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Protein

Rho guanine nucleotide exchange factor 12

Gene

ARHGEF12

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 the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei308 – 3092Breakpoint for translocation to form KMT2A/MLL1-ARHGEF12 oncogene

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 12
Alternative name(s):
Leukemia-associated RhoGEF
Gene namesi
Name:ARHGEF12
Synonyms:KIAA0382, LARG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:14193. ARHGEF12.

Subcellular locationi

  • Cytoplasm Curated
  • Membrane Curated

  • Note: Translocated to the membrane upon stimulation.Curated

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving ARHGEF12 may be a cause of acute leukemia. Translocation t(11;11)(q23;23) with KMT2A/MLL1.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA24969.

Polymorphism and mutation databases

BioMutaiARHGEF12.
DMDMi34395525.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 15441543Rho guanine nucleotide exchange factor 12PRO_0000080930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei309 – 3091Phosphoserine1 Publication
Modified residuei341 – 3411Phosphoserine1 Publication
Modified residuei637 – 6371Phosphoserine2 Publications
Modified residuei736 – 7361Phosphothreonine1 Publication
Modified residuei1327 – 13271Phosphoserine1 Publication
Modified residuei1377 – 13771Phosphoserine1 Publication
Modified residuei1457 – 14571Phosphoserine1 Publication
Modified residuei1541 – 15411Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NZN5.
PaxDbiQ9NZN5.
PRIDEiQ9NZN5.

PTM databases

PhosphoSiteiQ9NZN5.

Expressioni

Tissue specificityi

Ubiquitously expressed. Isoform 2 is found in jejunum and testis.

Gene expression databases

BgeeiQ9NZN5.
CleanExiHS_ARHGEF12.
ExpressionAtlasiQ9NZN5. baseline and differential.
GenevisibleiQ9NZN5. HS.

Organism-specific databases

HPAiCAB025581.
HPA018911.

Interactioni

Subunit structurei

Interacts with GNA12 and GNA13, probably through the RGS-like domain. Interacts with RHOA, PLXNB1 and PLXNB2. Interacts through its PDZ domain with IGF1R beta subunit. Interacts with GCSAM.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IGF1RP080697EBI-821440,EBI-475981
Lpar1P617933EBI-821440,EBI-7512335From a different organism.
RHOAP615862EBI-821440,EBI-446668

Protein-protein interaction databases

BioGridi116945. 18 interactions.
DIPiDIP-37887N.
IntActiQ9NZN5. 11 interactions.
MINTiMINT-1774807.
STRINGi9606.ENSP00000380942.

Structurei

Secondary structure

1
1544
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi70 – 767Combined sources
Beta strandi85 – 873Combined sources
Beta strandi89 – 913Combined sources
Beta strandi93 – 964Combined sources
Helixi102 – 1065Combined sources
Beta strandi112 – 1198Combined sources
Turni122 – 1243Combined sources
Helixi127 – 1359Combined sources
Beta strandi137 – 1459Combined sources
Helixi769 – 7724Combined sources
Helixi775 – 7784Combined sources
Helixi783 – 81230Combined sources
Helixi814 – 8207Combined sources
Helixi825 – 8328Combined sources
Helixi835 – 85319Combined sources
Beta strandi857 – 8604Combined sources
Helixi865 – 8728Combined sources
Helixi875 – 88915Combined sources
Helixi891 – 90414Combined sources
Helixi906 – 91712Combined sources
Helixi919 – 9213Combined sources
Helixi926 – 9294Combined sources
Helixi932 – 94918Combined sources
Helixi954 – 99340Combined sources
Beta strandi1001 – 10033Combined sources
Helixi1005 – 10073Combined sources
Helixi1008 – 10114Combined sources
Helixi1015 – 10173Combined sources
Beta strandi1020 – 103314Combined sources
Beta strandi1038 – 105316Combined sources
Beta strandi1056 – 10583Combined sources
Beta strandi1078 – 10814Combined sources
Helixi1082 – 10843Combined sources
Beta strandi1085 – 10895Combined sources
Beta strandi1091 – 10933Combined sources
Beta strandi1096 – 11027Combined sources
Beta strandi1107 – 11137Combined sources
Helixi1117 – 113721Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXDX-ray2.13A766-1138[»]
1X86X-ray3.22A/C/E/G766-1138[»]
2OMJNMR-A67-151[»]
2OS6NMR-A67-151[»]
ProteinModelPortaliQ9NZN5.
SMRiQ9NZN5. Positions 67-151, 766-1138.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZN5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 15180PDZPROSITE-ProRule annotationAdd
BLAST
Domaini367 – 558192RGSLAdd
BLAST
Domaini787 – 977191DHPROSITE-ProRule annotationAdd
BLAST
Domaini1019 – 1132114PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili194 – 26269Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 RGSL (RGS-like) domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5422.
GeneTreeiENSGT00760000119193.
HOGENOMiHOG000034046.
HOVERGENiHBG050571.
InParanoidiQ9NZN5.
KOiK07532.
OMAiEEVLMTS.
OrthoDBiEOG7GJ6CF.
PhylomeDBiQ9NZN5.
TreeFamiTF106495.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR016137. RGS.
IPR015212. RGS-like_dom.
IPR015721. RhoGEF-like.
[Graphical view]
PANTHERiPTHR22825. PTHR22825. 1 hit.
PfamiPF00595. PDZ. 1 hit.
PF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NZN5-1) [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
MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERIA SHDFDPTDSS
60 70 80 90 100
SKKTKSSSEE SRSEIYGLVQ RCVIIQKDDN GFGLTVSGDN PVFVQSVKED
110 120 130 140 150
GAAMRAGVQT GDRIIKVNGT LVTHSNHLEV VKLIKSGSYV ALTVQGRPPG
160 170 180 190 200
SPQIPLADSE VEPSVIGHMS PIMTSPHSPG ASGNMERITS PVLMGEENNV
210 220 230 240 250
VHNQKVEILR KMLQKEQERL QLLQEDYNRT PAQRLLKEIQ EAKKHIPQLQ
260 270 280 290 300
EQLSKATGSA QDGAVVTPSR PLGDTLTVSE AETDPGDVLG RTDCSSGDAS
310 320 330 340 350
RPSSDNADSP KSGPKERIYL EENPEKSETI QDTDTQSLVG SPSTRIAPHI
360 370 380 390 400
IGAEDDDFGT EHEQINGQCS CFQSIELLKS RPAHLAVFLH HVVSQFDPAT
410 420 430 440 450
LLCYLYSDLY KHTNSKETRR IFLEFHQFFL DRSAHLKVSV PDEMSADLEK
460 470 480 490 500
RRPELIPEDL HRHYIQTMQE RVHPEVQRHL EDFRQKRSMG LTLAESELTK
510 520 530 540 550
LDAERDKDRL TLEKERTCAE QIVAKIEEVL MTAQAVEEDK SSTMQYVILM
560 570 580 590 600
YMKHLGVKVK EPRNLEHKRG RIGFLPKIKQ SMKKDKEGEE KGKRRGFPSI
610 620 630 640 650
LGPPRRPSRH DNSAIGRAME LQKARHPKHL STPSSVSPEP QDSAKLRQSG
660 670 680 690 700
LANEGTDAGY LPANSMSSVA SGASFSQEGG KENDTGSKQV GETSAPGDTL
710 720 730 740 750
DGTPRTLNTV FDFPPPPLDQ VQEEECEVER VTEHGTPKPF RKFDSVAFGE
760 770 780 790 800
SQSEDEQFEN DLETDPPNWQ QLVSREVLLG LKPCEIKRQE VINELFYTER
810 820 830 840 850
AHVRTLKVLD QVFYQRVSRE GILSPSELRK IFSNLEDILQ LHIGLNEQMK
860 870 880 890 900
AVRKRNETSV IDQIGEDLLT WFSGPGEEKL KHAAATFCSN QPFALEMIKS
910 920 930 940 950
RQKKDSRFQT FVQDAESNPL CRRLQLKDII PTQMQRLTKY PLLLDNIAKY
960 970 980 990 1000
TEWPTEREKV KKAADHCRQI LNYVNQAVKE AENKQRLEDY QRRLDTSSLK
1010 1020 1030 1040 1050
LSEYPNVEEL RNLDLTKRKM IHEGPLVWKV NRDKTIDLYT LLLEDILVLL
1060 1070 1080 1090 1100
QKQDDRLVLR CHSKILASTA DSKHTFSPVI KLSTVLVRQV ATDNKALFVI
1110 1120 1130 1140 1150
SMSDNGAQIY ELVAQTVSEK TVWQDLICRM AASVKEQSTK PIPLPQSTPG
1160 1170 1180 1190 1200
EGDNDEEDPS KLKEEQHGIS VTGLQSPDRD LGLESTLISS KPQSHSLSTS
1210 1220 1230 1240 1250
GKSEVRDLFV AERQFAKEQH TDGTLKEVGE DYQIAIPDSH LPVSEERWAL
1260 1270 1280 1290 1300
DALRNLGLLK QLLVQQLGLT EKSVQEDWQH FPRYRTASQG PQTDSVIQNS
1310 1320 1330 1340 1350
ENIKAYHSGE GHMPFRTGTG DIATCYSPRT STESFAPRDS VGLAPQDSQA
1360 1370 1380 1390 1400
SNILVMDHMI MTPEMPTMEP EGGLDDSGEH FFDAREAHSD ENPSEGDGAV
1410 1420 1430 1440 1450
NKEEKDVNLR ISGNYLILDG YDPVQESSTD EEVASSLTLQ PMTGIPAVES
1460 1470 1480 1490 1500
THQQQHSPQN THSDGAISPF TPEFLVQQRW GAMEYSCFEI QSPSSCADSQ
1510 1520 1530 1540
SQIMEYIHKI EADLEHLKKV EESYTILCQR LAGSALTDKH SDKS
Length:1,544
Mass (Da):173,232
Last modified:October 1, 2000 - v1
Checksum:i0B7E319CF7C7A224
GO
Isoform 2 (identifier: Q9NZN5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-66: Missing.

Note: Contains a phosphoserine at position 41.3 Publications
Show »
Length:1,525
Mass (Da):171,115
Checksum:i47FF1323DE2DFF55
GO

Sequence cautioni

The sequence AAH63117.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti973 – 9731Y → F.1 Publication
Corresponds to variant rs2305013 [ dbSNP | Ensembl ].
VAR_020191

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei48 – 6619Missing in isoform 2. 2 PublicationsVSP_008131Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180681 mRNA. Translation: AAF36817.1.
AB002380 mRNA. Translation: BAA20836.2.
BC063117 mRNA. Translation: AAH63117.1. Sequence problems.
CCDSiCCDS41727.1. [Q9NZN5-1]
CCDS55794.1. [Q9NZN5-2]
RefSeqiNP_001185594.1. NM_001198665.1. [Q9NZN5-2]
NP_001288013.1. NM_001301084.1.
NP_056128.1. NM_015313.2. [Q9NZN5-1]
UniGeneiHs.24598.

Genome annotation databases

EnsembliENST00000356641; ENSP00000349056; ENSG00000196914. [Q9NZN5-2]
ENST00000397843; ENSP00000380942; ENSG00000196914. [Q9NZN5-1]
GeneIDi23365.
KEGGihsa:23365.
UCSCiuc001pxl.2. human. [Q9NZN5-1]
uc009zat.3. human. [Q9NZN5-2]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180681 mRNA. Translation: AAF36817.1.
AB002380 mRNA. Translation: BAA20836.2.
BC063117 mRNA. Translation: AAH63117.1. Sequence problems.
CCDSiCCDS41727.1. [Q9NZN5-1]
CCDS55794.1. [Q9NZN5-2]
RefSeqiNP_001185594.1. NM_001198665.1. [Q9NZN5-2]
NP_001288013.1. NM_001301084.1.
NP_056128.1. NM_015313.2. [Q9NZN5-1]
UniGeneiHs.24598.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXDX-ray2.13A766-1138[»]
1X86X-ray3.22A/C/E/G766-1138[»]
2OMJNMR-A67-151[»]
2OS6NMR-A67-151[»]
ProteinModelPortaliQ9NZN5.
SMRiQ9NZN5. Positions 67-151, 766-1138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116945. 18 interactions.
DIPiDIP-37887N.
IntActiQ9NZN5. 11 interactions.
MINTiMINT-1774807.
STRINGi9606.ENSP00000380942.

PTM databases

PhosphoSiteiQ9NZN5.

Polymorphism and mutation databases

BioMutaiARHGEF12.
DMDMi34395525.

Proteomic databases

MaxQBiQ9NZN5.
PaxDbiQ9NZN5.
PRIDEiQ9NZN5.

Protocols and materials databases

DNASUi23365.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356641; ENSP00000349056; ENSG00000196914. [Q9NZN5-2]
ENST00000397843; ENSP00000380942; ENSG00000196914. [Q9NZN5-1]
GeneIDi23365.
KEGGihsa:23365.
UCSCiuc001pxl.2. human. [Q9NZN5-1]
uc009zat.3. human. [Q9NZN5-2]

Organism-specific databases

CTDi23365.
GeneCardsiGC11P120207.
H-InvDBHIX0010202.
HIX0036240.
HGNCiHGNC:14193. ARHGEF12.
HPAiCAB025581.
HPA018911.
MIMi604763. gene.
neXtProtiNX_Q9NZN5.
PharmGKBiPA24969.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5422.
GeneTreeiENSGT00760000119193.
HOGENOMiHOG000034046.
HOVERGENiHBG050571.
InParanoidiQ9NZN5.
KOiK07532.
OMAiEEVLMTS.
OrthoDBiEOG7GJ6CF.
PhylomeDBiQ9NZN5.
TreeFamiTF106495.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.

Miscellaneous databases

ChiTaRSiARHGEF12. human.
EvolutionaryTraceiQ9NZN5.
GeneWikiiARHGEF12.
GenomeRNAii23365.
NextBioi45421.
PROiQ9NZN5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NZN5.
CleanExiHS_ARHGEF12.
ExpressionAtlasiQ9NZN5. baseline and differential.
GenevisibleiQ9NZN5. HS.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR016137. RGS.
IPR015212. RGS-like_dom.
IPR015721. RhoGEF-like.
[Graphical view]
PANTHERiPTHR22825. PTHR22825. 1 hit.
PfamiPF00595. PDZ. 1 hit.
PF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a gene at 11q23 encoding a guanine nucleotide exchange factor: evidence for its fusion with MLL in acute myeloid leukemia."
    Kourlas P.J., Strout M.P., Becknell B., Veronese M.L., Croce C.M., Theil K.S., Krahe R., Ruutu T., Knuutila S., Bloomfield C.D., Caligiuri M.A.
    Proc. Natl. Acad. Sci. U.S.A. 97:2145-2150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHROMOSOMAL TRANSLOCATION.
    Tissue: Prostate.
  2. "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] OF 1-584 (ISOFORM 2).
    Tissue: Thyroid.
  3. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-1544, VARIANT PHE-973.
    Tissue: Brain.
  4. Ohara O., Nagase T., Kikuno R., Nomura N.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  5. "Leukemia-associated Rho guanine nucleotide exchange factor (LARG) links heterotrimeric G proteins of the G(12) family to Rho."
    Fukuhara S., Chikumi H., Gutkind J.S.
    FEBS Lett. 485:183-188(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RHOA; GNA12 AND GNA13.
  6. "Direct interaction of insulin-like growth factor-1 receptor with leukemia-associated RhoGEF."
    Taya S., Inagaki N., Sengiku H., Makino H., Iwamatsu A., Urakawa I., Nagao K., Kataoka S., Kaibuchi K.
    J. Cell Biol. 155:809-820(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGF1R.
  7. Cited for: INTERACTION WITH PLXNB1 AND PLXNB2.
  8. "Plexin B regulates Rho through the guanine nucleotide exchange factors leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF."
    Perrot V., Vazquez-Prado J., Gutkind J.S.
    J. Biol. Chem. 277:43115-43120(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLXNB1 AND PLXNB2.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-736, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "HGAL, a germinal center specific protein, decreases lymphoma cell motility by modulation of the RhoA signaling pathway."
    Jiang X., Lu X., McNamara G., Liu X., Cubedo E., Sarosiek K.A., Sanchez-Garcia I., Helfman D.M., Lossos I.S.
    Blood 116:5217-5227(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCSAM.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-637; SER-1327; SER-1377; SER-1457 AND SER-1541, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor."
    Kristelly R., Gao G., Tesmer J.J.
    J. Biol. Chem. 279:47352-47362(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 766-1138 IN COMPLEX WITH RHOA, SUBUNIT.
  20. "Conformational change upon ligand binding and dynamics of the PDZ domain from leukemia-associated Rho guanine nucleotide exchange factor."
    Liu J., Zhang J., Yang Y., Huang H., Shen W., Hu Q., Wang X., Wu J., Shi Y.
    Protein Sci. 17:1003-1014(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 67-151 IN COMPLEX WITH PLXNB1, SUBUNIT.

Entry informationi

Entry nameiARHGC_HUMAN
AccessioniPrimary (citable) accession number: Q9NZN5
Secondary accession number(s): O15086, Q6P526
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 137 of the entry and version 1 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 11
    Human chromosome 11: 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

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 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.