BIRC2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BIRC2_MOUSE
• UniProt AC: Q62210
• Protein Name: Baculoviral IAP repeat-containing protein 2
• Gene Name: Birc2
• Organism: Mus musculus (Mouse).
• Sequence Length: 612
• Subcellular Localization: Cytoplasm. Nucleus. Agents that induce either the extrinsic or intrinsic apoptotic pathways promote its redistribution from the nuclear compartment to the cytoplasmic compartment. Associated with the midbody in telophase cells, and found diffusely in
• Protein Description: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle..
• Protein Sequence: MDKTVSQRLGQGTLHQKLKRIMEKSTILSNWTKESEEKMKFDFSCELYRMSTYSAFPRGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKQGDSPVEKHRQFYPSCSFVQTLLSASLQSPSKNMSPVKSRFAHSSPLERGGIHSNLCSSPLNSRAVEDFSSRMDPCSYAMSTEEARFLTYSMWPLSFLSPAELARAGFYYIGPGDRVACFACGGKLSNWEPKDDAMSEHRRHFPHCPFLENTSETQRFSISNLSMQTHSARLRTFLYWPPSVPVQPEQLASAGFYYVDRNDDVKCFCCDGGLRCWEPGDDPWIEHAKWFPRCEFLIRMKGQEFVDEIQARYPHLLEQLLSTSDTPGEENADPTETVVHFGPGESSEDVVMMSTPVVKAALEMGFSRSLVRQTVQRQILATGENYRTVNDIVSVLLNAEDERREEEKERQTEEMASGDLSLIRKNRMALFQQLTHVLPILDNLLEASVITKQEHDIIRQKTQIPLQARELIDTVLVKGNAAANIFKNSLKEIDSTLYENLFVEKNMKYIPTEDVSGLSLEEQLRRLQEERTCKVCMDREVSIVFIPCGHLVVCQECAPSLRKCPICRGTIKGTVRTFLS

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
82	Ubiquitination	TGVNDKVKCFCCGLM CCCCCCEEEEECCCC	27.60	-
94	Ubiquitination	GLMLDNWKQGDSPVE CCCCCCCCCCCCCHH	51.13	-
115	Phosphorylation	PSCSFVQTLLSASLQ CCCHHHHHHHHHHCC	25.10	22871156
118	Phosphorylation	SFVQTLLSASLQSPS HHHHHHHHHHCCCCC	20.94	22871156
120	Phosphorylation	VQTLLSASLQSPSKN HHHHHHHHCCCCCCC	24.46	26643407
123	Phosphorylation	LLSASLQSPSKNMSP HHHHHCCCCCCCCCC	36.11	26745281
125	Phosphorylation	SASLQSPSKNMSPVK HHHCCCCCCCCCCCH	41.74	26643407
129	Phosphorylation	QSPSKNMSPVKSRFA CCCCCCCCCCHHHCC	35.62	22871156
138	Phosphorylation	VKSRFAHSSPLERGG CHHHCCCCCCCCCCC	30.16	26643407
139	Phosphorylation	KSRFAHSSPLERGGI HHHCCCCCCCCCCCC	24.52	26643407
143	Methylation	AHSSPLERGGIHSNL CCCCCCCCCCCCCCC	57.21	24129315
148	Phosphorylation	LERGGIHSNLCSSPL CCCCCCCCCCCCCCC	29.58	29472430
152	Phosphorylation	GIHSNLCSSPLNSRA CCCCCCCCCCCCHHH	37.85	25266776
153	Phosphorylation	IHSNLCSSPLNSRAV CCCCCCCCCCCHHHH	32.20	26824392
157	Phosphorylation	LCSSPLNSRAVEDFS CCCCCCCHHHHHHHH	29.33	29472430
399	Phosphorylation	AALEMGFSRSLVRQT HHHHCCCCHHHHHHH	18.41	25159016
401	Phosphorylation	LEMGFSRSLVRQTVQ HHCCCCHHHHHHHHH	29.98	25159016
527	Phosphorylation	NSLKEIDSTLYENLF HHHHHHHHHHHHHHH	26.44	28285833
551	Phosphorylation	TEDVSGLSLEEQLRR CCCCCCCCHHHHHHH	36.94	26824392

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
-	K	Ubiquitination	E3 ubiquitin ligase	Traf6	P70196	PMID:19898473

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BIRC2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of BIRC2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GLMN_MOUSE	Glmn	physical	29191979

Drug and Disease Associations

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