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Q9R0G8

- NRK_MOUSE

UniProt

Q9R0G8 - NRK_MOUSE

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Protein

Nik-related protein kinase

Gene

Nrk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May phosphorylate cofilin-1 and induce actin polymerization through this process, during the late stages of embryogenesis. Involved in the TNF-alpha-induced signaling pathway.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541ATPPROSITE-ProRule annotation
Active sitei177 – 1771Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 399ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein kinase activity Source: MGI
  3. protein serine/threonine kinase activity Source: UniProtKB-KW
  4. small GTPase regulator activity Source: InterPro

GO - Biological processi

  1. activation of JNKK activity Source: MGI
  2. negative regulation of cell proliferation Source: MGI
  3. parturition Source: MGI
  4. regulation of spongiotrophoblast cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nik-related protein kinase (EC:2.7.11.1)
Alternative name(s):
Nck-interacting kinase-like embryo specific kinase
Short name:
NESK
Short name:
NIK-like embryo-specific kinase
Gene namesi
Name:Nrk
Synonyms:Nesk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1351326. Nrk.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541K → E: Kinase inactivation. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14551455Nik-related protein kinasePRO_0000250512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei847 – 8471PhosphoserineBy similarity
Modified residuei850 – 8501PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9R0G8.
PRIDEiQ9R0G8.

PTM databases

PhosphoSiteiQ9R0G8.

Expressioni

Developmental stagei

Predominantly expressed in skeletal muscle during embryogenesis. Expression was detected in the myotome at 10.5 dpc and, thereafter, was observed in developing skeletal musculature from 11.5 to 13.5 dpc and increased from 15 to 17 dpc. However, expression in skeletal muscle was not observed in adults. Its expression may be down-regulated as development proceeds.3 Publications

Gene expression databases

BgeeiQ9R0G8.
CleanExiMM_NRK.
ExpressionAtlasiQ9R0G8. baseline and differential.
GenevestigatoriQ9R0G8.

Interactioni

Protein-protein interaction databases

BioGridi205128. 1 interaction.
IntActiQ9R0G8. 1 interaction.
MINTiMINT-4130820.

Structurei

3D structure databases

ProteinModelPortaliQ9R0G8.
SMRiQ9R0G8. Positions 8-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 313289Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini1138 – 1425288CNHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili716 – 75035Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi398 – 531134Gln-richAdd
BLAST
Compositional biasi806 – 8138Poly-Gln
Compositional biasi958 – 1059102Gly-richAdd
BLAST

Sequence similaritiesi

Contains 1 CNH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118848.
HOGENOMiHOG000049277.
HOVERGENiHBG080612.
InParanoidiQ9R0G8.
KOiK16313.
OMAiEDIFNQH.
TreeFamiTF105138.

Family and domain databases

InterProiIPR001180. Citron.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00780. CNH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00036. CNH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50219. CNH. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R0G8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGPGSWRDK EVTDLGQLPD PTGIFSLDKA IGLGTYGRIF LGIHEKTGSL
60 70 80 90 100
VAVKVMSARK TPLPEIGRRV RVNKYQKSVG WRYSDEEEDL RTELNLLRKY
110 120 130 140 150
SFHKNIVTFY GAFFKLNPPG HQHQLWMVME LCAAGSVTDV VRMTRNQSLK
160 170 180 190 200
EDWIAYICRE ILQGLAHLHA HQVIHRDIKG QNVLLTHDAE VKIVDFGVSA
210 220 230 240 250
QVSRTNGRRN SFIGTPYWMA PEVIHCDEDP RCSYDYRSDV WSVGITAIEM
260 270 280 290 300
AEGAPPLCKL QPLEALCVIL REAAPKVKSS GWSRKFQNFM ENCMIKNFLF
310 320 330 340 350
RPTSGNMLLH PFVHDIKNER RVVESLTKHL TGIIQKREKK GIPVAFEGEE
360 370 380 390 400
AAKEQYITRR FRGPSCTPEL LRVPTSSRCR PLRVLHGEPP QPRWLPDQED
410 420 430 440 450
PQDQELQQLQ KAAGVFMPLH SQDNTSKLFP KQVEVAPYLR GAAQVVMPVL
460 470 480 490 500
VQVEAPPQVS KAAQMLKSLP TQDNKATSPE VQAPVAEGQQ AQHEALETEQ
510 520 530 540 550
PKDLDQVPEE FQGQDRAPEQ PRQGQAAEQQ QIHNPVPEQP PEEDREPEQA
560 570 580 590 600
EVQEEAVEPP QAEIEDKEPE VVQVHAQVLL PLLSQNRHVL LPLHLDRQLL
610 620 630 640 650
IPVGEQNEEV PRAQAWDLEA SRAVGAVQAL IEGLSRDLLR APNAFVTKPL
660 670 680 690 700
GPLQIFLENL STDGFYTEPE PTQKKKSKVA SLRKAIAKRL RPKRFRAKAL
710 720 730 740 750
WRLEDFEFSD VETSRRRRHR RWEDIFNQHE EQLRRVENDR EDDSSDNDEV
760 770 780 790 800
FHSIQAEVQI EPHAANPAGN EVHERSAPMP CNRNRTHRVK FSPSVGEEEP
810 820 830 840 850
SLEEAQPQQQ QQQPMNIRPR NCLNPQNFQA QSDSSSEEDS PVTRRKSQSS
860 870 880 890 900
PPYSTIDQKL LIDIHVPDGF KVGKISPPVY LTNEWVGYNA LSEIFWDDWI
910 920 930 940 950
MPTRPARPPE EDGDYVELYD ADANANGDEE VANGAYEDPR DGANGHDDMN
960 970 980 990 1000
NQLDQANGYE GHGAAGYNGG DVGGNHGAAF NGPRANYPRA GILKNGHNDG
1010 1020 1030 1040 1050
RALNRGAFGV FGDNAARAFH GAAGEAGAAF GNHGANRGNG RGNRNREANG
1060 1070 1080 1090 1100
RNEENGAFGR DQHVFPEFEH EESDRGTETS DSIALEITSF DGEQNSGRPV
1110 1120 1130 1140 1150
SSTTMGFPIG RSSPRGSDFG SDISYNSPIL HVYEKDFSSE VYCGSLWGVN
1160 1170 1180 1190 1200
LLLGTQSHLY LMDRSGKAEI VKLIKRRPFR QIQVVEQLNL LITISGKKNR
1210 1220 1230 1240 1250
LRVYHLSWLR NKILNNDPKS KKRQKAMRKK EEACKAIDKL IGCEHFSVLQ
1260 1270 1280 1290 1300
HEETTYIAVA VKSSIHLFAW APKSFDENTA IKVFPTRDLK PLTVDLAVGS
1310 1320 1330 1340 1350
EKTLKIFFSS ANGYHIIDAE SEVMSEVTLP NNNVVILPDC LGLGVMLSLN
1360 1370 1380 1390 1400
AEAASEEANE QLLKKILDVW KDIPSSVAFE CTKRITGWDQ KAIEVRSLQS
1410 1420 1430 1440 1450
TILENELKRR SIKKLRFLCA RGDKMFFAST LSNDHSRVYL MSLGKLEELH

RSYAV
Length:1,455
Mass (Da):163,647
Last modified:July 27, 2011 - v2
Checksum:i7588DBE31B15ED91
GO

Sequence cautioni

The sequence AAH68311.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741A → V in BAA84943. (PubMed:10559491)Curated
Sequence conflicti397 – 3971D → N in BAA84943. (PubMed:10559491)Curated
Sequence conflicti467 – 4671K → R in BAA87066. (PubMed:10801798)Curated
Sequence conflicti894 – 8941I → T in AAH68311. (PubMed:15489334)Curated
Sequence conflicti1008 – 10081F → S in AAH68311. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020741 mRNA. Translation: BAA84943.1.
AB035267 mRNA. Translation: BAA87066.1.
BC139029 mRNA. Translation: AAI39030.1.
BC139031 mRNA. Translation: AAI39032.1.
BC068311 mRNA. Translation: AAH68311.1. Sequence problems.
AK041377 mRNA. Translation: BAC30923.1.
CCDSiCCDS41143.1.
RefSeqiNP_038752.2. NM_013724.2.
UniGeneiMm.482319.

Genome annotation databases

EnsembliENSMUST00000064937; ENSMUSP00000063397; ENSMUSG00000052854.
GeneIDi27206.
KEGGimmu:27206.
UCSCiuc009ujx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020741 mRNA. Translation: BAA84943.1 .
AB035267 mRNA. Translation: BAA87066.1 .
BC139029 mRNA. Translation: AAI39030.1 .
BC139031 mRNA. Translation: AAI39032.1 .
BC068311 mRNA. Translation: AAH68311.1 . Sequence problems.
AK041377 mRNA. Translation: BAC30923.1 .
CCDSi CCDS41143.1.
RefSeqi NP_038752.2. NM_013724.2.
UniGenei Mm.482319.

3D structure databases

ProteinModelPortali Q9R0G8.
SMRi Q9R0G8. Positions 8-339.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205128. 1 interaction.
IntActi Q9R0G8. 1 interaction.
MINTi MINT-4130820.

PTM databases

PhosphoSitei Q9R0G8.

Proteomic databases

PaxDbi Q9R0G8.
PRIDEi Q9R0G8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000064937 ; ENSMUSP00000063397 ; ENSMUSG00000052854 .
GeneIDi 27206.
KEGGi mmu:27206.
UCSCi uc009ujx.2. mouse.

Organism-specific databases

CTDi 203447.
MGIi MGI:1351326. Nrk.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118848.
HOGENOMi HOG000049277.
HOVERGENi HBG080612.
InParanoidi Q9R0G8.
KOi K16313.
OMAi EDIFNQH.
TreeFami TF105138.

Miscellaneous databases

ChiTaRSi Nrk. mouse.
NextBioi 305075.
PROi Q9R0G8.
SOURCEi Search...

Gene expression databases

Bgeei Q9R0G8.
CleanExi MM_NRK.
ExpressionAtlasi Q9R0G8. baseline and differential.
Genevestigatori Q9R0G8.

Family and domain databases

InterProi IPR001180. Citron.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00780. CNH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00036. CNH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS50219. CNH. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nrk: a murine X-linked NIK (Nck-interacting kinase)-related kinase gene expressed in skeletal muscle."
    Kanai-Azuma M., Kanai Y., Okamoto M., Hayashi Y., Yonekawa H., Yazaki K.
    Mech. Dev. 89:155-159(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Strain: BALB/c.
    Tissue: Embryo.
  2. "NESK, a member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and is expressed during the late stages of embryogenesis."
    Nakano K., Yamauchi J., Nakagawa K., Itoh H., Kitamura N.
    J. Biol. Chem. 275:20533-20539(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-54, FUNCTION, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Brain and Embryo.
  4. "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] OF 1-334.
    Strain: C57BL/6J.
    Tissue: Thymus.
  5. "Cofilin phosphorylation and actin polymerization by NRK/NESK, a member of the germinal center kinase family."
    Nakano K., Kanai-Azuma M., Kanai Y., Moriyama K., Yazaki K., Hayashi Y., Kitamura N.
    Exp. Cell Res. 287:219-227(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-54, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiNRK_MOUSE
AccessioniPrimary (citable) accession number: Q9R0G8
Secondary accession number(s): B2RSW5
, Q6NV55, Q8C9S9, Q9R0S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 104 of the entry and version 2 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3