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Entry version 168 (29 Sep 2021)
Sequence version 1 (01 May 1999)
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Protein

ARF GTPase-activating protein GIT1

Gene

Git1

Organism
Rattus norvegicus (Rat)
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 (PubMed:9826657).

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 (PubMed:9826657).

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 (PubMed:10938112).

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 (PubMed:15923189).

Plays a role in brain development and function. Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (By similarity).

Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502, PubMed:15800193, PubMed:17310244, PubMed:24297929, PubMed:25009255).

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:12473661).

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 (PubMed:12473661).

In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (PubMed:12629171).

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 (PubMed:25284783).

May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (By similarity).

Required for successful bone regeneration during fracture healing. 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 (By similarity).

May also play a role in angiogenesis during fracture healing (By similarity).

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 (By similarity).

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-RNO-3928664, Ephrin signaling
R-RNO-9013148, CDC42 GTPase cycle
R-RNO-9013149, RAC1 GTPase cycle
R-RNO-9013404, RAC2 GTPase cycle
R-RNO-9013406, RHOQ GTPase cycle
R-RNO-9013420, RHOU GTPase cycle
R-RNO-9013423, RAC3 GTPase cycle
R-RNO-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):
Cool-associated and tyrosine-phosphorylated protein 1
Short name:
CAT-1
Short name:
CAT1
G protein-coupled receptor kinase-interactor 1
GRK-interacting protein 1
GRK-interactor 11 Publication
<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:Git11 Publication
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
69331, Git1

<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

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>Mutagenesisi285F → A: Loss of interaction with FAK1, decreased interaction with PCLO, no effect on interaction with ARHGEF7. 1 Publication1
Mutagenesisi288L → A: Loss of interaction with PCLO and FAK1, no effect on interaction with ARHGEF7. 1 Publication1
Mutagenesisi298R → A: Loss of interaction with FAK1, decreased interaction with PCLO, no effect on interaction with ARHGEF7. 1 Publication1
Mutagenesisi299R → A: Loss of interaction with FAK1, decreased interaction with PCLO, no effect on interaction with ARHGEF7. 1 Publication1
Mutagenesisi392Y → F: Loss of interaction with NCK2. 1 Publication1
Mutagenesisi432 – 483Missing : Decreased homooligomerization and loss of formation of a ternary complex between GIT1, ARHGEF7 and PCLO. Does not affect ARHGEF7- and PCLO-binding to GIT1 monomer. 1 PublicationAdd BLAST52

<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_00000742021 – 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 residuei224PhosphotyrosineBy similarity1
Modified residuei368PhosphoserineBy similarity1
Modified residuei371PhosphoserineCombined sources1
Modified residuei373PhosphothreonineBy similarity1
Modified residuei379PhosphoserineBy similarity1
Modified residuei384PhosphoserineCombined sources1
Modified residuei392PhosphotyrosineBy similarity1
Modified residuei394PhosphoserineBy similarity1
Modified residuei397PhosphoserineCombined sources1
Modified residuei401PhosphothreonineCombined sources1
Modified residuei419PhosphoserineCombined sources1
Modified residuei422PhosphoserineBy similarity1
Modified residuei426PhosphoserineBy similarity1
Modified residuei507PhosphoserineBy similarity1
Modified residuei545PhosphoserineBy similarity1
Modified residuei546PhosphothreonineBy similarity1
Modified residuei554PhosphotyrosineBy similarity1
Modified residuei563PhosphotyrosineBy similarity1
Modified residuei570PhosphoserineCombined sources1
Modified residuei580PhosphoserineCombined sources1
Modified residuei601PhosphoserineCombined sources1
Modified residuei605PhosphoserineBy similarity1
Modified residuei610PhosphothreonineBy similarity1
Modified residuei639PhosphoserineCombined sources1

<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 (PubMed:10938112). 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 (PubMed:17310244).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9Z272

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

More...
PaxDbi
Q9Z272

PRoteomics IDEntifications database

More...
PRIDEi
Q9Z272

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9Z272

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

More...
PhosphoSitePlusi
Q9Z272

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q9Z272

<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

Widely expressed (PubMed:9826657). Expressed at high levels in testis (at protein level) (PubMed:10938112). Expressed in the brain, including in CA1 hippocampal neurons, in the amygdala, and thalamic nuclei (at protein level) (PubMed:10938112, PubMed:12473661, PubMed:12695502, PubMed:12629171, PubMed:15800193, PubMed:17310244, PubMed:24297929, PubMed:25284783).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 the brain cortex and in the hippocampus, continuously expressed from P0 to adult age (at protein level).1 Publication

<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 (PubMed:12473661, PubMed:19136011). May forms heterooligomers with GIT2 (Probable).

Interacts with G protein-coupled receptor kinases, including GRK2, GRK3, GRK5 and GRK6 (PubMed:9826657).

Interacts with PPFIA1, PPFIA2 and PPFIA4 (PubMed:12473661, PubMed:12629171).

Interacts with GRIP1 and forms a ternary complex with PPFIA1 and GRIP1 (PubMed:12473661, PubMed:12629171). Directly interacts with ARHGEF7/beta-PIX, forming in vitro a heptameric complex made of a GIT1 dimer and an ARHGEF7 trimer (PubMed:10938112, PubMed:12473661, PubMed:12629171, PubMed:17310244, PubMed:19136011). Directly interacts with PXN/paxillin; this interaction is enhanced in the presence of ARHGEF7 (PubMed:10938112, PubMed:12153727, PubMed:12473661, PubMed:12629171). Directly interacts (via C-terminus) with TGFB1I1/Hic-5 (via LD motif 3) (PubMed:12153727). Directly interacts with PTK2/FAK1 (PubMed:10938112, PubMed:12473661, PubMed:12629171). May interact with PTK2B/PYK2; this interaction may be indirect (PubMed:12629171).

Interacts with AMPA receptors GRIA2/3 (PubMed:12629171). Directly interacts with protein Piccolo/PCLO (PubMed:12473661).

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 (PubMed:25284783).

Interacts with SCRIB (By similarity).

Interacts (via N- and C-terminus) with ENTR1/SDCCAG3 (via N-terminus); this interaction is direct. May form a tripartite complex with ENTR1 and PTPN13 (By similarity).

Interacts with YWHAZ (By similarity).

Interacts with PAK1 and 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 similarity1 Publication10 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)

More...
BioGRIDi
249809, 9 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q9Z272

Protein interaction database and analysis system

More...
IntActi
Q9Z272, 6 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000052961

<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

More...
SMRi
Q9Z272

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9Z272

<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 PCLO1 PublicationAdd BLAST130
Regioni253 – 424Interaction with PTK2/FAK11 PublicationAdd BLAST172
Regioni254 – 376Interaction with ARHGEF71 PublicationAdd BLAST123
Regioni363 – 425DisorderedSequence analysisAdd BLAST63
Regioni375 – 596Interaction with NCK2 and GRIN3A2 PublicationsAdd BLAST222
Regioni375 – 596Required for localization at synapsesBy similarityAdd BLAST222
Regioni420 – 475Interaction with MAPK1By similarityAdd BLAST56
Regioni429 – 629Interaction with IKBKGBy similarityAdd BLAST201
Regioni574 – 615DisorderedSequence analysisAdd BLAST42
Regioni646 – 770Interaction with PXN and TGFB1I12 PublicationsAdd 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 analysis1 PublicationAdd 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
Compositional biasi574 – 591Polar residuesSequence analysisAdd BLAST18

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The coiled coil region mediates dimerization.2 Publications

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

More...
eggNOGi
KOG0818, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9Z272

Database of Orthologous Groups

More...
OrthoDBi
349344at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9Z272

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.220.150, 1 hit
1.25.40.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

More...
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

More...
PRINTSi
PR00405, REVINTRACTNG

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48403, SSF48403, 1 hit
SSF57863, SSF57863, 1 hit

PROSITE; a protein domain and family database

More...
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

Q9Z272-1 [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 RNQSDLDDQH DYDSVASDED
410 420 430 440 450
TDQEPLPSAG ATRNNRARSM DSSDLSDGAV TLQEYLELKK ALATSEAKVQ
460 470 480 490 500
QLMKVNSSLS DELRKLQREI HKLQAENLQL RQPPGPVPVP SLPSERAEHT
510 520 530 540 550
LMGPGGSTHR RDRQAFSMYE PGSALKPFGG APGDELATRL QPFHSTELED
560 570 580 590 600
DAIYSVHVPA GLYRIRKGVS ASSVTFTPSS PLLSSSQEGS RHASKLSRHG
610 620 630 640 650
SGAESDYENT QSGEPLLGLE GKRFLELSKE DELHAELESL DGDPDPGLPS
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):85,231
Last modified:May 1, 1999 - 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:i797C8EB7FCB3F481
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
A0A0G2K527A0A0G2K527_RAT
ARF GTPase-activating protein GIT1
Git1
752Annotation score:

Annotation score:4 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

More...
DDBJi
Links Updated
AF085693 mRNA Translation: AAC83348.1

NCBI Reference Sequences

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RefSeqi
NP_114002.1, NM_031814.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
83709

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:83709

<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
AF085693 mRNA Translation: AAC83348.1
RefSeqiNP_114002.1, NM_031814.1

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
2JX0NMR-A640-770[»]
2W6AX-ray1.40A/B426-483[»]
6IUHX-ray1.80A/B645-770[»]
6IUIX-ray2.60A/B645-770[»]
SMRiQ9Z272
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi249809, 9 interactors
CORUMiQ9Z272
IntActiQ9Z272, 6 interactors
STRINGi10116.ENSRNOP00000052961

PTM databases

iPTMnetiQ9Z272
PhosphoSitePlusiQ9Z272
SwissPalmiQ9Z272

Proteomic databases

jPOSTiQ9Z272
PaxDbiQ9Z272
PRIDEiQ9Z272

Genome annotation databases

GeneIDi83709
KEGGirno:83709

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
28964
RGDi69331, Git1

Phylogenomic databases

eggNOGiKOG0818, Eukaryota
InParanoidiQ9Z272
OrthoDBi349344at2759
PhylomeDBiQ9Z272

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9Z272

Protein Ontology

More...
PROi
PR:Q9Z272

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

More...
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_RAT
<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: Q9Z272
<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: October 18, 2001
Last sequence update: May 1, 1999
Last modified: September 29, 2021
This is version 168 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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