Q9NZN5 (ARHGC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho guanine nucleotide exchange factor 12

Alternative name(s):
Leukemia-associated RhoGEF

Gene names

Name:	ARHGEF12
Synonyms:	KIAA0382, LARG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1544 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5
Subunit structure	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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.14 Ref.17 Ref.18
Subcellular location	Cytoplasm Probable. Membrane Probable. Note: Translocated to the membrane upon stimulation Probable.
Tissue specificity	Ubiquitously expressed. Isoform 2 is found in jejunum and testis.
Involvement in disease	A chromosomal aberration involving ARHGEF12 may be a cause of acute leukemia. Translocation t(11;11)(q23;23) with MLL.
Sequence similarities	Contains 1 DH (DBL-homology) domain. Contains 1 PDZ (DHR) domain. Contains 1 PH domain. Contains 1 RGSL (RGS-like) domain.
Sequence caution	The sequence AAH63117.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Coiled coil
Molecular function	GTPase activation Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Inferred from direct assay PubMed 15755723. Source: MGI apoptotic signaling pathway Traceable author statement. Source: Reactome axon guidance Traceable author statement. Source: Reactome neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC regulation of Rho protein signal transduction Inferred from electronic annotation. Source: InterPro regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome small GTPase mediated signal transduction Traceable author statement. Source: Reactome termination of G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	G-protein coupled receptor binding Inferred from direct assay PubMed 15755723. Source: MGI GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW Rho guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: InterPro phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NZN5-1)

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 2 (identifier: Q9NZN5-2)

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

Note: Contains a phosphoserine at position 41.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1544

1544

Rho guanine nucleotide exchange factor 12

PRO_0000080930

Regions

Domain

72 – 151

80

PDZ

Domain

367 – 558

192

RGSL

Domain

787 – 977

191

DH

Domain

1019 – 1132

114

PH

Coiled coil

194 – 262

69

Potential

Sites

Site

308 – 309

2

Breakpoint for translocation to form MLL-ARHGEF12 oncogene

Amino acid modifications

Modified residue

22

1

Phosphoserine By similarity

Modified residue

341

1

Phosphoserine Ref.12

Modified residue

637

1

Phosphoserine Ref.15

Modified residue

736

1

Phosphothreonine Ref.11

Natural variations

Alternative sequence

48 – 66

19

Missing in isoform 2.

VSP_008131

Natural variant

973

1

Y → F. Ref.3
Corresponds to variant rs2305013 [ dbSNP | Ensembl ].

VAR_020191

Secondary structure

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1544

Helix Strand Turn

Details...

Beta strand

70 – 76

7

Beta strand

85 – 87

3

Beta strand

89 – 91

3

Beta strand

93 – 96

4

Helix

102 – 106

5

Beta strand

112 – 119

8

Turn

122 – 124

3

Helix

127 – 135

9

Beta strand

137 – 145

9

Helix

769 – 772

4

Helix

775 – 778

4

Helix

783 – 812

30

Helix

814 – 820

7

Helix

825 – 832

8

Helix

835 – 853

19

Beta strand

857 – 860

4

Helix

865 – 872

8

Helix

875 – 889

15

Helix

891 – 904

14

Helix

906 – 917

12

Helix

919 – 921

3

Helix

926 – 929

4

Helix

932 – 949

18

Helix

954 – 993

40

Beta strand

1001 – 1003

3

Helix

1005 – 1007

3

Helix

1008 – 1011

4

Helix

1015 – 1017

3

Beta strand

1020 – 1033

14

Beta strand

1038 – 1053

16

Beta strand

1056 – 1058

3

Beta strand

1078 – 1081

4

Helix

1082 – 1084

3

Beta strand

1085 – 1089

5

Beta strand

1091 – 1093

3

Beta strand

1096 – 1102

7

Beta strand

1107 – 1113

7

Helix

1117 – 1137

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 0B7E319CF7C7A224	FASTA	1,544	173,232
	10 20 30 40 50 60 MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERIA SHDFDPTDSS SKKTKSSSEE 70 80 90 100 110 120 SRSEIYGLVQ RCVIIQKDDN GFGLTVSGDN PVFVQSVKED GAAMRAGVQT GDRIIKVNGT 130 140 150 160 170 180 LVTHSNHLEV VKLIKSGSYV ALTVQGRPPG SPQIPLADSE VEPSVIGHMS PIMTSPHSPG 190 200 210 220 230 240 ASGNMERITS PVLMGEENNV VHNQKVEILR KMLQKEQERL QLLQEDYNRT PAQRLLKEIQ 250 260 270 280 290 300 EAKKHIPQLQ EQLSKATGSA QDGAVVTPSR PLGDTLTVSE AETDPGDVLG RTDCSSGDAS 310 320 330 340 350 360 RPSSDNADSP KSGPKERIYL EENPEKSETI QDTDTQSLVG SPSTRIAPHI IGAEDDDFGT 370 380 390 400 410 420 EHEQINGQCS CFQSIELLKS RPAHLAVFLH HVVSQFDPAT LLCYLYSDLY KHTNSKETRR 430 440 450 460 470 480 IFLEFHQFFL DRSAHLKVSV PDEMSADLEK RRPELIPEDL HRHYIQTMQE RVHPEVQRHL 490 500 510 520 530 540 EDFRQKRSMG LTLAESELTK LDAERDKDRL TLEKERTCAE QIVAKIEEVL MTAQAVEEDK 550 560 570 580 590 600 SSTMQYVILM YMKHLGVKVK EPRNLEHKRG RIGFLPKIKQ SMKKDKEGEE KGKRRGFPSI 610 620 630 640 650 660 LGPPRRPSRH DNSAIGRAME LQKARHPKHL STPSSVSPEP QDSAKLRQSG LANEGTDAGY 670 680 690 700 710 720 LPANSMSSVA SGASFSQEGG KENDTGSKQV GETSAPGDTL DGTPRTLNTV FDFPPPPLDQ 730 740 750 760 770 780 VQEEECEVER VTEHGTPKPF RKFDSVAFGE SQSEDEQFEN DLETDPPNWQ QLVSREVLLG 790 800 810 820 830 840 LKPCEIKRQE VINELFYTER AHVRTLKVLD QVFYQRVSRE GILSPSELRK IFSNLEDILQ 850 860 870 880 890 900 LHIGLNEQMK AVRKRNETSV IDQIGEDLLT WFSGPGEEKL KHAAATFCSN QPFALEMIKS 910 920 930 940 950 960 RQKKDSRFQT FVQDAESNPL CRRLQLKDII PTQMQRLTKY PLLLDNIAKY TEWPTEREKV 970 980 990 1000 1010 1020 KKAADHCRQI LNYVNQAVKE AENKQRLEDY QRRLDTSSLK LSEYPNVEEL RNLDLTKRKM 1030 1040 1050 1060 1070 1080 IHEGPLVWKV NRDKTIDLYT LLLEDILVLL QKQDDRLVLR CHSKILASTA DSKHTFSPVI 1090 1100 1110 1120 1130 1140 KLSTVLVRQV ATDNKALFVI SMSDNGAQIY ELVAQTVSEK TVWQDLICRM AASVKEQSTK 1150 1160 1170 1180 1190 1200 PIPLPQSTPG EGDNDEEDPS KLKEEQHGIS VTGLQSPDRD LGLESTLISS KPQSHSLSTS 1210 1220 1230 1240 1250 1260 GKSEVRDLFV AERQFAKEQH TDGTLKEVGE DYQIAIPDSH LPVSEERWAL DALRNLGLLK 1270 1280 1290 1300 1310 1320 QLLVQQLGLT EKSVQEDWQH FPRYRTASQG PQTDSVIQNS ENIKAYHSGE GHMPFRTGTG 1330 1340 1350 1360 1370 1380 DIATCYSPRT STESFAPRDS VGLAPQDSQA SNILVMDHMI MTPEMPTMEP EGGLDDSGEH 1390 1400 1410 1420 1430 1440 FFDAREAHSD ENPSEGDGAV NKEEKDVNLR ISGNYLILDG YDPVQESSTD EEVASSLTLQ 1450 1460 1470 1480 1490 1500 PMTGIPAVES THQQQHSPQN THSDGAISPF TPEFLVQQRW GAMEYSCFEI QSPSSCADSQ 1510 1520 1530 1540 SQIMEYIHKI EADLEHLKKV EESYTILCQR LAGSALTDKH SDKS
	Isoform 2 [UniParc]. Checksum: 47FF1323DE2DFF55	FASTA	1,525	171,115
	10 20 30 40 50 60 MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERIA SHDFDPTGLV QRCVIIQKDD 70 80 90 100 110 120 NGFGLTVSGD NPVFVQSVKE DGAAMRAGVQ TGDRIIKVNG TLVTHSNHLE VVKLIKSGSY 130 140 150 160 170 180 VALTVQGRPP GSPQIPLADS EVEPSVIGHM SPIMTSPHSP GASGNMERIT SPVLMGEENN 190 200 210 220 230 240 VVHNQKVEIL RKMLQKEQER LQLLQEDYNR TPAQRLLKEI QEAKKHIPQL QEQLSKATGS 250 260 270 280 290 300 AQDGAVVTPS RPLGDTLTVS EAETDPGDVL GRTDCSSGDA SRPSSDNADS PKSGPKERIY 310 320 330 340 350 360 LEENPEKSET IQDTDTQSLV GSPSTRIAPH IIGAEDDDFG TEHEQINGQC SCFQSIELLK 370 380 390 400 410 420 SRPAHLAVFL HHVVSQFDPA TLLCYLYSDL YKHTNSKETR RIFLEFHQFF LDRSAHLKVS 430 440 450 460 470 480 VPDEMSADLE KRRPELIPED LHRHYIQTMQ ERVHPEVQRH LEDFRQKRSM GLTLAESELT 490 500 510 520 530 540 KLDAERDKDR LTLEKERTCA EQIVAKIEEV LMTAQAVEED KSSTMQYVIL MYMKHLGVKV 550 560 570 580 590 600 KEPRNLEHKR GRIGFLPKIK QSMKKDKEGE EKGKRRGFPS ILGPPRRPSR HDNSAIGRAM 610 620 630 640 650 660 ELQKARHPKH LSTPSSVSPE PQDSAKLRQS GLANEGTDAG YLPANSMSSV ASGASFSQEG 670 680 690 700 710 720 GKENDTGSKQ VGETSAPGDT LDGTPRTLNT VFDFPPPPLD QVQEEECEVE RVTEHGTPKP 730 740 750 760 770 780 FRKFDSVAFG ESQSEDEQFE NDLETDPPNW QQLVSREVLL GLKPCEIKRQ EVINELFYTE 790 800 810 820 830 840 RAHVRTLKVL DQVFYQRVSR EGILSPSELR KIFSNLEDIL QLHIGLNEQM KAVRKRNETS 850 860 870 880 890 900 VIDQIGEDLL TWFSGPGEEK LKHAAATFCS NQPFALEMIK SRQKKDSRFQ TFVQDAESNP 910 920 930 940 950 960 LCRRLQLKDI IPTQMQRLTK YPLLLDNIAK YTEWPTEREK VKKAADHCRQ ILNYVNQAVK 970 980 990 1000 1010 1020 EAENKQRLED YQRRLDTSSL KLSEYPNVEE LRNLDLTKRK MIHEGPLVWK VNRDKTIDLY 1030 1040 1050 1060 1070 1080 TLLLEDILVL LQKQDDRLVL RCHSKILAST ADSKHTFSPV IKLSTVLVRQ VATDNKALFV 1090 1100 1110 1120 1130 1140 ISMSDNGAQI YELVAQTVSE KTVWQDLICR MAASVKEQST KPIPLPQSTP GEGDNDEEDP 1150 1160 1170 1180 1190 1200 SKLKEEQHGI SVTGLQSPDR DLGLESTLIS SKPQSHSLST SGKSEVRDLF VAERQFAKEQ 1210 1220 1230 1240 1250 1260 HTDGTLKEVG EDYQIAIPDS HLPVSEERWA LDALRNLGLL KQLLVQQLGL TEKSVQEDWQ 1270 1280 1290 1300 1310 1320 HFPRYRTASQ GPQTDSVIQN SENIKAYHSG EGHMPFRTGT GDIATCYSPR TSTESFAPRD 1330 1340 1350 1360 1370 1380 SVGLAPQDSQ ASNILVMDHM IMTPEMPTME PEGGLDDSGE HFFDAREAHS DENPSEGDGA 1390 1400 1410 1420 1430 1440 VNKEEKDVNL RISGNYLILD GYDPVQESST DEEVASSLTL QPMTGIPAVE STHQQQHSPQ 1450 1460 1470 1480 1490 1500 NTHSDGAISP FTPEFLVQQR WGAMEYSCFE IQSPSSCADS QSQIMEYIHK IEADLEHLKK 1510 1520 VEESYTILCQ RLAGSALTDK HSDKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"B plexins activate Rho through PDZ-RhoGEF." Driessens M.H.E., Olivo C., Nagata K., Inagaki M., Collard J.G. FEBS Lett. 529:168-172(2002) [PubMed] [Europe PMC] [Abstract] 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]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] 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), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-736, MASS SPECTROMETRY. Tissue: Platelet.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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.
[14]	"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.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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.
[18]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF180681 mRNA. Translation: AAF36817.1.
AB002380 mRNA. Translation: BAA20836.2.
BC063117 mRNA. Translation: AAH63117.1. Sequence problems.

IPI

IPI00022164.
IPI00339353.

RefSeq

NP_001185594.1. NM_001198665.1.
NP_056128.1. NM_015313.2.

UniGene

Hs.24598.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TXD	X-ray	2.13	A	766-1138	[»]
1X86	X-ray	3.22	A/C/E/G	766-1138	[»]
2OMJ	NMR	-	A	67-151	[»]
2OS6	NMR	-	A	67-151	[»]

ProteinModelPortal

Q9NZN5.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37887N.

IntAct

Q9NZN5. 6 interactions.

MINT

MINT-1774807.

STRING

9606.ENSP00000380942.

PTM databases

PhosphoSite

Q9NZN5.

Polymorphism databases

DMDM

34395525.

Proteomic databases

PaxDb

Q9NZN5.

PRIDE

Q9NZN5.

Protocols and materials databases

DNASU

23365.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356641; ENSP00000349056; ENSG00000196914.
ENST00000397843; ENSP00000380942; ENSG00000196914.

GeneID

23365.

KEGG

hsa:23365.

UCSC

uc001pxl.2. human.
uc009zat.3. human.

Organism-specific databases

CTD

23365.

GeneCards

GC11P120207.

H-InvDB

HIX0010202.
HIX0036240.

HGNC

HGNC:14193. ARHGEF12.

HPA

CAB025581.
HPA018911.

MIM

604763. gene.

neXtProt

NX_Q9NZN5.

PharmGKB

PA24969.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5422.

HOGENOM

HOG000034046.

HOVERGEN

HBG050571.

InParanoid

Q9NZN5.

KO

K07532.

OMA

MTPEMPT.

OrthoDB

EOG4BRWK1.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q9NZN5.

Bgee

Q9NZN5.

CleanEx

HS_ARHGEF12.

Genevestigator

Q9NZN5.

GermOnline

ENSG00000196914. Homo sapiens.

Family and domain databases

Gene3D

1.20.900.10. 1 hit.
2.30.29.30. 1 hit.

InterPro

IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR015212. Regulat_G_prot_signal-like.
IPR016137. Regulat_G_prot_signal_superfam.
IPR015721. RhoGEF-like.
[Graphical view]

PANTHER

PTHR22825. PTHR22825. 1 hit.

Pfam

PF00595. PDZ. 1 hit.
PF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]

SMART

SM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]

SUPFAM

SSF48065. DH-domain. 1 hit.
SSF50156. PDZ. 1 hit.
SSF48097. Regulat_G_prot_signal_superfam. 1 hit.

PROSITE

PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

ARHGEF12. human.

EvolutionaryTrace

Q9NZN5.

GenomeRNAi

23365.

NextBio

45421.

SOURCE

Search...

Entry information

Entry name

ARHGC_HUMAN

Accession

Primary (citable) accession number: Q9NZN5
Secondary accession number(s): O15086, Q6P526

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2003
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.