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Q96QB1

- RHG07_HUMAN

UniProt

Q96QB1 - RHG07_HUMAN

Protein

Rho GTPase-activating protein 7

Gene

DLC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 4 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    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.3 Publications

    GO - Molecular functioni

    1. lipid binding Source: InterPro
    2. protein binding Source: UniProtKB
    3. Rho GTPase activator activity Source: UniProtKB
    4. SH2 domain binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    3. apoptotic process Source: UniProtKB
    4. focal adhesion assembly Source: UniProtKB
    5. forebrain development Source: UniProtKB
    6. heart morphogenesis Source: UniProtKB
    7. hindbrain morphogenesis Source: UniProtKB
    8. negative regulation of cell migration Source: UniProtKB
    9. negative regulation of cell proliferation Source: UniProtKB
    10. negative regulation of Rho protein signal transduction Source: UniProtKB
    11. negative regulation of stress fiber assembly Source: UniProtKB
    12. neural tube closure Source: UniProtKB
    13. positive regulation of execution phase of apoptosis Source: UniProtKB
    14. positive regulation of protein dephosphorylation Source: UniProtKB
    15. positive regulation of Rho GTPase activity Source: GOC
    16. regulation of actin cytoskeleton organization Source: UniProtKB
    17. regulation of cell shape Source: UniProtKB
    18. regulation of small GTPase mediated signal transduction Source: Reactome
    19. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:DLC1
    Synonyms:ARHGAP7, KIAA1723, STARD12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:2897. DLC1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. caveola Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. focal adhesion Source: UniProtKB
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi475 – 4751F → G: Abolishes interaction with EF1A1. 1 Publication
    Mutagenesisi476 – 4761L → G: Abolishes interaction with EF1A1. 1 Publication
    Mutagenesisi879 – 8791Y → F: Unable to displace endogenous DLC1 from focal adhesions. 1 Publication
    Mutagenesisi1114 – 11141R → E: No catalytic activity. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA27351.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15281528Rho GTPase-activating protein 7PRO_0000056707Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei523 – 5231PhosphoserineBy similarity
    Modified residuei526 – 5261PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96QB1.
    PaxDbiQ96QB1.
    PRIDEiQ96QB1.

    PTM databases

    PhosphoSiteiQ96QB1.

    Expressioni

    Tissue specificityi

    Highest level of expression in the spleen, with rather lower levels in prostate, testis, ovary, small intestine and colon, but none in the thymus.

    Gene expression databases

    ArrayExpressiQ96QB1.
    BgeeiQ96QB1.
    CleanExiHS_DLC1.
    GenevestigatoriQ96QB1.

    Organism-specific databases

    HPAiHPA017753.

    Interactioni

    Subunit structurei

    Interacts with EF1A1, facilitates EF1A1 distribution to the membrane periphery and ruffles upon growth factor stimulation and suppresses cell migration.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RASA1P209366EBI-2608428,EBI-1026476

    Protein-protein interaction databases

    BioGridi115667. 11 interactions.
    DIPiDIP-56928N.
    IntActiQ96QB1. 3 interactions.
    MINTiMINT-6942866.
    STRINGi9606.ENSP00000276297.

    Structurei

    Secondary structure

    1
    1528
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi451 – 46313
    Helixi468 – 4736
    Turni474 – 4763
    Helixi481 – 4877
    Turni488 – 4903
    Helixi493 – 50917
    Turni510 – 5145
    Helixi1080 – 10878
    Beta strandi1088 – 10914
    Helixi1093 – 110513
    Turni1110 – 11145
    Helixi1119 – 112911
    Beta strandi1131 – 11344
    Helixi1143 – 115614
    Beta strandi1157 – 11593
    Helixi1166 – 117611
    Helixi1179 – 11813
    Helixi1182 – 119110
    Helixi1195 – 121319
    Helixi1215 – 12184
    Helixi1222 – 123413
    Helixi1260 – 127819

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DKYNMR-A451-515[»]
    2GYTNMR-A451-513[»]
    2KAPNMR-A454-513[»]
    2LOZNMR-B811-824[»]
    3KUQX-ray2.30A1074-1283[»]
    ProteinModelPortaliQ96QB1.
    SMRiQ96QB1. Positions 454-513, 1070-1279, 1324-1515.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96QB1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini448 – 51568SAMAdd
    BLAST
    Domaini1078 – 1284207Rho-GAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini1314 – 1521208STARTPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni710 – 884175Focal adhesion-targeting (FAT)Add
    BLAST
    Regioni1051 – 107323Polybasic cluster (PBR)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi741 – 7477Poly-Ser
    Compositional biasi868 – 8747Poly-Ser

    Domaini

    The SAM domain mediates interaction with EF1A1, and functions as an autoinhibitory regulator of RhoGAP Activity.1 Publication
    The polybasic cluster is required for activation and mediates binding to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) containing membranes.1 Publication

    Sequence similaritiesi

    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
    Contains 1 START domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG236923.
    HOGENOMiHOG000039960.
    HOVERGENiHBG055955.
    OMAiHDRAPVA.
    OrthoDBiEOG7CG6Z8.
    PhylomeDBiQ96QB1.
    TreeFamiTF314044.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    3.30.530.20. 1 hit.
    InterProiIPR028854. 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]
    PANTHERiPTHR12659:SF2. PTHR12659:SF2. 1 hit.
    PfamiPF00620. RhoGAP. 1 hit.
    PF07647. SAM_2. 1 hit.
    PF01852. START. 1 hit.
    [Graphical view]
    SMARTiSM00324. RhoGAP. 1 hit.
    SM00454. SAM. 1 hit.
    SM00234. START. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF48350. SSF48350. 1 hit.
    PROSITEiPS50238. RHOGAP. 1 hit.
    PS50848. START. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 2 (identifier: Q96QB1-2) [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

    MSVAIRKRSW EEHVTHWMGQ PFNSDDRNTA CHHGLVADSL QASMEKDATL     50
    NVDRKEKCVS LPDCCHGSEL RDFPGRPMGH LSKDVDENDS HEGEDQFLSL 100
    EASTETLVHV SDEDNNADLC LTDDKQVLNT QGQKTSGQHM IQGAGSLEKA 150
    LPIIQSNQVS SNSWGIAGET ELALVKESGE RKVTDSISKS LELCNEISLS 200
    EIKDAPKVNA VDTLNVKDIA PEKQLLNSAV IAQQRRKPDP PKDENERSTC 250
    NVVQNEFLDT PCTNRGLPLL KTDFGSCLLQ PPSCPNGMSA ENGLEKSGFS 300
    QHQNKSPPKV KAEDGMQCLQ LKETLATQEP TDNQVRLRKR KEIREDRDRA 350
    RLDSMVLLIM KLDQLDQDIE NALSTSSSPS GTPTNLRRHV PDLESGSESG 400
    ADTISVNQTR VNLSSDTEST DLPSSTPVAN SGTKPKTTAI QGISEKEKAE 450
    IEAKEACDWL RATGFPQYAQ LYEDFLFPID ISLVKREHDF LDRDAIEALC 500
    RRLNTLNKCA VMKLEISPHR KRSDDSDEDE PCAISGKWTF QRDSKRWSRL 550
    EEFDVFSPKQ DLVPGSPDDS HPKDGPSPGG TLMDLSERQE VSSVRSLSST 600
    GSLPSHAPPS EDAATPRTNS VISVCSSSNL AGNDDSFGSL PSPKELSSFS 650
    FSMKGHEKTA KSKTRSLLKR MESLKLKSSH HSKHKAPSKL GLIISGPILQ 700
    EGMDEEKLKQ LNCVEISALN GNRINVPMVR KRSVSNSTQT SSSSSQSETS 750
    SAVSTPSPVT RTRSLSACNK RVGMYLEGFD PFNQSTFNNV VEQNFKNRES 800
    YPEDTVFYIP EDHKPGTFPK ALTNGSFSPS GNNGSVNWRT GSFHGPGHIS 850
    LRRENSSDSP KELKRRNSSS SMSSRLSIYD NVPGSILYSS SGDLADLENE 900
    DIFPELDDIL YHVKGMQRIV NQWSEKFSDE GDSDSALDSV SPCPSSPKQI 950
    HLDVDNDRTT PSDLDSTGNS LNEPEEPSEI PERRDSGVGA SLTRSNRHRL 1000
    RWHSFQSSHR PSLNSVSLQI NCQSVAQMNL LQKYSLLKLT ALLEKYTPSN 1050
    KHGFSWAVPK FMKRIKVPDY KDRSVFGVPL TVNVQRTGQP LPQSIQQAMR 1100
    YLRNHCLDQV GLFRKSGVKS RIQALRQMNE GAIDCVNYEG QSAYDVADML 1150
    KQYFRDLPEP LMTNKLSETF LQIYQYVPKD QRLQAIKAAI MLLPDENREV 1200
    LQTLLYFLSD VTAAVKENQM TPTNLAVCLA PSLFHLNTLK RENSSPRVMQ 1250
    RKQSLGKPDQ KDLNENLAAT QGLAHMIAEC KKLFQVPEEM SRCRNSYTEQ 1300
    ELKPLTLEAL GHLGNDDSAD YQHFLQDCVD GLFKEVKEKF KGWVSYSTSE 1350
    QAELSYKKVS EGPPLRLWRS VIEVPAVPEE ILKRLLKEQH LWDVDLLDSK 1400
    VIEILDSQTE IYQYVQNSMA PHPARDYVVL RTWRTNLPKG ACALLLTSVD 1450
    HDRAPVVGVR VNVLLSRYLI EPCGPGKSKL TYMCRVDLRG HMPEWYTKSF 1500
    GHLCAAEVVK IRDSFSNQNT ETKDTKSR 1528
    Length:1,528
    Mass (Da):170,591
    Last modified:November 30, 2010 - v4
    Checksum:i5D20F29CC606302E
    GO
    Isoform 1 (identifier: Q96QB1-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-437: Missing.
         438-450: TAIQGISEKEKAE → MCRKKPDTMILTQ

    Show »
    Length:1,091
    Mass (Da):122,827
    Checksum:i422B9D58B528E26C
    GO
    Isoform 3 (identifier: Q96QB1-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:498
    Mass (Da):54,552
    Checksum:iAA2A500A52492F1F
    GO
    Isoform 4 (identifier: Q96QB1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-437: Missing.
         438-511: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,017
    Mass (Da):114,152
    Checksum:iA001B182EDE65398
    GO
    Isoform 5 (identifier: Q96QB1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         450-463: EIEAKEACDWLRAT → GKLTFWFCFLANLF
         464-1528: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:463
    Mass (Da):50,890
    Checksum:i299AF4E12B29EEB1
    GO
    Isoform 6 (identifier: Q96QB1-6) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,125
    Mass (Da):126,746
    Checksum:iA93D84FF40E9B92A
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431S → C in BAB14996. (PubMed:14702039)Curated
    Sequence conflicti130 – 1301T → I in BAB14996. (PubMed:14702039)Curated
    Sequence conflicti571 – 5711H → L in BAB21814. (PubMed:11214970)Curated
    Sequence conflicti1114 – 11141R → K in AAB87700. (PubMed:9605766)Curated
    Sequence conflicti1364 – 13641P → R in AAB87700. (PubMed:9605766)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 271R → C.
    Corresponds to variant rs34575560 [ dbSNP | Ensembl ].
    VAR_059293
    Natural varianti81 – 811L → V.
    Corresponds to variant rs3816748 [ dbSNP | Ensembl ].
    VAR_059294
    Natural varianti254 – 2541Q → H.2 Publications
    Corresponds to variant rs11203495 [ dbSNP | Ensembl ].
    VAR_059295
    Natural varianti255 – 2551N → D.3 Publications
    Corresponds to variant rs11203494 [ dbSNP | Ensembl ].
    VAR_059296
    Natural varianti260 – 2601T → I.2 Publications
    Corresponds to variant rs3816747 [ dbSNP | Ensembl ].
    VAR_059297
    Natural varianti320 – 3201Q → H.
    Corresponds to variant rs34591797 [ dbSNP | Ensembl ].
    VAR_059298
    Natural varianti712 – 7121N → S.2 Publications
    Corresponds to variant rs1044092 [ dbSNP | Ensembl ].
    VAR_014229
    Natural varianti791 – 7911V → M.5 Publications
    Corresponds to variant rs532841 [ dbSNP | Ensembl ].
    VAR_014230
    Natural varianti959 – 9591T → A.1 Publication
    VAR_014231
    Natural varianti998 – 9981H → Q.1 Publication
    Corresponds to variant rs149295187 [ dbSNP | Ensembl ].
    VAR_014232
    Natural varianti1025 – 10251V → A.1 Publication
    VAR_014233
    Natural varianti1199 – 11991E → V.2 Publications
    Corresponds to variant rs1044093 [ dbSNP | Ensembl ].
    VAR_014234
    Natural varianti1209 – 12091S → C.2 Publications
    Corresponds to variant rs1044094 [ dbSNP | Ensembl ].
    VAR_014235

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 437437Missing in isoform 1 and isoform 4. 3 PublicationsVSP_037871Add
    BLAST
    Alternative sequencei1 – 4545MSVAI…QASME → MGDPKAHVMARPLRAPLRRS FSDHIRDSTARALDVIWKNT RDRRL in isoform 6. 1 PublicationVSP_053836Add
    BLAST
    Alternative sequencei46 – 448403Missing in isoform 6. 1 PublicationVSP_053837Add
    BLAST
    Alternative sequencei438 – 51174Missing in isoform 4. 1 PublicationVSP_044651Add
    BLAST
    Alternative sequencei438 – 45013TAIQG…KEKAE → MCRKKPDTMILTQ in isoform 1. 2 PublicationsVSP_037872Add
    BLAST
    Alternative sequencei450 – 49849EIEAK…DAIEA → AVKSVKLEVDEDKSTKGSNF SNSEVAIGLSPYTFPQKRLF HVAGEENIT in isoform 3. 1 PublicationVSP_037873Add
    BLAST
    Alternative sequencei450 – 46314EIEAK…WLRAT → GKLTFWFCFLANLF in isoform 5. 1 PublicationVSP_046331Add
    BLAST
    Alternative sequencei464 – 15281065Missing in isoform 5. 1 PublicationVSP_046332Add
    BLAST
    Alternative sequencei499 – 15281030Missing in isoform 3. 1 PublicationVSP_037874Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035119 mRNA. Translation: AAB87700.1.
    AF026219 mRNA. Translation: AAB81637.1. Different initiation.
    AF408781
    , 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.
    CCDSiCCDS55201.1. [Q96QB1-4]
    CCDS5989.1. [Q96QB1-2]
    CCDS5990.1. [Q96QB1-1]
    CCDS5991.2. [Q96QB1-5]
    RefSeqiNP_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]
    UniGeneiHs.134296.

    Genome annotation databases

    EnsembliENST00000276297; ENSP00000276297; ENSG00000164741. [Q96QB1-2]
    ENST00000316609; ENSP00000321034; ENSG00000164741. [Q96QB1-3]
    ENST00000358919; ENSP00000351797; ENSG00000164741. [Q96QB1-1]
    ENST00000511869; ENSP00000425878; ENSG00000164741. [Q96QB1-5]
    ENST00000512044; ENSP00000422595; ENSG00000164741. [Q96QB1-6]
    ENST00000520226; ENSP00000428028; ENSG00000164741. [Q96QB1-4]
    GeneIDi10395.
    KEGGihsa:10395.
    UCSCiuc003wwk.1. human. [Q96QB1-1]
    uc003wwm.2. human. [Q96QB1-2]
    uc003wwn.3. human. [Q96QB1-3]

    Polymorphism databases

    DMDMi313104315.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035119 mRNA. Translation: AAB87700.1 .
    AF026219 mRNA. Translation: AAB81637.1 . Different initiation.
    AF408781
    , 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 .
    CCDSi CCDS55201.1. [Q96QB1-4 ]
    CCDS5989.1. [Q96QB1-2 ]
    CCDS5990.1. [Q96QB1-1 ]
    CCDS5991.2. [Q96QB1-5 ]
    RefSeqi NP_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 ]
    UniGenei Hs.134296.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DKY NMR - A 451-515 [» ]
    2GYT NMR - A 451-513 [» ]
    2KAP NMR - A 454-513 [» ]
    2LOZ NMR - B 811-824 [» ]
    3KUQ X-ray 2.30 A 1074-1283 [» ]
    ProteinModelPortali Q96QB1.
    SMRi Q96QB1. Positions 454-513, 1070-1279, 1324-1515.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115667. 11 interactions.
    DIPi DIP-56928N.
    IntActi Q96QB1. 3 interactions.
    MINTi MINT-6942866.
    STRINGi 9606.ENSP00000276297.

    PTM databases

    PhosphoSitei Q96QB1.

    Polymorphism databases

    DMDMi 313104315.

    Proteomic databases

    MaxQBi Q96QB1.
    PaxDbi Q96QB1.
    PRIDEi Q96QB1.

    Protocols and materials databases

    DNASUi 10395.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000276297 ; ENSP00000276297 ; ENSG00000164741 . [Q96QB1-2 ]
    ENST00000316609 ; ENSP00000321034 ; ENSG00000164741 . [Q96QB1-3 ]
    ENST00000358919 ; ENSP00000351797 ; ENSG00000164741 . [Q96QB1-1 ]
    ENST00000511869 ; ENSP00000425878 ; ENSG00000164741 . [Q96QB1-5 ]
    ENST00000512044 ; ENSP00000422595 ; ENSG00000164741 . [Q96QB1-6 ]
    ENST00000520226 ; ENSP00000428028 ; ENSG00000164741 . [Q96QB1-4 ]
    GeneIDi 10395.
    KEGGi hsa:10395.
    UCSCi uc003wwk.1. human. [Q96QB1-1 ]
    uc003wwm.2. human. [Q96QB1-2 ]
    uc003wwn.3. human. [Q96QB1-3 ]

    Organism-specific databases

    CTDi 10395.
    GeneCardsi GC08M012940.
    HGNCi HGNC:2897. DLC1.
    HPAi HPA017753.
    MIMi 604258. gene.
    neXtProti NX_Q96QB1.
    PharmGKBi PA27351.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236923.
    HOGENOMi HOG000039960.
    HOVERGENi HBG055955.
    OMAi HDRAPVA.
    OrthoDBi EOG7CG6Z8.
    PhylomeDBi Q96QB1.
    TreeFami TF314044.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.

    Miscellaneous databases

    ChiTaRSi DLC1. human.
    EvolutionaryTracei Q96QB1.
    GeneWikii DLC1.
    GenomeRNAii 10395.
    NextBioi 35481526.
    PROi Q96QB1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96QB1.
    Bgeei Q96QB1.
    CleanExi HS_DLC1.
    Genevestigatori Q96QB1.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    3.30.530.20. 1 hit.
    InterProi IPR028854. 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 ]
    PANTHERi PTHR12659:SF2. PTHR12659:SF2. 1 hit.
    Pfami PF00620. RhoGAP. 1 hit.
    PF07647. SAM_2. 1 hit.
    PF01852. START. 1 hit.
    [Graphical view ]
    SMARTi SM00324. RhoGAP. 1 hit.
    SM00454. SAM. 1 hit.
    SM00234. START. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF48350. SSF48350. 1 hit.
    PROSITEi PS50238. RHOGAP. 1 hit.
    PS50848. START. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. Cited for: VARIANTS SER-712; MET-791; ALA-959; GLN-998; ALA-1025; VAL-1199 AND CYS-1209.

    Entry informationi

    Entry nameiRHG07_HUMAN
    AccessioniPrimary (citable) accession number: Q96QB1
    Secondary accession number(s): B4DR10
    , B8PTI0, E9PDZ8, E9PF76, E9PGY9, O14868, O43199, Q7Z5R8, Q86UC6, Q9C0E0, Q9H7A2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2002
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 127 of the entry and version 4 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 8
      Human chromosome 8: 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