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Q9BST9

- RTKN_HUMAN

UniProt

Q9BST9 - RTKN_HUMAN

Protein

Rhotekin

Gene

RTKN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      Previous versions | rss
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    Functioni

    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.3 Publications

    GO - Molecular functioni

    1. GTPase inhibitor activity Source: UniProtKB
    2. GTP binding Source: UniProtKB-KW
    3. GTP-Rho binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. negative regulation of catalytic activity Source: GOC
    3. Rho protein signal transduction Source: UniProtKB
    4. signal transduction Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rhotekin
    Gene namesi
    Name:RTKNImported
    Synonyms:RTKN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:10466. RTKN.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi561 – 5633SPV → APA: Impairs interaction with TAX1BP3. 1 Publication

    Organism-specific databases

    PharmGKBiPA34879.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 563563RhotekinPRO_0000233940Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei232 – 2321Phosphoserine2 Publications
    Modified residuei543 – 5431Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BST9.
    PaxDbiQ9BST9.
    PRIDEiQ9BST9.

    PTM databases

    PhosphoSiteiQ9BST9.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Gene expression databases

    ArrayExpressiQ9BST9.
    BgeeiQ9BST9.
    CleanExiHS_RTKN.
    GenevestigatoriQ9BST9.

    Organism-specific databases

    HPAiHPA030259.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi112156. 5 interactions.
    IntActiQ9BST9. 7 interactions.
    MINTiMINT-142514.
    STRINGi9606.ENSP00000272430.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BST9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati36 – 9964REMSequence AnalysisAdd
    BLAST
    Domaini309 – 416108PHPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi479 – 54466Pro-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 REM (Hr1) repeat.Sequence Analysis

    Phylogenomic databases

    eggNOGiNOG15986.
    HOGENOMiHOG000015094.
    HOVERGENiHBG059480.
    InParanoidiQ9BST9.
    OMAiAERSPCR.
    OrthoDBiEOG72VH6J.
    PhylomeDBiQ9BST9.
    TreeFamiTF331476.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR012966. DUF1709.
    IPR011072. HR1_rho-bd.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF08174. Anillin. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view]
    SMARTiSM00742. Hr1. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view]
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9BST9-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MFSRNHRSRV TVARGSALEM EFKRGRFRLS LFSDLPEDTE LQRKLDHEIR    50
    MREGACKLLA ACSQREQALE ATKSLLVCNS RILSYMGELQ RRKEAQVLGK 100
    TSRRPSDSGP PAERSPCRGR VCISDLRIPL MWKDTEYFKN KGDLHRWAVF 150
    LLLQLGEHIQ DTEMILVDRT LTDISFQSNV LFAEAGPDFE LRLELYGACV 200
    EEEGALTGGP KRLATKLSSS LGRSSGRRVR ASLDSAGGSG SSPILLPTPV 250
    VGGPRYHLLA HTTLTLAAVQ DGFRTHDLTL ASHEENPAWL PLYGSVCCRL 300
    AAQPLCMTQP TASGTLRVQQ AGEMQNWAQV HGVLKGTNLF CYRQPEDADT 350
    GEEPLLTIAV NKETRVRAGE LDQALGRPFT LSISNQYGDD EVTHTLQTES 400
    REALQSWMEA LWQLFFDMSQ WKQCCDEIMK IETPAPRKPP QALAKQGSLY 450
    HEMAIEPLDD IAAVTDILTQ REGARLETPP PWLAMFTDQP ALPNPCSPAS 500
    VAPAPDWTHP LPWGRPRTFS LDAVPPDHSP RARSVAPLPP QRSPRTRGLC 550
    SKGQPRTWLQ SPV 563
    Length:563
    Mass (Da):62,667
    Last modified:March 1, 2004 - v2
    Checksum:iB3C64CB737E88501
    GO
    Isoform 21 Publication (identifier: Q9BST9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: MFSRNHRSRVTVARGSALEMEFKRGRFRLSLFSDLP → MQDRLHILEDLNMLYIRQMALSL

    Note: No experimental confirmation available.

    Show »
    Length:550
    Mass (Da):61,229
    Checksum:i606C424DF55DD690
    GO
    Isoform 31 Publication (identifier: Q9BST9-3) [UniParc]FASTAAdd to Basket

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

    Note: Incomplete sequence.1 Publication

    Show »
    Length:513
    Mass (Da):56,666
    Checksum:i9846C3E5E95D609A
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 192LE → WR(PubMed:10873388)Curated
    Sequence conflicti55 – 551A → P in AAL16767. (PubMed:10873388)Curated
    Sequence conflicti61 – 611A → P in AAL16767. (PubMed:10873388)Curated
    Sequence conflicti65 – 662RE → AR in AAL16767. (PubMed:10873388)Curated
    Sequence conflicti102 – 1021S → N in AAL16767. (PubMed:10873388)Curated
    Sequence conflicti112 – 1121A → P in AAL16767. (PubMed:10873388)Curated
    Sequence conflicti160 – 1601Q → H in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti163 – 1631E → D in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti178 – 1781S → N in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti202 – 2054EEGA → KKRG in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti227 – 2271R → K in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti274 – 2741R → L in AAL16767. (PubMed:10873388)Curated
    Sequence conflicti336 – 3361G → S in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti356 – 3561L → F in AAL16767. (PubMed:10873388)Curated
    Sequence conflicti365 – 3662RV → PI in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti372 – 3721D → E in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti401 – 4066REALQS → LETLQN in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti437 – 4393RKP → PKT in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti454 – 4541A → V in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti540 – 5401P → T in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti549 – 5491L → F in AAG01181. (PubMed:10940294)Curated
    Sequence conflicti555 – 5551P → L in AAG01181. (PubMed:10940294)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5050Missing in isoform 3. 1 PublicationVSP_052005Add
    BLAST
    Alternative sequencei1 – 3636MFSRN…FSDLP → MQDRLHILEDLNMLYIRQMA LSL in isoform 2. 1 PublicationVSP_052004Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1941.1. [Q9BST9-2]
    CCDS33226.1. [Q9BST9-1]
    CCDS42699.1. [Q9BST9-3]
    RefSeqiNP_001015055.1. NM_001015055.1. [Q9BST9-1]
    NP_001015056.1. NM_001015056.1. [Q9BST9-3]
    NP_149035.1. NM_033046.2. [Q9BST9-2]
    UniGeneiHs.192854.

    Genome annotation databases

    EnsembliENST00000233330; ENSP00000233330; ENSG00000114993. [Q9BST9-3]
    ENST00000272430; ENSP00000272430; ENSG00000114993. [Q9BST9-1]
    ENST00000305557; ENSP00000305298; ENSG00000114993. [Q9BST9-2]
    GeneIDi6242.
    KEGGihsa:6242.
    UCSCiuc002slc.3. human. [Q9BST9-2]
    uc002sld.3. human. [Q9BST9-1]

    Polymorphism databases

    DMDMi74733052.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1941.1. [Q9BST9-2 ]
    CCDS33226.1. [Q9BST9-1 ]
    CCDS42699.1. [Q9BST9-3 ]
    RefSeqi NP_001015055.1. NM_001015055.1. [Q9BST9-1 ]
    NP_001015056.1. NM_001015056.1. [Q9BST9-3 ]
    NP_149035.1. NM_033046.2. [Q9BST9-2 ]
    UniGenei Hs.192854.

    3D structure databases

    ProteinModelPortali Q9BST9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112156. 5 interactions.
    IntActi Q9BST9. 7 interactions.
    MINTi MINT-142514.
    STRINGi 9606.ENSP00000272430.

    PTM databases

    PhosphoSitei Q9BST9.

    Polymorphism databases

    DMDMi 74733052.

    Proteomic databases

    MaxQBi Q9BST9.
    PaxDbi Q9BST9.
    PRIDEi Q9BST9.

    Protocols and materials databases

    DNASUi 6242.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233330 ; ENSP00000233330 ; ENSG00000114993 . [Q9BST9-3 ]
    ENST00000272430 ; ENSP00000272430 ; ENSG00000114993 . [Q9BST9-1 ]
    ENST00000305557 ; ENSP00000305298 ; ENSG00000114993 . [Q9BST9-2 ]
    GeneIDi 6242.
    KEGGi hsa:6242.
    UCSCi uc002slc.3. human. [Q9BST9-2 ]
    uc002sld.3. human. [Q9BST9-1 ]

    Organism-specific databases

    CTDi 6242.
    GeneCardsi GC02M074660.
    HGNCi HGNC:10466. RTKN.
    HPAi HPA030259.
    MIMi 602288. gene.
    neXtProti NX_Q9BST9.
    PharmGKBi PA34879.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG15986.
    HOGENOMi HOG000015094.
    HOVERGENi HBG059480.
    InParanoidi Q9BST9.
    OMAi AERSPCR.
    OrthoDBi EOG72VH6J.
    PhylomeDBi Q9BST9.
    TreeFami TF331476.

    Miscellaneous databases

    ChiTaRSi RTKN. human.
    GeneWikii RTKN.
    GenomeRNAii 6242.
    NextBioi 24241.
    PROi Q9BST9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BST9.
    Bgeei Q9BST9.
    CleanExi HS_RTKN.
    Genevestigatori Q9BST9.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR012966. DUF1709.
    IPR011072. HR1_rho-bd.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF08174. Anillin. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    SMARTi SM00742. Hr1. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view ]
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: Kidney1 Publication.
    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: Leukocyte1 Publication.
    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.
      , 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: BrainImported and PlacentaImported.
    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. 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.

    Entry informationi

    Entry nameiRTKN_HUMAN
    AccessioniPrimary (citable) accession number: Q9BST9
    Secondary accession number(s): H7BXD4
    , Q8WVN1, Q96PT6, Q9HB05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 113 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3