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Q96QB1

- RHG07_HUMAN

UniProt

Q96QB1 - RHG07_HUMAN

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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

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. Rho GTPase activator activity Source: UniProtKB
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ96QB1.
CleanExiHS_DLC1.
ExpressionAtlasiQ96QB1. baseline and differential.
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.
GeneTreeiENSGT00760000119123.
HOGENOMiHOG000039960.
HOVERGENiHBG055955.
InParanoidiQ96QB1.
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

        10         20         30         40         50
MSVAIRKRSW EEHVTHWMGQ PFNSDDRNTA CHHGLVADSL QASMEKDATL
60 70 80 90 100
NVDRKEKCVS LPDCCHGSEL RDFPGRPMGH LSKDVDENDS HEGEDQFLSL
110 120 130 140 150
EASTETLVHV SDEDNNADLC LTDDKQVLNT QGQKTSGQHM IQGAGSLEKA
160 170 180 190 200
LPIIQSNQVS SNSWGIAGET ELALVKESGE RKVTDSISKS LELCNEISLS
210 220 230 240 250
EIKDAPKVNA VDTLNVKDIA PEKQLLNSAV IAQQRRKPDP PKDENERSTC
260 270 280 290 300
NVVQNEFLDT PCTNRGLPLL KTDFGSCLLQ PPSCPNGMSA ENGLEKSGFS
310 320 330 340 350
QHQNKSPPKV KAEDGMQCLQ LKETLATQEP TDNQVRLRKR KEIREDRDRA
360 370 380 390 400
RLDSMVLLIM KLDQLDQDIE NALSTSSSPS GTPTNLRRHV PDLESGSESG
410 420 430 440 450
ADTISVNQTR VNLSSDTEST DLPSSTPVAN SGTKPKTTAI QGISEKEKAE
460 470 480 490 500
IEAKEACDWL RATGFPQYAQ LYEDFLFPID ISLVKREHDF LDRDAIEALC
510 520 530 540 550
RRLNTLNKCA VMKLEISPHR KRSDDSDEDE PCAISGKWTF QRDSKRWSRL
560 570 580 590 600
EEFDVFSPKQ DLVPGSPDDS HPKDGPSPGG TLMDLSERQE VSSVRSLSST
610 620 630 640 650
GSLPSHAPPS EDAATPRTNS VISVCSSSNL AGNDDSFGSL PSPKELSSFS
660 670 680 690 700
FSMKGHEKTA KSKTRSLLKR MESLKLKSSH HSKHKAPSKL GLIISGPILQ
710 720 730 740 750
EGMDEEKLKQ LNCVEISALN GNRINVPMVR KRSVSNSTQT SSSSSQSETS
760 770 780 790 800
SAVSTPSPVT RTRSLSACNK RVGMYLEGFD PFNQSTFNNV VEQNFKNRES
810 820 830 840 850
YPEDTVFYIP EDHKPGTFPK ALTNGSFSPS GNNGSVNWRT GSFHGPGHIS
860 870 880 890 900
LRRENSSDSP KELKRRNSSS SMSSRLSIYD NVPGSILYSS SGDLADLENE
910 920 930 940 950
DIFPELDDIL YHVKGMQRIV NQWSEKFSDE GDSDSALDSV SPCPSSPKQI
960 970 980 990 1000
HLDVDNDRTT PSDLDSTGNS LNEPEEPSEI PERRDSGVGA SLTRSNRHRL
1010 1020 1030 1040 1050
RWHSFQSSHR PSLNSVSLQI NCQSVAQMNL LQKYSLLKLT ALLEKYTPSN
1060 1070 1080 1090 1100
KHGFSWAVPK FMKRIKVPDY KDRSVFGVPL TVNVQRTGQP LPQSIQQAMR
1110 1120 1130 1140 1150
YLRNHCLDQV GLFRKSGVKS RIQALRQMNE GAIDCVNYEG QSAYDVADML
1160 1170 1180 1190 1200
KQYFRDLPEP LMTNKLSETF LQIYQYVPKD QRLQAIKAAI MLLPDENREV
1210 1220 1230 1240 1250
LQTLLYFLSD VTAAVKENQM TPTNLAVCLA PSLFHLNTLK RENSSPRVMQ
1260 1270 1280 1290 1300
RKQSLGKPDQ KDLNENLAAT QGLAHMIAEC KKLFQVPEEM SRCRNSYTEQ
1310 1320 1330 1340 1350
ELKPLTLEAL GHLGNDDSAD YQHFLQDCVD GLFKEVKEKF KGWVSYSTSE
1360 1370 1380 1390 1400
QAELSYKKVS EGPPLRLWRS VIEVPAVPEE ILKRLLKEQH LWDVDLLDSK
1410 1420 1430 1440 1450
VIEILDSQTE IYQYVQNSMA PHPARDYVVL RTWRTNLPKG ACALLLTSVD
1460 1470 1480 1490 1500
HDRAPVVGVR VNVLLSRYLI EPCGPGKSKL TYMCRVDLRG HMPEWYTKSF
1510 1520
GHLCAAEVVK IRDSFSNQNT ETKDTKSR
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.
GeneTreei ENSGT00760000119123.
HOGENOMi HOG000039960.
HOVERGENi HBG055955.
InParanoidi Q96QB1.
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

Bgeei Q96QB1.
CleanExi HS_DLC1.
ExpressionAtlasi Q96QB1. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 128 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