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Protein

Rho guanine nucleotide exchange factor 7

Gene

Arhgef7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. May function as a positive regulator of apoptosis. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons (By similarity).By similarity1 Publication

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: MGI
  • protein kinase binding Source: BHF-UCL
  • Rho guanyl-nucleotide exchange factor activity Source: InterPro

GO - Biological processi

  • focal adhesion assembly Source: MGI
  • Golgi organization Source: MGI
  • hematopoietic progenitor cell differentiation Source: MGI
  • intracellular signal transduction Source: InterPro
  • lamellipodium assembly Source: UniProtKB
  • nervous system development Source: UniProtKB-KW
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of fibroblast migration Source: MGI
  • positive regulation of growth hormone secretion Source: MGI
  • positive regulation of GTPase activity Source: UniProtKB
  • positive regulation of lamellipodium morphogenesis Source: MGI
  • positive regulation of protein binding Source: MGI
  • positive regulation of substrate adhesion-dependent cell spreading Source: MGI
  • regulation of GTP binding Source: MGI
  • regulation of Rho protein signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Neurogenesis

Enzyme and pathway databases

ReactomeiR-MMU-182971. EGFR downregulation.
R-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-3928664. Ephrin signaling.
R-MMU-416482. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 7
Alternative name(s):
Beta-Pix
PAK-interacting exchange factor beta
p85SPR
Gene namesi
Name:Arhgef7
Synonyms:Kiaa0142, Pak3bp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1860493. Arhgef7.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cytosol Source: MGI
  • focal adhesion Source: MGI
  • lamellipodium Source: UniProtKB
  • neuronal cell body Source: MGI
  • neuron projection Source: MGI
  • plasma membrane Source: MGI
  • protein complex Source: MGI
  • ruffle Source: UniProtKB-SubCell
  • storage vacuole Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 862862Rho guanine nucleotide exchange factor 7PRO_0000080922Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei132 – 1321PhosphoserineCombined sources
Modified residuei155 – 1551PhosphoserineCombined sources
Modified residuei164 – 1641PhosphoserineCombined sources
Modified residuei228 – 2281PhosphoserineBy similarity
Modified residuei236 – 2361PhosphoserineBy similarity
Modified residuei497 – 4971PhosphoserineCombined sources
Modified residuei673 – 6731PhosphoserineCombined sources
Modified residuei776 – 7761PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on Ser-673 by CaMK1; enhancement of GEF activity and downstream activation of RAC1 (By similarity). Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1.By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9ES28.
MaxQBiQ9ES28.
PaxDbiQ9ES28.
PRIDEiQ9ES28.

PTM databases

iPTMnetiQ9ES28.
PhosphoSiteiQ9ES28.

Expressioni

Tissue specificityi

Seems to be expressed in the central nervous system. Isoform B, isoform C and isoform E are expressed with highest levels in brain and testis.2 Publications

Gene expression databases

BgeeiQ9ES28.
CleanExiMM_ARHGEF7.
ExpressionAtlasiQ9ES28. baseline and differential.
GenevisibleiQ9ES28. MM.

Interactioni

Subunit structurei

Interacts with PAK kinases through the SH3 domain. Interacts with unphosphorylated PAK1. Interacts with ITCH. Interacts with SCRIB; interaction is direct and may play a role in regulation of apoptosis (By similarity). Interacts with GIT1 and TGFB1I1. Interacts with FRMPD4 (via N-terminus). Interacts with CaMK1. Interacts with BIN2 (By similarity). Interacts with PTK2/FAK1 and RAC1. Interacts with PARVB.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Git1Q68FF62EBI-642580,EBI-645933
Git1Q9Z2722EBI-642580,EBI-3842379From a different organism.
GIT2Q141612EBI-642580,EBI-1046878From a different organism.
Git2Q9JLQ26EBI-642580,EBI-642860
PARVBQ9HBI110EBI-642580,EBI-1047679From a different organism.
ParvbQ9ES462EBI-642580,EBI-6914996
Shank1Q9WV486EBI-8620514,EBI-80909From a different organism.
Shank2Q9QX744EBI-8620514,EBI-397902From a different organism.
Shank3Q9JLU42EBI-8620514,EBI-6271152From a different organism.

GO - Molecular functioni

  • protein kinase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi207566. 13 interactions.
IntActiQ9ES28. 19 interactions.
MINTiMINT-1786275.
STRINGi10090.ENSMUSP00000106534.

Structurei

Secondary structure

1
862
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi167 – 1726Combined sources
Beta strandi189 – 1957Combined sources
Beta strandi199 – 2057Combined sources
Beta strandi208 – 2136Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2193Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ESWX-ray2.01A/B164-220[»]
ProteinModelPortaliQ9ES28.
SMRiQ9ES28. Positions 1-116, 130-557, 803-862.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ES28.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 111111CHPROSITE-ProRule annotationAdd
BLAST
Domaini163 – 22260SH3PROSITE-ProRule annotationAdd
BLAST
Domaini250 – 430181DHPROSITE-ProRule annotationAdd
BLAST
Domaini452 – 557106PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili804 – 85451Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiKOG2070. Eukaryota.
ENOG410XNNP. LUCA.
GeneTreeiENSGT00760000118925.
HOVERGENiHBG050569.
InParanoidiQ9ES28.
KOiK13710.
OMAiPQMKSLY.
OrthoDBiEOG708W04.
PhylomeDBiQ9ES28.
TreeFamiTF316105.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR032409. GEF_CC.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF16523. betaPIX_CC. 1 hit.
PF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform B (identifier: Q9ES28-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNSAEQTVTW LITLGVLESP KKTISDPEVF LQASLKDGVV LCRLLERLLP
60 70 80 90 100
GTIEKVYPEP RNESECLSNI REFLRACGAS LRLETFDAND LYQGQNFNKV
110 120 130 140 150
LSSLVTLNKV TADIGLGSDS VCARPSSHRI KSFDSLGSQS SHSRTSKLLQ
160 170 180 190 200
SQYRSLDMTD NTNSQLVVRA KFNFQQTNED ELSFSKGDVI HVTRVEEGGW
210 220 230 240 250
WEGTHNGRTG WFPSNYVREI KPSEKPVSPK SGTLKSPPKG FDTTAINKSY
260 270 280 290 300
YNVVLQNILE TEHEYSKELQ SVLSTYLRPL QTSDKLSSAN TSYLMGNLEE
310 320 330 340 350
ISSFQQVLVQ SLEECTKSPE AQQRVGGCFL SLMPQMRTLY LAYCANHPSA
360 370 380 390 400
VSVLTEHSED LGEFMETKGA SSPGILVLTT GLSKPFMRLD KYPTLLKELE
410 420 430 440 450
RHMEDYHPDR QDIQKSMTAF KNLSAQCQEV RKRKELELQI LTEPIRSWEG
460 470 480 490 500
DDIKTLGSVT YMSQVTIQCA GSEEKNERYL LLFPNLLLML SASPRMSGFI
510 520 530 540 550
YQGKLPTTGM TITKLEDSEN HRNAFEISGS MIERILVSCT SQQDLHEWVE
560 570 580 590 600
HLQKQTKVTS VSNPTIKPHS VPSHTLPSHP LTPSSKHADS KPVALTPAYH
610 620 630 640 650
TLPHPSHHGT PHTTISWGPL EPPKTPKPWS LSCLRPAPPL RPSAALCYKE
660 670 680 690 700
DLSKSPKTMK KLLPKRKPER KPSDEEFAVR KSTAALEEDA QILKVIEAYC
710 720 730 740 750
TSAKTRQTLN STWQGTDLMH NHVLADDDQS SLDSLGRRSS LSRLEPSDLS
760 770 780 790 800
EDSEYDSIWT AHSYRMGSAS RSRKESAPQV LLPEEEKIIV EETKSNGQTV
810 820 830 840 850
IEEKSLVDTV YALKDEVQEL RQDNKKMKKS LEEEQRARKD LEKLVRKVLK
860
NMNDPAWDET NL
Length:862
Mass (Da):97,056
Last modified:February 6, 2007 - v2
Checksum:i46D61B606B8391B4
GO
Isoform A (identifier: Q9ES28-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     712-771: TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASR → S

Show »
Length:803
Mass (Da):90,390
Checksum:iC829852E0C7EA8CD
GO
Isoform C (identifier: Q9ES28-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     576-650: Missing.

Show »
Length:787
Mass (Da):88,950
Checksum:iEEB889F6BE45B63D
GO
Isoform D (identifier: Q9ES28-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.
     53-55: IEK → MLQ
     712-771: TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASR → S

Show »
Length:751
Mass (Da):84,698
Checksum:i43F22A9DF918F599
GO
Isoform E (identifier: Q9ES28-5) [UniParc]FASTAAdd to basket

Also known as: d

The sequence of this isoform differs from the canonical sequence as follows:
     772-824: SRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQELRQDN → KSCCSYISHQN
     825-862: Missing.

Show »
Length:782
Mass (Da):87,673
Checksum:i9B38100E66FFDAD9
GO
Isoform F (identifier: Q9ES28-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.
     53-55: IEK → MLQ
     712-820: TWQGTDLMHN...YALKDEVQEL → SECRSSPRVGTDYKQLLHGLAALEREVSGA
     821-862: Missing.

Show »
Length:689
Mass (Da):77,189
Checksum:i78B03ECBB4E8A3F4
GO
Isoform G (identifier: Q9ES28-7) [UniParc]FASTAAdd to basket

Also known as: b(L)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.
     53-55: IEK → MLQ

Show »
Length:810
Mass (Da):91,364
Checksum:i61F15448C29152B0
GO
Isoform H (identifier: Q9ES28-8) [UniParc]FASTAAdd to basket

Also known as: b

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.

Note: Produced by alternative initiation at Met-158 of isoform G.
Show »
Length:705
Mass (Da):79,696
Checksum:i60F3F1CA3589637C
GO

Sequence cautioni

The sequence AAB57691.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAG18017.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAG18018.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH44838.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAK97363.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC35033.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC97874.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE23905.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti485 – 4884NLLL → KPSV in AAO65479 (PubMed:15120616).Curated
Sequence conflicti485 – 4884NLLL → KPSV in AAG18017 (PubMed:10860822).Curated
Sequence conflicti485 – 4884NLLL → KPSV in AAG18018 (PubMed:10860822).Curated
Sequence conflicti485 – 4884NLLL → KPSV in AAB57691 (PubMed:9207241).Curated
Sequence conflicti492 – 4921A → P in AAO65479 (PubMed:15120616).Curated
Sequence conflicti492 – 4921A → P in AAG18017 (PubMed:10860822).Curated
Sequence conflicti492 – 4921A → P in AAG18018 (PubMed:10860822).Curated
Sequence conflicti492 – 4921A → P in AAB57691 (PubMed:9207241).Curated
Sequence conflicti616 – 6161S → R in AAO65479 (PubMed:15120616).Curated
Sequence conflicti616 – 6161S → R in AAG18017 (PubMed:10860822).Curated
Sequence conflicti616 – 6161S → R in AAB57691 (PubMed:9207241).Curated
Sequence conflicti624 – 6252KT → PH in AAB57691 (PubMed:9207241).Curated
Sequence conflicti628 – 6281P → A in AAO65479 (PubMed:15120616).Curated
Sequence conflicti628 – 6281P → A in AAB57691 (PubMed:9207241).Curated
Sequence conflicti630 – 6301S → G in AAB57691 (PubMed:9207241).Curated
Sequence conflicti633 – 6331C → W in AAO65479 (PubMed:15120616).Curated
Sequence conflicti633 – 6331C → W in AAG18017 (PubMed:10860822).Curated
Sequence conflicti633 – 6331C → W in AAB57691 (PubMed:9207241).Curated
Sequence conflicti635 – 6362RP → WT in AAB57691 (PubMed:9207241).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 157157Missing in isoform H. 2 PublicationsVSP_023051Add
BLAST
Alternative sequencei1 – 5252Missing in isoform D, isoform F and isoform G. 3 PublicationsVSP_023052Add
BLAST
Alternative sequencei53 – 553IEK → MLQ in isoform D, isoform F and isoform G. 3 PublicationsVSP_023053
Alternative sequencei576 – 65075Missing in isoform C. 1 PublicationVSP_001816Add
BLAST
Alternative sequencei712 – 820109TWQGT…EVQEL → SECRSSPRVGTDYKQLLHGL AALEREVSGA in isoform F. 1 PublicationVSP_023054Add
BLAST
Alternative sequencei712 – 77160TWQGT…GSASR → S in isoform A and isoform D. 3 PublicationsVSP_001817Add
BLAST
Alternative sequencei772 – 82453SRKES…LRQDN → KSCCSYISHQN in isoform E. 4 PublicationsVSP_023055Add
BLAST
Alternative sequencei821 – 86242Missing in isoform F. 1 PublicationVSP_023056Add
BLAST
Alternative sequencei825 – 86238Missing in isoform E. 4 PublicationsVSP_023057Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129064 mRNA. Translation: BAC97874.1. Different initiation.
AY220301 mRNA. Translation: AAO65479.1.
AK052545 mRNA. Translation: BAC35033.1. Different initiation.
AK139156 mRNA. Translation: BAE23905.1. Different initiation.
BC044838 mRNA. Translation: AAH44838.1. Different initiation.
AF247654 mRNA. Translation: AAG18017.1. Different initiation.
AF247655 mRNA. Translation: AAG18018.1. Different initiation.
AF343877 mRNA. Translation: AAK97363.1. Different initiation.
U96634 mRNA. Translation: AAB57691.1. Different initiation.
CCDSiCCDS52480.1. [Q9ES28-5]
CCDS52481.1. [Q9ES28-8]
RefSeqiNP_001106989.1. NM_001113517.1. [Q9ES28-5]
NP_001106990.1. NM_001113518.1. [Q9ES28-8]
NP_059098.2. NM_017402.4.
XP_006508904.2. XM_006508841.2. [Q9ES28-1]
XP_006508906.2. XM_006508843.2. [Q9ES28-2]
XP_006508907.2. XM_006508844.2. [Q9ES28-3]
UniGeneiMm.244068.

Genome annotation databases

EnsembliENSMUST00000098938; ENSMUSP00000096538; ENSMUSG00000031511. [Q9ES28-8]
ENSMUST00000110909; ENSMUSP00000106534; ENSMUSG00000031511. [Q9ES28-5]
GeneIDi54126.
KEGGimmu:54126.
UCSCiuc009kvu.2. mouse. [Q9ES28-2]
uc009kvv.2. mouse. [Q9ES28-5]
uc009kvw.2. mouse. [Q9ES28-4]
uc009kvx.2. mouse. [Q9ES28-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129064 mRNA. Translation: BAC97874.1. Different initiation.
AY220301 mRNA. Translation: AAO65479.1.
AK052545 mRNA. Translation: BAC35033.1. Different initiation.
AK139156 mRNA. Translation: BAE23905.1. Different initiation.
BC044838 mRNA. Translation: AAH44838.1. Different initiation.
AF247654 mRNA. Translation: AAG18017.1. Different initiation.
AF247655 mRNA. Translation: AAG18018.1. Different initiation.
AF343877 mRNA. Translation: AAK97363.1. Different initiation.
U96634 mRNA. Translation: AAB57691.1. Different initiation.
CCDSiCCDS52480.1. [Q9ES28-5]
CCDS52481.1. [Q9ES28-8]
RefSeqiNP_001106989.1. NM_001113517.1. [Q9ES28-5]
NP_001106990.1. NM_001113518.1. [Q9ES28-8]
NP_059098.2. NM_017402.4.
XP_006508904.2. XM_006508841.2. [Q9ES28-1]
XP_006508906.2. XM_006508843.2. [Q9ES28-2]
XP_006508907.2. XM_006508844.2. [Q9ES28-3]
UniGeneiMm.244068.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ESWX-ray2.01A/B164-220[»]
ProteinModelPortaliQ9ES28.
SMRiQ9ES28. Positions 1-116, 130-557, 803-862.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207566. 13 interactions.
IntActiQ9ES28. 19 interactions.
MINTiMINT-1786275.
STRINGi10090.ENSMUSP00000106534.

PTM databases

iPTMnetiQ9ES28.
PhosphoSiteiQ9ES28.

Proteomic databases

EPDiQ9ES28.
MaxQBiQ9ES28.
PaxDbiQ9ES28.
PRIDEiQ9ES28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098938; ENSMUSP00000096538; ENSMUSG00000031511. [Q9ES28-8]
ENSMUST00000110909; ENSMUSP00000106534; ENSMUSG00000031511. [Q9ES28-5]
GeneIDi54126.
KEGGimmu:54126.
UCSCiuc009kvu.2. mouse. [Q9ES28-2]
uc009kvv.2. mouse. [Q9ES28-5]
uc009kvw.2. mouse. [Q9ES28-4]
uc009kvx.2. mouse. [Q9ES28-1]

Organism-specific databases

CTDi8874.
MGIiMGI:1860493. Arhgef7.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG2070. Eukaryota.
ENOG410XNNP. LUCA.
GeneTreeiENSGT00760000118925.
HOVERGENiHBG050569.
InParanoidiQ9ES28.
KOiK13710.
OMAiPQMKSLY.
OrthoDBiEOG708W04.
PhylomeDBiQ9ES28.
TreeFamiTF316105.

Enzyme and pathway databases

ReactomeiR-MMU-182971. EGFR downregulation.
R-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-3928664. Ephrin signaling.
R-MMU-416482. G alpha (12/13) signalling events.

Miscellaneous databases

ChiTaRSiArhgef7. mouse.
EvolutionaryTraceiQ9ES28.
NextBioi310921.
PROiQ9ES28.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ES28.
CleanExiMM_ARHGEF7.
ExpressionAtlasiQ9ES28. baseline and differential.
GenevisibleiQ9ES28. MM.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR032409. GEF_CC.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF16523. betaPIX_CC. 1 hit.
PF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E).
    Tissue: Brain.
  2. "betaPix-b(L), a novel isoform of betaPix, is generated by alternative translation."
    Rhee S., Yang S.J., Lee S.J., Park D.
    Biochem. Biophys. Res. Commun. 318:415-421(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS G AND H).
    Strain: ICR.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS D AND F).
    Strain: C57BL/6J.
    Tissue: Cerebellum and Lung.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "Molecular cloning of neuronally expressed mouse betaPix isoforms."
    Kim S., Kim T., Lee D., Park S.-H., Kim H., Park D.
    Biochem. Biophys. Res. Commun. 272:721-725(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-862 (ISOFORM B), NUCLEOTIDE SEQUENCE [MRNA] OF 150-862 (ISOFORM C), TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. "Molecular cloning and characterization of a novel mouse betaPix isoform."
    Kim T., Park D.
    Mol. Cells 11:89-94(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-862 (ISOFORM E), TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Brain.
  7. "Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and its localization in focal adhesion."
    Oh W.K., Yoo J.C., Jo D., Song Y.H., Kim M.G., Park D.
    Biochem. Biophys. Res. Commun. 235:794-798(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-862 (ISOFORM A).
    Tissue: Thymus.
  8. "A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins."
    Bagrodia S., Bailey D., Lenard Z., Hart M., Guan J.L., Premont R.T., Taylor S.J., Cerione R.A.
    J. Biol. Chem. 274:22393-22400(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GIT1.
  9. "Hic-5 interacts with GIT1 with a different binding mode from paxillin."
    Nishiya N., Shirai T., Suzuki W., Nose K.
    J. Biochem. 132:279-289(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GIT1 AND TGFB1I1.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  11. "FAK potentiates Rac1 activation and localization to matrix adhesion sites: a role for betaPIX."
    Chang F., Lemmon C.A., Park D., Romer L.H.
    Mol. Biol. Cell 18:253-264(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK1.
  12. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PARVB.
  15. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-155; SER-164; SER-497; SER-673 AND SER-776, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  17. "Crystal structure of the N-terminal SH3 domain of mouse betaPIX, p21-activated kinase-interacting exchange factor."
    Li X., Liu X., Sun F., Gao J., Zhou H., Gao G.F., Bartlam M., Rao Z.
    Biochem. Biophys. Res. Commun. 339:407-414(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 164-220.

Entry informationi

Entry nameiARHG7_MOUSE
AccessioniPrimary (citable) accession number: Q9ES28
Secondary accession number(s): O08757
, Q3UTS5, Q6XPA5, Q6ZQI5, Q8C750, Q91ZZ6, Q9ES27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: February 6, 2007
Last modified: March 16, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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