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Q14155

- ARHG7_HUMAN

UniProt

Q14155 - ARHG7_HUMAN

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Protein

Rho guanine nucleotide exchange factor 7

Gene

ARHGEF7

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions By similarity. May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons.By similarity3 Publications

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activity Source: BHF-UCL
  2. protein kinase binding Source: BHF-UCL
  3. Rho guanyl-nucleotide exchange factor activity Source: InterPro

GO - Biological processi

  1. apoptotic signaling pathway Source: Reactome
  2. epidermal growth factor receptor signaling pathway Source: Reactome
  3. focal adhesion assembly Source: UniProtKB
  4. hematopoietic progenitor cell differentiation Source: Ensembl
  5. lamellipodium assembly Source: UniProtKB
  6. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
  7. nervous system development Source: UniProtKB-KW
  8. neurotrophin TRK receptor signaling pathway Source: Reactome
  9. positive regulation of apoptotic process Source: UniProtKB
  10. positive regulation of fibroblast migration Source: UniProtKB
  11. positive regulation of GTPase activity Source: BHF-UCL
  12. positive regulation of lamellipodium morphogenesis Source: UniProtKB
  13. positive regulation of Rac GTPase activity Source: UniProtKB
  14. positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  15. regulation of small GTPase mediated signal transduction Source: Reactome
  16. signal transduction Source: ProtInc
  17. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_12484. EGFR downregulation.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
SignaLinkiQ14155.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 7
Alternative name(s):
Beta-Pix
COOL-1
PAK-interacting exchange factor beta
p85
Gene namesi
Name:ARHGEF7
Synonyms:COOL1, KIAA0142, P85SPR, PAK3BP, PIXB
ORF Names:Nbla10314
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:15607. ARHGEF7.

Subcellular locationi

Cell junctionfocal adhesion By similarity. Cell projectionruffle By similarity. Cytoplasmcell cortex By similarity. Cell projectionlamellipodium By similarity
Note: Detected at cell adhesions. A small proportion is detected at focal adhesions.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. focal adhesion Source: UniProtKB
  3. lamellipodium Source: UniProtKB
  4. neuronal cell body Source: BHF-UCL
  5. neuron projection Source: BHF-UCL
  6. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24977.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 803803Rho guanine nucleotide exchange factor 7PRO_0000080921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761PhosphoserineBy similarity
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei518 – 5181Phosphoserine1 Publication
Modified residuei694 – 6941Phosphoserine; by CaMK13 Publications

Post-translational modificationi

Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1 By similarity. Phosphorylated on Ser-694 by CaMK1; enhancement of GEF activity and downstream activation of RAC1.By similarity4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14155.
PaxDbiQ14155.
PRIDEiQ14155.

PTM databases

PhosphoSiteiQ14155.

Expressioni

Gene expression databases

BgeeiQ14155.
ExpressionAtlasiQ14155. baseline and differential.
GenevestigatoriQ14155.

Organism-specific databases

HPAiHPA004744.

Interactioni

Subunit structurei

Interacts with PAK kinases through the SH3 domain. Interacts with GIT1 and TGFB1I1. Interacts with PTK2/FAK1 and RAC1. Interacts with ITCH and PARVB By similarity. Interacts with unphosphorylated PAK1. Interacts with SCRIB; interaction is direct and may play a role in regulation of apoptosis. Interacts with FRMPD4 (via N-terminus). Interacts with CaMK1. Interacts with BIN2. Isoform 1 and isoform 5 interact with SNX27.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBLP226819EBI-717515,EBI-518228
GIT1Q9Y2X74EBI-717515,EBI-466061
LRRK2Q5S0076EBI-717515,EBI-5323863
NAA10P412273EBI-717515,EBI-747693
PAK1Q131537EBI-717515,EBI-1307
PAK2Q131774EBI-717515,EBI-1045887
RAC1P630008EBI-717515,EBI-413628
SCRIBQ141604EBI-717515,EBI-357345
SH2D1AO608806EBI-717515,EBI-6983382

Protein-protein interaction databases

BioGridi114393. 25 interactions.
IntActiQ14155. 20 interactions.
MINTiMINT-92779.

Structurei

Secondary structure

1
803
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1311
Helixi27 – 359
Helixi39 – 4810
Helixi63 – 7917
Helixi109 – 1135
Helixi118 – 13518
Beta strandi188 – 1914
Beta strandi210 – 2156
Beta strandi218 – 2269
Beta strandi229 – 24012
Helixi271 – 30131
Turni302 – 3043
Beta strandi305 – 3106
Helixi311 – 3133
Helixi316 – 33823
Helixi346 – 37833
Turni379 – 3813
Helixi382 – 3854
Turni386 – 3894
Turni395 – 3973
Helixi398 – 4025
Turni406 – 4083
Helixi409 – 4113
Helixi413 – 42210
Beta strandi428 – 4303
Helixi432 – 45322
Turni454 – 4563

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BY1NMR-A260-467[»]
1ZSGNMR-A179-243[»]
2L3GNMR-A1-137[»]
ProteinModelPortaliQ14155.
SMRiQ14155. Positions 1-137, 151-578.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14155.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 132132CHPROSITE-ProRule annotationAdd
BLAST
Domaini184 – 24360SH3PROSITE-ProRule annotationAdd
BLAST
Domaini271 – 451181DHPROSITE-ProRule annotationAdd
BLAST
Domaini473 – 578106PHPROSITE-ProRule annotationAdd
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

SH3 domain

Phylogenomic databases

eggNOGiNOG314429.
GeneTreeiENSGT00760000118925.
HOVERGENiHBG050569.
InParanoidiQ14155.
KOiK13710.
OMAiHHEPARL.
OrthoDBiEOG708W04.
PhylomeDBiQ14155.
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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00307. 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.
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 (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 4 (identifier: Q14155-4) [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 KKTISDPEGF LQASLKDGVV LCRLLERLLP
60 70 80 90 100
GTIEKVYPEP RSESECLSNI REFLRGCGAS LRLELLFPPS QPPQHLVTTI
110 120 130 140 150
LLSASTFDAN DLYQGQNFNK VLSSLVTLNK VTADIGLGSD SVCARPSSHR
160 170 180 190 200
IKSFDSLGSQ SLHTRTSKLF QGQYRSLDMT DNSNNQLVVR AKFNFQQTNE
210 220 230 240 250
DELSFSKGDV IHVTRVEEGG WWEGTLNGRT GWFPSNYVRE VKASEKPVSP
260 270 280 290 300
KSGTLKSPPK GFDTTAINKS YYNVVLQNIL ETENEYSKEL QTVLSTYLRP
310 320 330 340 350
LQTSEKLSSA NISYLMGNLE EICSFQQMLV QSLEECTKLP EAQQRVGGCF
360 370 380 390 400
LNLMPQMKTL YLTYCANHPS AVNVLTEHSE ELGEFMETKG ASSPGILVLT
410 420 430 440 450
TGLSKPFMRL DKYPTLLKEL ERHMEDYHTD RQDIQKSMAA FKNLSAQCQE
460 470 480 490 500
VRKRKELELQ ILTEAIRNWE GDDIKTLGNV TYMSQVLIQC AGSEEKNERY
510 520 530 540 550
LLLFPNVLLM LSASPRMSGF IYQGKLPTTG MTITKLEDSE NHRNAFEISG
560 570 580 590 600
SMIERILVSC NNQQDLQEWV EHLQKQTKVT SVGNPTIKPH SVPSHTLPSH
610 620 630 640 650
PVTPSSKHAD SKPAPLTPAY HTLPHPSHHG TPHTTINWGP LEPPKTPKPW
660 670 680 690 700
SLSCLRPAPP LRPSAALCYK EDLSKSPKTM KKLLPKRKPE RKPSDEEFAS
710 720 730 740 750
RKSTAALEED AQILKVIEAY CTSAKTRQTL NSTWQGTDLM HNHVLADDDQ
760 770 780 790 800
PSLDSLGRRS SLSRLEPSDL SEDSDYDSIW TAHSYRMGST SRKSCCSYIS

HQN
Length:803
Mass (Da):90,012
Last modified:July 19, 2004 - v2
Checksum:i613EBA839E6FDBFD
GO
Isoform 1 (identifier: Q14155-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-178: Missing.
     733-803: TWQGTDLMHN...SCCSYISHQN → SSRKESAPQV...NDPAWDETNL

Note: Contains a phosphoserine at position 560. Contains a phosphoserine at position 579.

Show »
Length:646
Mass (Da):73,140
Checksum:iB5B5A83F0EBC28D2
GO
Isoform 2 (identifier: Q14155-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     56-105: Missing.

Show »
Length:753
Mass (Da):84,477
Checksum:i04178E64ACF43846
GO
Isoform 3 (identifier: Q14155-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-105: Missing.

Show »
Length:782
Mass (Da):87,770
Checksum:i9C602026D90A6D01
GO
Isoform 5 (identifier: Q14155-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-177: Missing.
     733-803: TWQGTDLMHN...SCCSYISHQN → SSRKESAPQV...NDPAWDETNL

Note: Contains a phosphoserine at position 645. Contains a phosphoserine at position 664.

Show »
Length:731
Mass (Da):82,571
Checksum:iE82D55E6187DADB2
GO
Isoform 6 (identifier: Q14155-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-178: Missing.

Show »
Length:625
Mass (Da):70,450
Checksum:i25DAD75DD4B0AC2E
GO

Sequence cautioni

The sequence AAH50521.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA09763.2 differs from that shown. Reason: Erroneous initiation.
The sequence CAD38906.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 554TIEK → EEKR in BAD66827. (PubMed:15491607)Curated
Sequence conflicti343 – 3431Q → K in AAH33905. (PubMed:15489334)Curated
Sequence conflicti552 – 5521M → V in AAH33905. (PubMed:15489334)Curated
Sequence conflicti595 – 5951H → D in BAD66827. (PubMed:15491607)Curated
Sequence conflicti636 – 6361I → T in AAH50521. (PubMed:15489334)Curated
Sequence conflicti740 – 7401M → L in AAH33905. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti790 – 7901T → A Found in a clear cell renal carcinoma case; somatic mutation. 1 Publication
VAR_064694

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 178178Missing in isoform 1 and isoform 6. 3 PublicationsVSP_011032Add
BLAST
Alternative sequencei56 – 10550Missing in isoform 2. 1 PublicationVSP_011033Add
BLAST
Alternative sequencei85 – 17793Missing in isoform 5. 1 PublicationVSP_034639Add
BLAST
Alternative sequencei85 – 10521Missing in isoform 3. 1 PublicationVSP_011034Add
BLAST
Alternative sequencei733 – 80371TWQGT…ISHQN → SSRKESAPQVLLPEEEKIIV EETKSNGQTVIEEKSLVDTV YALKDEVQELRQDNKKMKKS LEEEQRARKDLEKLVRKVLK NMNDPAWDETNL in isoform 1 and isoform 5. 4 PublicationsVSP_011035Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63476 mRNA. Translation: BAA09763.2. Different initiation.
AL834228 mRNA. Translation: CAD38906.1. Different initiation.
AL390754, AL139086 Genomic DNA. Translation: CAI12461.1.
AL139086, AL390754 Genomic DNA. Translation: CAI14671.1.
AL390754, AL139086 Genomic DNA. Translation: CAM13628.1.
AL139086, AL390754 Genomic DNA. Translation: CAM20788.1.
CH471085 Genomic DNA. Translation: EAX09143.1.
BC033905 mRNA. Translation: AAH33905.1.
BC050521 mRNA. Translation: AAH50521.1. Different initiation.
BC060776 mRNA. Translation: AAH60776.1.
AB177849 mRNA. Translation: BAD66827.1.
AB075521 mRNA. Translation: BAE45764.1.
CCDSiCCDS32009.1. [Q14155-3]
CCDS45068.1. [Q14155-4]
CCDS45069.1. [Q14155-2]
CCDS9521.1. [Q14155-1]
RefSeqiNP_001106983.1. NM_001113511.1. [Q14155-4]
NP_001106984.1. NM_001113512.1. [Q14155-2]
NP_001106985.1. NM_001113513.1. [Q14155-1]
NP_003890.1. NM_003899.3. [Q14155-1]
NP_663788.1. NM_145735.2. [Q14155-3]
XP_005254147.1. XM_005254090.1. [Q14155-5]
XP_005254152.1. XM_005254095.1. [Q14155-1]
UniGeneiHs.508738.

Genome annotation databases

EnsembliENST00000317133; ENSP00000325994; ENSG00000102606. [Q14155-3]
ENST00000375723; ENSP00000364875; ENSG00000102606. [Q14155-6]
ENST00000375736; ENSP00000364888; ENSG00000102606. [Q14155-1]
ENST00000375739; ENSP00000364891; ENSG00000102606. [Q14155-2]
ENST00000375741; ENSP00000364893; ENSG00000102606. [Q14155-4]
ENST00000426073; ENSP00000397068; ENSG00000102606. [Q14155-1]
GeneIDi8874.
KEGGihsa:8874.
UCSCiuc001vrr.2. human. [Q14155-3]
uc001vrs.2. human. [Q14155-4]
uc001vrt.2. human. [Q14155-2]
uc001vrv.4. human. [Q14155-1]

Polymorphism databases

DMDMi50403776.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63476 mRNA. Translation: BAA09763.2 . Different initiation.
AL834228 mRNA. Translation: CAD38906.1 . Different initiation.
AL390754 , AL139086 Genomic DNA. Translation: CAI12461.1 .
AL139086 , AL390754 Genomic DNA. Translation: CAI14671.1 .
AL390754 , AL139086 Genomic DNA. Translation: CAM13628.1 .
AL139086 , AL390754 Genomic DNA. Translation: CAM20788.1 .
CH471085 Genomic DNA. Translation: EAX09143.1 .
BC033905 mRNA. Translation: AAH33905.1 .
BC050521 mRNA. Translation: AAH50521.1 . Different initiation.
BC060776 mRNA. Translation: AAH60776.1 .
AB177849 mRNA. Translation: BAD66827.1 .
AB075521 mRNA. Translation: BAE45764.1 .
CCDSi CCDS32009.1. [Q14155-3 ]
CCDS45068.1. [Q14155-4 ]
CCDS45069.1. [Q14155-2 ]
CCDS9521.1. [Q14155-1 ]
RefSeqi NP_001106983.1. NM_001113511.1. [Q14155-4 ]
NP_001106984.1. NM_001113512.1. [Q14155-2 ]
NP_001106985.1. NM_001113513.1. [Q14155-1 ]
NP_003890.1. NM_003899.3. [Q14155-1 ]
NP_663788.1. NM_145735.2. [Q14155-3 ]
XP_005254147.1. XM_005254090.1. [Q14155-5 ]
XP_005254152.1. XM_005254095.1. [Q14155-1 ]
UniGenei Hs.508738.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BY1 NMR - A 260-467 [» ]
1ZSG NMR - A 179-243 [» ]
2L3G NMR - A 1-137 [» ]
ProteinModelPortali Q14155.
SMRi Q14155. Positions 1-137, 151-578.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114393. 25 interactions.
IntActi Q14155. 20 interactions.
MINTi MINT-92779.

PTM databases

PhosphoSitei Q14155.

Polymorphism databases

DMDMi 50403776.

Proteomic databases

MaxQBi Q14155.
PaxDbi Q14155.
PRIDEi Q14155.

Protocols and materials databases

DNASUi 8874.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000317133 ; ENSP00000325994 ; ENSG00000102606 . [Q14155-3 ]
ENST00000375723 ; ENSP00000364875 ; ENSG00000102606 . [Q14155-6 ]
ENST00000375736 ; ENSP00000364888 ; ENSG00000102606 . [Q14155-1 ]
ENST00000375739 ; ENSP00000364891 ; ENSG00000102606 . [Q14155-2 ]
ENST00000375741 ; ENSP00000364893 ; ENSG00000102606 . [Q14155-4 ]
ENST00000426073 ; ENSP00000397068 ; ENSG00000102606 . [Q14155-1 ]
GeneIDi 8874.
KEGGi hsa:8874.
UCSCi uc001vrr.2. human. [Q14155-3 ]
uc001vrs.2. human. [Q14155-4 ]
uc001vrt.2. human. [Q14155-2 ]
uc001vrv.4. human. [Q14155-1 ]

Organism-specific databases

CTDi 8874.
GeneCardsi GC13P111766.
H-InvDB HIX0037536.
HGNCi HGNC:15607. ARHGEF7.
HPAi HPA004744.
MIMi 605477. gene.
neXtProti NX_Q14155.
PharmGKBi PA24977.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG314429.
GeneTreei ENSGT00760000118925.
HOVERGENi HBG050569.
InParanoidi Q14155.
KOi K13710.
OMAi HHEPARL.
OrthoDBi EOG708W04.
PhylomeDBi Q14155.
TreeFami TF316105.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_12484. EGFR downregulation.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
SignaLinki Q14155.

Miscellaneous databases

ChiTaRSi ARHGEF7. human.
EvolutionaryTracei Q14155.
GeneWikii ARHGEF7.
GenomeRNAii 8874.
NextBioi 33313.
PROi Q14155.
SOURCEi Search...

Gene expression databases

Bgeei Q14155.
ExpressionAtlasi Q14155. baseline and differential.
Genevestigatori Q14155.

Family and domain databases

Gene3Di 1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEi PS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Amygdala.
  4. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1; 2 AND 4).
    Tissue: Brain and Testis.
  7. "Alternative splice variants encoding unstable protein domains exist in the human brain."
    Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.
    J. Mol. Biol. 343:1207-1220(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-803 (ISOFORM 5).
  8. "Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
    Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
    Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-803.
    Tissue: Neuroblastoma.
  9. Cited for: INTERACTION WITH SCRIB.
  10. "Deregulation of scribble promotes mammary tumorigenesis and reveals a role for cell polarity in carcinoma."
    Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B., Allred C., Muthuswamy S.K.
    Cell 135:865-878(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SCRIB.
  11. Cited for: FUNCTION IN CELL MIGRATION.
  12. "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that regulates dendritic spine morphogenesis."
    Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B., Eom S.H., Kim H., Kim E.
    J. Neurosci. 28:14546-14556(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FRMPD4.
  13. "Activity-dependent synaptogenesis: regulation by a CaM-kinase kinase/CaM-kinase I/betaPIX signaling complex."
    Saneyoshi T., Wayman G., Fortin D., Davare M., Hoshi N., Nozaki N., Natsume T., Soderling T.R.
    Neuron 57:94-107(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-694, INTERACTION WITH CAMK1.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Sorting nexin 27 protein regulates trafficking of a p21-activated kinase (PAK) interacting exchange factor (beta-Pix)-G protein-coupled receptor kinase interacting protein (GIT) complex via a PDZ domain interaction."
    Valdes J.L., Tang J., McDermott M.I., Kuo J.C., Zimmerman S.P., Wincovitch S.M., Waterman C.M., Milgram S.L., Playford M.P.
    J. Biol. Chem. 286:39403-39416(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX27.
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-694, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-579 (ISOFORM 1), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-664 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte podosomes, motility and phagocytosis."
    Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J., Veprintsev D.B., Evans P.R., McMahon H.T.
    PLoS ONE 7:E52401-E52401(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BIN2.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: STRUCTURE BY NMR OF 260-467.
  22. "Structural analysis of the SH3 domain of beta-PIX and its interaction with alpha-p21 activated kinase (PAK)."
    Mott H.R., Nietlispach D., Evetts K.A., Owen D.
    Biochemistry 44:10977-10983(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 179-243 OF COMPLEX WITH UNPHOSPHORYLATED PAK1.
  23. "Northeast structural genomics consortium target HR4495E."
    Northeast structural genomics consortium (NESG)
    Submitted (DEC-2010) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-137.
  24. Cited for: VARIANT ALA-790.

Entry informationi

Entry nameiARHG7_HUMAN
AccessioniPrimary (citable) accession number: Q14155
Secondary accession number(s): B1ALK6
, B1ALK8, Q3LIA4, Q5W9H0, Q6P9G3, Q6PII2, Q86W63, Q8N3M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 19, 2004
Last modified: October 29, 2014
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3