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Q96QB1 (RHG07_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho GTPase-activating protein 7
Alternative name(s):
Deleted in liver cancer 1 protein
Short name=DLC-1
HP protein
Rho-type GTPase-activating protein 7
START domain-containing protein 12
Short name=StARD12
StAR-related lipid transfer protein 12
Gene names
Name:DLC1
Synonyms:ARHGAP7, KIAA1723, STARD12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1528 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.9 Ref.10 Ref.11

Subunit structure

Interacts with EF1A1, facilitates EF1A1 distribution to the membrane periphery and ruffles upon growth factor stimulation and suppresses cell migration. Ref.14

Subcellular location

Cytoplasm. Cell junctionfocal adhesion. Membrane; Peripheral membrane protein. Note: Colocalizes with EF1A1 at actin-rich regions in the cell periphery. Ref.9 Ref.10 Ref.14

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. Ref.9

The polybasic cluster is required for activation and mediates binding to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) containing membranes. Ref.9

Sequence similarities

Contains 1 Rho-GAP domain.

Contains 1 SAM (sterile alpha motif) domain.

Contains 1 START domain.

Sequence caution

The sequence AAB81637.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB21814.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasm
Membrane
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DiseaseTumor suppressor
   Molecular functionGTPase activation
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 17888903. Source: UniProtKB

apoptotic process

Inferred from direct assay PubMed 17292327. Source: UniProtKB

focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

forebrain development

Inferred from sequence or structural similarity. Source: UniProtKB

heart morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

hindbrain morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of Rho protein signal transduction

Inferred from mutant phenotype PubMed 16951145. Source: UniProtKB

negative regulation of cell migration

Inferred from direct assay PubMed 17932950. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay PubMed 12545165PubMed 17932950. Source: UniProtKB

negative regulation of stress fiber assembly

Inferred from direct assay PubMed 17932950. Source: UniProtKB

neural tube closure

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Rho GTPase activity

Inferred from direct assay PubMed 17932950. Source: GOC

positive regulation of execution phase of apoptosis

Inferred from direct assay PubMed 17888903. Source: UniProtKB

positive regulation of protein dephosphorylation

Inferred from direct assay PubMed 17292327. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from mutant phenotype PubMed 17292327. Source: UniProtKB

regulation of cell shape

Inferred from mutant phenotype PubMed 17292327. Source: UniProtKB

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentcaveola

Inferred from direct assay PubMed 16951145. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 16951145PubMed 17888903. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from direct assay PubMed 16951145PubMed 17190795. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 17888903. Source: UniProtKB

   Molecular_functionRho GTPase activator activity

Inferred from direct assay PubMed 17932950. Source: UniProtKB

SH2 domain binding

Inferred from physical interaction PubMed 17190795. Source: UniProtKB

lipid binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 16951145. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RASA1P209366EBI-2608428,EBI-1026476

Alternative products

This entry describes 6 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q96QB1-2)

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 1 (identifier: Q96QB1-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-437: Missing.
     438-450: TAIQGISEKEKAE → MCRKKPDTMILTQ
Isoform 3 (identifier: Q96QB1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     450-498: EIEAKEACDW...DFLDRDAIEA → AVKSVKLEVD...FHVAGEENIT
     499-1528: Missing.
Isoform 4 (identifier: Q96QB1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-437: Missing.
     438-511: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q96QB1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     450-463: EIEAKEACDWLRAT → GKLTFWFCFLANLF
     464-1528: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q96QB1-6)

Also known as: i-4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: MSVAIRKRSW...VADSLQASME → MGDPKAHVMA...IWKNTRDRRL
     46-448: Missing.
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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15281528Rho GTPase-activating protein 7
PRO_0000056707

Regions

Domain448 – 51568SAM
Domain1078 – 1284207Rho-GAP
Domain1314 – 1521208START
Region710 – 884175Focal adhesion-targeting (FAT)
Region1051 – 107323Polybasic cluster (PBR)
Compositional bias741 – 7477Poly-Ser
Compositional bias868 – 8747Poly-Ser

Amino acid modifications

Modified residue5231Phosphoserine By similarity
Modified residue5261Phosphoserine By similarity

Natural variations

Alternative sequence1 – 437437Missing in isoform 1 and isoform 4.
VSP_037871
Alternative sequence1 – 4545MSVAI…QASME → MGDPKAHVMARPLRAPLRRS FSDHIRDSTARALDVIWKNT RDRRL in isoform 6.
VSP_053836
Alternative sequence46 – 448403Missing in isoform 6.
VSP_053837
Alternative sequence438 – 51174Missing in isoform 4.
VSP_044651
Alternative sequence438 – 45013TAIQG…KEKAE → MCRKKPDTMILTQ in isoform 1.
VSP_037872
Alternative sequence450 – 49849EIEAK…DAIEA → AVKSVKLEVDEDKSTKGSNF SNSEVAIGLSPYTFPQKRLF HVAGEENIT in isoform 3.
VSP_037873
Alternative sequence450 – 46314EIEAK…WLRAT → GKLTFWFCFLANLF in isoform 5.
VSP_046331
Alternative sequence464 – 15281065Missing in isoform 5.
VSP_046332
Alternative sequence499 – 15281030Missing in isoform 3.
VSP_037874
Natural variant271R → C.
Corresponds to variant rs34575560 [ dbSNP | Ensembl ].
VAR_059293
Natural variant811L → V.
Corresponds to variant rs3816748 [ dbSNP | Ensembl ].
VAR_059294
Natural variant2541Q → H. Ref.4 Ref.5
Corresponds to variant rs11203495 [ dbSNP | Ensembl ].
VAR_059295
Natural variant2551N → D. Ref.4 Ref.5 Ref.7
Corresponds to variant rs11203494 [ dbSNP | Ensembl ].
VAR_059296
Natural variant2601T → I. Ref.4 Ref.5
Corresponds to variant rs3816747 [ dbSNP | Ensembl ].
VAR_059297
Natural variant3201Q → H.
Corresponds to variant rs34591797 [ dbSNP | Ensembl ].
VAR_059298
Natural variant7121N → S. Ref.1 Ref.15
Corresponds to variant rs1044092 [ dbSNP | Ensembl ].
VAR_014229
Natural variant7911V → M. Ref.2 Ref.3 Ref.4 Ref.5 Ref.15
Corresponds to variant rs532841 [ dbSNP | Ensembl ].
VAR_014230
Natural variant9591T → A. Ref.15
VAR_014231
Natural variant9981H → Q. Ref.15
Corresponds to variant rs149295187 [ dbSNP | Ensembl ].
VAR_014232
Natural variant10251V → A. Ref.15
VAR_014233
Natural variant11991E → V. Ref.1 Ref.15
Corresponds to variant rs1044093 [ dbSNP | Ensembl ].
VAR_014234
Natural variant12091S → C. Ref.1 Ref.15
Corresponds to variant rs1044094 [ dbSNP | Ensembl ].
VAR_014235

Experimental info

Mutagenesis4751F → G: Abolishes interaction with EF1A1. Ref.14
Mutagenesis4761L → G: Abolishes interaction with EF1A1. Ref.14
Mutagenesis8791Y → F: Unable to displace endogenous DLC1 from focal adhesions. Ref.9
Mutagenesis11141R → E: No catalytic activity. Ref.14
Sequence conflict431S → C in BAB14996. Ref.5
Sequence conflict1301T → I in BAB14996. Ref.5
Sequence conflict5711H → L in BAB21814. Ref.4
Sequence conflict11141R → K in AAB87700. Ref.1
Sequence conflict13641P → R in AAB87700. Ref.1

Secondary structure

....................................... 1528
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified November 30, 2010. Version 4.
Checksum: 5D20F29CC606302E

FASTA1,528170,591
        10         20         30         40         50         60 
MSVAIRKRSW EEHVTHWMGQ PFNSDDRNTA CHHGLVADSL QASMEKDATL NVDRKEKCVS 

        70         80         90        100        110        120 
LPDCCHGSEL RDFPGRPMGH LSKDVDENDS HEGEDQFLSL EASTETLVHV SDEDNNADLC 

       130        140        150        160        170        180 
LTDDKQVLNT QGQKTSGQHM IQGAGSLEKA LPIIQSNQVS SNSWGIAGET ELALVKESGE 

       190        200        210        220        230        240 
RKVTDSISKS LELCNEISLS EIKDAPKVNA VDTLNVKDIA PEKQLLNSAV IAQQRRKPDP 

       250        260        270        280        290        300 
PKDENERSTC NVVQNEFLDT PCTNRGLPLL KTDFGSCLLQ PPSCPNGMSA ENGLEKSGFS 

       310        320        330        340        350        360 
QHQNKSPPKV KAEDGMQCLQ LKETLATQEP TDNQVRLRKR KEIREDRDRA RLDSMVLLIM 

       370        380        390        400        410        420 
KLDQLDQDIE NALSTSSSPS GTPTNLRRHV PDLESGSESG ADTISVNQTR VNLSSDTEST 

       430        440        450        460        470        480 
DLPSSTPVAN SGTKPKTTAI QGISEKEKAE IEAKEACDWL RATGFPQYAQ LYEDFLFPID 

       490        500        510        520        530        540 
ISLVKREHDF LDRDAIEALC RRLNTLNKCA VMKLEISPHR KRSDDSDEDE PCAISGKWTF 

       550        560        570        580        590        600 
QRDSKRWSRL EEFDVFSPKQ DLVPGSPDDS HPKDGPSPGG TLMDLSERQE VSSVRSLSST 

       610        620        630        640        650        660 
GSLPSHAPPS EDAATPRTNS VISVCSSSNL AGNDDSFGSL PSPKELSSFS FSMKGHEKTA 

       670        680        690        700        710        720 
KSKTRSLLKR MESLKLKSSH HSKHKAPSKL GLIISGPILQ EGMDEEKLKQ LNCVEISALN 

       730        740        750        760        770        780 
GNRINVPMVR KRSVSNSTQT SSSSSQSETS SAVSTPSPVT RTRSLSACNK RVGMYLEGFD 

       790        800        810        820        830        840 
PFNQSTFNNV VEQNFKNRES YPEDTVFYIP EDHKPGTFPK ALTNGSFSPS GNNGSVNWRT 

       850        860        870        880        890        900 
GSFHGPGHIS LRRENSSDSP KELKRRNSSS SMSSRLSIYD NVPGSILYSS SGDLADLENE 

       910        920        930        940        950        960 
DIFPELDDIL YHVKGMQRIV NQWSEKFSDE GDSDSALDSV SPCPSSPKQI HLDVDNDRTT 

       970        980        990       1000       1010       1020 
PSDLDSTGNS LNEPEEPSEI PERRDSGVGA SLTRSNRHRL RWHSFQSSHR PSLNSVSLQI 

      1030       1040       1050       1060       1070       1080 
NCQSVAQMNL LQKYSLLKLT ALLEKYTPSN KHGFSWAVPK FMKRIKVPDY KDRSVFGVPL 

      1090       1100       1110       1120       1130       1140 
TVNVQRTGQP LPQSIQQAMR YLRNHCLDQV GLFRKSGVKS RIQALRQMNE GAIDCVNYEG 

      1150       1160       1170       1180       1190       1200 
QSAYDVADML KQYFRDLPEP LMTNKLSETF LQIYQYVPKD QRLQAIKAAI MLLPDENREV 

      1210       1220       1230       1240       1250       1260 
LQTLLYFLSD VTAAVKENQM TPTNLAVCLA PSLFHLNTLK RENSSPRVMQ RKQSLGKPDQ 

      1270       1280       1290       1300       1310       1320 
KDLNENLAAT QGLAHMIAEC KKLFQVPEEM SRCRNSYTEQ ELKPLTLEAL GHLGNDDSAD 

      1330       1340       1350       1360       1370       1380 
YQHFLQDCVD GLFKEVKEKF KGWVSYSTSE QAELSYKKVS EGPPLRLWRS VIEVPAVPEE 

      1390       1400       1410       1420       1430       1440 
ILKRLLKEQH LWDVDLLDSK VIEILDSQTE IYQYVQNSMA PHPARDYVVL RTWRTNLPKG 

      1450       1460       1470       1480       1490       1500 
ACALLLTSVD HDRAPVVGVR VNVLLSRYLI EPCGPGKSKL TYMCRVDLRG HMPEWYTKSF 

      1510       1520 
GHLCAAEVVK IRDSFSNQNT ETKDTKSR 

« Hide

Isoform 1 [UniParc].

Checksum: 422B9D58B528E26C
Show »

FASTA1,091122,827
Isoform 3 [UniParc].

Checksum: AA2A500A52492F1F
Show »

FASTA49854,552
Isoform 4 [UniParc].

Checksum: A001B182EDE65398
Show »

FASTA1,017114,152
Isoform 5 [UniParc].

Checksum: 299AF4E12B29EEB1
Show »

FASTA46350,890
Isoform 6 (i-4) [UniParc].

Checksum: A93D84FF40E9B92A
Show »

FASTA1,125126,746

References

« Hide 'large scale' references
[1]"Cloning, characterization, and chromosomal localization of a gene frequently deleted in human liver cancer (DLC-1) homologous to rat RhoGAP."
Yuan B.Z., Miller M.J., Keck C.L., Zimonjic D.B., Thorgeirsson S.S., Popescu N.C.
Cancer Res. 58:2196-2199(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-712; VAL-1199 AND CYS-1209.
[2]"Cloning and molecular characterization of the human ortholog of the rat dual regulator p122RhoGAP."
Wei M.-H., Pack S., Ivanov S., Lerman M.I.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-791.
Tissue: Lung.
[3]"Identification of HP/DLC1 exon and introns."
Jeong S.-J., Dimtchev A., Lerman M., Dritschilo A., Jung M.
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT MET-791.
[4]"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."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS HIS-254; ASP-255 AND ILE-260 AND MET-791.
Tissue: Brain.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), VARIANTS HIS-254; ASP-255; ILE-260 AND MET-791.
Tissue: Smooth muscle.
[6]"DNA sequence and analysis of human chromosome 8."
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. expand/collapse author list , 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.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 2 AND 5), VARIANT ASP-255.
Tissue: Brain and Lung.
[8]"A novel isoform of the 8p22 tumor suppressor gene DLC1 suppresses tumor growth and is frequently silenced in multiple common tumors."
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.
Oncogene 30:1923-1935(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-50 (ISOFORM 6), ALTERNATIVE PROMOTER USAGE.
Tissue: Liver.
[9]"Effects of structure of Rho GTPase-activating protein DLC-1 on cell morphology and migration."
Kim T.Y., Healy K.D., Der C.J., Sciaky N., Bang Y.J., Juliano R.L.
J. Biol. Chem. 283:32762-32770(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN SAM, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-879.
[10]"Focal adhesion-localization of START-GAP1/DLC1 is essential for cell motility and morphology."
Kawai K., Iwamae Y., Yamaga M., Kiyota M., Ishii H., Hirata H., Homma Y., Yagisawa H.
Genes Cells 14:227-241(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, FOCAL ADHESION TARGETING.
[11]"DLC1 activation requires lipid interaction through a polybasic region preceding the RhoGAP domain."
Erlmann P., Schmid S., Horenkamp F.A., Geyer M., Pomorski T.G., Olayioye M.A.
Mol. Biol. Cell 20:4400-4411(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, LIPID-BINDING REGION.
[12]"Solution structure of the SAM-domain of rho-GTPase-activating protein 7."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 438-518.
[13]"Characterization of DLC1-SAM equilibrium unfolding at the amino acid residue level."
Yang S., Noble C.G., Yang D.
Biochemistry 48:4040-4049(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 454-513.
[14]"The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell migration."
Zhong D., Zhang J., Yang S., Soh U.J., Buschdorf J.P., Zhou Y.T., Yang D., Low B.C.
J. Cell Sci. 122:414-424(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 451-513, MUTAGENESIS OF PHE-475; LEU-476 AND ARG-1114, INTERACTION WITH EF1A1, SUBCELLULAR LOCATION.
[15]"Sequence variants of DLC1 in colorectal and ovarian tumours."
Wilson P.J., McGlinn E., Marsh A., Evans T., Arnold J., Wright K., Biden K., Young J., Wainwright B., Wicking C., Chenevix-Trench G.
Hum. Mutat. 15:156-165(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-712; MET-791; ALA-959; GLN-998; ALA-1025; VAL-1199 AND CYS-1209.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF035119 mRNA. Translation: AAB87700.1.
AF026219 mRNA. Translation: AAB81637.1. Different initiation.
AF408781 expand/collapse EMBL AC list , AF408768, AF408769, AF408770, AF408771, AF408772, AF408773, AF408774, AF408775, AF408776, AF408777, AF408778, AF408779, AF408780 Genomic DNA. Translation: AAK97501.1.
AB051510 mRNA. Translation: BAB21814.1. Different initiation.
AK024774 mRNA. Translation: BAB14996.1.
AK299049 mRNA. Translation: BAG61122.1.
AC015641 Genomic DNA. No translation available.
AC019270 Genomic DNA. No translation available.
AC022844 Genomic DNA. No translation available.
AC106845 Genomic DNA. No translation available.
BC049842 mRNA. Translation: AAH49842.1.
BC054511 mRNA. Translation: AAH54511.1.
EU159199 mRNA. Translation: ABX83661.1.
EU159200 mRNA. Translation: ABX83662.1.
CCDSCCDS55201.1. [Q96QB1-4]
CCDS5989.1. [Q96QB1-2]
CCDS5990.1. [Q96QB1-1]
CCDS5991.2. [Q96QB1-5]
RefSeqNP_001157743.1. NM_001164271.1. [Q96QB1-4]
NP_006085.2. NM_006094.4. [Q96QB1-1]
NP_079043.3. NM_024767.3. [Q96QB1-5]
NP_872584.2. NM_182643.2. [Q96QB1-2]
XP_005273431.1. XM_005273374.1. [Q96QB1-2]
XP_005273432.1. XM_005273375.1. [Q96QB1-6]
UniGeneHs.134296.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DKYNMR-A451-515[»]
2GYTNMR-A451-513[»]
2KAPNMR-A454-513[»]
2LOZNMR-B811-824[»]
3KUQX-ray2.30A1074-1283[»]
ProteinModelPortalQ96QB1.
SMRQ96QB1. Positions 454-513, 1070-1279, 1324-1515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115667. 11 interactions.
IntActQ96QB1. 3 interactions.
MINTMINT-6942866.
STRING9606.ENSP00000276297.

PTM databases

PhosphoSiteQ96QB1.

Polymorphism databases

DMDM313104315.

Proteomic databases

MaxQBQ96QB1.
PaxDbQ96QB1.
PRIDEQ96QB1.

Protocols and materials databases

DNASU10395.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276297; ENSP00000276297; ENSG00000164741. [Q96QB1-2]
ENST00000316609; ENSP00000321034; ENSG00000164741. [Q96QB1-3]
ENST00000358919; ENSP00000351797; ENSG00000164741. [Q96QB1-1]
ENST00000511869; ENSP00000425878; ENSG00000164741. [Q96QB1-5]
ENST00000512044; ENSP00000422595; ENSG00000164741.
ENST00000520226; ENSP00000428028; ENSG00000164741. [Q96QB1-4]
GeneID10395.
KEGGhsa:10395.
UCSCuc003wwk.1. human. [Q96QB1-1]
uc003wwm.2. human. [Q96QB1-2]
uc003wwn.3. human. [Q96QB1-3]

Organism-specific databases

CTD10395.
GeneCardsGC08M012940.
HGNCHGNC:2897. DLC1.
HPAHPA017753.
MIM604258. gene.
neXtProtNX_Q96QB1.
PharmGKBPA27351.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236923.
HOGENOMHOG000039960.
HOVERGENHBG055955.
OMAHDRAPVA.
OrthoDBEOG7CG6Z8.
PhylomeDBQ96QB1.
TreeFamTF314044.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ96QB1.
BgeeQ96QB1.
CleanExHS_DLC1.
GenevestigatorQ96QB1.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
3.30.530.20. 1 hit.
InterProIPR028854. DLC1.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PANTHERPTHR12659:SF2. PTHR12659:SF2. 1 hit.
PfamPF00620. RhoGAP. 1 hit.
PF07647. SAM_2. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTSM00324. RhoGAP. 1 hit.
SM00454. SAM. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF48350. SSF48350. 1 hit.
PROSITEPS50238. RHOGAP. 1 hit.
PS50848. START. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDLC1. human.
EvolutionaryTraceQ96QB1.
GeneWikiDLC1.
GenomeRNAi10395.
NextBio35481526.
PROQ96QB1.
SOURCESearch...

Entry information

Entry nameRHG07_HUMAN
AccessionPrimary (citable) accession number: Q96QB1
Secondary accession number(s): B4DR10 expand/collapse secondary AC list , B8PTI0, E9PDZ8, E9PF76, E9PGY9, O14868, O43199, Q7Z5R8, Q86UC6, Q9C0E0, Q9H7A2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 125 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM