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Q9ES28 (ARHG7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho guanine nucleotide exchange factor 7
Alternative name(s):
Beta-Pix
PAK-interacting exchange factor beta
p85SPR
Gene names
Name:Arhgef7
Synonyms:Kiaa0142, Pak3bp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length862 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Subunit structure

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. Ref.8 Ref.9 Ref.11 Ref.14

Subcellular location

Cell junction › focal adhesion. Cell projection › ruffle. Cytoplasm › cell cortex. Cell projection › lamellipodium. Note: Detected at cell adhesions. A small proportion is detected at focal adhesions. Ref.11 Ref.14

Tissue specificity

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. Ref.5 Ref.6

Post-translational modification

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. Ref.11

Sequence similarities

Contains 1 CH (calponin-homology) domain.

Contains 1 DH (DBL-homology) domain.

Contains 1 PH domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAB57691.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG18017.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG18018.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH44838.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAK97363.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC35033.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC97874.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE23905.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processNeurogenesis
   Cellular componentCell junction
Cell projection
Cytoplasm
   Coding sequence diversityAlternative initiation
Alternative splicing
   DomainCoiled coil
SH3 domain
   Molecular functionGuanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lamellipodium assembly

Inferred from mutant phenotype Ref.14. Source: UniProtKB

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of GTPase activity

Inferred from electronic annotation. Source: Compara

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Rho protein signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from direct assay Ref.14. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Compara

neuronal cell body

Inferred from electronic annotation. Source: Compara

protein complex

Inferred from electronic annotation. Source: Compara

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

phospholipid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Git1Q68FF62EBI-642580,EBI-645933
Git1Q9Z2722EBI-642580,EBI-3842379From a different organism.
GIT2Q141612EBI-642580,EBI-1046878From a different organism.
Git2Q9JLQ26EBI-642580,EBI-642860

Alternative products

This entry describes 8 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform B (identifier: Q9ES28-1)

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.
Isoform A (identifier: Q9ES28-2)

The sequence of this isoform differs from the canonical sequence as follows:
     712-771: TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASR → S
Isoform C (identifier: Q9ES28-3)

The sequence of this isoform differs from the canonical sequence as follows:
     576-650: Missing.
Isoform D (identifier: Q9ES28-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.
     53-55: IEK → MLQ
     712-771: TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASR → S
Isoform E (identifier: Q9ES28-5)

Also known as: d;

The sequence of this isoform differs from the canonical sequence as follows:
     772-824: SRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQELRQDN → KSCCSYISHQN
     825-862: Missing.
Isoform F (identifier: Q9ES28-6)

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.
Isoform G (identifier: Q9ES28-7)

Also known as: b(L);

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.
     53-55: IEK → MLQ
Isoform H (identifier: Q9ES28-8)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 862862Rho guanine nucleotide exchange factor 7
PRO_0000080922

Regions

Domain1 – 111111CH
Domain163 – 22260SH3
Domain250 – 430181DH
Domain452 – 557106PH
Coiled coil804 – 85451 Potential

Amino acid modifications

Modified residue1321Phosphoserine Ref.15
Modified residue1551Phosphoserine Ref.13
Modified residue1641Phosphoserine Ref.17
Modified residue2281Phosphoserine By similarity
Modified residue4971Phosphoserine Ref.12 Ref.16
Modified residue6731Phosphoserine; by CaMK1 By similarity
Modified residue7761Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 157157Missing in isoform H.
VSP_023051
Alternative sequence1 – 5252Missing in isoform D, isoform F and isoform G.
VSP_023052
Alternative sequence53 – 553IEK → MLQ in isoform D, isoform F and isoform G.
VSP_023053
Alternative sequence576 – 65075Missing in isoform C.
VSP_001816
Alternative sequence712 – 820109TWQGT…EVQEL → SECRSSPRVGTDYKQLLHGL AALEREVSGA in isoform F.
VSP_023054
Alternative sequence712 – 77160TWQGT…GSASR → S in isoform A and isoform D.
VSP_001817
Alternative sequence772 – 82453SRKES…LRQDN → KSCCSYISHQN in isoform E.
VSP_023055
Alternative sequence821 – 86242Missing in isoform F.
VSP_023056
Alternative sequence825 – 86238Missing in isoform E.
VSP_023057

Experimental info

Sequence conflict485 – 4884NLLL → KPSV in AAO65479. Ref.2
Sequence conflict485 – 4884NLLL → KPSV in AAG18017. Ref.5
Sequence conflict485 – 4884NLLL → KPSV in AAG18018. Ref.5
Sequence conflict485 – 4884NLLL → KPSV in AAB57691. Ref.7
Sequence conflict4921A → P in AAO65479. Ref.2
Sequence conflict4921A → P in AAG18017. Ref.5
Sequence conflict4921A → P in AAG18018. Ref.5
Sequence conflict4921A → P in AAB57691. Ref.7
Sequence conflict6161S → R in AAO65479. Ref.2
Sequence conflict6161S → R in AAG18017. Ref.5
Sequence conflict6161S → R in AAB57691. Ref.7
Sequence conflict624 – 6252KT → PH in AAB57691. Ref.7
Sequence conflict6281P → A in AAO65479. Ref.2
Sequence conflict6281P → A in AAB57691. Ref.7
Sequence conflict6301S → G in AAB57691. Ref.7
Sequence conflict6331C → W in AAO65479. Ref.2
Sequence conflict6331C → W in AAG18017. Ref.5
Sequence conflict6331C → W in AAB57691. Ref.7
Sequence conflict635 – 6362RP → WT in AAB57691. Ref.7

Secondary structure

1 ........... 862
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: 46D61B606B8391B4

FASTA86297,056
        10         20         30         40         50         60 
MNSAEQTVTW LITLGVLESP KKTISDPEVF LQASLKDGVV LCRLLERLLP GTIEKVYPEP 

        70         80         90        100        110        120 
RNESECLSNI REFLRACGAS LRLETFDAND LYQGQNFNKV LSSLVTLNKV TADIGLGSDS 

       130        140        150        160        170        180 
VCARPSSHRI KSFDSLGSQS SHSRTSKLLQ SQYRSLDMTD NTNSQLVVRA KFNFQQTNED 

       190        200        210        220        230        240 
ELSFSKGDVI HVTRVEEGGW WEGTHNGRTG WFPSNYVREI KPSEKPVSPK SGTLKSPPKG 

       250        260        270        280        290        300 
FDTTAINKSY YNVVLQNILE TEHEYSKELQ SVLSTYLRPL QTSDKLSSAN TSYLMGNLEE 

       310        320        330        340        350        360 
ISSFQQVLVQ SLEECTKSPE AQQRVGGCFL SLMPQMRTLY LAYCANHPSA VSVLTEHSED 

       370        380        390        400        410        420 
LGEFMETKGA SSPGILVLTT GLSKPFMRLD KYPTLLKELE RHMEDYHPDR QDIQKSMTAF 

       430        440        450        460        470        480 
KNLSAQCQEV RKRKELELQI LTEPIRSWEG DDIKTLGSVT YMSQVTIQCA GSEEKNERYL 

       490        500        510        520        530        540 
LLFPNLLLML SASPRMSGFI YQGKLPTTGM TITKLEDSEN HRNAFEISGS MIERILVSCT 

       550        560        570        580        590        600 
SQQDLHEWVE HLQKQTKVTS VSNPTIKPHS VPSHTLPSHP LTPSSKHADS KPVALTPAYH 

       610        620        630        640        650        660 
TLPHPSHHGT PHTTISWGPL EPPKTPKPWS LSCLRPAPPL RPSAALCYKE DLSKSPKTMK 

       670        680        690        700        710        720 
KLLPKRKPER KPSDEEFAVR KSTAALEEDA QILKVIEAYC TSAKTRQTLN STWQGTDLMH 

       730        740        750        760        770        780 
NHVLADDDQS SLDSLGRRSS LSRLEPSDLS EDSEYDSIWT AHSYRMGSAS RSRKESAPQV 

       790        800        810        820        830        840 
LLPEEEKIIV EETKSNGQTV IEEKSLVDTV YALKDEVQEL RQDNKKMKKS LEEEQRARKD 

       850        860 
LEKLVRKVLK NMNDPAWDET NL

« Hide

Isoform A [UniParc].

Checksum: C829852E0C7EA8CD
Show »

FASTA80390,390
Isoform C [UniParc].

Checksum: EEB889F6BE45B63D
Show »

FASTA78788,950
Isoform D [UniParc].

Checksum: 43F22A9DF918F599
Show »

FASTA75184,698
Isoform E (d) [UniParc].

Checksum: 9B38100E66FFDAD9
Show »

FASTA78287,673
Isoform F [UniParc].

Checksum: 78B03ECBB4E8A3F4
Show »

FASTA68977,189
Isoform G (b(L)) [UniParc].

Checksum: 61F15448C29152B0
Show »

FASTA81091,364
Isoform H (b) [UniParc].

Checksum: 60F3F1CA3589637C
Show »

FASTA70579,696

References

« Hide 'large scale' references
[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. expand/collapse author list , 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/6.
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/6.
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]"Proteomic analysis of in vivo phosphorylated synaptic proteins."
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G.
J. Biol. Chem. 280:5972-5982(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, MASS SPECTROMETRY.
Tissue: Forebrain.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, MASS SPECTROMETRY.
Tissue: Brain cortex.
[13]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, MASS SPECTROMETRY.
Tissue: Liver.
[14]"Affixin activates Rac1 via betaPIX in C2C12 myoblast."
Matsuda C., Kameyama K., Suzuki A., Mishima W., Yamaji S., Okamoto H., Nishino I., Hayashi Y.K.
FEBS Lett. 582:1189-1196(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PARVB.
[15]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-673 AND SER-776, MASS SPECTROMETRY.
Tissue: Melanoma.
[16]"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, MASS SPECTROMETRY.
Tissue: Macrophage.
[17]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
[18]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00230704.
IPI00331212.
IPI00387322.
IPI00655136.
IPI00828241.
IPI00828536.
IPI00828723.
IPI00828966.
RefSeqNP_001106989.1. NM_001113517.1.
NP_001106990.1. NM_001113518.1.
NP_059098.2. NM_017402.4.
UniGeneMm.244068.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ESWX-ray2.01A/B164-220[»]
ProteinModelPortalQ9ES28.
SMRQ9ES28. Positions 1-116, 130-557, 803-862.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9ES28. 11 interactions.
MINTMINT-1786275.

PTM databases

PhosphoSiteQ9ES28.

Proteomic databases

PaxDbQ9ES28.
PRIDEQ9ES28.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033908; ENSMUSP00000033908; ENSMUSG00000031511.
ENSMUST00000074856; ENSMUSP00000074399; ENSMUSG00000031511.
ENSMUST00000098938; ENSMUSP00000096538; ENSMUSG00000031511.
ENSMUST00000110909; ENSMUSP00000106534; ENSMUSG00000031511.
GeneID54126.
KEGGmmu:54126.
UCSCuc009kvu.2. mouse.
uc009kvv.2. mouse.
uc009kvw.2. mouse.
uc009kvx.2. mouse.

Organism-specific databases

CTD8874.
MGIMGI:1860493. Arhgef7.
RougeSearch...

Phylogenomic databases

eggNOGNOG314429.
GeneTreeENSGT00690000101859.
HOVERGENHBG050569.
InParanoidQ9ES28.
KOK13710.
OMAQCAGNEE.

Gene expression databases

ArrayExpressQ9ES28.
BgeeQ9ES28.
CleanExMM_ARHGEF7.
GenevestigatorQ9ES28.
GermOnlineENSMUSG00000031511. Mus musculus.

Family and domain databases

Gene3D1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF47576. Calponin-homology. 1 hit.
SSF48065. DH-domain. 1 hit.
SSF50044. SH3. 1 hit.
PROSITEPS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9ES28.
NextBio310921.
SOURCESearch...

Entry information

Entry nameARHG7_MOUSE
AccessionPrimary (citable) accession number: Q9ES28
Secondary accession number(s): O08757 expand/collapse secondary AC list , Q3UTS5, Q6XPA5, Q6ZQI5, Q8C750, Q91ZZ6, Q9ES27
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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