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Rho GTPase-activating protein 7 (Deleted in liver cancer 1 protein) (DLC-1) (HP protein) (Rho-type GTPase-activating protein 7) (START domain-containing protein 12) (StARD12) (StAR-related lipid transfer protein 12)

 RHG07_HUMAN             Reviewed;        1528 AA.
Q96QB1; B4DR10; B8PTI0; E9PDZ8; E9PF76; E9PGY9; O14868; O43199;
Q7Z5R8; Q86UC6; Q9C0E0; Q9H7A2;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 4.
22-NOV-2017, entry version 158.
RecName: Full=Rho GTPase-activating protein 7;
AltName: Full=Deleted in liver cancer 1 protein;
Short=DLC-1;
AltName: Full=HP protein;
AltName: Full=Rho-type GTPase-activating protein 7;
AltName: Full=START domain-containing protein 12;
Short=StARD12;
AltName: Full=StAR-related lipid transfer protein 12;
Name=DLC1; Synonyms=ARHGAP7, KIAA1723, STARD12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-712; VAL-1199
AND CYS-1209.
PubMed=9605766;
Yuan B.Z., Miller M.J., Keck C.L., Zimonjic D.B., Thorgeirsson S.S.,
Popescu N.C.;
"Cloning, characterization, and chromosomal localization of a gene
frequently deleted in human liver cancer (DLC-1) homologous to rat
RhoGAP.";
Cancer Res. 58:2196-2199(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-791.
TISSUE=Lung;
Wei M.-H., Pack S., Ivanov S., Lerman M.I.;
"Cloning and molecular characterization of the human ortholog of the
rat dual regulator p122RhoGAP.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT MET-791.
Jeong S.-J., Dimtchev A., Lerman M., Dritschilo A., Jung M.;
"Identification of HP/DLC1 exon and introns.";
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
HIS-254; ASP-255 AND ILE-260 AND MET-791.
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
VARIANTS HIS-254; ASP-255; ILE-260 AND MET-791.
TISSUE=Smooth muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), AND VARIANT
ASP-255.
TISSUE=Brain, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-50 (ISOFORM 6), AND ALTERNATIVE
PROMOTER USAGE.
TISSUE=Liver;
PubMed=21217778; DOI=10.1038/onc.2010.576;
Low J.S., Tao Q., Ng K.M., Goh H.K., Shu X.S., Woo W.L.,
Ambinder R.F., Srivastava G., Shamay M., Chan A.T., Popescu N.C.,
Hsieh W.S.;
"A novel isoform of the 8p22 tumor suppressor gene DLC1 suppresses
tumor growth and is frequently silenced in multiple common tumors.";
Oncogene 30:1923-1935(2011).
[9]
FUNCTION, DOMAIN SAM, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
TYR-879.
PubMed=18786931; DOI=10.1074/jbc.M800617200;
Kim T.Y., Healy K.D., Der C.J., Sciaky N., Bang Y.J., Juliano R.L.;
"Effects of structure of Rho GTPase-activating protein DLC-1 on cell
morphology and migration.";
J. Biol. Chem. 283:32762-32770(2008).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND FOCAL ADHESION TARGETING.
PubMed=19170769; DOI=10.1111/j.1365-2443.2008.01265.x;
Kawai K., Iwamae Y., Yamaga M., Kiyota M., Ishii H., Hirata H.,
Homma Y., Yagisawa H.;
"Focal adhesion-localization of START-GAP1/DLC1 is essential for cell
motility and morphology.";
Genes Cells 14:227-241(2009).
[11]
FUNCTION, AND LIPID-BINDING REGION.
PubMed=19710422; DOI=10.1091/mbc.E09-03-0247;
Erlmann P., Schmid S., Horenkamp F.A., Geyer M., Pomorski T.G.,
Olayioye M.A.;
"DLC1 activation requires lipid interaction through a polybasic region
preceding the RhoGAP domain.";
Mol. Biol. Cell 20:4400-4411(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-526 AND
SER-757, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
STRUCTURE BY NMR OF 438-518.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SAM-domain of rho-GTPase-activating protein
7.";
Submitted (APR-2007) to the PDB data bank.
[15]
STRUCTURE BY NMR OF 454-513.
PubMed=19317456; DOI=10.1021/bi9000936;
Yang S., Noble C.G., Yang D.;
"Characterization of DLC1-SAM equilibrium unfolding at the amino acid
residue level.";
Biochemistry 48:4040-4049(2009).
[16]
STRUCTURE BY NMR OF 451-513, MUTAGENESIS OF PHE-475; LEU-476 AND
ARG-1114, INTERACTION WITH EF1A1, AND SUBCELLULAR LOCATION.
PubMed=19158340; DOI=10.1242/jcs.027482;
Zhong D., Zhang J., Yang S., Soh U.J., Buschdorf J.P., Zhou Y.T.,
Yang D., Low B.C.;
"The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell
migration.";
J. Cell Sci. 122:414-424(2009).
[17]
VARIANTS SER-712; MET-791; ALA-959; GLN-998; ALA-1025; VAL-1199 AND
CYS-1209.
PubMed=10649492;
DOI=10.1002/(SICI)1098-1004(200002)15:2<156::AID-HUMU4>3.0.CO;2-4;
Wilson P.J., McGlinn E., Marsh A., Evans T., Arnold J., Wright K.,
Biden K., Young J., Wainwright B., Wicking C., Chenevix-Trench G.;
"Sequence variants of DLC1 in colorectal and ovarian tumours.";
Hum. Mutat. 15:156-165(2000).
-!- FUNCTION: Functions as a GTPase-activating protein for the small
GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream
signaling. This induces morphological changes and detachment
through cytoskeletal reorganization, playing a critical role in
biological processes such as cell migration and proliferation.
Also functions in vivo as an activator of the phospholipase PLCD1.
Active DLC1 increases cell migration velocity but reduces
directionality. {ECO:0000269|PubMed:18786931,
ECO:0000269|PubMed:19170769, ECO:0000269|PubMed:19710422}.
-!- SUBUNIT: Interacts with EF1A1, facilitates EF1A1 distribution to
the membrane periphery and ruffles upon growth factor stimulation
and suppresses cell migration. {ECO:0000269|PubMed:19158340}.
-!- INTERACTION:
P20936:RASA1; NbExp=7; IntAct=EBI-2608428, EBI-1026476;
Q04205:TNS (xeno); NbExp=7; IntAct=EBI-15638708, EBI-2607590;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion.
Membrane; Peripheral membrane protein. Note=Colocalizes with EF1A1
at actin-rich regions in the cell periphery.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
Name=2;
IsoId=Q96QB1-2; Sequence=Displayed;
Name=1;
IsoId=Q96QB1-1; Sequence=VSP_037871, VSP_037872;
Name=3;
IsoId=Q96QB1-3; Sequence=VSP_037873, VSP_037874;
Name=4;
IsoId=Q96QB1-4; Sequence=VSP_037871, VSP_044651;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q96QB1-5; Sequence=VSP_046331, VSP_046332;
Note=No experimental confirmation available.;
Name=6; Synonyms=i-4;
IsoId=Q96QB1-6; Sequence=VSP_053836, VSP_053837;
Note=Produced by alternative promoter usage. ubiquitously
expressed, significantly down-regulated in multiple carcinoma
cell lines. Ref.8 (ABX83661/ABX83662) sequences are in conflict
in positions: 49-50:EA->KP.;
-!- TISSUE SPECIFICITY: Highest level of expression in the spleen,
with rather lower levels in prostate, testis, ovary, small
intestine and colon, but none in the thymus.
-!- DOMAIN: The SAM domain mediates interaction with EF1A1, and
functions as an autoinhibitory regulator of RhoGAP Activity.
{ECO:0000269|PubMed:18786931}.
-!- DOMAIN: The polybasic cluster is required for activation and
mediates binding to phosphatidylinositol-4,5-bisphosphate
(PI(4,5)P(2)) containing membranes. {ECO:0000269|PubMed:18786931}.
-!- SEQUENCE CAUTION:
Sequence=AAB81637.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB21814.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DLC1ID40328ch8p22.html";
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EMBL; AF035119; AAB87700.1; -; mRNA.
EMBL; AF026219; AAB81637.1; ALT_INIT; mRNA.
EMBL; AF408781; AAK97501.1; -; Genomic_DNA.
EMBL; AF408768; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408769; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408770; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408771; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408772; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408773; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408774; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408775; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408776; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408777; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408778; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408779; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AF408780; AAK97501.1; JOINED; Genomic_DNA.
EMBL; AB051510; BAB21814.1; ALT_INIT; mRNA.
EMBL; AK024774; BAB14996.1; -; mRNA.
EMBL; AK299049; BAG61122.1; -; mRNA.
EMBL; AC015641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC019270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC106845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC049842; AAH49842.1; -; mRNA.
EMBL; BC054511; AAH54511.1; -; mRNA.
EMBL; EU159199; ABX83661.1; -; mRNA.
EMBL; EU159200; ABX83662.1; -; mRNA.
CCDS; CCDS55201.1; -. [Q96QB1-4]
CCDS; CCDS5989.1; -. [Q96QB1-2]
CCDS; CCDS5990.1; -. [Q96QB1-1]
CCDS; CCDS5991.2; -. [Q96QB1-5]
CCDS; CCDS83253.1; -. [Q96QB1-6]
RefSeq; NP_001157743.1; NM_001164271.1. [Q96QB1-4]
RefSeq; NP_001303597.1; NM_001316668.1. [Q96QB1-6]
RefSeq; NP_001335010.1; NM_001348081.1. [Q96QB1-2]
RefSeq; NP_001335011.1; NM_001348082.1. [Q96QB1-4]
RefSeq; NP_001335012.1; NM_001348083.1. [Q96QB1-4]
RefSeq; NP_001335013.1; NM_001348084.1. [Q96QB1-4]
RefSeq; NP_006085.2; NM_006094.4. [Q96QB1-1]
RefSeq; NP_079043.3; NM_024767.3. [Q96QB1-5]
RefSeq; NP_872584.2; NM_182643.2. [Q96QB1-2]
RefSeq; XP_005273431.1; XM_005273374.1. [Q96QB1-2]
UniGene; Hs.134296; -.
UniGene; Hs.738560; -.
PDB; 2DKY; NMR; -; A=451-515.
PDB; 2GYT; NMR; -; A=451-513.
PDB; 2KAP; NMR; -; A=454-513.
PDB; 2LOZ; NMR; -; B=811-824.
PDB; 3KUQ; X-ray; 2.30 A; A=1074-1283.
PDB; 5FZT; X-ray; 2.10 A; B=904-926.
PDBsum; 2DKY; -.
PDBsum; 2GYT; -.
PDBsum; 2KAP; -.
PDBsum; 2LOZ; -.
PDBsum; 3KUQ; -.
PDBsum; 5FZT; -.
ProteinModelPortal; Q96QB1; -.
SMR; Q96QB1; -.
BioGrid; 115667; 20.
DIP; DIP-56928N; -.
IntAct; Q96QB1; 34.
MINT; MINT-6942866; -.
STRING; 9606.ENSP00000276297; -.
iPTMnet; Q96QB1; -.
PhosphoSitePlus; Q96QB1; -.
BioMuta; DLC1; -.
DMDM; 313104315; -.
EPD; Q96QB1; -.
PaxDb; Q96QB1; -.
PeptideAtlas; Q96QB1; -.
PRIDE; Q96QB1; -.
DNASU; 10395; -.
Ensembl; ENST00000276297; ENSP00000276297; ENSG00000164741. [Q96QB1-2]
Ensembl; ENST00000316609; ENSP00000321034; ENSG00000164741. [Q96QB1-3]
Ensembl; ENST00000358919; ENSP00000351797; ENSG00000164741. [Q96QB1-1]
Ensembl; ENST00000511869; ENSP00000425878; ENSG00000164741. [Q96QB1-5]
Ensembl; ENST00000512044; ENSP00000422595; ENSG00000164741. [Q96QB1-6]
Ensembl; ENST00000520226; ENSP00000428028; ENSG00000164741. [Q96QB1-4]
GeneID; 10395; -.
KEGG; hsa:10395; -.
UCSC; uc003wwk.2; human. [Q96QB1-2]
CTD; 10395; -.
DisGeNET; 10395; -.
EuPathDB; HostDB:ENSG00000164741.14; -.
GeneCards; DLC1; -.
HGNC; HGNC:2897; DLC1.
HPA; HPA017753; -.
MalaCards; DLC1; -.
MIM; 604258; gene.
neXtProt; NX_Q96QB1; -.
OpenTargets; ENSG00000164741; -.
PharmGKB; PA27351; -.
eggNOG; KOG2200; Eukaryota.
eggNOG; ENOG410XQ10; LUCA.
GeneTree; ENSGT00760000119123; -.
HOGENOM; HOG000147792; -.
HOVERGEN; HBG055955; -.
InParanoid; Q96QB1; -.
KO; K20632; -.
OMA; CGPGKSK; -.
OrthoDB; EOG091G00OE; -.
PhylomeDB; Q96QB1; -.
TreeFam; TF314044; -.
Reactome; R-HSA-194840; Rho GTPase cycle.
SIGNOR; Q96QB1; -.
ChiTaRS; DLC1; human.
EvolutionaryTrace; Q96QB1; -.
GeneWiki; DLC1; -.
GenomeRNAi; 10395; -.
PRO; PR:Q96QB1; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000164741; -.
CleanEx; HS_DLC1; -.
ExpressionAtlas; Q96QB1; baseline and differential.
Genevisible; Q96QB1; HS.
GO; GO:0005901; C:caveola; IDA:UniProtKB.
GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IEA:InterPro.
GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; ISS:UniProtKB.
GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
GO; GO:0021575; P:hindbrain morphogenesis; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:UniProtKB.
GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IDA:UniProtKB.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 3.30.530.20; -; 1.
InterPro; IPR028854; DLC1.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR023393; START-like_dom_sf.
InterPro; IPR002913; START_lipid-bd_dom.
PANTHER; PTHR12659:SF2; PTHR12659:SF2; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF07647; SAM_2; 1.
Pfam; PF01852; START; 1.
SMART; SM00324; RhoGAP; 1.
SMART; SM00234; START; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF48350; SSF48350; 1.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50848; START; 1.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Alternative splicing;
Cell junction; Complete proteome; Cytoplasm; GTPase activation;
Membrane; Phosphoprotein; Polymorphism; Reference proteome;
Tumor suppressor.
CHAIN 1 1528 Rho GTPase-activating protein 7.
/FTId=PRO_0000056707.
DOMAIN 448 515 SAM.
DOMAIN 1078 1284 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
DOMAIN 1314 1521 START. {ECO:0000255|PROSITE-
ProRule:PRU00197}.
REGION 710 884 Focal adhesion-targeting (FAT).
REGION 1051 1073 Polybasic cluster (PBR).
COMPBIAS 741 747 Poly-Ser.
COMPBIAS 868 874 Poly-Ser.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 566 566 Phosphoserine.
{ECO:0000250|UniProtKB:Q63744}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 437 Missing (in isoform 1 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9605766,
ECO:0000303|Ref.2}.
/FTId=VSP_037871.
VAR_SEQ 1 45 MSVAIRKRSWEEHVTHWMGQPFNSDDRNTACHHGLVADSLQ
ASME -> MGDPKAHVMARPLRAPLRRSFSDHIRDSTARAL
DVIWKNTRDRRL (in isoform 6).
{ECO:0000303|PubMed:21217778}.
/FTId=VSP_053836.
VAR_SEQ 46 448 Missing (in isoform 6).
{ECO:0000303|PubMed:21217778}.
/FTId=VSP_053837.
VAR_SEQ 438 511 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044651.
VAR_SEQ 438 450 TAIQGISEKEKAE -> MCRKKPDTMILTQ (in
isoform 1). {ECO:0000303|PubMed:9605766,
ECO:0000303|Ref.2}.
/FTId=VSP_037872.
VAR_SEQ 450 498 EIEAKEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDF
LDRDAIEA -> AVKSVKLEVDEDKSTKGSNFSNSEVAIGL
SPYTFPQKRLFHVAGEENIT (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037873.
VAR_SEQ 450 463 EIEAKEACDWLRAT -> GKLTFWFCFLANLF (in
isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046331.
VAR_SEQ 464 1528 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046332.
VAR_SEQ 499 1528 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037874.
VARIANT 27 27 R -> C (in dbSNP:rs34575560).
/FTId=VAR_059293.
VARIANT 81 81 L -> V (in dbSNP:rs3816748).
/FTId=VAR_059294.
VARIANT 254 254 Q -> H (in dbSNP:rs11203495).
{ECO:0000269|PubMed:11214970,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_059295.
VARIANT 255 255 N -> D (in dbSNP:rs11203494).
{ECO:0000269|PubMed:11214970,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_059296.
VARIANT 260 260 T -> I (in dbSNP:rs3816747).
{ECO:0000269|PubMed:11214970,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_059297.
VARIANT 320 320 Q -> H (in dbSNP:rs34591797).
/FTId=VAR_059298.
VARIANT 712 712 N -> S (in dbSNP:rs1044092).
{ECO:0000269|PubMed:10649492,
ECO:0000269|PubMed:9605766}.
/FTId=VAR_014229.
VARIANT 791 791 V -> M (in dbSNP:rs532841).
{ECO:0000269|PubMed:10649492,
ECO:0000269|PubMed:11214970,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_014230.
VARIANT 959 959 T -> A (in dbSNP:rs121908500).
{ECO:0000269|PubMed:10649492}.
/FTId=VAR_014231.
VARIANT 998 998 H -> Q (in dbSNP:rs149295187).
{ECO:0000269|PubMed:10649492}.
/FTId=VAR_014232.
VARIANT 1025 1025 V -> A. {ECO:0000269|PubMed:10649492}.
/FTId=VAR_014233.
VARIANT 1199 1199 E -> V (in dbSNP:rs1044093).
{ECO:0000269|PubMed:10649492,
ECO:0000269|PubMed:9605766}.
/FTId=VAR_014234.
VARIANT 1209 1209 S -> C (in dbSNP:rs1044094).
{ECO:0000269|PubMed:10649492,
ECO:0000269|PubMed:9605766}.
/FTId=VAR_014235.
MUTAGEN 475 475 F->G: Abolishes interaction with EF1A1.
{ECO:0000269|PubMed:19158340}.
MUTAGEN 476 476 L->G: Abolishes interaction with EF1A1.
{ECO:0000269|PubMed:19158340}.
MUTAGEN 879 879 Y->F: Unable to displace endogenous DLC1
from focal adhesions.
{ECO:0000269|PubMed:18786931}.
MUTAGEN 1114 1114 R->E: No catalytic activity.
{ECO:0000269|PubMed:19158340}.
CONFLICT 43 43 S -> C (in Ref. 5; BAB14996).
{ECO:0000305}.
CONFLICT 130 130 T -> I (in Ref. 5; BAB14996).
{ECO:0000305}.
CONFLICT 571 571 H -> L (in Ref. 4; BAB21814).
{ECO:0000305}.
CONFLICT 1114 1114 R -> K (in Ref. 1; AAB87700).
{ECO:0000305}.
CONFLICT 1364 1364 P -> R (in Ref. 1; AAB87700).
{ECO:0000305}.
HELIX 449 463 {ECO:0000244|PDB:2DKY}.
HELIX 468 473 {ECO:0000244|PDB:2DKY}.
TURN 474 476 {ECO:0000244|PDB:2KAP}.
HELIX 481 487 {ECO:0000244|PDB:2DKY}.
TURN 488 490 {ECO:0000244|PDB:2DKY}.
HELIX 493 509 {ECO:0000244|PDB:2DKY}.
TURN 510 514 {ECO:0000244|PDB:2DKY}.
HELIX 906 920 {ECO:0000244|PDB:5FZT}.
HELIX 1080 1087 {ECO:0000244|PDB:3KUQ}.
STRAND 1088 1091 {ECO:0000244|PDB:3KUQ}.
HELIX 1093 1105 {ECO:0000244|PDB:3KUQ}.
TURN 1110 1114 {ECO:0000244|PDB:3KUQ}.
HELIX 1119 1129 {ECO:0000244|PDB:3KUQ}.
STRAND 1131 1134 {ECO:0000244|PDB:3KUQ}.
HELIX 1143 1156 {ECO:0000244|PDB:3KUQ}.
STRAND 1157 1159 {ECO:0000244|PDB:3KUQ}.
HELIX 1166 1176 {ECO:0000244|PDB:3KUQ}.
HELIX 1179 1181 {ECO:0000244|PDB:3KUQ}.
HELIX 1182 1191 {ECO:0000244|PDB:3KUQ}.
HELIX 1195 1213 {ECO:0000244|PDB:3KUQ}.
HELIX 1215 1218 {ECO:0000244|PDB:3KUQ}.
HELIX 1222 1234 {ECO:0000244|PDB:3KUQ}.
HELIX 1260 1278 {ECO:0000244|PDB:3KUQ}.
SEQUENCE 1528 AA; 170591 MW; 5D20F29CC606302E CRC64;
MSVAIRKRSW EEHVTHWMGQ PFNSDDRNTA CHHGLVADSL QASMEKDATL NVDRKEKCVS
LPDCCHGSEL RDFPGRPMGH LSKDVDENDS HEGEDQFLSL EASTETLVHV SDEDNNADLC
LTDDKQVLNT QGQKTSGQHM IQGAGSLEKA LPIIQSNQVS SNSWGIAGET ELALVKESGE
RKVTDSISKS LELCNEISLS EIKDAPKVNA VDTLNVKDIA PEKQLLNSAV IAQQRRKPDP
PKDENERSTC NVVQNEFLDT PCTNRGLPLL KTDFGSCLLQ PPSCPNGMSA ENGLEKSGFS
QHQNKSPPKV KAEDGMQCLQ LKETLATQEP TDNQVRLRKR KEIREDRDRA RLDSMVLLIM
KLDQLDQDIE NALSTSSSPS GTPTNLRRHV PDLESGSESG ADTISVNQTR VNLSSDTEST
DLPSSTPVAN SGTKPKTTAI QGISEKEKAE IEAKEACDWL RATGFPQYAQ LYEDFLFPID
ISLVKREHDF LDRDAIEALC RRLNTLNKCA VMKLEISPHR KRSDDSDEDE PCAISGKWTF
QRDSKRWSRL EEFDVFSPKQ DLVPGSPDDS HPKDGPSPGG TLMDLSERQE VSSVRSLSST
GSLPSHAPPS EDAATPRTNS VISVCSSSNL AGNDDSFGSL PSPKELSSFS FSMKGHEKTA
KSKTRSLLKR MESLKLKSSH HSKHKAPSKL GLIISGPILQ EGMDEEKLKQ LNCVEISALN
GNRINVPMVR KRSVSNSTQT SSSSSQSETS SAVSTPSPVT RTRSLSACNK RVGMYLEGFD
PFNQSTFNNV VEQNFKNRES YPEDTVFYIP EDHKPGTFPK ALTNGSFSPS GNNGSVNWRT
GSFHGPGHIS LRRENSSDSP KELKRRNSSS SMSSRLSIYD NVPGSILYSS SGDLADLENE
DIFPELDDIL YHVKGMQRIV NQWSEKFSDE GDSDSALDSV SPCPSSPKQI HLDVDNDRTT
PSDLDSTGNS LNEPEEPSEI PERRDSGVGA SLTRSNRHRL RWHSFQSSHR PSLNSVSLQI
NCQSVAQMNL LQKYSLLKLT ALLEKYTPSN KHGFSWAVPK FMKRIKVPDY KDRSVFGVPL
TVNVQRTGQP LPQSIQQAMR YLRNHCLDQV GLFRKSGVKS RIQALRQMNE GAIDCVNYEG
QSAYDVADML KQYFRDLPEP LMTNKLSETF LQIYQYVPKD QRLQAIKAAI MLLPDENREV
LQTLLYFLSD VTAAVKENQM TPTNLAVCLA PSLFHLNTLK RENSSPRVMQ RKQSLGKPDQ
KDLNENLAAT QGLAHMIAEC KKLFQVPEEM SRCRNSYTEQ ELKPLTLEAL GHLGNDDSAD
YQHFLQDCVD GLFKEVKEKF KGWVSYSTSE QAELSYKKVS EGPPLRLWRS VIEVPAVPEE
ILKRLLKEQH LWDVDLLDSK VIEILDSQTE IYQYVQNSMA PHPARDYVVL RTWRTNLPKG
ACALLLTSVD HDRAPVVGVR VNVLLSRYLI EPCGPGKSKL TYMCRVDLRG HMPEWYTKSF
GHLCAAEVVK IRDSFSNQNT ETKDTKSR


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