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Protein

Krev interaction trapped protein 1

Gene

KRIT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity7 Publications

GO - Molecular functioni

  • GTPase regulator activity Source: ProtInc
  • microtubule binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • protein complex binding Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • cell redox homeostasis Source: UniProtKB
  • negative regulation of angiogenesis Source: UniProtKB
  • negative regulation of endothelial cell apoptotic process Source: UniProtKB
  • negative regulation of endothelial cell migration Source: UniProtKB
  • negative regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of protein binding Source: Ensembl
  • regulation of establishment of cell polarity Source: UniProtKB
  • small GTPase mediated signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Angiogenesis

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000001631-MONOMER.
ZFISH:ENSG00000001631-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Krev interaction trapped protein 1
Short name:
Krev interaction trapped 1
Alternative name(s):
Cerebral cavernous malformations 1 protein
Gene namesi
Name:KRIT1
Synonyms:CCM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:1573. KRIT1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • extracellular space Source: UniProtKB
  • microtubule Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Cerebral cavernous malformations 1 (CCM1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:116860
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02357397F → S in CCM1. 1 Publication1
Natural variantiVAR_023574569K → E in CCM1. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi47 – 50KKRK → AAAA: Reduces interaction with microtubules, but not with ITGB1BP1. 1 Publication4
Mutagenesisi176A → D: Strongly reduces ITGB1BP1 binding; when associated with D-182. 1 Publication1
Mutagenesisi179R → A: Strongly reduces ITGB1BP1 binding; when associated with A-179. 1 Publication1
Mutagenesisi182P → D: Strongly reduces ITGB1BP1 binding; when associated with D-176. 1 Publication1
Mutagenesisi185R → A: Strongly reduces ITGB1BP1 binding; when associated with A-179. 1 Publication1
Mutagenesisi192 – 195NPAY → APAA: Reduces interaction with ITGB1BP1. 1 Publication4
Mutagenesisi192N → A: Reduces ITGB1BP1 binding; when associated with A-195. 3 Publications1
Mutagenesisi195Y → A: Reduces ITGB1BP1 binding; when associated with A-192. 3 Publications1
Mutagenesisi430S → E: Impairs interaction with RAP1B. 1 Publication1
Mutagenesisi432R → E: Impairs interaction with RAP1B. 1 Publication1
Mutagenesisi452R → E: 40-fold-reduced affinity for Rap1A. 2 Publications1
Mutagenesisi452R → E: Impairs interaction with RAP1B. 2 Publications1
Mutagenesisi717L → A: Strongly reduced affinity for HEG1; when associated with A-721. 1 Publication1
Mutagenesisi721L → A: Strongly reduced affinity for HEG1; when associated with A-717. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi889.
MalaCardsiKRIT1.
MIMi116860. phenotype.
OpenTargetsiENSG00000001631.
Orphaneti221061. Hereditary cerebral cavernous malformation.
PharmGKBiPA26144.

Polymorphism and mutation databases

BioMutaiKRIT1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000670231 – 736Krev interaction trapped protein 1Add BLAST736

Proteomic databases

EPDiO00522.
MaxQBiO00522.
PaxDbiO00522.
PeptideAtlasiO00522.
PRIDEiO00522.

PTM databases

iPTMnetiO00522.
PhosphoSitePlusiO00522.

Expressioni

Tissue specificityi

Low levels in brain. Very weak expression found in heart and muscle.1 Publication

Gene expression databases

BgeeiENSG00000001631.
CleanExiHS_KRIT1.
ExpressionAtlasiO00522. baseline and differential.
GenevisibleiO00522. HS.

Organism-specific databases

HPAiHPA049606.

Interactioni

Subunit structurei

Interacts with CDH5 (By similarity). 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.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCM2Q9BSQ54EBI-1573121,EBI-1573056

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • protein complex binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107330. 17 interactors.
DIPiDIP-40610N.
IntActiO00522. 5 interactors.
STRINGi9606.ENSP00000344668.

Structurei

Secondary structure

1736
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 17Combined sources9
Helixi30 – 32Combined sources3
Beta strandi33 – 39Combined sources7
Beta strandi54 – 57Combined sources4
Helixi64 – 75Combined sources12
Beta strandi92 – 98Combined sources7
Beta strandi107 – 114Combined sources8
Beta strandi131 – 134Combined sources4
Helixi135 – 141Combined sources7
Helixi151 – 170Combined sources20
Helixi173 – 178Combined sources6
Helixi182 – 185Combined sources4
Beta strandi186 – 191Combined sources6
Helixi193 – 195Combined sources3
Turni232 – 235Combined sources4
Helixi291 – 297Combined sources7
Helixi301 – 309Combined sources9
Helixi324 – 330Combined sources7
Helixi334 – 342Combined sources9
Helixi358 – 364Combined sources7
Helixi368 – 376Combined sources9
Helixi392 – 399Combined sources8
Helixi404 – 412Combined sources9
Beta strandi415 – 417Combined sources3
Beta strandi421 – 425Combined sources5
Beta strandi431 – 435Combined sources5
Helixi439 – 441Combined sources3
Helixi444 – 449Combined sources6
Helixi455 – 458Combined sources4
Beta strandi461 – 467Combined sources7
Beta strandi470 – 473Combined sources4
Helixi480 – 485Combined sources6
Helixi487 – 494Combined sources8
Helixi499 – 501Combined sources3
Beta strandi505 – 510Combined sources6
Helixi516 – 519Combined sources4
Helixi525 – 541Combined sources17
Helixi548 – 563Combined sources16
Helixi568 – 571Combined sources4
Beta strandi572 – 574Combined sources3
Helixi578 – 581Combined sources4
Turni582 – 584Combined sources3
Helixi587 – 589Combined sources3
Turni590 – 593Combined sources4
Helixi594 – 596Combined sources3
Helixi598 – 610Combined sources13
Beta strandi612 – 614Combined sources3
Helixi618 – 629Combined sources12
Turni633 – 636Combined sources4
Beta strandi638 – 645Combined sources8
Turni650 – 652Combined sources3
Beta strandi655 – 662Combined sources8
Beta strandi664 – 671Combined sources8
Turni672 – 674Combined sources3
Beta strandi677 – 682Combined sources6
Beta strandi685 – 690Combined sources6
Beta strandi694 – 701Combined sources8
Turni702 – 705Combined sources4
Beta strandi706 – 711Combined sources6
Helixi715 – 728Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3U7DX-ray2.49A/C417-736[»]
4DX8X-ray2.54H/I/J/K1-198[»]
4DXAX-ray1.95B420-736[»]
4HDOX-ray1.67A417-736[»]
4HDQX-ray1.95A417-736[»]
4JIFX-ray1.70B170-198[»]
4TKNX-ray3.00D/E/F225-237[»]
5D68X-ray2.91A/B/C259-736[»]
ProteinModelPortaliO00522.
SMRiO00522.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati287 – 316ANK 1Add BLAST30
Repeati320 – 350ANK 2Add BLAST31
Repeati354 – 383ANK 3Add BLAST30
Repeati388 – 419ANK 4Add BLAST32
Domaini420 – 734FERMPROSITE-ProRule annotationAdd BLAST315

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 170N-terminal domain similar to Nudix hydrolase domainAdd BLAST170
Regioni172 – 195Interaction with ITGB1BP1Add BLAST24
Regioni430 – 452Interaction with RAP1B1 PublicationAdd BLAST23

Domaini

The FERM domain mediates binding to RAP1A and RAP1B and is necessary for binding to phosphatidylinositol 4,5-bisphosphate (PIP2).1 Publication
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.1 Publication

Sequence similaritiesi

Contains 4 ANK repeats.PROSITE-ProRule annotation
Contains 1 FERM domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG4335. Eukaryota.
ENOG410ZV6V. LUCA.
GeneTreeiENSGT00530000063721.
HOGENOMiHOG000252958.
HOVERGENiHBG052292.
InParanoidiO00522.
KOiK17705.
OMAiVCEENKQ.
OrthoDBiEOG091G0IG7.
PhylomeDBiO00522.
TreeFamiTF317921.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR032022. NUDIX.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF16705. NUDIX_5. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 3 hits.
SM00295. B41. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00522-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGNPENIEDA YVAVIRPKNT ASLNSREYRA KSYEILLHEV PIEGQKKKRK
60 70 80 90 100
KVLLETKLQG NSEITQGILD YVVETTKPIS PANQGIRGKR VVLMKKFPLD
110 120 130 140 150
GEKMGREASL FIVPSVVKDN TKYTYTPGCP IFYCLQDIMR VCSESSTHFA
160 170 180 190 200
TLTARMLIAL DKWLDERHAQ SHFIPALFRP SPLERIKTNV INPAYATESG
210 220 230 240 250
QTENSLHMGY SALEIKSKML ALEKADTCIY NPLFGSDLQY TNRVDKVVIN
260 270 280 290 300
PYFGLGAPDY SKIQIPKQEK WQRSMSSVTE DKERQWVDDF PLHRSACEGD
310 320 330 340 350
SELLSRLLSE RFSVNQLDSD HWAPIHYACW YGKVEATRIL LEKGKCNPNL
360 370 380 390 400
LNGQLSSPLH FAAGGGHAEI VQILLNHPET DRHITDQQGR SPLNICEENK
410 420 430 440 450
QNNWEEAAKL LKEAINKPYE KVRIYRMDGS YRSVELKHGN NTTVQQIMEG
460 470 480 490 500
MRLSQETQQY FTIWICSENL SLQLKPYHKP LQHVRDWPEI LAELTNLDPQ
510 520 530 540 550
RETPQLFLRR DVRLPLEVEK QIEDPLAILI LFDEARYNLL KGFYTAPDAK
560 570 580 590 600
LITLASLLLQ IVYGNYESKK HKQGFLNEEN LKSIVPVTKL KSKAPHWTNR
610 620 630 640 650
ILHEYKNLST SEGVSKEMHH LQRMFLQNCW EIPTYGAAFF TGQIFTKASP
660 670 680 690 700
SNHKVIPVYV GVNIKGLHLL NMETKALLIS LKYGCFMWQL GDTDTCFQIH
710 720 730
SMENKMSFIV HTKQAGLVVK LLMKLNGQLM PTERNS
Length:736
Mass (Da):84,348
Last modified:October 11, 2005 - v2
Checksum:iD11F75ED629E85AC
GO
Isoform 2 (identifier: O00522-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-207: Missing.

Show »
Length:529
Mass (Da):60,945
Checksum:iD56082828EEB7094
GO
Isoform 3 (identifier: O00522-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     283-330: Missing.

Note: No experimental confirmation available.
Show »
Length:688
Mass (Da):78,650
Checksum:iE62A1A28360F87F1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti138I → T in AAQ94072 (Ref. 5) Curated1
Sequence conflicti234F → G in AAB58582 (PubMed:9285558).Curated1
Sequence conflicti731P → A in AAB58582 (PubMed:9285558).Curated1
Sequence conflicti731P → A in AAG47774 (PubMed:11161791).Curated1
Sequence conflicti731P → A in AAQ94072 (Ref. 5) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02357397F → S in CCM1. 1 Publication1
Natural variantiVAR_023574569K → E in CCM1. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0158001 – 207Missing in isoform 2. 1 PublicationAdd BLAST207
Alternative sequenceiVSP_043327283 – 330Missing in isoform 3. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90268 mRNA. Translation: AAB58582.1.
U90269 Genomic DNA. Translation: AAC01535.1.
AF310133 mRNA. Translation: AAG47774.1.
AF296765 mRNA. Translation: AAG10220.2.
AF388384 mRNA. Translation: AAM19465.1.
AY380057 mRNA. Translation: AAQ94072.1.
AK055305 mRNA. Translation: BAG51497.1.
AC000120 Genomic DNA. Translation: AAS07420.1.
BC094684 mRNA. Translation: AAH94684.1.
BC098442 mRNA. Translation: AAH98442.1.
AJ294850 mRNA. Translation: CAC17608.1.
AY993945 Genomic DNA. Translation: AAY25568.1.
CCDSiCCDS34679.1. [O00522-3]
CCDS5624.1. [O00522-1]
RefSeqiNP_001013424.1. NM_001013406.1. [O00522-3]
NP_004903.2. NM_004912.3. [O00522-1]
NP_919436.1. NM_194454.1. [O00522-1]
NP_919437.1. NM_194455.1. [O00522-1]
NP_919438.1. NM_194456.1. [O00522-1]
XP_005250717.1. XM_005250660.3. [O00522-1]
XP_005250719.1. XM_005250662.3. [O00522-1]
XP_005250722.1. XM_005250665.3. [O00522-1]
XP_005250723.1. XM_005250666.3. [O00522-1]
XP_005250724.1. XM_005250667.2. [O00522-1]
XP_005250725.1. XM_005250668.3. [O00522-1]
XP_005250726.1. XM_005250669.3. [O00522-1]
XP_006716224.1. XM_006716161.3. [O00522-1]
XP_006716225.1. XM_006716162.3. [O00522-1]
XP_006716226.1. XM_006716163.3. [O00522-1]
XP_011514953.1. XM_011516651.2. [O00522-1]
XP_011514955.1. XM_011516653.2. [O00522-1]
XP_011514956.1. XM_011516654.2. [O00522-1]
XP_011514957.1. XM_011516655.2. [O00522-1]
XP_011514958.1. XM_011516656.2. [O00522-1]
XP_011514959.1. XM_011516657.2. [O00522-1]
XP_011514960.1. XM_011516658.2. [O00522-1]
XP_011514961.1. XM_011516659.2. [O00522-1]
XP_011514962.1. XM_011516660.2. [O00522-1]
XP_011514963.1. XM_011516661.2. [O00522-1]
XP_016868244.1. XM_017012755.1. [O00522-1]
XP_016868245.1. XM_017012756.1. [O00522-1]
XP_016868246.1. XM_017012757.1. [O00522-1]
UniGeneiHs.531987.

Genome annotation databases

EnsembliENST00000340022; ENSP00000344668; ENSG00000001631. [O00522-1]
ENST00000394503; ENSP00000378011; ENSG00000001631. [O00522-3]
ENST00000394505; ENSP00000378013; ENSG00000001631. [O00522-1]
ENST00000394507; ENSP00000378015; ENSG00000001631. [O00522-1]
ENST00000412043; ENSP00000410909; ENSG00000001631. [O00522-1]
GeneIDi889.
KEGGihsa:889.
UCSCiuc003ulr.2. human. [O00522-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90268 mRNA. Translation: AAB58582.1.
U90269 Genomic DNA. Translation: AAC01535.1.
AF310133 mRNA. Translation: AAG47774.1.
AF296765 mRNA. Translation: AAG10220.2.
AF388384 mRNA. Translation: AAM19465.1.
AY380057 mRNA. Translation: AAQ94072.1.
AK055305 mRNA. Translation: BAG51497.1.
AC000120 Genomic DNA. Translation: AAS07420.1.
BC094684 mRNA. Translation: AAH94684.1.
BC098442 mRNA. Translation: AAH98442.1.
AJ294850 mRNA. Translation: CAC17608.1.
AY993945 Genomic DNA. Translation: AAY25568.1.
CCDSiCCDS34679.1. [O00522-3]
CCDS5624.1. [O00522-1]
RefSeqiNP_001013424.1. NM_001013406.1. [O00522-3]
NP_004903.2. NM_004912.3. [O00522-1]
NP_919436.1. NM_194454.1. [O00522-1]
NP_919437.1. NM_194455.1. [O00522-1]
NP_919438.1. NM_194456.1. [O00522-1]
XP_005250717.1. XM_005250660.3. [O00522-1]
XP_005250719.1. XM_005250662.3. [O00522-1]
XP_005250722.1. XM_005250665.3. [O00522-1]
XP_005250723.1. XM_005250666.3. [O00522-1]
XP_005250724.1. XM_005250667.2. [O00522-1]
XP_005250725.1. XM_005250668.3. [O00522-1]
XP_005250726.1. XM_005250669.3. [O00522-1]
XP_006716224.1. XM_006716161.3. [O00522-1]
XP_006716225.1. XM_006716162.3. [O00522-1]
XP_006716226.1. XM_006716163.3. [O00522-1]
XP_011514953.1. XM_011516651.2. [O00522-1]
XP_011514955.1. XM_011516653.2. [O00522-1]
XP_011514956.1. XM_011516654.2. [O00522-1]
XP_011514957.1. XM_011516655.2. [O00522-1]
XP_011514958.1. XM_011516656.2. [O00522-1]
XP_011514959.1. XM_011516657.2. [O00522-1]
XP_011514960.1. XM_011516658.2. [O00522-1]
XP_011514961.1. XM_011516659.2. [O00522-1]
XP_011514962.1. XM_011516660.2. [O00522-1]
XP_011514963.1. XM_011516661.2. [O00522-1]
XP_016868244.1. XM_017012755.1. [O00522-1]
XP_016868245.1. XM_017012756.1. [O00522-1]
XP_016868246.1. XM_017012757.1. [O00522-1]
UniGeneiHs.531987.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3U7DX-ray2.49A/C417-736[»]
4DX8X-ray2.54H/I/J/K1-198[»]
4DXAX-ray1.95B420-736[»]
4HDOX-ray1.67A417-736[»]
4HDQX-ray1.95A417-736[»]
4JIFX-ray1.70B170-198[»]
4TKNX-ray3.00D/E/F225-237[»]
5D68X-ray2.91A/B/C259-736[»]
ProteinModelPortaliO00522.
SMRiO00522.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107330. 17 interactors.
DIPiDIP-40610N.
IntActiO00522. 5 interactors.
STRINGi9606.ENSP00000344668.

PTM databases

iPTMnetiO00522.
PhosphoSitePlusiO00522.

Polymorphism and mutation databases

BioMutaiKRIT1.

Proteomic databases

EPDiO00522.
MaxQBiO00522.
PaxDbiO00522.
PeptideAtlasiO00522.
PRIDEiO00522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340022; ENSP00000344668; ENSG00000001631. [O00522-1]
ENST00000394503; ENSP00000378011; ENSG00000001631. [O00522-3]
ENST00000394505; ENSP00000378013; ENSG00000001631. [O00522-1]
ENST00000394507; ENSP00000378015; ENSG00000001631. [O00522-1]
ENST00000412043; ENSP00000410909; ENSG00000001631. [O00522-1]
GeneIDi889.
KEGGihsa:889.
UCSCiuc003ulr.2. human. [O00522-1]

Organism-specific databases

CTDi889.
DisGeNETi889.
GeneCardsiKRIT1.
GeneReviewsiKRIT1.
HGNCiHGNC:1573. KRIT1.
HPAiHPA049606.
MalaCardsiKRIT1.
MIMi116860. phenotype.
604214. gene.
neXtProtiNX_O00522.
OpenTargetsiENSG00000001631.
Orphaneti221061. Hereditary cerebral cavernous malformation.
PharmGKBiPA26144.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4335. Eukaryota.
ENOG410ZV6V. LUCA.
GeneTreeiENSGT00530000063721.
HOGENOMiHOG000252958.
HOVERGENiHBG052292.
InParanoidiO00522.
KOiK17705.
OMAiVCEENKQ.
OrthoDBiEOG091G0IG7.
PhylomeDBiO00522.
TreeFamiTF317921.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000001631-MONOMER.
ZFISH:ENSG00000001631-MONOMER.

Miscellaneous databases

GeneWikiiKRIT1.
GenomeRNAii889.
PROiO00522.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000001631.
CleanExiHS_KRIT1.
ExpressionAtlasiO00522. baseline and differential.
GenevisibleiO00522. HS.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR032022. NUDIX.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF16705. NUDIX_5. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 3 hits.
SM00295. B41. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKRIT1_HUMAN
AccessioniPrimary (citable) accession number: O00522
Secondary accession number(s): A6NNU0
, O43894, Q506L6, Q6U276, Q75N19, Q9H180, Q9H264, Q9HAX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 11, 2005
Last modified: November 2, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.