KRIT1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KRIT1_MOUSE
• UniProt AC: Q6S5J6
• Protein Name: Krev interaction trapped protein 1
• Gene Name: Krit1
• Organism: Mus musculus (Mouse).
• Sequence Length: 736
• Subcellular Localization: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell junction. KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions. Association with RAP1 relocalizes KRIT1 from microtubules to cell junction
• Protein Description: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits ERK1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Microtubule-associated protein that binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes in a GTP-bound RAP1-dependent manner (By similarity). Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels..
• Protein Sequence: MGNPENIEDAYVAVIRPKNTASLNSREYRAKSYEILLHEVPIEGQKKKRKKVLLETKLQSNSEIAQGILDYVVETTKPISPANQGIKGKRVVLMRKFPLDGEKTGREAALFIVPSVVKDNTKYAYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTNVINPAYAAELGQVDNSLHMGYSALEIKSKMLALEKADTCIYNPLFGSDLQYTNRVDKVVINPYFGLGAPDYSKIQIPKQEKWQRSMSSVVEDKERQWVDDFPLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLTHPDIDRHITDQQGRSPLNVCEENKQNNWEEAAKLLKDAINKPYEKVRIYRMDGSYRSVELKHGNNTTAQQIMEGMRLSQETQRYFTIWICSENLSLQFKPYHKPLQQVHDWPEILAELTNLDPQRETPQLFLRRDVGLPLEVEKKIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEETLKSIVPITKLKSKAPHWINRILHEYKNLSLSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYCCFTWQLGDAGTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLMPSERNS

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
20	Phosphorylation	AVIRPKNTASLNSRE EEECCCCCCCCCCHH	24.61	22324799
22	Phosphorylation	IRPKNTASLNSREYR ECCCCCCCCCCHHHH	26.50	25521595
25	Phosphorylation	KNTASLNSREYRAKS CCCCCCCCHHHHHHH	31.61	29550500
32	Phosphorylation	SREYRAKSYEILLHE CHHHHHHHHEEEEEE	27.32	28833060
33	Phosphorylation	REYRAKSYEILLHEV HHHHHHHHEEEEEEC	13.29	28833060
145	Phosphorylation	IMRVCSESSTHFATL HHHHHCCCCCHHHHH	25.01	28066266
146	Phosphorylation	MRVCSESSTHFATLT HHHHCCCCCHHHHHH	23.11	28066266
147	Phosphorylation	RVCSESSTHFATLTA HHHCCCCCHHHHHHH	30.23	28066266
151	Phosphorylation	ESSTHFATLTARMLI CCCCHHHHHHHHHHH	24.57	28066266
153	Phosphorylation	STHFATLTARMLIAL CCHHHHHHHHHHHHH	14.09	28066266
260	Phosphorylation	FGLGAPDYSKIQIPK CCCCCCCCCCCCCCC	15.71	29514104
274	Phosphorylation	KQEKWQRSMSSVVED CHHHHHHHHHHHHHH	14.12	26060331
276	Phosphorylation	EKWQRSMSSVVEDKE HHHHHHHHHHHHHHH	22.64	23684622
277	Phosphorylation	KWQRSMSSVVEDKER HHHHHHHHHHHHHHH	22.88	23684622
430	Phosphorylation	RIYRMDGSYRSVELK EEEECCCCEEEEEEE	17.07	28059163
521	Ubiquitination	LPLEVEKKIEDPLAI CCHHHHHCCCCCEEE	37.51	-
732	Phosphorylation	LNGQLMPSERNS--- HCCCCCCCCCCC---	34.91	28285833

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

Oops, there are no upstream regulatory protein records of KRIT1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KRIT1_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 KRIT1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of KRIT1_MOUSE !!

Drug and Disease Associations

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