RHG28_HUMAN
ID RHG28_HUMAN Reviewed; 729 AA.
AC Q9P2N2; A8MQB7; A8MU88; Q6P160; Q8N4T3; Q9NW53;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Rho GTPase-activating protein 28;
DE AltName: Full=Rho-type GTPase-activating protein 28;
GN Name=ARHGAP28; Synonyms=KIAA1314;
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 [LARGE SCALE MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP VARIANT PRO-727.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 334-729 (ISOFORM 1), AND VARIANT PRO-727.
RC TISSUE=Brain, and Skin;
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 [LARGE SCALE MRNA] OF 298-729 (ISOFORM 3), AND VARIANT
RP PRO-727.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9P2N2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2N2-2; Sequence=VSP_023726, VSP_023728;
CC Name=3;
CC IsoId=Q9P2N2-3; Sequence=VSP_023725, VSP_023727, VSP_023728;
CC Name=5;
CC IsoId=Q9P2N2-5; Sequence=VSP_039971;
CC -!- TISSUE SPECIFICITY: Expressed in testis. Expressed at moderate level in
CC kidney and ovary, and weakly expressed in spleen and skeletal muscle.
CC {ECO:0000269|PubMed:10718198}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91533.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92552.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB037735; BAA92552.1; ALT_INIT; mRNA.
DR EMBL; BX648684; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AP005205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033668; AAH33668.2; -; mRNA.
DR EMBL; BC065274; AAH65274.1; -; mRNA.
DR EMBL; AK001174; BAA91533.1; ALT_INIT; mRNA.
DR CCDS; CCDS32785.1; -. [Q9P2N2-5]
DR PIR; E59436; E59436.
DR AlphaFoldDB; Q9P2N2; -.
DR SMR; Q9P2N2; -.
DR IntAct; Q9P2N2; 5.
DR STRING; 9606.ENSP00000392660; -.
DR GlyConnect; 2070; 1 N-Linked glycan (1 site).
DR GlyGen; Q9P2N2; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9P2N2; -.
DR PhosphoSitePlus; Q9P2N2; -.
DR BioMuta; ARHGAP28; -.
DR DMDM; 311033539; -.
DR EPD; Q9P2N2; -.
DR jPOST; Q9P2N2; -.
DR MassIVE; Q9P2N2; -.
DR MaxQB; Q9P2N2; -.
DR PaxDb; Q9P2N2; -.
DR PeptideAtlas; Q9P2N2; -.
DR PRIDE; Q9P2N2; -.
DR ProteomicsDB; 83851; -. [Q9P2N2-1]
DR ProteomicsDB; 83852; -. [Q9P2N2-2]
DR ProteomicsDB; 83853; -. [Q9P2N2-3]
DR ProteomicsDB; 83854; -. [Q9P2N2-5]
DR Antibodypedia; 21924; 123 antibodies from 23 providers.
DR Ensembl; ENST00000262227.7; ENSP00000262227.3; ENSG00000088756.13. [Q9P2N2-2]
DR Ensembl; ENST00000314319.7; ENSP00000313506.3; ENSG00000088756.13. [Q9P2N2-5]
DR Ensembl; ENST00000383472.9; ENSP00000372964.4; ENSG00000088756.13. [Q9P2N2-1]
DR Ensembl; ENST00000419673.6; ENSP00000392660.2; ENSG00000088756.13. [Q9P2N2-5]
DR Ensembl; ENST00000532996.5; ENSP00000435990.1; ENSG00000088756.13. [Q9P2N2-3]
DR MANE-Select; ENST00000383472.9; ENSP00000372964.4; NM_001366230.1; NP_001353159.1.
DR UCSC; uc002knc.5; human. [Q9P2N2-1]
DR GeneCards; ARHGAP28; -.
DR HGNC; HGNC:25509; ARHGAP28.
DR HPA; ENSG00000088756; Group enriched (placenta, testis).
DR MIM; 610592; gene.
DR neXtProt; NX_Q9P2N2; -.
DR OpenTargets; ENSG00000088756; -.
DR PharmGKB; PA134915320; -.
DR VEuPathDB; HostDB:ENSG00000088756; -.
DR eggNOG; KOG2200; Eukaryota.
DR GeneTree; ENSGT00940000158929; -.
DR HOGENOM; CLU_023268_2_0_1; -.
DR InParanoid; Q9P2N2; -.
DR OMA; PNAESRC; -.
DR OrthoDB; 700544at2759; -.
DR PhylomeDB; Q9P2N2; -.
DR TreeFam; TF314044; -.
DR PathwayCommons; Q9P2N2; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR SignaLink; Q9P2N2; -.
DR SIGNOR; Q9P2N2; -.
DR ChiTaRS; ARHGAP28; human.
DR Pharos; Q9P2N2; Tdark.
DR PRO; PR:Q9P2N2; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9P2N2; protein.
DR Bgee; ENSG00000088756; Expressed in sperm and 132 other tissues.
DR ExpressionAtlas; Q9P2N2; baseline and differential.
DR Genevisible; Q9P2N2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:1904425; P:negative regulation of GTP binding; IBA:GO_Central.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..729
FT /note="Rho GTPase-activating protein 28"
FT /id="PRO_0000280476"
FT DOMAIN 380..577
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 20..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BN58"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BN58"
FT VAR_SEQ 1..177
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023725"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039971"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_023726"
FT VAR_SEQ 178..181
FT /note="SESP -> MNEL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023727"
FT VAR_SEQ 677..729
FT /note="SHGSSECIKIQNQRLYEIGGNIGEHCLDPDAYILDVYRINPQAEWVIKPQQS
FT S -> RILHWQRAALSFLNGKWVKKEREESTETNRSPKHVFLFTIGLDIST (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10718198,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_023728"
FT VARIANT 168
FT /note="I -> V (in dbSNP:rs2303978)"
FT /id="VAR_055833"
FT VARIANT 190
FT /note="T -> S (in dbSNP:rs6506448)"
FT /id="VAR_031155"
FT VARIANT 727
FT /note="Q -> P (in dbSNP:rs1056408)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_031156"
FT CONFLICT 598
FT /note="K -> E (in Ref. 2; BX648684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 82060 MW; 3272A9A651BB0CF6 CRC64;
MEVEDSGGVV LTAYHSYARA QPPNAESRCA PRAAASHPLS RKSIPRCRRI NRMLSNESLH
PPAFSRSNSE ASVDSASMED FWREIESIKD SSMGGQEEPP PAEVTPVDEG ELEAEWLQDV
GLSTLISGDE EEDGKALLST LTRTQAAAVQ KRYHTYTQTM RKKDKQSIRD VRDIFGVSES
PPRDTCGNHT NQLDGTKEER ELPRVIKTSG SMPDDASLNS TTLSDASQDK EGSFAVPRSD
SVAILETIPV LPVHSNGSPE PGQPVQNAIS DDDFLEKNIP PEAEELSFEV SYSEMVTEAL
KRNKLKKSEI KKEDYVLTKF NVQKTRFGLT EAGDLSAEDM KKIRHLSLIE LTAFFDAFGI
QLKRNKTEKV KGRDNGIFGV PLTVLLDGDR KKDPGVKVPL VLQKFFEKVE ESGLESEGIF
RLSGCTAKVK QYREELDAKF NADKFKWDKM CHREAAVMLK AFFRELPTSL FPVEYIPAFI
SLMERGPHVK VQFQALHLMV MALPDANRDA AQALMTFFNK VIANESKNRM SLWNISTVMA
PNLFFSRSKH SDYEELLLAN TAAHIIRLML KYQKILWKVP SFLITQVRRM NEATMLLKKQ
LPSVRKLLRR KTLERETASP KTSKVLQKSP SARRMSDVPE GVIRVHAPLL SKVSMAIQLN
NQTKAKDILA KFQYENSHGS SECIKIQNQR LYEIGGNIGE HCLDPDAYIL DVYRINPQAE
WVIKPQQSS
