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Protein

Rho GTPase-activating protein 15

Gene

ARHGAP15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction.1 Publication

GO - Molecular functioni

  • GTPase activator activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 15
Alternative name(s):
ArhGAP15
Rho-type GTPase-activating protein 15
Gene namesi
ORF Names:BM-024, BM-030, BM-046
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:21030. ARHGAP15.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134938065.

Polymorphism and mutation databases

BioMutaiARHGAP15.
DMDMi166977704.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475Rho GTPase-activating protein 15PRO_0000317574Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineCombined sources
Modified residuei103 – 1031PhosphoserineCombined sources
Modified residuei196 – 1961PhosphoserineBy similarity
Modified residuei199 – 1991PhosphoserineBy similarity
Modified residuei243 – 2431PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ53QZ3.
MaxQBiQ53QZ3.
PaxDbiQ53QZ3.
PeptideAtlasiQ53QZ3.
PRIDEiQ53QZ3.

PTM databases

iPTMnetiQ53QZ3.
PhosphoSiteiQ53QZ3.

Expressioni

Tissue specificityi

Expressed in lung, liver and lymphoid cells.1 Publication

Gene expression databases

BgeeiQ53QZ3.
ExpressionAtlasiQ53QZ3. baseline and differential.
GenevisibleiQ53QZ3. HS.

Organism-specific databases

HPAiHPA032125.

Interactioni

Protein-protein interaction databases

BioGridi120945. 7 interactions.
IntActiQ53QZ3. 2 interactions.
MINTiMINT-261797.
STRINGi9606.ENSP00000295095.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi265 – 2706Combined sources
Helixi283 – 2908Combined sources
Helixi296 – 30813Combined sources
Turni309 – 3113Combined sources
Turni313 – 3175Combined sources
Helixi322 – 33312Combined sources
Helixi343 – 3453Combined sources
Helixi348 – 36114Combined sources
Beta strandi362 – 3643Combined sources
Helixi369 – 37911Combined sources
Beta strandi381 – 3833Combined sources
Helixi384 – 39714Combined sources
Helixi400 – 41819Combined sources
Helixi420 – 4234Combined sources
Helixi427 – 43913Combined sources
Beta strandi444 – 4463Combined sources
Helixi448 – 46417Combined sources
Helixi466 – 4705Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BYIX-ray2.25A/B/C/D262-473[»]
ProteinModelPortaliQ53QZ3.
SMRiQ53QZ3. Positions 80-191, 262-471.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53QZ3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 189111PHPROSITE-ProRule annotationAdd
BLAST
Domaini281 – 470190Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Domaini

The PH domain is required for localization to the membrane.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1449. Eukaryota.
KOG1450. Eukaryota.
ENOG410ZP6T. LUCA.
GeneTreeiENSGT00840000129684.
HOVERGENiHBG005328.
InParanoidiQ53QZ3.
OMAiQDNATRI.
PhylomeDBiQ53QZ3.
TreeFamiTF329345.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR015767. Rho_GTPase_act.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PANTHERiPTHR23181. PTHR23181. 1 hit.
PfamiPF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q53QZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKSTNSDTS VETLNSTRQG TGAVQMRIKN ANSHHDRLSQ SKSMILTDVG
60 70 80 90 100
KVTEPISRHR RNHSQHILKD VIPPLEQLMV EKEGYLQKAK IADGGKKLRK
110 120 130 140 150
NWSTSWIVLS SRRIEFYKES KQQALSNMKT GHKPESVDLC GAHIEWAKEK
160 170 180 190 200
SSRKNVFQIT TVSGNEFLLQ SDIDFIILDW FHAIKNAIDR LPKDSSCPSR
210 220 230 240 250
NLELFKIQRS SSTELLSHYD SDIKEQKPEH RKSLMFRLHH SASDTSDKNR
260 270 280 290 300
VKSRLKKFIT RRPSLKTLQE KGLIKDQIFG SHLHKVCERE NSTVPWFVKQ
310 320 330 340 350
CIEAVEKRGL DVDGIYRVSG NLATIQKLRF IVNQEEKLNL DDSQWEDIHV
360 370 380 390 400
VTGALKMFFR ELPEPLFPYS FFEQFVEAIK KQDNNTRIEA VKSLVQKLPP
410 420 430 440 450
PNRDTMKVLF GHLTKIVAKA SKNLMSTQSL GIVFGPTLLR AENETGNMAI
460 470
HMVYQNQIAE LMLSEYSKIF GSEED
Length:475
Mass (Da):54,544
Last modified:February 5, 2008 - v2
Checksum:i35C26B1960694119
GO

Sequence cautioni

The sequence AAF67618.1 differs from that shown. Reason: Frameshift at positions 140, 185, 195, 202, 260, 265, 268, 311, 316, 323 and 332. Curated
The sequence AAF67633.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAF87324.1 differs from that shown. Reason: Frameshift at positions 202, 233, 255, 259, 265, 268, 311, 314, 316, 320, 322, 326, 332, 338, 340 and 418. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2601T → P in AAF67618 (PubMed:11042152).Curated
Sequence conflicti261 – 2611R → P in AAF87324 (PubMed:11042152).Curated
Sequence conflicti314 – 3141G → A in AAO34684 (PubMed:12650940).Curated
Sequence conflicti323 – 3231A → G in AAF67618 (PubMed:11042152).Curated
Sequence conflicti323 – 3231A → Q in AAO34684 (PubMed:12650940).Curated
Sequence conflicti409 – 4091L → P in AAH16701 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY219338 mRNA. Translation: AAO34684.1.
AF212222 mRNA. Translation: AAF87324.1. Frameshift.
AF217507 mRNA. Translation: AAF67618.1. Frameshift.
AF217522 mRNA. Translation: AAF67633.1. Frameshift.
AC013437 Genomic DNA. Translation: AAX93160.1.
AC079584 Genomic DNA. Translation: AAX82009.1.
AC079793 Genomic DNA. Translation: AAY24215.1.
AC092652 Genomic DNA. Translation: AAY14811.1.
AC096558 Genomic DNA. Translation: AAX93158.1.
AC098857 Genomic DNA. Translation: AAX93245.1.
CH471058 Genomic DNA. Translation: EAX11590.1.
BC016701 mRNA. Translation: AAH16701.1.
BC038976 mRNA. Translation: AAH38976.2.
CCDSiCCDS2184.1.
RefSeqiNP_060930.3. NM_018460.3.
XP_011509781.1. XM_011511479.1.
UniGeneiHs.171011.

Genome annotation databases

EnsembliENST00000295095; ENSP00000295095; ENSG00000075884.
GeneIDi55843.
KEGGihsa:55843.
UCSCiuc002tvm.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY219338 mRNA. Translation: AAO34684.1.
AF212222 mRNA. Translation: AAF87324.1. Frameshift.
AF217507 mRNA. Translation: AAF67618.1. Frameshift.
AF217522 mRNA. Translation: AAF67633.1. Frameshift.
AC013437 Genomic DNA. Translation: AAX93160.1.
AC079584 Genomic DNA. Translation: AAX82009.1.
AC079793 Genomic DNA. Translation: AAY24215.1.
AC092652 Genomic DNA. Translation: AAY14811.1.
AC096558 Genomic DNA. Translation: AAX93158.1.
AC098857 Genomic DNA. Translation: AAX93245.1.
CH471058 Genomic DNA. Translation: EAX11590.1.
BC016701 mRNA. Translation: AAH16701.1.
BC038976 mRNA. Translation: AAH38976.2.
CCDSiCCDS2184.1.
RefSeqiNP_060930.3. NM_018460.3.
XP_011509781.1. XM_011511479.1.
UniGeneiHs.171011.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BYIX-ray2.25A/B/C/D262-473[»]
ProteinModelPortaliQ53QZ3.
SMRiQ53QZ3. Positions 80-191, 262-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120945. 7 interactions.
IntActiQ53QZ3. 2 interactions.
MINTiMINT-261797.
STRINGi9606.ENSP00000295095.

PTM databases

iPTMnetiQ53QZ3.
PhosphoSiteiQ53QZ3.

Polymorphism and mutation databases

BioMutaiARHGAP15.
DMDMi166977704.

Proteomic databases

EPDiQ53QZ3.
MaxQBiQ53QZ3.
PaxDbiQ53QZ3.
PeptideAtlasiQ53QZ3.
PRIDEiQ53QZ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295095; ENSP00000295095; ENSG00000075884.
GeneIDi55843.
KEGGihsa:55843.
UCSCiuc002tvm.5. human.

Organism-specific databases

CTDi55843.
GeneCardsiARHGAP15.
HGNCiHGNC:21030. ARHGAP15.
HPAiHPA032125.
MIMi610578. gene.
neXtProtiNX_Q53QZ3.
PharmGKBiPA134938065.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1449. Eukaryota.
KOG1450. Eukaryota.
ENOG410ZP6T. LUCA.
GeneTreeiENSGT00840000129684.
HOVERGENiHBG005328.
InParanoidiQ53QZ3.
OMAiQDNATRI.
PhylomeDBiQ53QZ3.
TreeFamiTF329345.

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiARHGAP15. human.
EvolutionaryTraceiQ53QZ3.
GenomeRNAii55843.
NextBioi61081.
PROiQ53QZ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ53QZ3.
ExpressionAtlasiQ53QZ3. baseline and differential.
GenevisibleiQ53QZ3. HS.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR015767. Rho_GTPase_act.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PANTHERiPTHR23181. PTHR23181. 1 hit.
PfamiPF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ArhGAP15, a novel human RacGAP protein with GTPase binding property."
    Seoh M.L., Ng C.H., Yong J., Lim L., Leung T.
    FEBS Lett. 539:131-137(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DOMAIN PH, TISSUE SPECIFICITY.
  2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Bone marrow and Lymph.
  5. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Crystal structure of human Rho GTPase activating protein 15 (ARHGAP15)."
    Structural genomics consortium (SGC)
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 262-473.

Entry informationi

Entry nameiRHG15_HUMAN
AccessioniPrimary (citable) accession number: Q53QZ3
Secondary accession number(s): Q53R36
, Q53RD7, Q53RT6, Q53SX9, Q584N9, Q6PJE6, Q86WP1, Q8IXX1, Q9NRL8, Q9NZ77, Q9NZ91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: May 11, 2016
This is version 100 of the entry and version 2 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 2
    Human chromosome 2: 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.