O00522 · KRIT1_HUMAN
- ProteinKrev interaction trapped protein 1
- GeneKRIT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids736 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. May play a role in the regulation of macroautophagy through the down-regulation of the mTOR pathway (PubMed:26417067).
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. May play a role in the regulation of macroautophagy through the down-regulation of the mTOR pathway (PubMed:26417067).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell-cell junction | |
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | extracellular space | |
Cellular Component | plasma membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | GTPase regulator activity | |
Molecular Function | microtubule binding | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate binding | |
Biological Process | angiogenesis | |
Biological Process | cell redox homeostasis | |
Biological Process | endothelium development | |
Biological Process | integrin activation | |
Biological Process | negative regulation of angiogenesis | |
Biological Process | negative regulation of endothelial cell apoptotic process | |
Biological Process | negative regulation of endothelial cell migration | |
Biological Process | negative regulation of endothelial cell proliferation | |
Biological Process | regulation of angiogenesis | |
Biological Process | regulation of establishment of cell polarity | |
Biological Process | small GTPase-mediated signal transduction |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKrev interaction trapped protein 1
- Short namesKrev interaction trapped 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00522
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions. Association with RAP1 relocalizes KRIT1 from microtubules to cell junction membranes. Translocates from the cytoplasm along microtubules to the cell membrane in a ITGB1BP1-dependent manner.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cerebral cavernous malformations 1 (CCM1)
- Note
- DescriptionA form of cerebral cavernous malformations, a congenital vascular anomaly of the central nervous system that can result in hemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. The lesions are characterized by grossly enlarged blood vessels consisting of a single layer of endothelium and without any intervening neural tissue, ranging in diameter from a few millimeters to several centimeters. CCM1 inheritance is autosomal dominant.
- See alsoMIM:116860
Natural variants in CCM1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_023573 | 97 | F>S | in CCM1 | |
VAR_023574 | 569 | K>E | in CCM1 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 47-50 | Reduces interaction with microtubules, but not with ITGB1BP1. | ||||
Sequence: KKRK → AAAA | ||||||
Natural variant | VAR_023573 | 97 | in CCM1 | |||
Sequence: F → S | ||||||
Mutagenesis | 176 | Strongly reduces ITGB1BP1 binding; when associated with D-182. | ||||
Sequence: A → D | ||||||
Mutagenesis | 179 | Strongly reduces ITGB1BP1 binding; when associated with A-179. | ||||
Sequence: R → A | ||||||
Mutagenesis | 182 | Strongly reduces ITGB1BP1 binding; when associated with D-176. | ||||
Sequence: P → D | ||||||
Mutagenesis | 185 | Strongly reduces ITGB1BP1 binding; when associated with A-179. | ||||
Sequence: R → A | ||||||
Mutagenesis | 192 | Reduces ITGB1BP1 binding; when associated with A-195. | ||||
Sequence: N → A | ||||||
Mutagenesis | 192-195 | Reduces interaction with ITGB1BP1. | ||||
Sequence: NPAY → APAA | ||||||
Mutagenesis | 195 | Reduces ITGB1BP1 binding; when associated with A-192. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 430 | Impairs interaction with RAP1B. | ||||
Sequence: S → E | ||||||
Mutagenesis | 432 | Impairs interaction with RAP1B. | ||||
Sequence: R → E | ||||||
Mutagenesis | 452 | 40-fold-reduced affinity for Rap1A. | ||||
Sequence: R → E | ||||||
Mutagenesis | 452 | Impairs interaction with RAP1B. | ||||
Sequence: R → E | ||||||
Natural variant | VAR_023574 | 569 | in CCM1 | |||
Sequence: K → E | ||||||
Mutagenesis | 717 | Strongly reduced affinity for HEG1; when associated with A-721. | ||||
Sequence: L → A | ||||||
Mutagenesis | 721 | Strongly reduced affinity for HEG1; when associated with A-717. | ||||
Sequence: L → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 962 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000067023 | 1-736 | UniProt | Krev interaction trapped protein 1 | |||
Sequence: MGNPENIEDAYVAVIRPKNTASLNSREYRAKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREASLFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTNVINPAYATESGQTENSLHMGYSALEIKSKMLALEKADTCIYNPLFGSDLQYTNRVDKVVINPYFGLGAPDYSKIQIPKQEKWQRSMSSVTEDKERQWVDDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRHITDQQGRSPLNICEENKQNNWEEAAKLLKEAINKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKAPHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLMPTERNS | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 230 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 391 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 736 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Expression
Tissue specificity
Low levels in brain. Very weak expression found in heart and muscle.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with CDH5 (PubMed:20332120).
Found in a complex, at least composed of ITGB1BP1, KRIT1 and RAP1A. Interacts (via C-terminus FERM domain) with RAP1A (active GTP-bound form preferentially); the interaction does not induce the opening conformation of KRIT1. Interacts (via FERM domain) with RAP1B. Interacts (via N-terminus NPXY motif) with ITGB1BP1; the interaction induces the opening conformation of KRIT1 and competes with ITGB1 for ITGB1BP1 interaction. Interacts with HEG1 and CCM2; greatly facilitates CCM2-binding to HEG1. Associates (via N-terminus and C-terminus regions) with microtubules; the interaction is inhibited in presence of ITGB1BP1 and active GTP-bound RAP1A
Found in a complex, at least composed of ITGB1BP1, KRIT1 and RAP1A. Interacts (via C-terminus FERM domain) with RAP1A (active GTP-bound form preferentially); the interaction does not induce the opening conformation of KRIT1. Interacts (via FERM domain) with RAP1B. Interacts (via N-terminus NPXY motif) with ITGB1BP1; the interaction induces the opening conformation of KRIT1 and competes with ITGB1 for ITGB1BP1 interaction. Interacts with HEG1 and CCM2; greatly facilitates CCM2-binding to HEG1. Associates (via N-terminus and C-terminus regions) with microtubules; the interaction is inhibited in presence of ITGB1BP1 and active GTP-bound RAP1A
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00522 | CCM2 Q9BSQ5 | 17 | EBI-1573121, EBI-1573056 | |
BINARY | O00522 | CCM2 Q9BSQ5-1 | 2 | EBI-1573121, EBI-16157769 | |
BINARY | O00522 | HEG1 Q9ULI3 | 6 | EBI-1573121, EBI-12734419 | |
BINARY | O00522 | ITGB1BP1 O14713 | 5 | EBI-1573121, EBI-2127319 | |
BINARY | O00522 | UBE2K P61086 | 3 | EBI-1573121, EBI-473850 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-170 | N-terminal domain similar to Nudix hydrolase domain | ||||
Sequence: MGNPENIEDAYVAVIRPKNTASLNSREYRAKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREASLFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQ | ||||||
Region | 172-195 | Interaction with ITGB1BP1 | ||||
Sequence: HFIPALFRPSPLERIKTNVINPAY | ||||||
Repeat | 287-316 | ANK 1 | ||||
Sequence: VDDFPLHRSACEGDSELLSRLLSERFSVNQ | ||||||
Repeat | 320-350 | ANK 2 | ||||
Sequence: DHWAPIHYACWYGKVEATRILLEKGKCNPNL | ||||||
Repeat | 354-383 | ANK 3 | ||||
Sequence: QLSSPLHFAAGGGHAEIVQILLNHPETDRH | ||||||
Repeat | 388-419 | ANK 4 | ||||
Sequence: QGRSPLNICEENKQNNWEEAAKLLKEAINKPY | ||||||
Domain | 420-734 | FERM | ||||
Sequence: EKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKAPHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLMPTER | ||||||
Region | 430-452 | Interaction with RAP1B | ||||
Sequence: SYRSVELKHGNNTTVQQIMEGMR |
Domain
The FERM domain mediates binding to RAP1A and RAP1B and is necessary for binding to phosphatidylinositol 4,5-bisphosphate (PIP2).
The N-terminal domain has structural similarity to the nudix hydrolase domain, despite the absence of a nudix box and low sequence similarity with nudix hydrolase domains. The N-terminus and the C-terminus part associate together via the NPAY binding motif and adopt a lose conformation that is disrupted by ITGB1BP1, but not by RAP1A.
Contains 4 ANK repeats that precede the FERM domain.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O00522-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length736
- Mass (Da)84,348
- Last updated2005-10-11 v2
- ChecksumD11F75ED629E85AC
O00522-2
- Name2
- Differences from canonical
- 1-207: Missing
O00522-3
- Name3
- Differences from canonical
- 283-330: Missing
Computationally mapped potential isoform sequences
There are 18 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J718 | C9J718_HUMAN | KRIT1 | 582 | ||
C9JXI9 | C9JXI9_HUMAN | KRIT1 | 34 | ||
C9JJM9 | C9JJM9_HUMAN | KRIT1 | 51 | ||
C9JIY2 | C9JIY2_HUMAN | KRIT1 | 526 | ||
C9JD43 | C9JD43_HUMAN | KRIT1 | 11 | ||
C9JF32 | C9JF32_HUMAN | KRIT1 | 483 | ||
C9JEW7 | C9JEW7_HUMAN | KRIT1 | 112 | ||
A0A8I5KQH3 | A0A8I5KQH3_HUMAN | KRIT1 | 262 | ||
A0A8I5KQD8 | A0A8I5KQD8_HUMAN | KRIT1 | 424 | ||
A0A8I5KRK7 | A0A8I5KRK7_HUMAN | KRIT1 | 99 | ||
A0A8I5KUF9 | A0A8I5KUF9_HUMAN | KRIT1 | 677 | ||
A0A8I5KVY1 | A0A8I5KVY1_HUMAN | KRIT1 | 120 | ||
A0A8I5KVY4 | A0A8I5KVY4_HUMAN | KRIT1 | 89 | ||
A0A8I5KVW5 | A0A8I5KVW5_HUMAN | KRIT1 | 201 | ||
A0A8I5KX77 | A0A8I5KX77_HUMAN | KRIT1 | 169 | ||
A0A8I5KWG2 | A0A8I5KWG2_HUMAN | KRIT1 | 162 | ||
A0A8I5KW41 | A0A8I5KW41_HUMAN | KRIT1 | 629 | ||
A0A0C4DG23 | A0A0C4DG23_HUMAN | KRIT1 | 243 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_015800 | 1-207 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 138 | in Ref. 5; AAQ94072 | ||||
Sequence: I → T | ||||||
Sequence conflict | 234 | in Ref. 1; AAB58582 | ||||
Sequence: F → G | ||||||
Alternative sequence | VSP_043327 | 283-330 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 731 | in Ref. 1; AAB58582, 2; AAG47774 and 5; AAQ94072 | ||||
Sequence: P → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U90268 EMBL· GenBank· DDBJ | AAB58582.1 EMBL· GenBank· DDBJ | mRNA | ||
U90269 EMBL· GenBank· DDBJ | AAC01535.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF310133 EMBL· GenBank· DDBJ | AAG47774.1 EMBL· GenBank· DDBJ | mRNA | ||
AF296765 EMBL· GenBank· DDBJ | AAG10220.2 EMBL· GenBank· DDBJ | mRNA | ||
AF388384 EMBL· GenBank· DDBJ | AAM19465.1 EMBL· GenBank· DDBJ | mRNA | ||
AY380057 EMBL· GenBank· DDBJ | AAQ94072.1 EMBL· GenBank· DDBJ | mRNA | ||
AK055305 EMBL· GenBank· DDBJ | BAG51497.1 EMBL· GenBank· DDBJ | mRNA | ||
AC000120 EMBL· GenBank· DDBJ | AAS07420.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC094684 EMBL· GenBank· DDBJ | AAH94684.1 EMBL· GenBank· DDBJ | mRNA | ||
BC098442 EMBL· GenBank· DDBJ | AAH98442.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ294850 EMBL· GenBank· DDBJ | CAC17608.1 EMBL· GenBank· DDBJ | mRNA | ||
AY993945 EMBL· GenBank· DDBJ | AAY25568.1 EMBL· GenBank· DDBJ | Genomic DNA |