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Q9BST9 (RTKN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhotekin
Gene names
Name:RTKN
Synonyms:RTKN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.5 Ref.6

Subunit structure

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. Ref.2 Ref.6 UniProtKB Q8C6B2

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. Ref.1 Ref.5

Sequence similarities

Contains 1 PH domain.

Contains 1 REM (Hr1) repeat.

Sequence caution

The sequence AAL16767.1 differs from that shown. Reason: Frameshift at positions 15 and 20.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RHOAP615865EBI-446694,EBI-446668
RhoaQ9QUI02EBI-446694,EBI-643583From a different organism.
SORBS3O605043EBI-446694,EBI-741237
SORBS3O60504-23EBI-446694,EBI-1222956

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q9BST9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.4 (identifier: Q9BST9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MFSRNHRSRVTVARGSALEMEFKRGRFRLSLFSDLP → MQDRLHILEDLNMLYIRQMALSL
Note: No experimental confirmation available.
Isoform 3 Ref.2 (identifier: Q9BST9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.
Note: Incomplete sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 563563Rhotekin
PRO_0000233940

Regions

Repeat36 – 9964REM
Domain309 – 416108PH
Compositional bias479 – 54466Pro-rich

Amino acid modifications

Modified residue2321Phosphoserine Ref.7 Ref.8
Modified residue5431Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 5050Missing in isoform 3.
VSP_052005
Alternative sequence1 – 3636MFSRN…FSDLP → MQDRLHILEDLNMLYIRQMA LSL in isoform 2. Ref.2 Ref.4
VSP_052004

Experimental info

Mutagenesis561 – 5633SPV → APA: Impairs interaction with TAX1BP3. Ref.2
Sequence conflict18 – 192LE → WR Ref.1
Sequence conflict551A → P in AAL16767. Ref.1
Sequence conflict611A → P in AAL16767. Ref.1
Sequence conflict65 – 662RE → AR in AAL16767. Ref.1
Sequence conflict1021S → N in AAL16767. Ref.1
Sequence conflict1121A → P in AAL16767. Ref.1
Sequence conflict1601Q → H in AAG01181. Ref.2
Sequence conflict1631E → D in AAG01181. Ref.2
Sequence conflict1781S → N in AAG01181. Ref.2
Sequence conflict202 – 2054EEGA → KKRG in AAG01181. Ref.2
Sequence conflict2271R → K in AAG01181. Ref.2
Sequence conflict2741R → L in AAL16767. Ref.1
Sequence conflict3361G → S in AAG01181. Ref.2
Sequence conflict3561L → F in AAL16767. Ref.1
Sequence conflict365 – 3662RV → PI in AAG01181. Ref.2
Sequence conflict3721D → E in AAG01181. Ref.2
Sequence conflict401 – 4066REALQS → LETLQN in AAG01181. Ref.2
Sequence conflict437 – 4393RKP → PKT in AAG01181. Ref.2
Sequence conflict4541A → V in AAG01181. Ref.2
Sequence conflict5401P → T in AAG01181. Ref.2
Sequence conflict5491L → F in AAG01181. Ref.2
Sequence conflict5551P → L in AAG01181. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: B3C64CB737E88501

FASTA56362,667
        10         20         30         40         50         60 
MFSRNHRSRV TVARGSALEM EFKRGRFRLS LFSDLPEDTE LQRKLDHEIR MREGACKLLA 

        70         80         90        100        110        120 
ACSQREQALE ATKSLLVCNS RILSYMGELQ RRKEAQVLGK TSRRPSDSGP PAERSPCRGR 

       130        140        150        160        170        180 
VCISDLRIPL MWKDTEYFKN KGDLHRWAVF LLLQLGEHIQ DTEMILVDRT LTDISFQSNV 

       190        200        210        220        230        240 
LFAEAGPDFE LRLELYGACV EEEGALTGGP KRLATKLSSS LGRSSGRRVR ASLDSAGGSG 

       250        260        270        280        290        300 
SSPILLPTPV VGGPRYHLLA HTTLTLAAVQ DGFRTHDLTL ASHEENPAWL PLYGSVCCRL 

       310        320        330        340        350        360 
AAQPLCMTQP TASGTLRVQQ AGEMQNWAQV HGVLKGTNLF CYRQPEDADT GEEPLLTIAV 

       370        380        390        400        410        420 
NKETRVRAGE LDQALGRPFT LSISNQYGDD EVTHTLQTES REALQSWMEA LWQLFFDMSQ 

       430        440        450        460        470        480 
WKQCCDEIMK IETPAPRKPP QALAKQGSLY HEMAIEPLDD IAAVTDILTQ REGARLETPP 

       490        500        510        520        530        540 
PWLAMFTDQP ALPNPCSPAS VAPAPDWTHP LPWGRPRTFS LDAVPPDHSP RARSVAPLPP 

       550        560 
QRSPRTRGLC SKGQPRTWLQ SPV 

« Hide

Isoform 2 [UniParc].

Checksum: 606C424DF55DD690
Show »

FASTA55061,229
Isoform 3 [UniParc].

Checksum: 9846C3E5E95D609A
Show »

FASTA51356,666

References

« Hide 'large scale' references
[1]"Molecular cloning, expression characterization, and mapping of a novel putative inhibitor of rho GTPase activity, RTKN, to D2S145-D2S286."
Fu Q., Yu L., Liu Q., Zhang J., Zhang H., Zhao S.
Genomics 66:328-332(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element."
Reynaud C., Fabre S., Jalinot P.
J. Biol. Chem. 275:33962-33968(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH RHOA AND TAX1BP3, MUTAGENESIS OF 561-SER--VAL-563.
Tissue: Leukocyte.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 1 AND 2).
Tissue: Brain and Placenta.
[5]"Rho/Rhotekin-mediated NF-kappaB activation confers resistance to apoptosis."
Liu C.-A., Wang M.-J., Chi C.-W., Wu C.-W., Chen J.-Y.
Oncogene 23:8731-8742(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[6]"Possible role of Rho/Rhotekin signaling in mammalian septin organization."
Ito H., Iwamoto I., Morishita R., Nozawa Y., Narumiya S., Asano T., Nagata K.
Oncogene 24:7064-7072(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SEPT9.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-543, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF049227 mRNA. Translation: AAL16767.1. Frameshift.
AF290512 mRNA. Translation: AAG01181.1.
AC005041 Genomic DNA. No translation available.
BC004558 mRNA. Translation: AAH04558.2.
BC017727 mRNA. Translation: AAH17727.1.
CCDSCCDS1941.1. [Q9BST9-2]
CCDS33226.1. [Q9BST9-1]
CCDS42699.1. [Q9BST9-3]
RefSeqNP_001015055.1. NM_001015055.1. [Q9BST9-1]
NP_001015056.1. NM_001015056.1. [Q9BST9-3]
NP_149035.1. NM_033046.2. [Q9BST9-2]
UniGeneHs.192854.

3D structure databases

ProteinModelPortalQ9BST9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112156. 5 interactions.
IntActQ9BST9. 7 interactions.
MINTMINT-142514.
STRING9606.ENSP00000272430.

PTM databases

PhosphoSiteQ9BST9.

Polymorphism databases

DMDM74733052.

Proteomic databases

MaxQBQ9BST9.
PaxDbQ9BST9.
PRIDEQ9BST9.

Protocols and materials databases

DNASU6242.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233330; ENSP00000233330; ENSG00000114993. [Q9BST9-3]
ENST00000272430; ENSP00000272430; ENSG00000114993. [Q9BST9-1]
ENST00000305557; ENSP00000305298; ENSG00000114993. [Q9BST9-2]
GeneID6242.
KEGGhsa:6242.
UCSCuc002slc.3. human. [Q9BST9-2]
uc002sld.3. human. [Q9BST9-1]

Organism-specific databases

CTD6242.
GeneCardsGC02M074660.
HGNCHGNC:10466. RTKN.
HPAHPA030259.
MIM602288. gene.
neXtProtNX_Q9BST9.
PharmGKBPA34879.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG15986.
HOGENOMHOG000015094.
HOVERGENHBG059480.
InParanoidQ9BST9.
OMAAERSPCR.
OrthoDBEOG72VH6J.
PhylomeDBQ9BST9.
TreeFamTF331476.

Gene expression databases

ArrayExpressQ9BST9.
BgeeQ9BST9.
CleanExHS_RTKN.
GenevestigatorQ9BST9.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR012966. DUF1709.
IPR011072. HR1_rho-bd.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF08174. Anillin. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTSM00742. Hr1. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRTKN. human.
GeneWikiRTKN.
GenomeRNAi6242.
NextBio24241.
PROQ9BST9.
SOURCESearch...

Entry information

Entry nameRTKN_HUMAN
AccessionPrimary (citable) accession number: Q9BST9
Secondary accession number(s): H7BXD4 expand/collapse secondary AC list , Q8WVN1, Q96PT6, Q9HB05
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 1, 2004
Last modified: July 9, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM