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Protein

Rho GTPase-activating protein 35

Gene

ARHGAP35

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Rho GTPase-activating protein (GAP), binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity (PubMed:19673492). This binding is inhibited by phosphorylation by PRKCA (PubMed:19673492). Involved in cell differentiation as well as cell adhesion and migration, plays an important role in retinal tissue morphogenesis, neural tube fusion, midline fusion of the cerebral hemispheres and mammary gland branching morphogenesis (By similarity). Transduces signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP) (By similarity). Transduces SRC-dependent signal from cell-surface adhesion molecules, such as laminin, to promote neurite outgrowth. Regulates axon outgrowth, guidance and fasciculation (By similarity). Modulates Rho GTPase-dependent F-actin polymerization, organization and assembly, is involved in polarized cell migration and in the positive regulation of ciliogenesis and cilia elongation (By similarity). During mammary gland development, is required in both the epithelial and stromal compartments for ductal outgrowth (By similarity). Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this function is however unclear and would need additional experimental evidences (PubMed:1894621).By similarity2 Publications

Enzyme regulationi

Binding of acidic phospholipids inhibits the Rho GAP activity and promote the Rac GAP activity.1 Publication

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • GTPase activator activity Source: UniProtKB
  • GTP binding Source: InterPro
  • phospholipid binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: NTNU_SB
  • transcription corepressor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160007-MONOMER.
ReactomeiR-HSA-194840. Rho GTPase cycle.
R-HSA-416550. Sema4D mediated inhibition of cell attachment and migration.
R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLinkiQ9NRY4.
SIGNORiQ9NRY4.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 35Imported
Alternative name(s):
Glucocorticoid receptor DNA-binding factor 1
Glucocorticoid receptor repression factor 1
Short name:
GRF-1
Rho GAP p190A
Short name:
p190-A
Gene namesi
Name:ARHGAP35Imported
Synonyms:GRF11 Publication, GRLF11 Publication, KIAA1722, P190A1 Publication, p190ARHOGAP1 Publication
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:4591. ARHGAP35.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcytoskeletoncilium basal body By similarity
  • Cell membrane By similarity
  • Nucleus 1 Publication

  • Note: In response to integrins and SDC4 and upon phosphorylation by PKC, relocalizes from the cytoplasm to regions of plasma membrane ruffling where it colocalizes with polymerized actin.By similarity

GO - Cellular componenti

  • actin cytoskeleton Source: Ensembl
  • ciliary basal body Source: UniProtKB
  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1221S → A: No effect on total phosphorylation levels. Abolishes inhibition of phospholipid binding by PRKCA phosphorylation. Decreases phosphorylation by PRKCA; when associated with A-1226. Abolishes phosphorylation by PRKCA; when associated with A-1126 and A-1236. 1 Publication1
Mutagenesisi1221S → D: Enhances Rac GAP activity. 1 Publication1
Mutagenesisi1226T → A: No effect on total phosphorylation levels. Abolishes inhibition of phospholipid binding by PRKCA phosphorylation. Decreases phosphorylation by PRKCA; when associated with A-1221. Abolishes phosphorylation by PRKCA; when associated with A-1121 and A-1236. 1 Publication1
Mutagenesisi1226T → D: Enhances Rac GAP activity. 1 Publication1
Mutagenesisi1236S → A: No effect on total phosphorylation levels. No effect on inhibition of phospholipid binding by PRKCA phosphorylation. Abolishes phosphorylation by PRKCA; when associated with A-1121 and A-1226. 1 Publication1

Organism-specific databases

DisGeNETi2909.
OpenTargetsiENSG00000160007.
PharmGKBiPA28988.

Polymorphism and mutation databases

BioMutaiARHGAP35.
DMDMi408360250.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000567301 – 1499Rho GTPase-activating protein 35Add BLAST1499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei308Phosphotyrosine1 Publication1
Modified residuei589PhosphoserineCombined sources1
Modified residuei770PhosphoserineCombined sources1
Modified residuei773PhosphoserineCombined sources1
Modified residuei970PhosphoserineCombined sources1
Modified residuei975PhosphoserineCombined sources1
Modified residuei985PhosphoserineBy similarity1
Modified residuei1001PhosphoserineCombined sources1
Modified residuei1072PhosphoserineCombined sources1
Modified residuei1087PhosphotyrosineCombined sources1
Modified residuei1105Phosphotyrosine; by ABL2 and PTK6Combined sources1 Publication1
Modified residuei1134PhosphoserineCombined sources1
Modified residuei1142PhosphoserineBy similarity1
Modified residuei1150PhosphoserineCombined sources1
Modified residuei1176PhosphoserineCombined sources1
Modified residuei1179PhosphoserineCombined sources1
Modified residuei1221Phosphoserine; by PKC/PRKCA1 Publication1
Modified residuei1226Phosphothreonine; by PKC/PRKCA1 Publication1
Modified residuei1236Phosphoserine; by PKC/PRKCA1 Publication1
Modified residuei1472PhosphoserineBy similarity1
Modified residuei1476PhosphoserineBy similarity1
Modified residuei1480PhosphothreonineBy similarity1
Modified residuei1483PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation of Tyr-1105 by PTK6 promotes the association with RASA1, inactivating RHOA while activating RAS. Phosphorylation at Tyr-308 by PDGFRA inhibits binding to GTF2I (PubMed:18829532, PubMed:19393245). Phosphorylated by PRKCA at Ser-1221 and Thr-1226, induces relocalization from the cytoplasm to regions of plasma membrane ruffling and prevents the binding and substrate specificity regulation by phospholipids (PubMed:19673492). In brain, phosphorylated by FYN and SRC (By similarity). During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483. Phosphorylation by MAPK1 and MAPK3 inhibits GAP function and localizes ARGHAP35 away from newly forming focal adhesions and stress fibers in cells spreading on fibronectin (By similarity). Phosphorylation at Ser-1476 and Thr-1480 by GSK3B requires priming by MAPK and inhibits RhoGAP activity and modulates polarized cell migration (By similarity).By similarity3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NRY4.
PaxDbiQ9NRY4.
PeptideAtlasiQ9NRY4.
PRIDEiQ9NRY4.

PTM databases

iPTMnetiQ9NRY4.
PhosphoSitePlusiQ9NRY4.

Expressioni

Tissue specificityi

Detected in neutrophils (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000160007.
CleanExiHS_GRLF1.
ExpressionAtlasiQ9NRY4. baseline and differential.
GenevisibleiQ9NRY4. HS.

Organism-specific databases

HPAiCAB037311.
HPA055184.
HPA056470.

Interactioni

Subunit structurei

Interacts with RASA1. Interacts with the general transcription factor GTF2I, the interaction sequesters GTF2I in the cytoplasm.1 Publication

Protein-protein interaction databases

BioGridi109166. 13 interactors.
DIPiDIP-34578N.
IntActiQ9NRY4. 2 interactors.
STRINGi9606.ENSP00000385720.

Structurei

Secondary structure

11499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 21Combined sources8
Turni25 – 30Combined sources6
Helixi35 – 43Combined sources9
Turni47 – 49Combined sources3
Helixi60 – 63Combined sources4
Turni66 – 70Combined sources5
Beta strandi72 – 79Combined sources8
Beta strandi91 – 96Combined sources6
Turni102 – 104Combined sources3
Helixi110 – 112Combined sources3
Helixi116 – 120Combined sources5
Beta strandi123 – 126Combined sources4
Helixi136 – 138Combined sources3
Helixi142 – 144Combined sources3
Helixi151 – 153Combined sources3
Beta strandi154 – 156Combined sources3
Beta strandi159 – 165Combined sources7
Helixi174 – 190Combined sources17
Beta strandi195 – 200Combined sources6
Helixi202 – 204Combined sources3
Helixi207 – 218Combined sources12
Beta strandi220 – 222Combined sources3
Beta strandi225 – 227Combined sources3
Turni230 – 233Combined sources4
Helixi236 – 248Combined sources13
Turni268 – 271Combined sources4
Helixi272 – 284Combined sources13
Beta strandi286 – 288Combined sources3
Helixi292 – 299Combined sources8
Helixi303 – 311Combined sources9
Helixi314 – 330Combined sources17
Helixi1251 – 1254Combined sources4
Beta strandi1257 – 1259Combined sources3
Helixi1263 – 1275Combined sources13
Turni1280 – 1284Combined sources5
Helixi1289 – 1301Combined sources13
Helixi1308 – 1310Combined sources3
Helixi1314 – 1327Combined sources14
Beta strandi1328 – 1330Combined sources3
Helixi1335 – 1344Combined sources10
Helixi1350 – 1362Combined sources13
Helixi1366 – 1383Combined sources18
Helixi1386 – 1389Combined sources4
Helixi1393 – 1405Combined sources13
Beta strandi1409 – 1412Combined sources4
Helixi1414 – 1430Combined sources17
Helixi1432 – 1436Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K85NMR-A267-331[»]
3C5HX-ray1.80A13-249[»]
3FK2X-ray2.80A/B/C/D1212-1439[»]
ProteinModelPortaliQ9NRY4.
SMRiQ9NRY4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NRY4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini270 – 327FF 1Add BLAST58
Domaini368 – 422FF 2Add BLAST55
Domaini429 – 483FF 3Add BLAST55
Domaini485 – 550FF 4Add BLAST66
Domaini1249 – 1436Rho-GAPPROSITE-ProRule annotationAdd BLAST188

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 266Has GTPase activity, required for proper localizationBy similarityAdd BLAST266
Regioni1213 – 1236Required for phospholipid binding and regulation of the substrate preference1 PublicationAdd BLAST24

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1440 – 1490Pro-richAdd BLAST51

Domaini

N-terminal part (1-266) has GTPase activity. Required for proper cellular localization.By similarity

Sequence similaritiesi

Contains 4 FF domains.Curated
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4271. Eukaryota.
ENOG410XR4E. LUCA.
GeneTreeiENSGT00760000118863.
HOVERGENiHBG051844.
InParanoidiQ9NRY4.
KOiK05732.
OMAiPITEPPG.
OrthoDBiEOG091G00ZO.
TreeFamiTF324451.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR032835. RhoGAP-FF1.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
PF16512. RhoGAP-FF1. 1 hit.
[Graphical view]
SMARTiSM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEiPS51676. FF. 4 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NRY4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF
60 70 80 90 100
HLDHTSVLST SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI
110 120 130 140 150
DDQTFQPHRS TALQPYIKRA AATKLASAEK LMYFCTDQLG LEQDFEQKQM
160 170 180 190 200
PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF VSNLYNQLAK TKKPIVVVLT
210 220 230 240 250
KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF STLVQLIDKS
260 270 280 290 300
RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWLSVSRKMQ
310 320 330 340 350
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA
360 370 380 390 400
LIPNLDEIDH LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE
410 420 430 440 450
RIPFDLMDTV PAEQLYEAHL EKLRNERKRV EMRRAFKENL ETSPFITPGK
460 470 480 490 500
PWEEARSFIM NEDFYQWLEE SVYMDIYGKH QKQIIDKAKE EFQELLLEYS
510 520 530 540 550
ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER DALILKHIHF
560 570 580 590 600
VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDPNIDRINL
610 620 630 640 650
VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS
660 670 680 690 700
FQTPTFQPHG CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL
710 720 730 740 750
ILVNKRGDTS GETLHSLIQQ GQQIASKLQC VFLDPASAGI GYGRNINEKQ
760 770 780 790 800
ISQVLKGLLD SKRNLNLVSS TASIKDLADV DLRIVMCLMC GDPFSADDIL
810 820 830 840 850
FPVLQSQTCK SSHCGSNNSV LLELPIGLHK KRIELSVLSY HSSFSIRKSR
860 870 880 890 900
LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAVDVLDNDL
910 920 930 940 950
SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LEIFHPFFKD VVEKKNIIEA
960 970 980 990 1000
THMYDNAAEA CSTTEEVFNS PRAGSPLCNS NLQDSEEDIE PSYSLFREDT
1010 1020 1030 1040 1050
SLPSLSKDHS KLSMELEGND GLSFIMSNFE SKLNNKVPPP VKPKPPVHFE
1060 1070 1080 1090 1100
ITKGDLSYLD QGHRDGQRKS VSSSPWLPQD GFDPSDYAEP MDAVVKPRNE
1110 1120 1130 1140 1150
EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT SSLERGRKVS
1160 1170 1180 1190 1200
IVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG
1210 1220 1230 1240 1250
DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP
1260 1270 1280 1290 1300
LTTVVTPEKP IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD
1310 1320 1330 1340 1350
QDHNLDLAEK DFTVNTVAGA MKSFFSELPD PLVPYNMQID LVEAHKINDR
1360 1370 1380 1390 1400
EQKLHALKEV LKKFPKENHE VFKYVISHLN KVSHNNKVNL MTSENLSICF
1410 1420 1430 1440 1450
WPTLMRPDFS TMDALTATRT YQTIIELFIQ QCPFFFYNRP ITEPPGARPS
1460 1470 1480 1490
SPSAVASTVP FLTSTPVTSQ PSPPQSPPPT PQSPMQPLLP SQLQAEHTL
Length:1,499
Mass (Da):170,514
Last modified:October 3, 2012 - v3
Checksum:i8CCB493414A7E3E6
GO

Sequence cautioni

The sequence AAA58618 differs from that shown. Reason: Frameshift at positions 389, 533, 540, 607, 614, 1167, 1241, 1292, 1334 and 1446.Curated
The sequence AAF80386 differs from that shown. Unlikely isoform. Aberrant splice sites.Curated
The sequence AAF80386 differs from that shown. Reason: Frameshift at positions 533, 540, 607 and 614.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti251R → P in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti309V → D in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti362S → G in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti414Q → A in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti414Q → A in AAA58618 (PubMed:1894621).Curated1
Sequence conflicti474M → T in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti474M → T in AAA58618 (PubMed:1894621).Curated1
Sequence conflicti978C → S in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti1292M → I in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti1452 – 1453PS → RN in AAA58618 (PubMed:1894621).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051509 mRNA. Translation: BAB21813.2.
CH471126 Genomic DNA. Translation: EAW57450.1.
BC150257 mRNA. Translation: AAI50258.1.
AF159851 mRNA. Translation: AAF80386.1. Sequence problems.
M73077 mRNA. Translation: AAA58618.1. Frameshift.
CCDSiCCDS46127.1.
RefSeqiNP_004482.4. NM_004491.4.
XP_016882203.1. XM_017026714.1.
UniGeneiHs.509447.

Genome annotation databases

EnsembliENST00000404338; ENSP00000385720; ENSG00000160007.
ENST00000614079; ENSP00000483730; ENSG00000160007.
GeneIDi2909.
KEGGihsa:2909.
UCSCiuc010ekv.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051509 mRNA. Translation: BAB21813.2.
CH471126 Genomic DNA. Translation: EAW57450.1.
BC150257 mRNA. Translation: AAI50258.1.
AF159851 mRNA. Translation: AAF80386.1. Sequence problems.
M73077 mRNA. Translation: AAA58618.1. Frameshift.
CCDSiCCDS46127.1.
RefSeqiNP_004482.4. NM_004491.4.
XP_016882203.1. XM_017026714.1.
UniGeneiHs.509447.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K85NMR-A267-331[»]
3C5HX-ray1.80A13-249[»]
3FK2X-ray2.80A/B/C/D1212-1439[»]
ProteinModelPortaliQ9NRY4.
SMRiQ9NRY4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109166. 13 interactors.
DIPiDIP-34578N.
IntActiQ9NRY4. 2 interactors.
STRINGi9606.ENSP00000385720.

PTM databases

iPTMnetiQ9NRY4.
PhosphoSitePlusiQ9NRY4.

Polymorphism and mutation databases

BioMutaiARHGAP35.
DMDMi408360250.

Proteomic databases

EPDiQ9NRY4.
PaxDbiQ9NRY4.
PeptideAtlasiQ9NRY4.
PRIDEiQ9NRY4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000404338; ENSP00000385720; ENSG00000160007.
ENST00000614079; ENSP00000483730; ENSG00000160007.
GeneIDi2909.
KEGGihsa:2909.
UCSCiuc010ekv.4. human.

Organism-specific databases

CTDi2909.
DisGeNETi2909.
GeneCardsiARHGAP35.
H-InvDBHIX0015264.
HGNCiHGNC:4591. ARHGAP35.
HPAiCAB037311.
HPA055184.
HPA056470.
MIMi605277. gene.
neXtProtiNX_Q9NRY4.
OpenTargetsiENSG00000160007.
PharmGKBiPA28988.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4271. Eukaryota.
ENOG410XR4E. LUCA.
GeneTreeiENSGT00760000118863.
HOVERGENiHBG051844.
InParanoidiQ9NRY4.
KOiK05732.
OMAiPITEPPG.
OrthoDBiEOG091G00ZO.
TreeFamiTF324451.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160007-MONOMER.
ReactomeiR-HSA-194840. Rho GTPase cycle.
R-HSA-416550. Sema4D mediated inhibition of cell attachment and migration.
R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLinkiQ9NRY4.
SIGNORiQ9NRY4.

Miscellaneous databases

ChiTaRSiARHGAP35. human.
EvolutionaryTraceiQ9NRY4.
GeneWikiiGRLF1.
GenomeRNAii2909.
PROiQ9NRY4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000160007.
CleanExiHS_GRLF1.
ExpressionAtlasiQ9NRY4. baseline and differential.
GenevisibleiQ9NRY4. HS.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR032835. RhoGAP-FF1.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
PF16512. RhoGAP-FF1. 1 hit.
[Graphical view]
SMARTiSM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEiPS51676. FF. 4 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRHG35_HUMAN
AccessioniPrimary (citable) accession number: Q9NRY4
Secondary accession number(s): A7E2A4, Q14452, Q9C0E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: October 3, 2012
Last modified: November 30, 2016
This is version 166 of the entry and version 3 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.