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Entry version 169 (29 Sep 2021)
Sequence version 1 (11 Oct 2004)
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Protein

ARF GTPase-activating protein GIT1

Gene

Git1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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:25138700, PubMed:24586541, 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).

By similarity11 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri11 – 34C4-typePROSITE-ProRule annotationAdd BLAST24

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGTPase activation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-3928664, Ephrin signaling
R-MMU-9013148, CDC42 GTPase cycle
R-MMU-9013149, RAC1 GTPase cycle
R-MMU-9013404, RAC2 GTPase cycle
R-MMU-9013406, RHOQ GTPase cycle
R-MMU-9013420, RHOU GTPase cycle
R-MMU-9013423, RAC3 GTPase cycle
R-MMU-9013424, RHOV GTPase cycle

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ARF GTPase-activating protein GIT1
Short name:
ARF GAP GIT1
Alternative name(s):
G protein-coupled receptor kinase-interactor 1
GRK-interacting protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Git1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:1927140, Git1

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSMUSG00000011877

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

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:25138700, PubMed:24586541). The healing callus exhibits reduced blood vessel volume and number, as well as a reduced osteoclast number (PubMed:24586541, PubMed:31502302).11 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi420 – 475Missing : Loss of interaction with MAPK1. 1 PublicationAdd BLAST56

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000742011 – 770ARF GTPase-activating protein GIT1Add BLAST770

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei224PhosphotyrosineCombined sources1
Modified residuei368PhosphoserineCombined sources1
Modified residuei371PhosphoserineCombined sources1
Modified residuei373PhosphothreonineBy similarity1
Modified residuei379PhosphoserineBy similarity1
Modified residuei384PhosphoserineBy similarity1
Modified residuei392PhosphotyrosineBy similarity1
Modified residuei394PhosphoserineCombined sources1
Modified residuei397PhosphoserineCombined sources1
Modified residuei401PhosphothreonineCombined sources1
Modified residuei419PhosphoserineCombined sources1
Modified residuei422PhosphoserineCombined sources1
Modified residuei426PhosphoserineCombined sources1
Modified residuei507PhosphoserineBy similarity1
Modified residuei545PhosphoserineCombined sources1
Modified residuei546PhosphothreonineCombined sources1
Modified residuei554PhosphotyrosineCombined sources1
Modified residuei563PhosphotyrosineCombined sources1
Modified residuei570PhosphoserineCombined sources1
Modified residuei580PhosphoserineBy similarity1
Modified residuei601PhosphoserineCombined sources1
Modified residuei605PhosphoserineCombined sources1
Modified residuei610PhosphothreonineCombined sources1
Modified residuei639PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q68FF6

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q68FF6

MaxQB - The MaxQuant DataBase

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MaxQBi
Q68FF6

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q68FF6

PeptideAtlas

More...
PeptideAtlasi
Q68FF6

PRoteomics IDEntifications database

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PRIDEi
Q68FF6

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
268825

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q68FF6

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q68FF6

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q68FF6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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).9 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000011877, Expressed in cerebral cortex and 293 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q68FF6, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q68FF6, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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 recruitement to focal adhesions (PubMed:15923189).

By similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
229822, 31 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q68FF6

Protein interaction database and analysis system

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IntActi
Q68FF6, 35 interactors

Molecular INTeraction database

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MINTi
Q68FF6

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000037210

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q68FF6, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1770
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q68FF6

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 124Arf-GAPPROSITE-ProRule annotationAdd BLAST124
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati132 – 161ANK 1Add BLAST30
Repeati166 – 195ANK 2Add BLAST30
Repeati199 – 228ANK 3Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 124Interaction with gamma-tubulin and localization to the centrosomeBy similarityAdd BLAST124
Regioni245 – 374Interaction with PCLOBy similarityAdd BLAST130
Regioni253 – 424Interaction with PTK2/FAK1By similarityAdd BLAST172
Regioni254 – 376Interaction with ARHGEF7By similarityAdd BLAST123
Regioni363 – 425DisorderedSequence analysisAdd BLAST63
Regioni375 – 596Interaction with NCK2 and GRIN3ABy similarityAdd BLAST222
Regioni375 – 596Required for localization at synapsesBy similarityAdd BLAST222
Regioni420 – 475Interaction with MAPK11 PublicationAdd BLAST56
Regioni429 – 629Interaction with IKBKGBy similarityAdd BLAST201
Regioni578 – 615DisorderedSequence analysisAdd BLAST38
Regioni646 – 770Interaction with PXN and TGFB1I1By similarityAdd BLAST125

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili449 – 483Sequence analysisAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi363 – 380Polar residuesSequence analysisAdd BLAST18
Compositional biasi407 – 425Polar residuesSequence analysisAdd BLAST19

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri11 – 34C4-typePROSITE-ProRule annotationAdd BLAST24

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0818, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000159604

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q68FF6

Identification of Orthologs from Complete Genome Data

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OMAi
YSVHVPS

Database of Orthologous Groups

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OrthoDBi
349344at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q68FF6

TreeFam database of animal gene trees

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TreeFami
TF317762

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.220.150, 1 hit
1.25.40.20, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR037278, ARFGAP/RecO
IPR001164, ArfGAP_dom
IPR038508, ArfGAP_dom_sf
IPR032352, GIT1/2_CC
IPR022018, GIT1_C
IPR013724, GIT_SHD

Pfam protein domain database

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Pfami
View protein in Pfam
PF12796, Ank_2, 1 hit
PF01412, ArfGap, 1 hit
PF12205, GIT1_C, 1 hit
PF16559, GIT_CC, 1 hit
PF08518, GIT_SHD, 2 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00405, REVINTRACTNG

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00248, ANK, 3 hits
SM00105, ArfGap, 1 hit
SM00555, GIT, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48403, SSF48403, 1 hit
SSF57863, SSF57863, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 1 hit
PS50115, ARFGAP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q68FF6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRKGPRAEV CADCSAPDPG WASISRGVLV CDECCSVHRS LGRHISIVKH
60 70 80 90 100
LRHSAWPPTL LQMVHTLASN GANSIWEHSL LDPAQVQSGR RKANPQDKVH
110 120 130 140 150
PIKSEFIRAK YQMLAFVHKL PCRDDDGVTA KDLSKQLHSS VRTGNLETCL
160 170 180 190 200
RLLSLGAQAN FFHPEKGTTP LHVAAKAGQT LQAELLVVYG ADPGSPDVNG
210 220 230 240 250
RTPIDYARQA GHHELAERLV ECQYELTDRL AFYLCGRKPD HKNGHYIIPQ
260 270 280 290 300
MADRSRQKCM SQSLDLSELA KAAKKKLQAL SNRLFEELAM DVYDEVDRRE
310 320 330 340 350
NDAVWLATQN HSTLVTERSA VPFLPVNPEY SATRNQGRQK LARFNAREFA
360 370 380 390 400
TLIIDILSEA KRRQQGKSLS SPTDNLELSA RSQSELDDQH DYDSVASDED
410 420 430 440 450
TDQEPLPSAG ATRNNRARSM DSSDLSDGAV TLQEYLELKK ALATSEAKVQ
460 470 480 490 500
QLMKVNSSLS DELRRLQREI HKLQAENLQL RQPPGPVPPP SLPSERAEHT
510 520 530 540 550
LMGPGGSTHR RDRQAFSMYE PGSALKPFGG TPGDELATRL QPFHSTELED
560 570 580 590 600
DAIYSVHVPA GLYRIRKGVS ASSVPFTPSS PLLSCSQEGS RHASKLSRHG
610 620 630 640 650
SGADSDYENT QSGDPLLGLE GKRFLELSKE DELHPELESL DGDLDPGLPS
660 670 680 690 700
TEDVILKTEQ VTKNIQELLR AAQEFKHDSF VPCSEKIHLA VTEMASLFPK
710 720 730 740 750
RPALEPVRSS LRLLNASAYR LQSECRKTVP PEPGAPVDFQ LLTQQVIQCA
760 770
YDIAKAAKQL VTITTREKKQ
Length:770
Mass (Da):85,300
Last modified:October 11, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC516E7A49578D0B4
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5F258Q5F258_MOUSE
ARF GTPase-activating protein GIT1
Git1
761Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AL607072 Genomic DNA No translation available.
BC079870 mRNA Translation: AAH79870.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS25080.1

NCBI Reference Sequences

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RefSeqi
NP_001004144.1, NM_001004144.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000037285; ENSMUSP00000037210; ENSMUSG00000011877

Database of genes from NCBI RefSeq genomes

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GeneIDi
216963

UCSC genome browser

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UCSCi
uc007kgy.1, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL607072 Genomic DNA No translation available.
BC079870 mRNA Translation: AAH79870.1
CCDSiCCDS25080.1
RefSeqiNP_001004144.1, NM_001004144.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6JMUX-ray2.00A/B640-770[»]
SMRiQ68FF6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi229822, 31 interactors
CORUMiQ68FF6
IntActiQ68FF6, 35 interactors
MINTiQ68FF6
STRINGi10090.ENSMUSP00000037210

PTM databases

iPTMnetiQ68FF6
PhosphoSitePlusiQ68FF6
SwissPalmiQ68FF6

Proteomic databases

EPDiQ68FF6
jPOSTiQ68FF6
MaxQBiQ68FF6
PaxDbiQ68FF6
PeptideAtlasiQ68FF6
PRIDEiQ68FF6
ProteomicsDBi268825

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
1365, 486 antibodies

The DNASU plasmid repository

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DNASUi
216963

Genome annotation databases

EnsembliENSMUST00000037285; ENSMUSP00000037210; ENSMUSG00000011877
GeneIDi216963
UCSCiuc007kgy.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
28964
MGIiMGI:1927140, Git1
VEuPathDBiHostDB:ENSMUSG00000011877

Phylogenomic databases

eggNOGiKOG0818, Eukaryota
GeneTreeiENSGT00940000159604
InParanoidiQ68FF6
OMAiYSVHVPS
OrthoDBi349344at2759
PhylomeDBiQ68FF6
TreeFamiTF317762

Enzyme and pathway databases

ReactomeiR-MMU-3928664, Ephrin signaling
R-MMU-9013148, CDC42 GTPase cycle
R-MMU-9013149, RAC1 GTPase cycle
R-MMU-9013404, RAC2 GTPase cycle
R-MMU-9013406, RHOQ GTPase cycle
R-MMU-9013420, RHOU GTPase cycle
R-MMU-9013423, RAC3 GTPase cycle
R-MMU-9013424, RHOV GTPase cycle

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
216963, 0 hits in 61 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Git1, mouse

Protein Ontology

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PROi
PR:Q68FF6
RNActiQ68FF6, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000011877, Expressed in cerebral cortex and 293 other tissues
ExpressionAtlasiQ68FF6, baseline and differential
GenevisibleiQ68FF6, MM

Family and domain databases

Gene3Di1.10.220.150, 1 hit
1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR037278, ARFGAP/RecO
IPR001164, ArfGAP_dom
IPR038508, ArfGAP_dom_sf
IPR032352, GIT1/2_CC
IPR022018, GIT1_C
IPR013724, GIT_SHD
PfamiView protein in Pfam
PF12796, Ank_2, 1 hit
PF01412, ArfGap, 1 hit
PF12205, GIT1_C, 1 hit
PF16559, GIT_CC, 1 hit
PF08518, GIT_SHD, 2 hits
PRINTSiPR00405, REVINTRACTNG
SMARTiView protein in SMART
SM00248, ANK, 3 hits
SM00105, ArfGap, 1 hit
SM00555, GIT, 2 hits
SUPFAMiSSF48403, SSF48403, 1 hit
SSF57863, SSF57863, 1 hit
PROSITEiView protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 1 hit
PS50115, ARFGAP, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGIT1_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q68FF6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 11, 2004
Last modified: September 29, 2021
This is version 169 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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