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Protein

Receptor-interacting serine/threonine-protein kinase 4

Gene

Ripk4

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

Functioni

Involved in stratified epithelial development (By similarity). It is a direct transcriptional target of TP63. Plays a role in NF-kappa-B activation.By similarity2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATPPROSITE-ProRule annotation
Active sitei143 – 1431Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi28 – 369ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-interacting serine/threonine-protein kinase 4 (EC:2.7.11.1)
Alternative name(s):
Ankyrin repeat domain-containing protein 3
PKC-associated protein kinase
PKC-regulated protein kinase
Gene namesi
Name:Ripk4
Synonyms:Ankrd3, Pkk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1919638. Ripk4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 786786Receptor-interacting serine/threonine-protein kinase 4PRO_0000273726Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki51 – 51Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki145 – 145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

May be phosphorylated by MAP3K2 and MAP3K3.2 Publications
Proteolytically cleaved by during Fas-induced apoptosis. Cleavage at Asp-342 and Asp-380.1 Publication
Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei342 – 3432Cleavage
Sitei380 – 3812Cleavage

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9ERK0.
PRIDEiQ9ERK0.

PTM databases

iPTMnetiQ9ERK0.
PhosphoSiteiQ9ERK0.

Expressioni

Tissue specificityi

Ubiquitously expressed, with an abundant expression in the thymus, bone marrow, pro-B, pre-B and immature B cells and a weak expression in the spleen.1 Publication

Developmental stagei

Expressed at 10.5 dpc at diverse locations including the embryonic forebrain, otic vesicle, branchial arches, primitive gut, and genitourinary system. Transient expression in the ventral neural tube at 12.5 dpc. By 14.5 dpc, strong expression throughout the gastrointestinal tract was observed in the luminal tissues of the esophagus, stomach, duodenum, and intestines, as well as transient expression in the skin. Not expressed in kidney.1 Publication

Gene expression databases

BgeeiQ9ERK0.
CleanExiMM_RIPK4.
ExpressionAtlasiQ9ERK0. baseline and differential.
GenevisibleiQ9ERK0. MM.

Interactioni

Subunit structurei

Interacts with PRKCB. Interacts with TRAF1, TRAF2, TRAF3 and TRAF5. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TRAF7Q6Q0C02EBI-6116422,EBI-307556From a different organism.

Protein-protein interaction databases

IntActiQ9ERK0. 2 interactions.
MINTiMINT-4129114.
STRINGi10090.ENSMUSP00000019386.

Structurei

3D structure databases

ProteinModelPortaliQ9ERK0.
SMRiQ9ERK0. Positions 14-350, 368-778.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 286265Protein kinasePROSITE-ProRule annotationAdd
BLAST
Repeati439 – 46830ANK 1Add
BLAST
Repeati472 – 50130ANK 2Add
BLAST
Repeati505 – 53430ANK 3Add
BLAST
Repeati538 – 56730ANK 4Add
BLAST
Repeati571 – 60131ANK 5Add
BLAST
Repeati605 – 63430ANK 6Add
BLAST
Repeati638 – 66730ANK 7Add
BLAST
Repeati671 – 70030ANK 8Add
BLAST
Repeati704 – 73431ANK 9Add
BLAST
Repeati736 – 76530ANK 10Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi305 – 39288Ser-richAdd
BLAST

Sequence similaritiesi

Contains 10 ANK repeats.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0192. Eukaryota.
KOG0504. Eukaryota.
COG0515. LUCA.
COG0666. LUCA.
GeneTreeiENSGT00550000074536.
HOGENOMiHOG000294086.
HOVERGENiHBG061582.
InParanoidiQ9ERK0.
KOiK08848.
OMAiPPERIME.
OrthoDBiEOG78H3SS.
PhylomeDBiQ9ERK0.
TreeFamiTF106506.

Family and domain databases

Gene3Di1.25.40.20. 5 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF12796. Ank_2. 3 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 10 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 9 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ERK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGEGRGRWA LGLLRTFDAG EFAGWEKVGS GGFGQVYKVR HVHWKTWLAI
60 70 80 90 100
KCSPSLHVDD RERMELLEEA KKMEMAKFRY ILPVYGICQE PVGLVMEYME
110 120 130 140 150
TGSLEKLLAS EPLPWDLRFR IVHETAVGMN FLHCMSPPLL HLDLKPANIL
160 170 180 190 200
LDAHYHVKIS DFGLAKCNGM SHSHDLSMDG LFGTIAYLPP ERIREKSRLF
210 220 230 240 250
DTKHDVYSFA IVIWGVLTQK KPFADEKNIL HIMMKVVKGH RPELPPICRP
260 270 280 290 300
RPRACASLIG LMQRCWHADP QVRPTFQEIT SETEDLCEKP DEEVKDLAHE
310 320 330 340 350
PGEKSSLESK SEARPESSRL KRASAPPFDN DCSLSELLSQ LDSGISQTLE
360 370 380 390 400
GPEELSRSSS ECKLPSSSSG KRLSGVSSVD SAFSSRGSLS LSFEREASTG
410 420 430 440 450
DLGPTDIQKK KLVDAIISGD TSRLMKILQP QDVDLVLDSS ASLLHLAVEA
460 470 480 490 500
GQEECVKWLL LNNANPNLTN RKGSTPLHMA VERKGRGIVE LLLARKTSVN
510 520 530 540 550
AKDEDQWTAL HFAAQNGDEA STRLLLEKNA SVNEVDFEGR TPMHVACQHG
560 570 580 590 600
QENIVRTLLR RGVDVGLQGK DAWLPLHYAA WQGHLPIVKL LAKQPGVSVN
610 620 630 640 650
AQTLDGRTPL HLAAQRGHYR VARILIDLCS DVNICSLQAQ TPLHVAAETG
660 670 680 690 700
HTSTARLLLH RGAGKEALTS EGYTALHLAA QNGHLATVKL LIEEKADVMA
710 720 730 740 750
RGPLNQTALH LAAARGHSEV VEELVSADLI DLSDEQGLSA LHLAAQGRHS
760 770 780
QTVETLLKHG AHINLQSLKF QGGQSSAATL LRRSKT
Length:786
Mass (Da):86,613
Last modified:March 1, 2002 - v2
Checksum:i66CE2C25EE96A40C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti718 – 7181S → T in BAE26294 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302127 mRNA. Translation: AAG30871.2.
AK145203 mRNA. Translation: BAE26294.1.
BC057871 mRNA. Translation: AAH57871.1.
CCDSiCCDS28360.1.
RefSeqiNP_076152.2. NM_023663.6.
UniGeneiMm.35290.

Genome annotation databases

EnsembliENSMUST00000019386; ENSMUSP00000019386; ENSMUSG00000005251.
GeneIDi72388.
KEGGimmu:72388.
UCSCiuc008adn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302127 mRNA. Translation: AAG30871.2.
AK145203 mRNA. Translation: BAE26294.1.
BC057871 mRNA. Translation: AAH57871.1.
CCDSiCCDS28360.1.
RefSeqiNP_076152.2. NM_023663.6.
UniGeneiMm.35290.

3D structure databases

ProteinModelPortaliQ9ERK0.
SMRiQ9ERK0. Positions 14-350, 368-778.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9ERK0. 2 interactions.
MINTiMINT-4129114.
STRINGi10090.ENSMUSP00000019386.

PTM databases

iPTMnetiQ9ERK0.
PhosphoSiteiQ9ERK0.

Proteomic databases

PaxDbiQ9ERK0.
PRIDEiQ9ERK0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019386; ENSMUSP00000019386; ENSMUSG00000005251.
GeneIDi72388.
KEGGimmu:72388.
UCSCiuc008adn.1. mouse.

Organism-specific databases

CTDi54101.
MGIiMGI:1919638. Ripk4.

Phylogenomic databases

eggNOGiKOG0192. Eukaryota.
KOG0504. Eukaryota.
COG0515. LUCA.
COG0666. LUCA.
GeneTreeiENSGT00550000074536.
HOGENOMiHOG000294086.
HOVERGENiHBG061582.
InParanoidiQ9ERK0.
KOiK08848.
OMAiPPERIME.
OrthoDBiEOG78H3SS.
PhylomeDBiQ9ERK0.
TreeFamiTF106506.

Miscellaneous databases

PROiQ9ERK0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ERK0.
CleanExiMM_RIPK4.
ExpressionAtlasiQ9ERK0. baseline and differential.
GenevisibleiQ9ERK0. MM.

Family and domain databases

Gene3Di1.25.40.20. 5 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF12796. Ank_2. 3 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 10 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 9 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Protein kinase C-associated kinase (PKK), a novel membrane-associated, ankyrin repeat-containing protein kinase."
    Chen L., Haider K., Ponda M., Cariappa A., Rowitch D., Pillai S.
    J. Biol. Chem. 276:21737-21744(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PRKCB, PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: BALB/cJ.
  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].
    Tissue: Mammary gland.
  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: NMRI.
    Tissue: Mammary tumor.
  4. "RIP4 (DIK/PKK), a novel member of the RIP kinase family, activates NF-kappa B and is processed during apoptosis."
    Meylan E., Martinon F., Thome M., Gschwendt M., Tschopp J.
    EMBO Rep. 3:1201-1208(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE AT ASP-342 AND ASP-380, INTERACTION WITH TRAF1; TRAF2; TRAF3 AND TRAF5, FUNCTION.
  5. "Protein kinase C-associated kinase can activate NFkappaB in both a kinase-dependent and a kinase-independent manner."
    Moran S.T., Haider K., Ow Y., Milton P., Chen L., Pillai S.
    J. Biol. Chem. 278:21526-21533(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  6. Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRIPK4_MOUSE
AccessioniPrimary (citable) accession number: Q9ERK0
Secondary accession number(s): Q3UM04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 119 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

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.