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Rhotekin

 RTKN_HUMAN              Reviewed;         563 AA.
Q9BST9; H7BXD4; Q8WVN1; Q96PT6; Q9HB05;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
20-JUN-2018, entry version 147.
RecName: Full=Rhotekin;
Name=RTKN {ECO:0000312|HGNC:HGNC:10466}; Synonyms=RTKN1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL16767.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Kidney {ECO:0000269|PubMed:10873388};
PubMed=10873388; DOI=10.1006/geno.2000.6212;
Fu Q., Yu L., Liu Q., Zhang J., Zhang H., Zhao S.;
"Molecular cloning, expression characterization, and mapping of a
novel putative inhibitor of rho GTPase activity, RTKN, to D2S145-
D2S286.";
Genomics 66:328-332(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAG01181.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH
RHOA AND TAX1BP3, AND MUTAGENESIS OF 561-SER--VAL-563.
TISSUE=Leukocyte {ECO:0000269|PubMed:10940294};
PubMed=10940294; DOI=10.1074/jbc.M000465200;
Reynaud C., Fabre S., Jalinot P.;
"The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is
involved in Rho signaling to the serum response element.";
J. Biol. Chem. 275:33962-33968(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4] {ECO:0000305, ECO:0000312|EMBL:AAH04558.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain {ECO:0000312|EMBL:AAH17727.1}, and
Placenta {ECO:0000312|EMBL:AAH04558.2};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15480428; DOI=10.1038/sj.onc.1208106;
Liu C.-A., Wang M.-J., Chi C.-W., Wu C.-W., Chen J.-Y.;
"Rho/Rhotekin-mediated NF-kappaB activation confers resistance to
apoptosis.";
Oncogene 23:8731-8742(2004).
[6] {ECO:0000305}
FUNCTION, AND INTERACTION WITH SEPT9.
PubMed=16007136; DOI=10.1038/sj.onc.1208862;
Ito H., Iwamoto I., Morishita R., Nozawa Y., Narumiya S., Asano T.,
Nagata K.;
"Possible role of Rho/Rhotekin signaling in mammalian septin
organization.";
Oncogene 24:7064-7072(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-543, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520 AND SER-529, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-106, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-14, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Mediates Rho signaling to activate NF-kappa-B and may
confer increased resistance to apoptosis to cells in gastric
tumorigenesis. May play a novel role in the organization of septin
structures. {ECO:0000269|PubMed:10940294,
ECO:0000269|PubMed:15480428, ECO:0000269|PubMed:16007136}.
-!- SUBUNIT: Interacts via its C-terminal region with the TAX1BP3 PDZ
domain. This interaction facilitates Rho-mediated activation of
the c-Fos serum response element (SRE). Interacts with SEPT9.
Specifically binds to GTP-bound RHOA, RHOB and RHOC and inhibits
their GTPase activity. {ECO:0000250|UniProtKB:Q8C6B2,
ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:16007136}.
-!- INTERACTION:
P61586:RHOA; NbExp=6; IntAct=EBI-446694, EBI-446668;
Q9QUI0:Rhoa (xeno); NbExp=2; IntAct=EBI-446694, EBI-643583;
O60504:SORBS3; NbExp=3; IntAct=EBI-446694, EBI-741237;
O60504-2:SORBS3; NbExp=3; IntAct=EBI-446694, EBI-1222956;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1 {ECO:0000269|PubMed:10873388};
IsoId=Q9BST9-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:15489334};
IsoId=Q9BST9-2; Sequence=VSP_052004;
Note=No experimental confirmation available.;
Name=3 {ECO:0000269|PubMed:10940294};
IsoId=Q9BST9-3; Sequence=VSP_052005;
Note=Incomplete sequence. {ECO:0000269|PubMed:10940294};
-!- TISSUE SPECIFICITY: Highly expressed in prostate, moderately in
kidney, heart, brain, spleen, testis, placenta, small intestine,
pancreas, skeletal muscle and peripheral blood leukocytes, and
weakly in ovary, colon and thymus. Weakly expressed in all normal
cell lines tested. Overexpressed in various cancer cell lines.
{ECO:0000269|PubMed:10873388, ECO:0000269|PubMed:15480428}.
-!- SEQUENCE CAUTION:
Sequence=AAL16767.1; Type=Frameshift; Positions=15, 20; Evidence={ECO:0000305};
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EMBL; AF049227; AAL16767.1; ALT_FRAME; mRNA.
EMBL; AF290512; AAG01181.1; -; mRNA.
EMBL; AC005041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004558; AAH04558.2; -; mRNA.
EMBL; BC017727; AAH17727.1; -; mRNA.
CCDS; CCDS1941.1; -. [Q9BST9-2]
CCDS; CCDS33226.1; -. [Q9BST9-1]
CCDS; CCDS42699.1; -. [Q9BST9-3]
RefSeq; NP_001015055.1; NM_001015055.1. [Q9BST9-1]
RefSeq; NP_001015056.1; NM_001015056.1. [Q9BST9-3]
RefSeq; NP_149035.1; NM_033046.2. [Q9BST9-2]
RefSeq; XP_016860124.1; XM_017004635.1. [Q9BST9-2]
UniGene; Hs.192854; -.
ProteinModelPortal; Q9BST9; -.
SMR; Q9BST9; -.
BioGrid; 112156; 76.
DIP; DIP-31098N; -.
IntAct; Q9BST9; 11.
MINT; Q9BST9; -.
STRING; 9606.ENSP00000272430; -.
iPTMnet; Q9BST9; -.
PhosphoSitePlus; Q9BST9; -.
BioMuta; RTKN; -.
DMDM; 74733052; -.
EPD; Q9BST9; -.
MaxQB; Q9BST9; -.
PaxDb; Q9BST9; -.
PeptideAtlas; Q9BST9; -.
PRIDE; Q9BST9; -.
ProteomicsDB; 78923; -.
ProteomicsDB; 78924; -. [Q9BST9-2]
ProteomicsDB; 78925; -. [Q9BST9-3]
DNASU; 6242; -.
Ensembl; ENST00000233330; ENSP00000233330; ENSG00000114993. [Q9BST9-3]
Ensembl; ENST00000272430; ENSP00000272430; ENSG00000114993. [Q9BST9-1]
Ensembl; ENST00000305557; ENSP00000305298; ENSG00000114993. [Q9BST9-2]
GeneID; 6242; -.
KEGG; hsa:6242; -.
UCSC; uc002slc.4; human. [Q9BST9-1]
CTD; 6242; -.
DisGeNET; 6242; -.
EuPathDB; HostDB:ENSG00000114993.15; -.
GeneCards; RTKN; -.
HGNC; HGNC:10466; RTKN.
HPA; HPA030259; -.
MIM; 602288; gene.
neXtProt; NX_Q9BST9; -.
OpenTargets; ENSG00000114993; -.
PharmGKB; PA34879; -.
eggNOG; ENOG410IIHF; Eukaryota.
eggNOG; ENOG410ZX8Y; LUCA.
GeneTree; ENSGT00390000000104; -.
HOGENOM; HOG000015094; -.
HOVERGEN; HBG059480; -.
InParanoid; Q9BST9; -.
OMA; AERSPCR; -.
OrthoDB; EOG091G09OJ; -.
PhylomeDB; Q9BST9; -.
TreeFam; TF331476; -.
Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
SIGNOR; Q9BST9; -.
ChiTaRS; RTKN; human.
GeneWiki; RTKN; -.
GenomeRNAi; 6242; -.
PRO; PR:Q9BST9; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000114993; -.
CleanEx; HS_RTKN; -.
ExpressionAtlas; Q9BST9; baseline and differential.
Genevisible; Q9BST9; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0017049; F:GTP-Rho binding; IDA:UniProtKB.
GO; GO:0005095; F:GTPase inhibitor activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
GO; GO:0032185; P:septin cytoskeleton organization; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR012966; AHD.
InterPro; IPR011072; HR1_rho-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR030471; RTKN.
PANTHER; PTHR21538:SF19; PTHR21538:SF19; 1.
Pfam; PF08174; Anillin; 1.
Pfam; PF00169; PH; 1.
SMART; SM00742; Hr1; 1.
SMART; SM00233; PH; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS51860; REM_1; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Coiled coil; Complete proteome;
GTP-binding; Methylation; Nucleotide-binding; Phosphoprotein;
Reference proteome.
CHAIN 1 563 Rhotekin.
/FTId=PRO_0000233940.
DOMAIN 17 98 REM-1. {ECO:0000255|PROSITE-
ProRule:PRU01207}.
DOMAIN 309 416 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
COMPBIAS 479 544 Pro-rich. {ECO:0000255}.
MOD_RES 14 14 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 230 230 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8C6B2}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 543 543 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 1 50 Missing (in isoform 3).
{ECO:0000303|PubMed:10940294}.
/FTId=VSP_052005.
VAR_SEQ 1 36 MFSRNHRSRVTVARGSALEMEFKRGRFRLSLFSDLP -> M
QDRLHILEDLNMLYIRQMALSL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_052004.
MUTAGEN 561 563 SPV->APA: Impairs interaction with
TAX1BP3. {ECO:0000269|PubMed:10940294}.
CONFLICT 18 19 LE -> WR (in Ref. 1). {ECO:0000305}.
CONFLICT 55 55 A -> P (in Ref. 1; AAL16767).
{ECO:0000305}.
CONFLICT 61 61 A -> P (in Ref. 1; AAL16767).
{ECO:0000305}.
CONFLICT 65 66 RE -> AR (in Ref. 1; AAL16767).
{ECO:0000305}.
CONFLICT 102 102 S -> N (in Ref. 1; AAL16767).
{ECO:0000305}.
CONFLICT 112 112 A -> P (in Ref. 1; AAL16767).
{ECO:0000305}.
CONFLICT 160 160 Q -> H (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 163 163 E -> D (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 178 178 S -> N (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 202 205 EEGA -> KKRG (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 227 227 R -> K (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 274 274 R -> L (in Ref. 1; AAL16767).
{ECO:0000305}.
CONFLICT 336 336 G -> S (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 356 356 L -> F (in Ref. 1; AAL16767).
{ECO:0000305}.
CONFLICT 365 366 RV -> PI (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 372 372 D -> E (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 401 406 REALQS -> LETLQN (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 437 439 RKP -> PKT (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 454 454 A -> V (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 540 540 P -> T (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 549 549 L -> F (in Ref. 2; AAG01181).
{ECO:0000305}.
CONFLICT 555 555 P -> L (in Ref. 2; AAG01181).
{ECO:0000305}.
SEQUENCE 563 AA; 62667 MW; B3C64CB737E88501 CRC64;
MFSRNHRSRV TVARGSALEM EFKRGRFRLS LFSDLPEDTE LQRKLDHEIR MREGACKLLA
ACSQREQALE ATKSLLVCNS RILSYMGELQ RRKEAQVLGK TSRRPSDSGP PAERSPCRGR
VCISDLRIPL MWKDTEYFKN KGDLHRWAVF LLLQLGEHIQ DTEMILVDRT LTDISFQSNV
LFAEAGPDFE LRLELYGACV EEEGALTGGP KRLATKLSSS LGRSSGRRVR ASLDSAGGSG
SSPILLPTPV VGGPRYHLLA HTTLTLAAVQ DGFRTHDLTL ASHEENPAWL PLYGSVCCRL
AAQPLCMTQP TASGTLRVQQ AGEMQNWAQV HGVLKGTNLF CYRQPEDADT GEEPLLTIAV
NKETRVRAGE LDQALGRPFT LSISNQYGDD EVTHTLQTES REALQSWMEA LWQLFFDMSQ
WKQCCDEIMK IETPAPRKPP QALAKQGSLY HEMAIEPLDD IAAVTDILTQ REGARLETPP
PWLAMFTDQP ALPNPCSPAS VAPAPDWTHP LPWGRPRTFS LDAVPPDHSP RARSVAPLPP
QRSPRTRGLC SKGQPRTWLQ SPV


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