KRIT1_HUMAN - dbPTM
KRIT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KRIT1_HUMAN
UniProt AC O00522
Protein Name Krev interaction trapped protein 1
Gene Name KRIT1
Organism Homo sapiens (Human).
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 (By similarity). 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. 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 MGNPENIEDAYVAVIRPKNTASLNSREYRAKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREASLFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTNVINPAYATESGQTENSLHMGYSALEIKSKMLALEKADTCIYNPLFGSDLQYTNRVDKVVINPYFGLGAPDYSKIQIPKQEKWQRSMSSVTEDKERQWVDDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRHITDQQGRSPLNICEENKQNNWEEAAKLLKEAINKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKAPHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLMPTERNS
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
11PhosphorylationPENIEDAYVAVIRPK
HHHHHCEEEEEECCC		10.9827642862
20PhosphorylationAVIRPKNTASLNSRE
EEECCCCCCCCCCHH		24.6126699800
22PhosphorylationIRPKNTASLNSREYR
ECCCCCCCCCCHHHH		26.5023401153
25PhosphorylationKNTASLNSREYRAKS
CCCCCCCCHHHHHHH		31.6126074081
28PhosphorylationASLNSREYRAKSYEI
CCCCCHHHHHHHHEE		18.1122817900
32PhosphorylationSREYRAKSYEILLHE
CHHHHHHHHEEEEEE		27.3228857561
33PhosphorylationREYRAKSYEILLHEV
HHHHHHHHEEEEEEC		13.2923312004
46UbiquitinationEVPIEGQKKKRKKVL
ECCCCCCCCCCCEEE		71.73-
109PhosphorylationEKMGREASLFIVPSV
CCCCCCEEEEEEEEE		21.0428857561
122UbiquitinationSVVKDNTKYTYTPGC
EEECCCCCEEECCCC		41.68-
124PhosphorylationVKDNTKYTYTPGCPI
ECCCCCEEECCCCCH		23.6023836654
125PhosphorylationKDNTKYTYTPGCPIF
CCCCCEEECCCCCHH		14.0923836654
143PhosphorylationQDIMRVCSESSTHFA
HHHHHHHCCCCCHHH		37.3427080861
145PhosphorylationIMRVCSESSTHFATL
HHHHHCCCCCHHHHH		25.0127080861
146PhosphorylationMRVCSESSTHFATLT
HHHHCCCCCHHHHHH		23.1129255136
147PhosphorylationRVCSESSTHFATLTA
HHHCCCCCHHHHHHH		30.2329255136
151PhosphorylationESSTHFATLTARMLI
CCCCHHHHHHHHHHH		24.5728387310
153PhosphorylationSTHFATLTARMLIAL
CCHHHHHHHHHHHHH		14.0929255136
224AcetylationSKMLALEKADTCIYN
HHHHHHHCCCCEEEC		53.0319829769
227PhosphorylationLALEKADTCIYNPLF
HHHHCCCCEEECCCC		12.9821945579
230PhosphorylationEKADTCIYNPLFGSD
HCCCCEEECCCCCCC		16.9321945579
236PhosphorylationIYNPLFGSDLQYTNR
EECCCCCCCCCCCCC		28.0121945579
240PhosphorylationLFGSDLQYTNRVDKV
CCCCCCCCCCCCCEE		17.1821945579
241PhosphorylationFGSDLQYTNRVDKVV
CCCCCCCCCCCCEEE		12.0021945579
246UbiquitinationQYTNRVDKVVINPYF
CCCCCCCEEEECCCC		35.23-
252PhosphorylationDKVVINPYFGLGAPD
CEEEECCCCCCCCCC		13.0421945579
260PhosphorylationFGLGAPDYSKIQIPK
CCCCCCCCCCCCCCC		15.7121945579
261PhosphorylationGLGAPDYSKIQIPKQ
CCCCCCCCCCCCCCH		30.5721945579
262UbiquitinationLGAPDYSKIQIPKQE
CCCCCCCCCCCCCHH		32.19-
267UbiquitinationYSKIQIPKQEKWQRS
CCCCCCCCHHHHHHH		73.12-
274PhosphorylationKQEKWQRSMSSVTED
CHHHHHHHHHCCCCC		14.1225849741
276PhosphorylationEKWQRSMSSVTEDKE
HHHHHHHHCCCCCHH		23.9326657352
277PhosphorylationKWQRSMSSVTEDKER
HHHHHHHCCCCCHHH		25.1528857561
279PhosphorylationQRSMSSVTEDKERQW
HHHHHCCCCCHHHCC		40.1830576142
305PhosphorylationEGDSELLSRLLSERF
CCCHHHHHHHHHCCC		33.2424719451
391PhosphorylationITDQQGRSPLNICEE
CCCCCCCCCCCCCHH		40.3325159151
400UbiquitinationLNICEENKQNNWEEA
CCCCHHHHCCCHHHH		58.65-
409UbiquitinationNNWEEAAKLLKEAIN
CCHHHHHHHHHHHHC		62.49-
412UbiquitinationEEAAKLLKEAINKPY
HHHHHHHHHHHCCCH		56.38-
430PhosphorylationRIYRMDGSYRSVELK
EEEECCCCEEEEEEE		17.07-
431PhosphorylationIYRMDGSYRSVELKH
EEECCCCEEEEEEEC		16.67-
605PhosphorylationTNRILHEYKNLSTSE
HHHHHHHHHCCCCCC		8.4020058876
606UbiquitinationNRILHEYKNLSTSEG
HHHHHHHHCCCCCCC		48.72-
611PhosphorylationEYKNLSTSEGVSKEM
HHHCCCCCCCCCHHH		29.0422985185
615PhosphorylationLSTSEGVSKEMHHLQ
CCCCCCCCHHHHHHH		33.4822985185
659PhosphorylationNHKVIPVYVGVNIKG
CCCEEEEEEEEEECC		6.02-
680PhosphorylationETKALLISLKYGCFM
CHHHHHHHHHHCEEE		20.8324719451
707PhosphorylationHSMENKMSFIVHTKQ
EECCCCEEEEEEHHH		17.2730631047
732PhosphorylationLNGQLMPTERNS---
HCCEECCCCCCC---		33.3425159151
736PhosphorylationLMPTERNS-------
ECCCCCCC-------		48.0625627689
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

Oops, there are no upstream regulatory protein records of KRIT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KRIT1_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 KRIT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAP1A_HUMANRAP1Aphysical
9285558
ITBP1_HUMANITGB1BP1physical
11741838
DAPK1_HUMANDAPK1physical
12911633
ITBP1_HUMANITGB1BP1physical
11854171
ZN363_HUMANRCHY1physical
17568776
RGS4_HUMANRGS4physical
10747990
PLCB3_HUMANPLCB3physical
12821674
PLCB1_HUMANPLCB1physical
12821674
PK3C3_HUMANPIK3C3physical
12925680
PI3R4_HUMANPIK3R4physical
12925680
TNR6_HUMANFASphysical
14594800
RAP1B_HUMANRAP1Bphysical
22577140
ITBP1_HUMANITGB1BP1physical
28514442
HEG1_HUMANHEG1physical
28514442
NPT2B_HUMANSLC34A2physical
28514442
UBFD1_HUMANUBFD1physical
28514442
Drug and Disease Associations
Kegg Disease
H00534 Cerebral cavernous malformation
OMIM Disease
116860Cerebral cavernous malformations 1 (CCM1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KRIT1_HUMAN

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Related Literatures of Post-Translational Modification

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