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Protein

Rho guanine nucleotide exchange factor 25

Gene

ARHGEF25

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. It works as a guanine nucleotide exchange factor for Rho family of small GTPases. Links specifically G alpha q/11-coupled receptors to RHOA activation. May be an important regulator of processes involved in axon and dendrite formation. In neurons seems to be an exchange factor primarily for RAC1. Involved in skeletal myogenesis (By similarity).By similarity6 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiR-HSA-416476. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 25
Alternative name(s):
Guanine nucleotide exchange factor GEFT
Rac/Cdc42/Rho exchange factor GEFT
RhoA/Rac/Cdc42 guanine nucleotide exchange factor GEFT
p63RhoGEF
Gene namesi
Name:ARHGEF25
Synonyms:GEFT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:30275. ARHGEF25.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi301 – 3011L → E: Abolishes its exchange activity on RHOA. 1 Publication
Mutagenesisi471 – 4711F → A: Reduces exchange activity mediated by GNAQ activation; in truncated construct. 1 Publication
Mutagenesisi472 – 4721L → A: Reduces exchange activity mediated by GNAQ activation; in truncated construct. 1 Publication
Mutagenesisi475 – 4751L → A: Reduces exchange activity mediated by GNAQ activation; in truncated construct. 1 Publication
Mutagenesisi478 – 4781P → A: Reduces exchange activity mediated by GNAQ activation; in truncated construct. 1 Publication
Mutagenesisi479 – 4791I → A: Reduces exchange activity mediated by GNAQ activation; in truncated construct. 1 Publication

Polymorphism and mutation databases

BioMutaiARHGEF25.
DMDMi172046695.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580Rho guanine nucleotide exchange factor 25PRO_0000322132Add
BLAST

Proteomic databases

PaxDbiQ86VW2.
PRIDEiQ86VW2.

PTM databases

PhosphoSiteiQ86VW2.
SwissPalmiQ86VW2.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are highly expressed in excitable tissues, such as brain, heart and muscle. Also detected in kidney and liver.3 Publications

Gene expression databases

BgeeiQ86VW2.
ExpressionAtlasiQ86VW2. baseline and differential.
GenevisibleiQ86VW2. HS.

Organism-specific databases

HPAiHPA052016.

Interactioni

Subunit structurei

Interacts (via the DH domain) with BVES (via the C-terminus cytoplasmic tail) (By similarity). Interacts with activated GNAQ and GNA11. Interacts with RHOA, CDC42 and RAC1.By similarity4 Publications

Protein-protein interaction databases

BioGridi125438. 7 interactions.
STRINGi9606.ENSP00000335560.

Structurei

Secondary structure

1
580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi151 – 1544Combined sources
Helixi156 – 18328Combined sources
Helixi186 – 1938Combined sources
Beta strandi197 – 1993Combined sources
Helixi200 – 2023Combined sources
Helixi203 – 2075Combined sources
Helixi210 – 21910Combined sources
Helixi221 – 2299Combined sources
Helixi232 – 2343Combined sources
Helixi235 – 2417Combined sources
Turni242 – 2465Combined sources
Helixi247 – 2548Combined sources
Helixi257 – 2637Combined sources
Turni264 – 2663Combined sources
Helixi268 – 27811Combined sources
Helixi284 – 2874Combined sources
Helixi290 – 2956Combined sources
Helixi298 – 30811Combined sources
Beta strandi310 – 3123Combined sources
Helixi316 – 33823Combined sources
Helixi339 – 3413Combined sources
Beta strandi355 – 36410Combined sources
Beta strandi378 – 39316Combined sources
Beta strandi406 – 4138Combined sources
Helixi414 – 4163Combined sources
Beta strandi417 – 4226Combined sources
Helixi423 – 4253Combined sources
Beta strandi429 – 4357Combined sources
Beta strandi437 – 4393Combined sources
Beta strandi441 – 45010Combined sources
Helixi451 – 47525Combined sources
Helixi478 – 48912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RGNX-ray3.50B/E149-502[»]
ProteinModelPortaliQ86VW2.
SMRiQ86VW2. Positions 149-490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86VW2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini160 – 336177DHPROSITE-ProRule annotationAdd
BLAST
Domaini348 – 466119PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 29922Important for binding to Rho GTPasesAdd
BLAST
Regioni467 – 49327Sufficient to bind activated GNAQAdd
BLAST

Domaini

The guanine nucleotide exchange activity is autoinhibited by the PH domain.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IQSV. Eukaryota.
ENOG410ZKYJ. LUCA.
GeneTreeiENSGT00760000119030.
HOGENOMiHOG000112709.
HOVERGENiHBG065330.
InParanoidiQ86VW2.
OMAiQCLKDPD.
OrthoDBiEOG7B8S3F.
PhylomeDBiQ86VW2.
TreeFamiTF318080.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR030738. ARHGEF25.
IPR000219. DH-domain.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR22826:SF117. PTHR22826:SF117. 1 hit.
PfamiPF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86VW2-1) [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
MRGGHKGGRC ACPRVIRKVL AKCGCCFARG GRESYSIAGS EGSISASAAS
60 70 80 90 100
GLAAPSGPSS GLSSGPCSPG PPGPVSGLRR WLDHSKHCLS VETEADSGQA
110 120 130 140 150
GPYENWMLEP ALATGEELPE LTLLTTLLEG PGDKTQPPEE ETLSQAPESE
160 170 180 190 200
EEQKKKALER SMYVLSELVE TEKMYVDDLG QIVEGYMATM AAQGVPESLR
210 220 230 240 250
GRDRIVFGNI QQIYEWHRDY FLQELQRCLK DPDWLAQLFI KHERRLHMYV
260 270 280 290 300
VYCQNKPKSE HVVSEFGDSY FEELRQQLGH RLQLNDLLIK PVQRIMKYQL
310 320 330 340 350
LLKDFLKYYN RAGMDTADLE QAVEVMCFVP KRCNDMMTLG RLRGFEGKLT
360 370 380 390 400
AQGKLLGQDT FWVTEPEAGG LLSSRGRERR VFLFEQIIIF SEALGGGVRG
410 420 430 440 450
GTQPGYVYKN SIKVSCLGLE GNLQGDPCRF ALTSRGPEGG IQRYVLQAAD
460 470 480 490 500
PAISQAWIKH VAQILESQRD FLNALQSPIE YQRRESQTNS LGRPRGPGVG
510 520 530 540 550
SPGRIQLGDQ AQGSTHTPIN GSLPSLLLSP KGEVARALLP LDKQALGDIP
560 570 580
QAPHDSPPVS PTPKTPPCQA RLAKLDEDEL
Length:580
Mass (Da):63,843
Last modified:February 26, 2008 - v2
Checksum:iF3EC80445D965BFB
GO
Isoform 2 (identifier: Q86VW2-2) [UniParc]FASTAAdd to basket

Also known as: p63RhoGef

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.

Show »
Length:474
Mass (Da):53,173
Checksum:i627A0D3DCEC92F99
GO
Isoform 3 (identifier: Q86VW2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MRGGHKGGRCACPRVIRKVLAKCGCCFARGGR → MKPPDRPAPG...HEVLAGALQP

Show »
Length:619
Mass (Da):68,114
Checksum:iDF18CD3D7D3B1AFD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti253 – 2531C → Y.2 Publications
Corresponds to variant rs17857333 [ dbSNP | Ensembl ].
VAR_039402
Natural varianti397 – 3971G → R.1 Publication
Corresponds to variant rs17854492 [ dbSNP | Ensembl ].
VAR_039403
Natural varianti506 – 5061Q → R.2 Publications
Corresponds to variant rs1564374 [ dbSNP | Ensembl ].
VAR_039404

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 106106Missing in isoform 2. 1 PublicationVSP_031875Add
BLAST
Alternative sequencei1 – 3232MRGGH…ARGGR → MKPPDRPAPGRTDRILGVMG GMLRACALPGQEGPPRRSPL GLVGTEPESERTEGDHRRDR EHEVLAGALQP in isoform 3. 1 PublicationVSP_047254Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF487514 mRNA. Translation: AAO49463.2.
AB370196 mRNA. Translation: BAF94999.1.
AC025165 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97037.1.
BC012860 mRNA. Translation: AAH12860.1.
BC018536 mRNA. Translation: AAH18536.1.
BC047559 mRNA. Translation: AAH47559.1.
CCDSiCCDS44931.1. [Q86VW2-3]
CCDS8947.1. [Q86VW2-1]
RefSeqiNP_001104740.1. NM_001111270.2.
NP_891992.2. NM_182947.3.
UniGeneiHs.61581.

Genome annotation databases

EnsembliENST00000286494; ENSP00000286494; ENSG00000240771. [Q86VW2-1]
ENST00000333972; ENSP00000335560; ENSG00000240771. [Q86VW2-3]
ENST00000616622; ENSP00000484303; ENSG00000240771. [Q86VW2-2]
GeneIDi115557.
KEGGihsa:115557.
UCSCiuc001spa.5. human. [Q86VW2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF487514 mRNA. Translation: AAO49463.2.
AB370196 mRNA. Translation: BAF94999.1.
AC025165 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97037.1.
BC012860 mRNA. Translation: AAH12860.1.
BC018536 mRNA. Translation: AAH18536.1.
BC047559 mRNA. Translation: AAH47559.1.
CCDSiCCDS44931.1. [Q86VW2-3]
CCDS8947.1. [Q86VW2-1]
RefSeqiNP_001104740.1. NM_001111270.2.
NP_891992.2. NM_182947.3.
UniGeneiHs.61581.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RGNX-ray3.50B/E149-502[»]
ProteinModelPortaliQ86VW2.
SMRiQ86VW2. Positions 149-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125438. 7 interactions.
STRINGi9606.ENSP00000335560.

PTM databases

PhosphoSiteiQ86VW2.
SwissPalmiQ86VW2.

Polymorphism and mutation databases

BioMutaiARHGEF25.
DMDMi172046695.

Proteomic databases

PaxDbiQ86VW2.
PRIDEiQ86VW2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000286494; ENSP00000286494; ENSG00000240771. [Q86VW2-1]
ENST00000333972; ENSP00000335560; ENSG00000240771. [Q86VW2-3]
ENST00000616622; ENSP00000484303; ENSG00000240771. [Q86VW2-2]
GeneIDi115557.
KEGGihsa:115557.
UCSCiuc001spa.5. human. [Q86VW2-1]

Organism-specific databases

CTDi115557.
GeneCardsiARHGEF25.
HGNCiHGNC:30275. ARHGEF25.
HPAiHPA052016.
MIMi610215. gene.
neXtProtiNX_Q86VW2.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQSV. Eukaryota.
ENOG410ZKYJ. LUCA.
GeneTreeiENSGT00760000119030.
HOGENOMiHOG000112709.
HOVERGENiHBG065330.
InParanoidiQ86VW2.
OMAiQCLKDPD.
OrthoDBiEOG7B8S3F.
PhylomeDBiQ86VW2.
TreeFamiTF318080.

Enzyme and pathway databases

ReactomeiR-HSA-416476. G alpha (q) signalling events.

Miscellaneous databases

EvolutionaryTraceiQ86VW2.
GeneWikiiGEFT.
GenomeRNAii115557.
NextBioi35512852.
PROiQ86VW2.
SOURCEiSearch...

Gene expression databases

BgeeiQ86VW2.
ExpressionAtlasiQ86VW2. baseline and differential.
GenevisibleiQ86VW2. HS.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR030738. ARHGEF25.
IPR000219. DH-domain.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR22826:SF117. PTHR22826:SF117. 1 hit.
PfamiPF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A Rac/Cdc42-specific exchange factor, GEFT, induces cell proliferation, transformation, and migration."
    Guo X., Stafford L.J., Bryan B., Xia C., Ma W., Wu X., Liu D., Songyang Z., Liu M.
    J. Biol. Chem. 278:13207-13215(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDC42 AND RAC1, TISSUE SPECIFICITY, VARIANT TYR-253.
  2. "Human cDNA derived from mRNA for adult brain."
    Nagase T., Kikuno R.F., Ohara O.
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT ARG-506.
    Tissue: Brain.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 AND 2), VARIANTS TYR-253; ARG-397 AND ARG-506.
    Tissue: Brain.
  6. "Human p63RhoGEF, a novel RhoA-specific guanine nucleotide exchange factor, is localized in cardiac sarcomere."
    Souchet M., Portales-Casamar E., Mazurais D., Schmidt S., Leger I., Javre J.L., Robert P., Berrebi-Bertrand I., Bril A., Gout B., Debant A., Calmels T.P.
    J. Cell Sci. 115:629-640(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LEU-301.
  7. "p63RhoGEF and GEFT are Rho-specific guanine nucleotide exchange factors encoded by the same gene."
    Lutz S., Freichel-Blomquist A., Rumenapp U., Schmidt M., Jakobs K.H., Wieland T.
    Naunyn Schmiedebergs Arch. Pharmacol. 369:540-546(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "The guanine nucleotide exchange factor p63RhoGEF, a specific link between Gq/11-coupled receptor signaling and RhoA."
    Lutz S., Freichel-Blomquist A., Yang Y., Rumenapp U., Jakobs K.H., Schmidt M., Wieland T.
    J. Biol. Chem. 280:11134-11139(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GNAQ AND GNA11.
  9. "Modulation of muscle regeneration, myogenesis, and adipogenesis by the Rho family guanine nucleotide exchange factor GEFT."
    Bryan B.A., Mitchell D.C., Zhao L., Ma W., Stafford L.J., Teng B.B., Liu M.
    Mol. Cell. Biol. 25:11089-11101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RHO-FAMILY SMALL GTPASES.
  10. "Galphaq directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain."
    Rojas R.J., Yohe M.E., Gershburg S., Kawano T., Kozasa T., Sondek J.
    J. Biol. Chem. 282:29201-29210(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GNAQ, DOMAIN, REGION, MUTAGENESIS OF PHE-471; LEU-472; LEU-475; PRO-478 AND ILE-479.
  11. "Structure of Galphaq-p63RhoGEF-RhoA complex reveals a pathway for the activation of RhoA by GPCRs."
    Lutz S., Shankaranarayanan A., Coco C., Ridilla M., Nance M.R., Vettel C., Baltus D., Evelyn C.R., Neubig R.R., Wieland T., Tesmer J.J.
    Science 318:1923-1927(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 149-502.

Entry informationi

Entry nameiARHGP_HUMAN
AccessioniPrimary (citable) accession number: Q86VW2
Secondary accession number(s): A6NJH5
, A9CQZ6, F8W7Z4, Q8WV84, Q96E63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: May 11, 2016
This is version 123 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 12
    Human chromosome 12: 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

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.