RHG26_HUMAN
ID RHG26_HUMAN Reviewed; 814 AA.
AC Q9UNA1; O75117; Q5D035; Q9BYS6; Q9BYS7; Q9UJ00;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Rho GTPase-activating protein 26;
DE AltName: Full=GTPase regulator associated with focal adhesion kinase;
DE AltName: Full=Oligophrenin-1-like protein;
DE AltName: Full=Rho-type GTPase-activating protein 26;
GN Name=ARHGAP26; Synonyms=GRAF, KIAA0621, OPHN1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart, Liver, and Placenta;
RA Xia J.H., Tang X.X., Yu K.P., Pan Q., Dai H.P.;
RT "Molecular cloning of human oligophrenin-1 like (OPHN1L) gene, complete
RT CDS.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), DISEASE, AND VARIANT JMML
RP SER-417.
RX PubMed=10908648; DOI=10.1073/pnas.150079597;
RA Borkhardt A., Bojesen S., Haas O.A., Fuchs U., Bartelheimer D.,
RA Loncarevic I.F., Bohle R.M., Harbott J., Repp R., Jaeger U., Viehmann S.,
RA Henn T., Korth P., Scharr D., Lampert F.;
RT "The human GRAF gene is fused to MLL in a unique t(5;11)(q31;q23) and both
RT alleles are disrupted in three cases of myelodysplastic syndrome/acute
RT myeloid leukemia with a deletion 5q.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9168-9173(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-785.
RA Bojesen S.E., Link C., Borkhardt A.;
RT "Genomic structure of the human GRAF gene.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-814 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP STRUCTURE BY NMR OF 754-814.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of human oligophrenin-1-like protein
RT (KIAA0621).";
RL Submitted (DEC-2003) to the PDB data bank.
CC -!- FUNCTION: GTPase-activating protein for RHOA and CDC42.
CC -!- SUBUNIT: Interacts with NYAP1, NYAP2 and MYO16 (By similarity). Binds
CC to the C-terminus of PTK2/FAK1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UNA1; O14613: CDC42EP2; NbExp=3; IntAct=EBI-1390913, EBI-3438291;
CC Q9UNA1; Q6P5Z2: PKN3; NbExp=5; IntAct=EBI-1390913, EBI-1384335;
CC Q9UNA1-2; O14613: CDC42EP2; NbExp=3; IntAct=EBI-16430964, EBI-3438291;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with actin
CC stress fibers and cortical actin structures. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNA1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNA1-2; Sequence=VSP_001659;
CC -!- DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An
CC aggressive pediatric myelodysplastic syndrome/myeloproliferative
CC disorder characterized by malignant transformation in the hematopoietic
CC stem cell compartment with proliferation of differentiated progeny.
CC Patients have splenomegaly, enlarged lymph nodes, rashes, and
CC hemorrhages. Note=The gene represented in this entry is involved in
CC disease pathogenesis. A chromosomal translocation t(5;11)(q31;q23) with
CC KMT2A/MLL1 has been found in leukemic cells from JMML patients, also
CC carrying inactivating mutations on the second allele (PubMed:10908648).
CC {ECO:0000269|PubMed:10908648}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GRAFID291.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Graf1 entry;
CC URL="https://en.wikipedia.org/wiki/Graf1";
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DR EMBL; AF141884; AAD39482.1; -; mRNA.
DR EMBL; Y10388; CAA71414.2; -; Genomic_DNA.
DR EMBL; CH471062; EAW61876.1; -; Genomic_DNA.
DR EMBL; BC068555; AAH68555.1; -; mRNA.
DR EMBL; AJ309466; CAC29145.2; -; Genomic_DNA.
DR EMBL; AJ309467; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309468; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309469; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309470; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309471; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309472; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309473; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309474; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309475; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309476; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309477; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309478; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309479; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309480; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309481; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309482; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309483; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309484; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309485; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309486; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309487; CAC29145.2; JOINED; Genomic_DNA.
DR EMBL; AJ309466; CAC29146.2; -; Genomic_DNA.
DR EMBL; AJ309467; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309468; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309469; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309470; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309471; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309472; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309473; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309474; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309475; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309476; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309477; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309478; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309479; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309480; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309481; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309482; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309483; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309484; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309485; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AJ309487; CAC29146.2; JOINED; Genomic_DNA.
DR EMBL; AB014521; BAA31596.1; -; mRNA.
DR CCDS; CCDS4277.1; -. [Q9UNA1-1]
DR CCDS; CCDS47297.1; -. [Q9UNA1-2]
DR PIR; F59430; F59430.
DR RefSeq; NP_001129080.1; NM_001135608.1. [Q9UNA1-2]
DR RefSeq; NP_055886.1; NM_015071.4. [Q9UNA1-1]
DR PDB; 1UGV; NMR; -; A=756-814.
DR PDBsum; 1UGV; -.
DR AlphaFoldDB; Q9UNA1; -.
DR BMRB; Q9UNA1; -.
DR SMR; Q9UNA1; -.
DR BioGRID; 116720; 60.
DR IntAct; Q9UNA1; 31.
DR MINT; Q9UNA1; -.
DR STRING; 9606.ENSP00000274498; -.
DR iPTMnet; Q9UNA1; -.
DR PhosphoSitePlus; Q9UNA1; -.
DR SwissPalm; Q9UNA1; -.
DR BioMuta; ARHGAP26; -.
DR DMDM; 21759332; -.
DR EPD; Q9UNA1; -.
DR jPOST; Q9UNA1; -.
DR MassIVE; Q9UNA1; -.
DR MaxQB; Q9UNA1; -.
DR PaxDb; Q9UNA1; -.
DR PeptideAtlas; Q9UNA1; -.
DR PRIDE; Q9UNA1; -.
DR ProteomicsDB; 85274; -. [Q9UNA1-1]
DR ProteomicsDB; 85275; -. [Q9UNA1-2]
DR Antibodypedia; 27437; 257 antibodies from 33 providers.
DR DNASU; 23092; -.
DR Ensembl; ENST00000274498.9; ENSP00000274498.4; ENSG00000145819.18. [Q9UNA1-1]
DR Ensembl; ENST00000645722.2; ENSP00000495131.1; ENSG00000145819.18. [Q9UNA1-2]
DR GeneID; 23092; -.
DR KEGG; hsa:23092; -.
DR MANE-Select; ENST00000645722.2; ENSP00000495131.1; NM_001135608.3; NP_001129080.1. [Q9UNA1-2]
DR UCSC; uc003lmt.4; human. [Q9UNA1-1]
DR CTD; 23092; -.
DR DisGeNET; 23092; -.
DR GeneCards; ARHGAP26; -.
DR HGNC; HGNC:17073; ARHGAP26.
DR HPA; ENSG00000145819; Low tissue specificity.
DR MalaCards; ARHGAP26; -.
DR MIM; 605370; gene.
DR MIM; 607785; phenotype.
DR neXtProt; NX_Q9UNA1; -.
DR OpenTargets; ENSG00000145819; -.
DR PharmGKB; PA134946198; -.
DR VEuPathDB; HostDB:ENSG00000145819; -.
DR eggNOG; KOG1451; Eukaryota.
DR GeneTree; ENSGT00940000157254; -.
DR HOGENOM; CLU_011532_2_0_1; -.
DR InParanoid; Q9UNA1; -.
DR OMA; LAXIFNT; -.
DR OrthoDB; 693048at2759; -.
DR PhylomeDB; Q9UNA1; -.
DR TreeFam; TF316851; -.
DR PathwayCommons; Q9UNA1; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; Q9UNA1; -.
DR SIGNOR; Q9UNA1; -.
DR BioGRID-ORCS; 23092; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; ARHGAP26; human.
DR EvolutionaryTrace; Q9UNA1; -.
DR GeneWiki; ARHGAP26; -.
DR GenomeRNAi; 23092; -.
DR Pharos; Q9UNA1; Tbio.
DR PRO; PR:Q9UNA1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UNA1; protein.
DR Bgee; ENSG00000145819; Expressed in sural nerve and 184 other tissues.
DR ExpressionAtlas; Q9UNA1; baseline and differential.
DR Genevisible; Q9UNA1; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IDA:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07636; BAR_GRAF; 1.
DR CDD; cd12064; SH3_GRAF; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR030061; GRAF.
DR InterPro; IPR035483; GRAF_BAR.
DR InterPro; IPR035481; GRAF_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12552:SF4; PTHR12552:SF4; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction;
KW Chromosomal rearrangement; Cytoplasm; Cytoskeleton; Disease variant;
KW GTPase activation; Proto-oncogene; Reference proteome; SH3 domain.
FT CHAIN 1..814
FT /note="Rho GTPase-activating protein 26"
FT /id="PRO_0000056718"
FT DOMAIN 265..369
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 383..568
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 756..814
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 624..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..682
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 700..754
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001659"
FT VARIANT 417
FT /note="N -> S (in JMML; somatic mutation;
FT dbSNP:rs121918546)"
FT /evidence="ECO:0000269|PubMed:10908648"
FT /id="VAR_013623"
FT CONFLICT 355
FT /note="E -> G (in Ref. 2; CAA71414 and 3; CAC29145/
FT CAC29146)"
FT /evidence="ECO:0000305"
FT STRAND 761..765
FT /evidence="ECO:0007829|PDB:1UGV"
FT STRAND 771..774
FT /evidence="ECO:0007829|PDB:1UGV"
FT STRAND 782..785
FT /evidence="ECO:0007829|PDB:1UGV"
FT STRAND 794..801
FT /evidence="ECO:0007829|PDB:1UGV"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:1UGV"
FT HELIX 808..810
FT /evidence="ECO:0007829|PDB:1UGV"
FT STRAND 811..813
FT /evidence="ECO:0007829|PDB:1UGV"
SQ SEQUENCE 814 AA; 92235 MW; 5C81DBDECB32B18A CRC64;
MGLPALEFSD CCLDSPHFRE TLKSHEAELD KTNKFIKELI KDGKSLISAL KNLSSAKRKF
ADSLNEFKFQ CIGDAETDDE MCIARSLQEF ATVLRNLEDE RIRMIENASE VLITPLEKFR
KEQIGAAKEA KKKYDKETEK YCGILEKHLN LSSKKKESQL QEADSQVDLV RQHFYEVSLE
YVFKVQEVQE RKMFEFVEPL LAFLQGLFTF YHHGYELAKD FGDFKTQLTI SIQNTRNRFE
GTRSEVESLM KKMKENPLEH KTISPYTMEG YLYVQEKRHF GTSWVKHYCT YQRDSKQITM
VPFDQKSGGK GGEDESVILK SCTRRKTDSI EKRFCFDVEA VDRPGVITMQ ALSEEDRRLW
MEAMDGREPV YNSNKDSQSE GTAQLDSIGF SIIRKCIHAV ETRGINEQGL YRIVGVNSRV
QKLLSVLMDP KTASETETDI CAEWEIKTIT SALKTYLRML PGPLMMYQFQ RSFIKAAKLE
NQESRVSEIH SLVHRLPEKN RQMLQLLMNH LANVANNHKQ NLMTVANLGV VFGPTLLRPQ
EETVAAIMDI KFQNIVIEIL IENHEKIFNT VPDMPLTNAQ LHLSRKKSSD SKPPSCSERP
LTLFHTVQST EKQEQRNSII NSSLESVSSN PNSILNSSSS LQPNMNSSDP DLAVVKPTRP
NSLPPNPSPT SPLSPSWPMF SAPSSPMPTS STSSDSSPVR SVAGFVWFSV AAVVLSLARS
SLHAVFSLLV NFVPCHPNLH LLFDRPEEAV HEDSSTPFRK AKALYACKAE HDSELSFTAG
TVFDNVHPSQ EPGWLEGTLN GKTGLIPENY VEFL
