Q68FF6 · GIT1_MOUSE
- ProteinARF GTPase-activating protein GIT1
- GeneGit1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids770 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity).
Through PAK1 activation, positively regulates microtubule nucleation during interphase. Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (By similarity).
May promote cell motility both by regulating focal complex dynamics and by the activation of RAC1 (By similarity).
May act as scaffold for MAPK1/3 signal transduction, recruiting MAPK1/3 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (By similarity).
Plays a role in brain development and function (PubMed:25792865, PubMed:33010377).
Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (PubMed:20043896, PubMed:29554125).
Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502).
In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502).
May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity).
In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity).
In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (By similarity).
May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (PubMed:21499268).
Required for successful bone regeneration during fracture healing (PubMed:24586541, PubMed:25138700, PubMed:32460388).
The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (PubMed:32460388).
May play a role in angiogenesis during fracture healing (PubMed:24586541, PubMed:31502302).
In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (By similarity).
Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721).
Through PAK1 activation, positively regulates microtubule nucleation during interphase. Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (By similarity).
May promote cell motility both by regulating focal complex dynamics and by the activation of RAC1 (By similarity).
May act as scaffold for MAPK1/3 signal transduction, recruiting MAPK1/3 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (By similarity).
Plays a role in brain development and function (PubMed:25792865, PubMed:33010377).
Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (PubMed:20043896, PubMed:29554125).
Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502).
In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502).
May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity).
In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity).
In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (By similarity).
May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (PubMed:21499268).
Required for successful bone regeneration during fracture healing (PubMed:24586541, PubMed:25138700, PubMed:32460388).
The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (PubMed:32460388).
May play a role in angiogenesis during fracture healing (PubMed:24586541, PubMed:31502302).
In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (By similarity).
Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721).
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameARF GTPase-activating protein GIT1
- Short namesARF GAP GIT1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ68FF6
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Cycles between at least 3 distinct intracellular compartments, including focal adhesions, cytosolic complexes, containing at least PXN/paxillin, ARHGEF7 and PAK1, and membrane protrusions. During cell migration, moves from the disassembling adhesions into the cytosol and towards the leading edge. In adherent cells, localizes to adhesions. Recruitment to adhesions may be mediated by RAC1 and active tyrosine-phosphorylated PXN (By similarity).
May be present in both excitatory and inhibitory synapses. In hippocampal neurons, recruitment of GIT1 to synapses is regulated by ephrinB activation and ephrinB downstream effector GRB4/NCK2. In hippocampal neurons, partially colocalizes with PCLO (By similarity).
Interaction with GRIN3A limits GIT1 synaptic localization (By similarity).
Localization to the centrosome does not depend upon the presence of gamma-tubulin (By similarity).
May be present in both excitatory and inhibitory synapses. In hippocampal neurons, recruitment of GIT1 to synapses is regulated by ephrinB activation and ephrinB downstream effector GRB4/NCK2. In hippocampal neurons, partially colocalizes with PCLO (By similarity).
Interaction with GRIN3A limits GIT1 synaptic localization (By similarity).
Localization to the centrosome does not depend upon the presence of gamma-tubulin (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Knockout mice are born at the expected Mendelian ratio, but have decreased survival compared to wild-type littermates, with about 50% of mutant mice dying postnatally. Surviving animals develop normally and are fertile (PubMed:19273721, PubMed:19383529, PubMed:21499268, PubMed:33010377).
They are however 60-70% smaller than wild-type littermates (PubMed:21499268).
A major abnormality in knockout mice is impaired lung development, characterized by markedly reduced numbers of pulmonary blood vessels and increased alveolar spaces (PubMed:19273721).
Although knockout mice show an unaltered brain gross morphology and neuronal density, they display microcephaly, with an overall brain size about 32% smaller compared to wild-type controls. This phenotype may be due to smaller neuronal size, rather than reduced neuron number, compared to wild-type littermates (PubMed:20043896, PubMed:25792865, PubMed:33010377).
Mutant mice exhibit reduced dendritic length and spine density in the hippocampus and the cortex, which may lead to poor adaptation to new environments and impaired fear response (PubMed:19383529, PubMed:20043896, PubMed:25792865, PubMed:29554125).
This effect on the brain is not uniform. Multiple brain regions suffer local atrophy, including extensive areas of the cortex, thalamus, and hippocampus, white matter tracts have a reduced volume, most notably in the anterior commissure, but also in the cerebral peduncle, fornix, and spinal trigeminal tract. On the other hand, local hypertrophy is detected in the basal ganglia, the accumbens, caudate putamen, and amygdala, as well as in the cortical layer IV, and cerebellum (PubMed:33010377).
The analysis of a genetrap mouse strain lacking GIT1 showed phenotypic traits similar to attention deficit-hyperactivity disorder (ADHD), including hyperactivity, impaired learning and memory, and enhanced theta rhythms. These phenotypic traits could be reversed by amphetamines and methylphenidate (PubMed:21499268, PubMed:26113791).
Abnormal thalamic oscillations, cortical theta rhythms and behavioral hyperactivity were also normalized by ethosuximide (PubMed:26113791).
The abnormal behaviors decreased with age (PubMed:21499268).
ADHD phenotype and response to amphetamines were not seen in other knockout mouse models (PubMed:29554125).
Mutant animals show altered gait (PubMed:25792865).
They exhibit defects in motor coordination and motor learning in rotarod test and abnormal spatial learning and memory (PubMed:25792865, PubMed:29554125).
Knockout mice exhibit delayed bone fracture healing process. They display a persistence of cartilagenous callus and decreased chondrocyte proliferation and apoptosis, leading to their accumulation in the fracture area (PubMed:24586541, PubMed:25138700).
The healing callus exhibits reduced blood vessel volume and number, as well as a reduced osteoclast number (PubMed:24586541, PubMed:31502302).
They are however 60-70% smaller than wild-type littermates (PubMed:21499268).
A major abnormality in knockout mice is impaired lung development, characterized by markedly reduced numbers of pulmonary blood vessels and increased alveolar spaces (PubMed:19273721).
Although knockout mice show an unaltered brain gross morphology and neuronal density, they display microcephaly, with an overall brain size about 32% smaller compared to wild-type controls. This phenotype may be due to smaller neuronal size, rather than reduced neuron number, compared to wild-type littermates (PubMed:20043896, PubMed:25792865, PubMed:33010377).
Mutant mice exhibit reduced dendritic length and spine density in the hippocampus and the cortex, which may lead to poor adaptation to new environments and impaired fear response (PubMed:19383529, PubMed:20043896, PubMed:25792865, PubMed:29554125).
This effect on the brain is not uniform. Multiple brain regions suffer local atrophy, including extensive areas of the cortex, thalamus, and hippocampus, white matter tracts have a reduced volume, most notably in the anterior commissure, but also in the cerebral peduncle, fornix, and spinal trigeminal tract. On the other hand, local hypertrophy is detected in the basal ganglia, the accumbens, caudate putamen, and amygdala, as well as in the cortical layer IV, and cerebellum (PubMed:33010377).
The analysis of a genetrap mouse strain lacking GIT1 showed phenotypic traits similar to attention deficit-hyperactivity disorder (ADHD), including hyperactivity, impaired learning and memory, and enhanced theta rhythms. These phenotypic traits could be reversed by amphetamines and methylphenidate (PubMed:21499268, PubMed:26113791).
Abnormal thalamic oscillations, cortical theta rhythms and behavioral hyperactivity were also normalized by ethosuximide (PubMed:26113791).
The abnormal behaviors decreased with age (PubMed:21499268).
ADHD phenotype and response to amphetamines were not seen in other knockout mouse models (PubMed:29554125).
Mutant animals show altered gait (PubMed:25792865).
They exhibit defects in motor coordination and motor learning in rotarod test and abnormal spatial learning and memory (PubMed:25792865, PubMed:29554125).
Knockout mice exhibit delayed bone fracture healing process. They display a persistence of cartilagenous callus and decreased chondrocyte proliferation and apoptosis, leading to their accumulation in the fracture area (PubMed:24586541, PubMed:25138700).
The healing callus exhibits reduced blood vessel volume and number, as well as a reduced osteoclast number (PubMed:24586541, PubMed:31502302).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 420-475 | Loss of interaction with MAPK1. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 37 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000074201 | 1-770 | ARF GTPase-activating protein GIT1 | |||
Sequence: MSRKGPRAEVCADCSAPDPGWASISRGVLVCDECCSVHRSLGRHISIVKHLRHSAWPPTLLQMVHTLASNGANSIWEHSLLDPAQVQSGRRKANPQDKVHPIKSEFIRAKYQMLAFVHKLPCRDDDGVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGTTPLHVAAKAGQTLQAELLVVYGADPGSPDVNGRTPIDYARQAGHHELAERLVECQYELTDRLAFYLCGRKPDHKNGHYIIPQMADRSRQKCMSQSLDLSELAKAAKKKLQALSNRLFEELAMDVYDEVDRRENDAVWLATQNHSTLVTERSAVPFLPVNPEYSATRNQGRQKLARFNAREFATLIIDILSEAKRRQQGKSLSSPTDNLELSARSQSELDDQHDYDSVASDEDTDQEPLPSAGATRNNRARSMDSSDLSDGAVTLQEYLELKKALATSEAKVQQLMKVNSSLSDELRRLQREIHKLQAENLQLRQPPGPVPPPSLPSERAEHTLMGPGGSTHRRDRQAFSMYEPGSALKPFGGTPGDELATRLQPFHSTELEDDAIYSVHVPAGLYRIRKGVSASSVPFTPSSPLLSCSQEGSRHASKLSRHGSGADSDYENTQSGDPLLGLEGKRFLELSKEDELHPELESLDGDLDPGLPSTEDVILKTEQVTKNIQELLRAAQEFKHDSFVPCSEKIHLAVTEMASLFPKRPALEPVRSSLRLLNASAYRLQSECRKTVPPEPGAPVDFQLLTQQVIQCAYDIAKAAKQLVTITTREKKQ | ||||||
Modified residue | 224 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 368 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 371 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 373 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 379 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 384 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 392 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 394 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 397 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 401 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 419 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 422 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 426 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 507 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 545 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 546 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 554 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 563 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 570 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 580 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 601 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 605 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 610 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 639 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on tyrosine residues by PTK2/FAK1 and SRC in growing fibroblasts. Phosphorylation at Tyr-392 is induced by activation of Ephrin-B1/EFNB1 and catalyzed by SRC family kinases. It is required for the interaction with NCK2 and for GIT1 recruitment to synapses in hippocampal neurons.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the brain (at protein level) (PubMed:15182672, PubMed:16959763, PubMed:17310244, PubMed:19273721, PubMed:19383529, PubMed:21499268, PubMed:24297929).
Also expressed at high levels in lung and heart (PubMed:19273721).
In lung, expressed in endothelial cells, especially in capillaries; also expressed in smooth muscle and epithelial cells of bronchi (at protein level) (PubMed:19273721).
Expressed in bone marrow mesenchymal stem cells, as well as in osteoclasts and bone marrow-derived macrophages (at protein level) (PubMed:25138700, PubMed:32460388).
Also expressed at high levels in lung and heart (PubMed:19273721).
In lung, expressed in endothelial cells, especially in capillaries; also expressed in smooth muscle and epithelial cells of bronchi (at protein level) (PubMed:19273721).
Expressed in bone marrow mesenchymal stem cells, as well as in osteoclasts and bone marrow-derived macrophages (at protein level) (PubMed:25138700, PubMed:32460388).
Developmental stage
In lung, up-regulated from postnatal day 3 (P3). Expression levels decrease after P5 and at P25, they are similar to those observed at P0 (PubMed:19273721).
During the fracture healing process, expression is strongly up-regulated in the healing callus 14 days after the lesion and remains highly expressed at day 21 (PubMed:24586541).
During the fracture healing process, expression is strongly up-regulated in the healing callus 14 days after the lesion and remains highly expressed at day 21 (PubMed:24586541).
Gene expression databases
Interaction
Subunit
Forms homodimers and possibly oligomers (By similarity).
May forms heterooligomers with GIT2 (By similarity).
Interacts with G protein-coupled receptor kinases, including GRK2, GRK3, GRK5 and GRK6 (By similarity).
Interacts with PPFIA1, PPFIA2 and PPFIA4 (By similarity).
Interacts with GRIP1 and forms a ternary complex with PPFIA1 and GRIP1 (By similarity).
Directly interacts with ARHGEF7/beta-PIX, forming in vitro a heptameric complex made of a GIT1 dimer and an ARHGEF7 trimer (By similarity).
Directly interacts with PXN/paxillin; this interaction is enhanced in the presence of ARHGEF7 (By similarity).
Directly interacts (via C-terminus) with TGFB1I1/Hic-5 (via LD motif 3) (PubMed:12153727).
Directly interacts with PTK2/FAK1 (By similarity).
May interact with PTK2B/PYK2; this interaction may be indirect (By similarity).
Interacts with AMPA receptors GRIA2/3 (By similarity).
Directly interacts with protein Piccolo/PCLO (By similarity).
Forms a complex with Ephrin-B1/EFNB1 and NCK2/GRB4 (via SH2); this interaction is important for spine morphogenesis and synapse formation. Interaction with NCK2 is transient and depends upon GIT1 phosphorylation at Tyr-392 (PubMed:17310244).
Interacts with GRIN3A/GluN3A (via C-terminus); this interaction competes with GIT1 interaction with ARHGEF7 and limits synaptic localization of GIT1 (PubMed:24297929).
Interacts with IKBKG/NEMO in resting bone mesenchymal stem cells, as well as in TNF-stimulated cells; this interaction may increase IKBKG affinity for 'Lys-63'-linked polyubiquitin chains (By similarity).
Interacts with GABA(A) receptors, including GABRB3 and GABRG2 (By similarity).
Interacts with SCRIB (PubMed:15182672).
Interacts (via N- and C-terminus) with ENTR1/SDCCAG3 (via N-terminus); this interaction is direct (PubMed:23108400).
May form a tripartite complex with ENTR1 and PTPN13 (By similarity).
Interacts with YWHAZ (PubMed:16959763).
Interacts with PAK1 (By similarity).
Interacts with PAK3 (By similarity).
Directly interacts (via N-terminus) with gamma-tubulin (By similarity).
Interacts with MAPK1 and MAPK3; this interaction is required for MAPK1/3 recruitment to focal adhesions (PubMed:15923189).
May forms heterooligomers with GIT2 (By similarity).
Interacts with G protein-coupled receptor kinases, including GRK2, GRK3, GRK5 and GRK6 (By similarity).
Interacts with PPFIA1, PPFIA2 and PPFIA4 (By similarity).
Interacts with GRIP1 and forms a ternary complex with PPFIA1 and GRIP1 (By similarity).
Directly interacts with ARHGEF7/beta-PIX, forming in vitro a heptameric complex made of a GIT1 dimer and an ARHGEF7 trimer (By similarity).
Directly interacts with PXN/paxillin; this interaction is enhanced in the presence of ARHGEF7 (By similarity).
Directly interacts (via C-terminus) with TGFB1I1/Hic-5 (via LD motif 3) (PubMed:12153727).
Directly interacts with PTK2/FAK1 (By similarity).
May interact with PTK2B/PYK2; this interaction may be indirect (By similarity).
Interacts with AMPA receptors GRIA2/3 (By similarity).
Directly interacts with protein Piccolo/PCLO (By similarity).
Forms a complex with Ephrin-B1/EFNB1 and NCK2/GRB4 (via SH2); this interaction is important for spine morphogenesis and synapse formation. Interaction with NCK2 is transient and depends upon GIT1 phosphorylation at Tyr-392 (PubMed:17310244).
Interacts with GRIN3A/GluN3A (via C-terminus); this interaction competes with GIT1 interaction with ARHGEF7 and limits synaptic localization of GIT1 (PubMed:24297929).
Interacts with IKBKG/NEMO in resting bone mesenchymal stem cells, as well as in TNF-stimulated cells; this interaction may increase IKBKG affinity for 'Lys-63'-linked polyubiquitin chains (By similarity).
Interacts with GABA(A) receptors, including GABRB3 and GABRG2 (By similarity).
Interacts with SCRIB (PubMed:15182672).
Interacts (via N- and C-terminus) with ENTR1/SDCCAG3 (via N-terminus); this interaction is direct (PubMed:23108400).
May form a tripartite complex with ENTR1 and PTPN13 (By similarity).
Interacts with YWHAZ (PubMed:16959763).
Interacts with PAK1 (By similarity).
Interacts with PAK3 (By similarity).
Directly interacts (via N-terminus) with gamma-tubulin (By similarity).
Interacts with MAPK1 and MAPK3; this interaction is required for MAPK1/3 recruitment to focal adhesions (PubMed:15923189).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q68FF6 | Arhgef7 Q9ES28 | 2 | EBI-645933, EBI-642580 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, zinc finger, repeat, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-124 | Arf-GAP | ||||
Sequence: MSRKGPRAEVCADCSAPDPGWASISRGVLVCDECCSVHRSLGRHISIVKHLRHSAWPPTLLQMVHTLASNGANSIWEHSLLDPAQVQSGRRKANPQDKVHPIKSEFIRAKYQMLAFVHKLPCRD | ||||||
Region | 1-124 | Interaction with gamma-tubulin and localization to the centrosome | ||||
Sequence: MSRKGPRAEVCADCSAPDPGWASISRGVLVCDECCSVHRSLGRHISIVKHLRHSAWPPTLLQMVHTLASNGANSIWEHSLLDPAQVQSGRRKANPQDKVHPIKSEFIRAKYQMLAFVHKLPCRD | ||||||
Zinc finger | 11-34 | C4-type | ||||
Sequence: CADCSAPDPGWASISRGVLVCDEC | ||||||
Repeat | 132-161 | ANK 1 | ||||
Sequence: DLSKQLHSSVRTGNLETCLRLLSLGAQANF | ||||||
Repeat | 166-195 | ANK 2 | ||||
Sequence: KGTTPLHVAAKAGQTLQAELLVVYGADPGS | ||||||
Repeat | 199-228 | ANK 3 | ||||
Sequence: NGRTPIDYARQAGHHELAERLVECQYELTD | ||||||
Region | 245-374 | Interaction with PCLO | ||||
Sequence: HYIIPQMADRSRQKCMSQSLDLSELAKAAKKKLQALSNRLFEELAMDVYDEVDRRENDAVWLATQNHSTLVTERSAVPFLPVNPEYSATRNQGRQKLARFNAREFATLIIDILSEAKRRQQGKSLSSPTD | ||||||
Region | 253-424 | Interaction with PTK2/FAK1 | ||||
Sequence: DRSRQKCMSQSLDLSELAKAAKKKLQALSNRLFEELAMDVYDEVDRRENDAVWLATQNHSTLVTERSAVPFLPVNPEYSATRNQGRQKLARFNAREFATLIIDILSEAKRRQQGKSLSSPTDNLELSARSQSELDDQHDYDSVASDEDTDQEPLPSAGATRNNRARSMDSSD | ||||||
Region | 254-376 | Interaction with ARHGEF7 | ||||
Sequence: RSRQKCMSQSLDLSELAKAAKKKLQALSNRLFEELAMDVYDEVDRRENDAVWLATQNHSTLVTERSAVPFLPVNPEYSATRNQGRQKLARFNAREFATLIIDILSEAKRRQQGKSLSSPTDNL | ||||||
Compositional bias | 363-380 | Polar residues | ||||
Sequence: RQQGKSLSSPTDNLELSA | ||||||
Region | 363-425 | Disordered | ||||
Sequence: RQQGKSLSSPTDNLELSARSQSELDDQHDYDSVASDEDTDQEPLPSAGATRNNRARSMDSSDL | ||||||
Region | 375-596 | Interaction with NCK2 and GRIN3A | ||||
Sequence: NLELSARSQSELDDQHDYDSVASDEDTDQEPLPSAGATRNNRARSMDSSDLSDGAVTLQEYLELKKALATSEAKVQQLMKVNSSLSDELRRLQREIHKLQAENLQLRQPPGPVPPPSLPSERAEHTLMGPGGSTHRRDRQAFSMYEPGSALKPFGGTPGDELATRLQPFHSTELEDDAIYSVHVPAGLYRIRKGVSASSVPFTPSSPLLSCSQEGSRHASKL | ||||||
Region | 375-596 | Required for localization at synapses | ||||
Sequence: NLELSARSQSELDDQHDYDSVASDEDTDQEPLPSAGATRNNRARSMDSSDLSDGAVTLQEYLELKKALATSEAKVQQLMKVNSSLSDELRRLQREIHKLQAENLQLRQPPGPVPPPSLPSERAEHTLMGPGGSTHRRDRQAFSMYEPGSALKPFGGTPGDELATRLQPFHSTELEDDAIYSVHVPAGLYRIRKGVSASSVPFTPSSPLLSCSQEGSRHASKL | ||||||
Compositional bias | 407-425 | Polar residues | ||||
Sequence: PSAGATRNNRARSMDSSDL | ||||||
Region | 420-475 | Interaction with MAPK1 | ||||
Sequence: MDSSDLSDGAVTLQEYLELKKALATSEAKVQQLMKVNSSLSDELRRLQREIHKLQA | ||||||
Region | 429-629 | Interaction with IKBKG | ||||
Sequence: AVTLQEYLELKKALATSEAKVQQLMKVNSSLSDELRRLQREIHKLQAENLQLRQPPGPVPPPSLPSERAEHTLMGPGGSTHRRDRQAFSMYEPGSALKPFGGTPGDELATRLQPFHSTELEDDAIYSVHVPAGLYRIRKGVSASSVPFTPSSPLLSCSQEGSRHASKLSRHGSGADSDYENTQSGDPLLGLEGKRFLELSK | ||||||
Coiled coil | 449-483 | |||||
Sequence: VQQLMKVNSSLSDELRRLQREIHKLQAENLQLRQP | ||||||
Region | 578-615 | Disordered | ||||
Sequence: PSSPLLSCSQEGSRHASKLSRHGSGADSDYENTQSGDP | ||||||
Region | 646-770 | Interaction with PXN and TGFB1I1 | ||||
Sequence: PGLPSTEDVILKTEQVTKNIQELLRAAQEFKHDSFVPCSEKIHLAVTEMASLFPKRPALEPVRSSLRLLNASAYRLQSECRKTVPPEPGAPVDFQLLTQQVIQCAYDIAKAAKQLVTITTREKKQ |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length770
- Mass (Da)85,300
- Last updated2004-10-11 v1
- ChecksumC516E7A49578D0B4
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5F258 | Q5F258_MOUSE | Git1 | 761 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 363-380 | Polar residues | ||||
Sequence: RQQGKSLSSPTDNLELSA | ||||||
Compositional bias | 407-425 | Polar residues | ||||
Sequence: PSAGATRNNRARSMDSSDL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL607072 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC079870 EMBL· GenBank· DDBJ | AAH79870.1 EMBL· GenBank· DDBJ | mRNA |