UniProtKB - Q9NRY4 (RHG35_HUMAN)

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History
Entry version 181 (20 Jun 2018)
Sequence version 3 (03 Oct 2012)
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Protein

Rho GTPase-activating protein 35

Gene

ARHGAP35

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Rho GTPase-activating protein (GAP) (PubMed:19673492, PubMed:28894085). 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 signals 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 similarity3 Publications

Enzyme regulationⁱ

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	28	GTPCombined sources1 Publication	1
Binding siteⁱ	52	GTP; via carbonyl oxygenCombined sources1 Publication	1
Binding siteⁱ	56	GTPCombined sources1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	33 – 37	GTPCombined sources1 Publication	5
Nucleotide bindingⁱ	95 – 97	GTPCombined sources1 Publication	3
Nucleotide bindingⁱ	201 – 203	GTPCombined sources1 Publication	3
Nucleotide bindingⁱ	229 – 231	GTPCombined sources1 Publication	3

GO - Molecular functionⁱ

DNA binding
Source: ProtInc
Traceable author statementⁱ
- 1894621
GTPase activator activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19673492
GTPase activity Source: InterPro
GTP binding Source: UniProtKB-KW
phospholipid binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19673492
RNA polymerase II regulatory region sequence-specific DNA binding
Source: NTNU_SB
Inferred from direct assayⁱ
- 1894621
transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding
Source: NTNU_SB
Inferred from direct assayⁱ
- 1894621
transcription corepressor activity
Source: ProtInc
Traceable author statementⁱ
- 1894621

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

axonal fasciculation Source: UniProtKB
axon guidance Source: UniProtKB
camera-type eye development Source: Ensembl
cell migration Source: UniProtKB
cellular response to extracellular stimulus Source: UniProtKB
central nervous system neuron axonogenesis Source: UniProtKB
establishment or maintenance of actin cytoskeleton polarity Source: UniProtKB
forebrain development Source: Ensembl
mammary gland development Source: UniProtKB
negative regulation of Rho protein signal transduction Source: Ensembl
negative regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 1894621
negative regulation of transcription by RNA polymerase II
Source: NTNU_SB
Inferred from direct assayⁱ
- 1894621
negative regulation of vascular permeability Source: Ensembl
neural tube closure Source: Ensembl
neuron projection guidance Source: UniProtKB
positive regulation of cilium assembly Source: UniProtKB
positive regulation of neuron projection development Source: UniProtKB
regulation of actin cytoskeleton organization Source: UniProtKB
regulation of actin polymerization or depolymerization Source: UniProtKB
regulation of axonogenesis Source: UniProtKB
regulation of cell shape Source: Ensembl
regulation of small GTPase mediated signal transduction Source: Reactome
signal transduction Source: InterPro
transcription, DNA-templated
Source: ProtInc
Traceable author statementⁱ
- 1894621
wound healing, spreading of cells Source: UniProtKB

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, GTPase activation, Repressor
Biological process	Transcription, Transcription regulation
Ligand	GTP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

Reactomeⁱ	R-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
SignaLinkⁱ	Q9NRY4
SIGNORⁱ	Q9NRY4

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-A1 Publication
Gene namesⁱ	Name:ARHGAP35Imported Synonyms:GRF11 Publication, GRLF11 Publication, KIAA1722, P190A1 Publication, p190ARHOGAP1 Publication
Organismⁱ	Homo sapiens (Human)Imported
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 19

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000160007.17
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4591 ARHGAP35
MIMⁱ	605277 gene
neXtProtⁱ	NX_Q9NRY4

Keywords - Cellular componentⁱ

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

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	1221	S → 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 Publication	1
Mutagenesisⁱ	1221	S → D: Enhances Rac GAP activity. 1 Publication	1
Mutagenesisⁱ	1226	T → 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 Publication	1
Mutagenesisⁱ	1226	T → D: Enhances Rac GAP activity. 1 Publication	1
Mutagenesisⁱ	1236	S → 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 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2909
Open Targets More...OpenTargetsⁱ	ENSG00000160007
PharmGKBⁱ	PA28988

Polymorphism and mutation databases

BioMutaⁱ	ARHGAP35
DMDMⁱ	408360250

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000056730	1 – 1499	Rho GTPase-activating protein 35Add BLAST		1499

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	308	Phosphotyrosine1 Publication	1
Modified residueⁱ	589	PhosphoserineCombined sources	1
Modified residueⁱ	770	PhosphoserineCombined sources	1
Modified residueⁱ	773	PhosphoserineCombined sources	1
Modified residueⁱ	970	PhosphoserineCombined sources	1
Modified residueⁱ	975	PhosphoserineCombined sources	1
Modified residueⁱ	985	PhosphoserineBy similarity	1
Modified residueⁱ	1001	PhosphoserineCombined sources	1
Modified residueⁱ	1072	PhosphoserineCombined sources	1
Modified residueⁱ	1087	PhosphotyrosineCombined sources	1
Modified residueⁱ	1105	Phosphotyrosine; by ABL2 and PTK6Combined sources1 Publication	1
Modified residueⁱ	1134	PhosphoserineCombined sources	1
Modified residueⁱ	1142	PhosphoserineBy similarity	1
Modified residueⁱ	1150	PhosphoserineCombined sources	1
Modified residueⁱ	1176	PhosphoserineCombined sources	1
Modified residueⁱ	1179	PhosphoserineCombined sources	1
Modified residueⁱ	1221	Phosphoserine; by PKC/PRKCA1 Publication	1
Modified residueⁱ	1226	Phosphothreonine; by PKC/PRKCA1 Publication	1
Modified residueⁱ	1236	Phosphoserine; by PKC/PRKCA1 Publication	1
Modified residueⁱ	1472	PhosphoserineBy similarity	1
Modified residueⁱ	1476	PhosphoserineBy similarity	1
Modified residueⁱ	1480	PhosphothreonineBy similarity	1
Modified residueⁱ	1483	PhosphoserineBy similarity	1

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

EPDⁱ	Q9NRY4
PaxDbⁱ	Q9NRY4
PeptideAtlas More...PeptideAtlasⁱ	Q9NRY4
PRIDEⁱ	Q9NRY4
ProteomicsDBⁱ	82441

PTM databases

iPTMnetⁱ	Q9NRY4
PhosphoSitePlusⁱ	Q9NRY4

Expressionⁱ

Tissue specificityⁱ

Detected in neutrophils (at protein level).1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000160007
CleanExⁱ	HS_GRLF1
Genevisibleⁱ	Q9NRY4 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB037311 HPA055184 HPA056470

HPAⁱ

CAB037311
HPA055184
HPA056470

Interactionⁱ

Subunit structureⁱ

Interacts with RASA1 (By similarity). Interacts with the general transcription factor GTF2I, the interaction sequesters GTF2I in the cytoplasm (PubMed:19393245).By similarity1 Publication

Protein-protein interaction databases

BioGridⁱ	109166, 13 interactors
Database of interacting proteins More...DIPⁱ	DIP-34578N
IntActⁱ	Q9NRY4, 4 interactors
Molecular INTeraction database More...MINTⁱ	Q9NRY4
STRINGⁱ	9606.ENSP00000385720

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	14 – 21	Combined sources	8
Turnⁱ	25 – 30	Combined sources	6
Helixⁱ	35 – 43	Combined sources	9
Turnⁱ	47 – 49	Combined sources	3
Helixⁱ	60 – 63	Combined sources	4
Turnⁱ	66 – 70	Combined sources	5
Beta strandⁱ	72 – 79	Combined sources	8
Beta strandⁱ	91 – 96	Combined sources	6
Turnⁱ	102 – 104	Combined sources	3
Helixⁱ	110 – 112	Combined sources	3
Helixⁱ	116 – 120	Combined sources	5
Beta strandⁱ	123 – 126	Combined sources	4
Helixⁱ	136 – 138	Combined sources	3
Helixⁱ	142 – 144	Combined sources	3
Helixⁱ	151 – 153	Combined sources	3
Beta strandⁱ	154 – 156	Combined sources	3
Beta strandⁱ	159 – 165	Combined sources	7
Helixⁱ	174 – 190	Combined sources	17
Beta strandⁱ	195 – 200	Combined sources	6
Helixⁱ	202 – 204	Combined sources	3
Helixⁱ	207 – 218	Combined sources	12
Beta strandⁱ	220 – 222	Combined sources	3
Beta strandⁱ	225 – 227	Combined sources	3
Turnⁱ	230 – 233	Combined sources	4
Helixⁱ	236 – 248	Combined sources	13
Turnⁱ	268 – 271	Combined sources	4
Helixⁱ	272 – 284	Combined sources	13
Beta strandⁱ	286 – 288	Combined sources	3
Helixⁱ	292 – 299	Combined sources	8
Helixⁱ	303 – 311	Combined sources	9
Helixⁱ	314 – 330	Combined sources	17
Helixⁱ	1251 – 1254	Combined sources	4
Beta strandⁱ	1257 – 1259	Combined sources	3
Helixⁱ	1263 – 1275	Combined sources	13
Turnⁱ	1280 – 1284	Combined sources	5
Helixⁱ	1289 – 1301	Combined sources	13
Helixⁱ	1308 – 1310	Combined sources	3
Helixⁱ	1314 – 1327	Combined sources	14
Beta strandⁱ	1328 – 1330	Combined sources	3
Helixⁱ	1335 – 1344	Combined sources	10
Helixⁱ	1350 – 1362	Combined sources	13
Helixⁱ	1366 – 1383	Combined sources	18
Helixⁱ	1386 – 1389	Combined sources	4
Helixⁱ	1393 – 1405	Combined sources	13
Beta strandⁱ	1409 – 1412	Combined sources	4
Helixⁱ	1414 – 1430	Combined sources	17
Helixⁱ	1432 – 1436	Combined sources	5

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2K85	NMR	-	A	267-331	[»]
	3C5H	X-ray	1.80	A	13-249	[»]
	3FK2	X-ray	2.80	A/B/C/D	1212-1439	[»]
ProteinModelPortalⁱ	Q9NRY4
SMRⁱ	Q9NRY4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9NRY4

EvolutionaryTraceⁱ

Q9NRY4

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	270 – 327	FF 1Add BLAST	58
Domainⁱ	368 – 422	FF 2Add BLAST	55
Domainⁱ	429 – 483	FF 3Add BLAST	55
Domainⁱ	485 – 550	FF 4Add BLAST	66
Domainⁱ	592 – 767	pG1 pseudoGTPasePROSITE-ProRule annotationAdd BLAST	176
Domainⁱ	783 – 947	pG2 pseudoGTPasePROSITE-ProRule annotationAdd BLAST	165
Domainⁱ	1249 – 1436	Rho-GAPPROSITE-ProRule annotationAdd BLAST	188

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	1 – 266	Has GTPase activity, required for proper localizationBy similarityAdd BLAST		266
Regionⁱ	1213 – 1236	Required for phospholipid binding and regulation of the substrate preference1 PublicationAdd BLAST		24

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	1440 – 1490	Pro-richAdd BLAST		51

Domainⁱ

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

The pG1 pseudoGTPase domain does not bind GTP.1 Publication

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG4271 Eukaryota ENOG410XR4E LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00920000148997
HOVERGENⁱ	HBG051844
InParanoidⁱ	Q9NRY4
KEGG Orthology (KO) More...KOⁱ	K05732
OMAⁱ	MLRAFLC
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G00ZO
TreeFamⁱ	TF324451

Family and domain databases

Gene3Dⁱ	1.10.10.440, 2 hits 1.10.555.10, 1 hit
InterProⁱ	View protein in InterPro IPR002713 FF_domain IPR036517 FF_domain_sf IPR027417 P-loop_NTPase IPR039007 pG1 IPR008936 Rho_GTPase_activation_prot IPR032835 RhoGAP-FF1 IPR000198 RhoGAP_dom IPR039006 RhoGAP_pG2 IPR001806 Small_GTPase
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01846 FF, 1 hit PF00071 Ras, 1 hit PF00620 RhoGAP, 1 hit PF16512 RhoGAP-FF1, 1 hit
SMARTⁱ	View protein in SMART SM00441 FF, 4 hits SM00324 RhoGAP, 1 hit
SUPFAMⁱ	SSF48350 SSF48350, 1 hit SSF52540 SSF52540, 2 hits SSF81698 SSF81698, 1 hit
PROSITEⁱ	View protein in PROSITE PS51676 FF, 4 hits PS51852 PG1, 1 hit PS51853 PG2, 1 hit PS50238 RHOGAP, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q9NRY4-1 [UniParc]FASTA Add 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

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 key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	251	R → P in AAF80386 (PubMed:11054565).Curated	1
Sequence conflictⁱ	309	V → D in AAF80386 (PubMed:11054565).Curated	1
Sequence conflictⁱ	362	S → G in AAF80386 (PubMed:11054565).Curated	1
Sequence conflictⁱ	414	Q → A in AAF80386 (PubMed:11054565).Curated	1
Sequence conflictⁱ	414	Q → A in AAA58618 (PubMed:1894621).Curated	1
Sequence conflictⁱ	474	M → T in AAF80386 (PubMed:11054565).Curated	1
Sequence conflictⁱ	474	M → T in AAA58618 (PubMed:1894621).Curated	1
Sequence conflictⁱ	978	C → S in AAF80386 (PubMed:11054565).Curated	1
Sequence conflictⁱ	1292	M → I in AAF80386 (PubMed:11054565).Curated	1
Sequence conflictⁱ	1452 – 1453	PS → RN in AAA58618 (PubMed:1894621).Curated	2

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.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS46127.1
NCBI Reference Sequences More...RefSeqⁱ	NP_004482.4, NM_004491.4 XP_016882203.1, XM_017026714.1
UniGeneⁱ	Hs.509447

Genome annotation databases

Ensemblⁱ	ENST00000404338; ENSP00000385720; ENSG00000160007 ENST00000614079; ENSP00000483730; ENSG00000160007
GeneIDⁱ	2909
KEGGⁱ	hsa:2909
UCSC genome browser More...UCSCⁱ	uc010ekv.4 human

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
Q9NRY4	Rho GTPase-activating protein 35		MOUSE		1499
Rho GTPase activating protein 35		PANTR		1519
Rho GTPase activating protein 35		SAIBB		1514
Uncharacterized protein		MACMU		1513
Uncharacterized protein		MACFA		1513
+147

Protein	Similar proteins		Species	Score	Length
Q9NRY4	Rho GTPase-activating protein 35		MOUSE		1499
Rho GTPase activating protein 35		PANTR		1519
Rho GTPase activating protein 35		SAIBB		1514
Uncharacterized protein		MACMU		1513
Uncharacterized protein		MACFA		1513
+231

Structural Biology Knowledgebase	Search...

CTDⁱ	2909
DisGeNET More...DisGeNETⁱ	2909
EuPathDBⁱ	HostDB:ENSG00000160007.17
GeneCardsⁱ	ARHGAP35
H-InvDBⁱ	HIX0015264
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4591 ARHGAP35
Human Protein Atlas More...HPAⁱ	CAB037311 HPA055184 HPA056470
MIMⁱ	605277 gene
neXtProtⁱ	NX_Q9NRY4
Open Targets More...OpenTargetsⁱ	ENSG00000160007
PharmGKBⁱ	PA28988
HUGEⁱ	Search...
GenAtlas: human gene database More...GenAtlasⁱ	Search...

ChiTaRSⁱ	ARHGAP35 human
EvolutionaryTraceⁱ	Q9NRY4
GeneWikiⁱ	GRLF1
GenomeRNAiⁱ	2909
Protein Ontology More...PROⁱ	PR:Q9NRY4
SOURCEⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RHG35_HUMAN
Accessionⁱ	Q9NRY4Primary (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:	June 20, 2018
	This is version 181 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

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UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9NRY4 (RHG35_HUMAN)

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Rho GTPase-activating protein 35

ARHGAP35

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoskeleton

Plasma membrane

Nucleus

Other locations

Cytoskeleton

Cytosol

Nucleus

Plasma Membrane

Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Compositional bias

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

Enzyme regulationⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ