ASSTKSATQVVSNDE CCCCCCCCEEECCCC	29.05	22673903
500	Phosphorylation	KSATQVVSNDENTEL CCCCEEECCCCCCCC	39.44	22673903
505	Phosphorylation	VVSNDENTEL----- EECCCCCCCC-----	36.29	22673903

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of BIN2_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BIN2_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of BIN2_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of BIN2_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.