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Protein

Rhotekin

Gene

RTKN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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
Complete GO annotation...

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 Componenti: 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 residuei30 – 301Phosphoserine1 Publication
Modified residuei106 – 1061Phosphoserine1 Publication
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

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. 7 interactions.
DIPiDIP-31098N.
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.
GeneTreeiENSGT00390000000104.
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. AlignAdd to basket

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

        10         20         30         40         50
MFSRNHRSRV TVARGSALEM EFKRGRFRLS LFSDLPEDTE LQRKLDHEIR
60 70 80 90 100
MREGACKLLA ACSQREQALE ATKSLLVCNS RILSYMGELQ RRKEAQVLGK
110 120 130 140 150
TSRRPSDSGP PAERSPCRGR VCISDLRIPL MWKDTEYFKN KGDLHRWAVF
160 170 180 190 200
LLLQLGEHIQ DTEMILVDRT LTDISFQSNV LFAEAGPDFE LRLELYGACV
210 220 230 240 250
EEEGALTGGP KRLATKLSSS LGRSSGRRVR ASLDSAGGSG SSPILLPTPV
260 270 280 290 300
VGGPRYHLLA HTTLTLAAVQ DGFRTHDLTL ASHEENPAWL PLYGSVCCRL
310 320 330 340 350
AAQPLCMTQP TASGTLRVQQ AGEMQNWAQV HGVLKGTNLF CYRQPEDADT
360 370 380 390 400
GEEPLLTIAV NKETRVRAGE LDQALGRPFT LSISNQYGDD EVTHTLQTES
410 420 430 440 450
REALQSWMEA LWQLFFDMSQ WKQCCDEIMK IETPAPRKPP QALAKQGSLY
460 470 480 490 500
HEMAIEPLDD IAAVTDILTQ REGARLETPP PWLAMFTDQP ALPNPCSPAS
510 520 530 540 550
VAPAPDWTHP LPWGRPRTFS LDAVPPDHSP RARSVAPLPP QRSPRTRGLC
560
SKGQPRTWLQ SPV
Length:563
Mass (Da):62,667
Last modified:February 29, 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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9BST9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112156. 7 interactions.
DIPiDIP-31098N.
IntActiQ9BST9. 7 interactions.
MINTiMINT-142514.
STRINGi9606.ENSP00000272430.

PTM databases

PhosphoSiteiQ9BST9.

Polymorphism databases

DMDMi74733052.

Proteomic databases

MaxQBiQ9BST9.
PaxDbiQ9BST9.
PRIDEiQ9BST9.

Protocols and materials databases

DNASUi6242.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi6242.
GeneCardsiGC02M074667.
HGNCiHGNC:10466. RTKN.
HPAiHPA030259.
MIMi602288. gene.
neXtProtiNX_Q9BST9.
PharmGKBiPA34879.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG15986.
GeneTreeiENSGT00390000000104.
HOGENOMiHOG000015094.
HOVERGENiHBG059480.
InParanoidiQ9BST9.
OMAiAERSPCR.
OrthoDBiEOG72VH6J.
PhylomeDBiQ9BST9.
TreeFamiTF331476.

Miscellaneous databases

ChiTaRSiRTKN. human.
GeneWikiiRTKN.
GenomeRNAii6242.
NextBioi24241.
PROiQ9BST9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BST9.
CleanExiHS_RTKN.
GenevestigatoriQ9BST9.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(1999) [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(2004) [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(2003) [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(2003) [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(2004) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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 1, 2006
Last sequence update: February 29, 2004
Last modified: March 3, 2015
This is version 116 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.