Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Rhotekin

Gene

Rtkn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Molecular functioni

  • GTPase inhibitor activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • GTP-Rho binding Source: UniProtKB
  • Rho GTPase binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5666185. RHO GTPases Activate Rhotekin and Rhophilins.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhotekin
Gene namesi
Name:RtknImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:107371. Rtkn.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 564564RhotekinPRO_0000233941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301PhosphoserineBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei232 – 2321PhosphoserineBy similarity
Modified residuei520 – 5201PhosphoserineBy similarity
Modified residuei544 – 5441PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8C6B2.
PaxDbiQ8C6B2.
PRIDEiQ8C6B2.

PTM databases

iPTMnetiQ8C6B2.
PhosphoSiteiQ8C6B2.

Expressioni

Tissue specificityi

Abundantly expressed in brain and kidney. Weakly expressed in lung, testis, skeletal muscle, heart and thymus.1 Publication

Gene expression databases

BgeeiQ8C6B2.
CleanExiMM_RTKN.
ExpressionAtlasiQ8C6B2. baseline and differential.
GenevisibleiQ8C6B2. MM.

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 (By similarity). Specifically binds to GTP-bound RHOA, RHOB and RHOC and inhibits their GTPase activity.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RHOAP615863EBI-1162441,EBI-446668From a different organism.

GO - Molecular functioni

  • GTP-Rho binding Source: UniProtKB
  • Rho GTPase binding Source: MGI

Protein-protein interaction databases

BioGridi203032. 3 interactions.
DIPiDIP-29983N.
IntActiQ8C6B2. 5 interactions.
MINTiMINT-1791510.
STRINGi10090.ENSMUSP00000065571.

Structurei

3D structure databases

ProteinModelPortaliQ8C6B2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati36 – 9964REMSequence analysisAdd
BLAST
Domaini309 – 416108PHSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi479 – 54567Pro-richSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 PH domain.Sequence analysis
Contains 1 REM (Hr1) repeat.Sequence analysis

Phylogenomic databases

eggNOGiENOG410IIHF. Eukaryota.
ENOG410ZX8Y. LUCA.
GeneTreeiENSGT00390000000104.
HOGENOMiHOG000015094.
HOVERGENiHBG059480.
InParanoidiQ8C6B2.
OMAiAERSPCR.
OrthoDBiEOG72VH6J.
TreeFamiTF331476.

Family and domain databases

InterProiIPR012966. AHD.
IPR011072. HR1_rho-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF08174. Anillin. 1 hit.
[Graphical view]
SMARTiSM00742. Hr1. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q8C6B2-1) [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
MFSRNHRSRI TVARGSALEM EFKRGRFRLS FFSESPEDTE LQRKLDHEIR
60 70 80 90 100
MRDGACKLLA ACSQREQALE ATKSLLVCNS RILSYMGELQ RRKEAQVLEK
110 120 130 140 150
TGRRPSDSVQ PAQHSPCRGR VCISDLRIPL MWKDTEYFKN KGDLHRWAVF
160 170 180 190 200
LLLQIGEQIQ DTEMVLVDRT LTDISFQNNV LFAEAEPDFE LRLELYGACV
210 220 230 240 250
EEEGALAGAP KRLATKLSSS LGRSSGKRVR ASLDSAGASG NSPVLLPTPA
260 270 280 290 300
VGGPRFHLLA HTTLTLEEVQ DGFRTHDLTL TSHEENPAWL PLYGSVCCRL
310 320 330 340 350
AAQPLCMIQP TASGALRVQQ AGELQNGTLV HGVLKGTNLF CYWRSEDADT
360 370 380 390 400
GQEPLFTIVI NKETRVRAGE LEQAPEWPFT LSISNKYGDD EVTNTLQLES
410 420 430 440 450
REALQNWMEA LWQLFFDMSQ WRHCCDEVMK IETPAPRKPP QALAKQGSLY
460 470 480 490 500
HEMAIEPLDD IAAVTDILAQ REGTRLEPSP PWLAMFTDQP ALPSSCSPAS
510 520 530 540 550
VAPVPTWMQP LPWGRPRTFS LDAAPADHSL GPSRSVAPLP PQRSPKSRGF
560
YSKSQLGPWL QSPV
Note: No experimental confirmation available.Curated
Length:564
Mass (Da):63,013
Last modified:July 27, 2011 - v3
Checksum:i0934EEBF09B12A3E
GO
Isoform 21 Publication (identifier: Q8C6B2-2) [UniParc]FASTAAdd to basket

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

Show »
Length:551
Mass (Da):61,557
Checksum:iEA3D925FFF0FB85B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671Q → L in BAC36222 (PubMed:16141072).Curated
Sequence conflicti365 – 3651R → G in AAH13820 (PubMed:15489334).Curated
Sequence conflicti444 – 4441A → V in AAC52605 (PubMed:8662891).Curated
Sequence conflicti444 – 4441A → V in AAH13820 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MFSRN…FSESP → MQDRLRILEDLNMLYIRQMA LSL in isoform 2. 2 PublicationsVSP_052006Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54638 mRNA. Translation: AAC52605.1.
AK076155 mRNA. Translation: BAC36222.1.
AC104324 Genomic DNA. No translation available.
BC013820 mRNA. Translation: AAH13820.1.
CCDSiCCDS20274.1. [Q8C6B2-2]
CCDS51817.1. [Q8C6B2-1]
RefSeqiNP_001129699.1. NM_001136227.1. [Q8C6B2-1]
NP_033132.2. NM_009106.2. [Q8C6B2-2]
NP_598396.2. NM_133641.2. [Q8C6B2-2]
UniGeneiMm.4139.

Genome annotation databases

EnsembliENSMUST00000065512; ENSMUSP00000065571; ENSMUSG00000034930. [Q8C6B2-1]
ENSMUST00000087938; ENSMUSP00000085249; ENSMUSG00000034930. [Q8C6B2-2]
ENSMUST00000121093; ENSMUSP00000112501; ENSMUSG00000034930. [Q8C6B2-2]
GeneIDi20166.
KEGGimmu:20166.
UCSCiuc009cms.2. mouse. [Q8C6B2-1]
uc009cmt.2. mouse. [Q8C6B2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54638 mRNA. Translation: AAC52605.1.
AK076155 mRNA. Translation: BAC36222.1.
AC104324 Genomic DNA. No translation available.
BC013820 mRNA. Translation: AAH13820.1.
CCDSiCCDS20274.1. [Q8C6B2-2]
CCDS51817.1. [Q8C6B2-1]
RefSeqiNP_001129699.1. NM_001136227.1. [Q8C6B2-1]
NP_033132.2. NM_009106.2. [Q8C6B2-2]
NP_598396.2. NM_133641.2. [Q8C6B2-2]
UniGeneiMm.4139.

3D structure databases

ProteinModelPortaliQ8C6B2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203032. 3 interactions.
DIPiDIP-29983N.
IntActiQ8C6B2. 5 interactions.
MINTiMINT-1791510.
STRINGi10090.ENSMUSP00000065571.

PTM databases

iPTMnetiQ8C6B2.
PhosphoSiteiQ8C6B2.

Proteomic databases

MaxQBiQ8C6B2.
PaxDbiQ8C6B2.
PRIDEiQ8C6B2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065512; ENSMUSP00000065571; ENSMUSG00000034930. [Q8C6B2-1]
ENSMUST00000087938; ENSMUSP00000085249; ENSMUSG00000034930. [Q8C6B2-2]
ENSMUST00000121093; ENSMUSP00000112501; ENSMUSG00000034930. [Q8C6B2-2]
GeneIDi20166.
KEGGimmu:20166.
UCSCiuc009cms.2. mouse. [Q8C6B2-1]
uc009cmt.2. mouse. [Q8C6B2-2]

Organism-specific databases

CTDi6242.
MGIiMGI:107371. Rtkn.

Phylogenomic databases

eggNOGiENOG410IIHF. Eukaryota.
ENOG410ZX8Y. LUCA.
GeneTreeiENSGT00390000000104.
HOGENOMiHOG000015094.
HOVERGENiHBG059480.
InParanoidiQ8C6B2.
OMAiAERSPCR.
OrthoDBiEOG72VH6J.
TreeFamiTF331476.

Enzyme and pathway databases

ReactomeiR-MMU-5666185. RHO GTPases Activate Rhotekin and Rhophilins.

Miscellaneous databases

PROiQ8C6B2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C6B2.
CleanExiMM_RTKN.
ExpressionAtlasiQ8C6B2. baseline and differential.
GenevisibleiQ8C6B2. MM.

Family and domain databases

InterProiIPR012966. AHD.
IPR011072. HR1_rho-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF08174. Anillin. 1 hit.
[Graphical view]
SMARTiSM00742. Hr1. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain."
    Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N., Fujisawa K., Morii N., Madaule P., Narumiya S.
    J. Biol. Chem. 271:13556-13560(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH RHOA; RHOB AND RHOC, TISSUE SPECIFICITY.
    Tissue: BrainImported.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6JImported.
    Tissue: HeadImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] (ISOFORM 2).
    Strain: FVB/NImported.
    Tissue: Mammary glandImported.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney and Lung.

Entry informationi

Entry nameiRTKN_MOUSE
AccessioniPrimary (citable) accession number: Q8C6B2
Secondary accession number(s): E9QM24, Q61192, Q8VIG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.