Q96QB1 (RHG07_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DLC1
Synonyms:	ARHGAP7, KIAA1723, STARD12

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1528 AA.
Sequence status	Complete.
Protein existence	Evidence 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.8 Ref.9 Ref.10
Subunit structure	Interacts with EF1A1, facilitates EF1A1 distribution to the membrane periphery and ruffles upon growth factor stimulation and suppresses cell migration. Ref.13
Subcellular location	Cytoplasm. Cell junction › focal adhesion. Membrane; Peripheral membrane protein. Note: Colocalizes with EF1A1 at actin-rich regions in the cell periphery. Ref.8 Ref.9 Ref.13
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.8 The polybasic cluster is required for activation and mediates binding to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) containing membranes. Ref.8
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 component	Cell junction Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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 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 induction of apoptosis Inferred from direct assay PubMed 17292327PubMed 17888903. 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 protein dephosphorylation Inferred from direct assay PubMed 17292327. Source: UniProtKB regulation of cell shape Inferred from mutant phenotype PubMed 17292327. Source: UniProtKB small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular_component	caveola Inferred from direct assay PubMed 16951145. 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_function	Rho GTPase activator activity Inferred from direct assay PubMed 17932950. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1528

1528

Rho GTPase-activating protein 7

PRO_0000056707

Regions

Domain

448 – 515

68

SAM

Domain

1078 – 1284

207

Rho-GAP

Domain

1314 – 1521

208

START

Region

710 – 884

175

Focal adhesion-targeting (FAT)

Region

1051 – 1073

23

Polybasic cluster (PBR)

Compositional bias

741 – 747

7

Poly-Ser

Compositional bias

868 – 874

7

Poly-Ser

Amino acid modifications

Modified residue

523

1

Phosphoserine By similarity

Modified residue

526

1

Phosphoserine By similarity

Modified residue

741

1

Phosphoserine By similarity

Modified residue

742

1

Phosphoserine By similarity

Modified residue

747

1

Phosphoserine By similarity

Modified residue

749

1

Phosphothreonine By similarity

Modified residue

750

1

Phosphoserine By similarity

Modified residue

754

1

Phosphoserine By similarity

Modified residue

755

1

Phosphothreonine By similarity

Modified residue

850

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 437

437

Missing in isoform 1 and isoform 4.

VSP_037871

Alternative sequence

438 – 511

74

Missing in isoform 4.

VSP_044651

Alternative sequence

438 – 450

13

TAIQG…KEKAE → MCRKKPDTMILTQ in isoform 1.

VSP_037872

Alternative sequence

450 – 498

49

EIEAK…DAIEA → AVKSVKLEVDEDKSTKGSNF SNSEVAIGLSPYTFPQKRLF HVAGEENIT in isoform 3.

VSP_037873

Alternative sequence

450 – 463

14

EIEAK…WLRAT → GKLTFWFCFLANLF in isoform 5.

VSP_046331

Alternative sequence

464 – 1528

1065

Missing in isoform 5.

VSP_046332

Alternative sequence

499 – 1528

1030

Missing in isoform 3.

VSP_037874

Natural variant

27

1

R → C.
Corresponds to variant rs34575560 [ dbSNP | Ensembl ].

VAR_059293

Natural variant

81

1

L → V.
Corresponds to variant rs3816748 [ dbSNP | Ensembl ].

VAR_059294

Natural variant

254

1

Q → H. Ref.4 Ref.5
Corresponds to variant rs11203495 [ dbSNP | Ensembl ].

VAR_059295

Natural variant

255

1

N → D. Ref.4 Ref.5 Ref.7
Corresponds to variant rs11203494 [ dbSNP | Ensembl ].

VAR_059296

Natural variant

260

1

T → I. Ref.4 Ref.5
Corresponds to variant rs3816747 [ dbSNP | Ensembl ].

VAR_059297

Natural variant

320

1

Q → H.
Corresponds to variant rs34591797 [ dbSNP | Ensembl ].

VAR_059298

Natural variant

712

1

N → S. Ref.1 Ref.14
Corresponds to variant rs1044092 [ dbSNP | Ensembl ].

VAR_014229

Natural variant

791

1

V → M. Ref.2 Ref.3 Ref.4 Ref.5 Ref.14
Corresponds to variant rs532841 [ dbSNP | Ensembl ].

VAR_014230

Natural variant

959

1

T → A. Ref.14

VAR_014231

Natural variant

998

1

H → Q. Ref.14

VAR_014232

Natural variant

1025

1

V → A. Ref.14

VAR_014233

Natural variant

1199

1

E → V. Ref.1 Ref.14
Corresponds to variant rs1044093 [ dbSNP | Ensembl ].

VAR_014234

Natural variant

1209

1

S → C. Ref.1 Ref.14
Corresponds to variant rs1044094 [ dbSNP | Ensembl ].

VAR_014235

Experimental info

Mutagenesis

475

1

F → G: Abolishes interaction with EF1A1. Ref.13

Mutagenesis

476

1

L → G: Abolishes interaction with EF1A1. Ref.13

Mutagenesis

879

1

Y → F: Unable to displace endogenous DLC1 from focal adhesions. Ref.8

Mutagenesis

1114

1

R → E: No catalytic activity. Ref.13

Sequence conflict

43

1

S → C in BAB14996. Ref.5

Sequence conflict

130

1

T → I in BAB14996. Ref.5

Sequence conflict

571

1

H → L in BAB21814. Ref.4

Sequence conflict

1114

1

R → K in AAB87700. Ref.1

Sequence conflict

1364

1

P → R in AAB87700. Ref.1

Secondary structure

1

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1528

Helix Strand Turn

Details...

Helix

451 – 463

13

Helix

468 – 473

6

Turn

474 – 476

3

Helix

481 – 487

7

Turn

488 – 490

3

Helix

493 – 509

17

Turn

510 – 514

5

Helix

1080 – 1087

8

Beta strand

1088 – 1091

4

Helix

1093 – 1105

13

Turn

1110 – 1114

5

Helix

1119 – 1129

11

Beta strand

1131 – 1134

4

Helix

1143 – 1156

14

Beta strand

1157 – 1159

3

Helix

1166 – 1176

11

Helix

1179 – 1181

3

Helix

1182 – 1191

10

Helix

1195 – 1213

19

Helix

1215 – 1218

4

Helix

1222 – 1234

13

Helix

1260 – 1278

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified November 30, 2010. Version 4. Checksum: 5D20F29CC606302E	FASTA	1,528	170,591
	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
	Isoform 1 [UniParc]. Checksum: 422B9D58B528E26C	FASTA	1,091	122,827
	10 20 30 40 50 60 MCRKKPDTMI LTQIEAKEAC DWLRATGFPQ YAQLYEDFLF PIDISLVKRE HDFLDRDAIE 70 80 90 100 110 120 ALCRRLNTLN KCAVMKLEIS PHRKRSDDSD EDEPCAISGK WTFQRDSKRW SRLEEFDVFS 130 140 150 160 170 180 PKQDLVPGSP DDSHPKDGPS PGGTLMDLSE RQEVSSVRSL SSTGSLPSHA PPSEDAATPR 190 200 210 220 230 240 TNSVISVCSS SNLAGNDDSF GSLPSPKELS SFSFSMKGHE KTAKSKTRSL LKRMESLKLK 250 260 270 280 290 300 SSHHSKHKAP SKLGLIISGP ILQEGMDEEK LKQLNCVEIS ALNGNRINVP MVRKRSVSNS 310 320 330 340 350 360 TQTSSSSSQS ETSSAVSTPS PVTRTRSLSA CNKRVGMYLE GFDPFNQSTF NNVVEQNFKN 370 380 390 400 410 420 RESYPEDTVF YIPEDHKPGT FPKALTNGSF SPSGNNGSVN WRTGSFHGPG HISLRRENSS 430 440 450 460 470 480 DSPKELKRRN SSSSMSSRLS IYDNVPGSIL YSSSGDLADL ENEDIFPELD DILYHVKGMQ 490 500 510 520 530 540 RIVNQWSEKF SDEGDSDSAL DSVSPCPSSP KQIHLDVDND RTTPSDLDST GNSLNEPEEP 550 560 570 580 590 600 SEIPERRDSG VGASLTRSNR HRLRWHSFQS SHRPSLNSVS LQINCQSVAQ MNLLQKYSLL 610 620 630 640 650 660 KLTALLEKYT PSNKHGFSWA VPKFMKRIKV PDYKDRSVFG VPLTVNVQRT GQPLPQSIQQ 670 680 690 700 710 720 AMRYLRNHCL DQVGLFRKSG VKSRIQALRQ MNEGAIDCVN YEGQSAYDVA DMLKQYFRDL 730 740 750 760 770 780 PEPLMTNKLS ETFLQIYQYV PKDQRLQAIK AAIMLLPDEN REVLQTLLYF LSDVTAAVKE 790 800 810 820 830 840 NQMTPTNLAV CLAPSLFHLN TLKRENSSPR VMQRKQSLGK PDQKDLNENL AATQGLAHMI 850 860 870 880 890 900 AECKKLFQVP EEMSRCRNSY TEQELKPLTL EALGHLGNDD SADYQHFLQD CVDGLFKEVK 910 920 930 940 950 960 EKFKGWVSYS TSEQAELSYK KVSEGPPLRL WRSVIEVPAV PEEILKRLLK EQHLWDVDLL 970 980 990 1000 1010 1020 DSKVIEILDS QTEIYQYVQN SMAPHPARDY VVLRTWRTNL PKGACALLLT SVDHDRAPVV 1030 1040 1050 1060 1070 1080 GVRVNVLLSR YLIEPCGPGK SKLTYMCRVD LRGHMPEWYT KSFGHLCAAE VVKIRDSFSN 1090 QNTETKDTKS R
	Isoform 3 [UniParc]. Checksum: AA2A500A52492F1F	FASTA	498	54,552
	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 QGISEKEKAA VKSVKLEVDE DKSTKGSNFS NSEVAIGLSP 490 YTFPQKRLFH VAGEENIT
	Isoform 4 [UniParc]. Checksum: A001B182EDE65398	FASTA	1,017	114,152
	10 20 30 40 50 60 MKLEISPHRK RSDDSDEDEP CAISGKWTFQ RDSKRWSRLE EFDVFSPKQD LVPGSPDDSH 70 80 90 100 110 120 PKDGPSPGGT LMDLSERQEV SSVRSLSSTG SLPSHAPPSE DAATPRTNSV ISVCSSSNLA 130 140 150 160 170 180 GNDDSFGSLP SPKELSSFSF SMKGHEKTAK SKTRSLLKRM ESLKLKSSHH SKHKAPSKLG 190 200 210 220 230 240 LIISGPILQE GMDEEKLKQL NCVEISALNG NRINVPMVRK RSVSNSTQTS SSSSQSETSS 250 260 270 280 290 300 AVSTPSPVTR TRSLSACNKR VGMYLEGFDP FNQSTFNNVV EQNFKNRESY PEDTVFYIPE 310 320 330 340 350 360 DHKPGTFPKA LTNGSFSPSG NNGSVNWRTG SFHGPGHISL RRENSSDSPK ELKRRNSSSS 370 380 390 400 410 420 MSSRLSIYDN VPGSILYSSS GDLADLENED IFPELDDILY HVKGMQRIVN QWSEKFSDEG 430 440 450 460 470 480 DSDSALDSVS PCPSSPKQIH LDVDNDRTTP SDLDSTGNSL NEPEEPSEIP ERRDSGVGAS 490 500 510 520 530 540 LTRSNRHRLR WHSFQSSHRP SLNSVSLQIN CQSVAQMNLL QKYSLLKLTA LLEKYTPSNK 550 560 570 580 590 600 HGFSWAVPKF MKRIKVPDYK DRSVFGVPLT VNVQRTGQPL PQSIQQAMRY LRNHCLDQVG 610 620 630 640 650 660 LFRKSGVKSR IQALRQMNEG AIDCVNYEGQ SAYDVADMLK QYFRDLPEPL MTNKLSETFL 670 680 690 700 710 720 QIYQYVPKDQ RLQAIKAAIM LLPDENREVL QTLLYFLSDV TAAVKENQMT PTNLAVCLAP 730 740 750 760 770 780 SLFHLNTLKR ENSSPRVMQR KQSLGKPDQK DLNENLAATQ GLAHMIAECK KLFQVPEEMS 790 800 810 820 830 840 RCRNSYTEQE LKPLTLEALG HLGNDDSADY QHFLQDCVDG LFKEVKEKFK GWVSYSTSEQ 850 860 870 880 890 900 AELSYKKVSE GPPLRLWRSV IEVPAVPEEI LKRLLKEQHL WDVDLLDSKV IEILDSQTEI 910 920 930 940 950 960 YQYVQNSMAP HPARDYVVLR TWRTNLPKGA CALLLTSVDH DRAPVVGVRV NVLLSRYLIE 970 980 990 1000 1010 PCGPGKSKLT YMCRVDLRGH MPEWYTKSFG HLCAAEVVKI RDSFSNQNTE TKDTKSR
	Isoform 5 [UniParc]. Checksum: 299AF4E12B29EEB1	FASTA	463	50,890
	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 DLPSSTPVAN SGTKPKTTAI QGISEKEKAG KLTFWFCFLA NLF

References

	« Hide 'large scale' referencesShow '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. , 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]	"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, SAM DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-879.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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 , 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.

IPI

IPI00015556.
IPI00335259.
IPI00374033.
IPI00796273.
IPI00979269.

RefSeq

NP_001157743.1. NM_001164271.1.
NP_006085.2. NM_006094.4.
NP_079043.3. NM_024767.3.
NP_872584.2. NM_182643.2.

UniGene

Hs.134296.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q96QB1.

SMR

Q96QB1. Positions 454-513, 1070-1279, 1324-1515.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96QB1. 2 interactions.

STRING

9606.ENSP00000276297.

PTM databases

PhosphoSite

Q96QB1.

Polymorphism databases

DMDM

257051065.

Proteomic databases

PaxDb

Q96QB1.

PRIDE

Q96QB1.

Protocols and materials databases

DNASU

10395.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000276297; ENSP00000276297; ENSG00000164741.
ENST00000316609; ENSP00000321034; ENSG00000164741.
ENST00000358919; ENSP00000351797; ENSG00000164741.
ENST00000511869; ENSP00000425878; ENSG00000164741.
ENST00000520226; ENSP00000428028; ENSG00000164741.

GeneID

10395.

KEGG

hsa:10395.

UCSC

uc003wwk.1. human.
uc003wwm.2. human.
uc003wwn.3. human.

Organism-specific databases

CTD

10395.

GeneCards

GC08M012940.

HGNC

HGNC:2897. DLC1.

HPA

HPA017753.

MIM

604258. gene.

neXtProt

NX_Q96QB1.

PharmGKB

PA27351.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG236923.

HOGENOM

HOG000039960.

HOVERGEN

HBG055955.

OMA

PRVMQRK.

OrthoDB

EOG4P2Q1D.

PhylomeDB

Q96QB1.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q96QB1.

Bgee

Q96QB1.

CleanEx

HS_DLC1.

Genevestigator

Q96QB1.

GermOnline

ENSG00000164741. Homo sapiens.

Family and domain databases

Gene3D

1.10.555.10. 1 hit.
3.30.530.20. 1 hit.

InterPro

IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001660. SAM.
IPR011510. SAM_2.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]

Pfam

PF00620. RhoGAP. 1 hit.
PF07647. SAM_2. 1 hit.
PF01852. START. 1 hit.
[Graphical view]

SMART

SM00324. RhoGAP. 1 hit.
SM00454. SAM. 1 hit.
SM00234. START. 1 hit.
[Graphical view]

SUPFAM

SSF48350. Rho_GAP. 1 hit.

PROSITE

PS50238. RHOGAP. 1 hit.
PS50105. SAM_DOMAIN. False negative.
PS50848. START. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DLC1. human.

EvolutionaryTrace

Q96QB1.

GenomeRNAi

10395.

NextBio

39382.

SOURCE

Search...

Entry information

Entry name

RHG07_HUMAN

Accession

Primary (citable) accession number: Q96QB1
Secondary accession number(s): B4DR10 , 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:	May 1, 2013
This is version 112 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.