Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9QZL0 (RIPK3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-interacting serine/threonine-protein kinase 3

EC=2.7.11.1
Alternative name(s):
RIP-like protein kinase 3
Receptor-interacting protein 3
Short name=RIP-3
Short name=mRIP3
Gene names
Name:Ripk3
Synonyms:Rip3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production. Ref.7 Ref.10 Ref.11 Ref.13

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.13

Enzyme regulation

Inhibited by necrostatin-1 By similarity.

Subunit structure

Interacts (via RIP homotypic interaction motif) with RIPK1 (via RIP homotypic interaction motif); this interaction induces RIPK1 phosphorylation and formation of a RIPK1-RIPK3 necroptosis-inducing complex. Upon TNF-induced necrosis, the RIPK1-RIPK3 dimer further interacts with PGAM5 and MLKL; the formation of this complex leads to PGAM5 phosphorylation and increase in PGAM5 phosphatase activity By similarity. Binds TRAF2 and is recruited to the TNFR-1 signaling complex By similarity. Interacts with MLKL; the interaction is direct. Interacts with PYGL, GLUL and GLUD1; these interactions result in activation of these metabolic enzymes. Interacts (via RIP homotypic interaction motif) with murid herpesvirus 1 viral inhibitor of RIP activation; this interaction disrupts RIP3-RIP1 interactions characteristic of TNF-alpha induced necroptosis, thereby suppressing this death pathway. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4 By similarity. Interacts with ARHGEF2 By similarity. Ref.6 Ref.7 Ref.11 Ref.12

Subcellular location

Cytoplasmcytosol Probable. Cell membrane. Mitochondrion Potential.

Tissue specificity

Expressed in embryo and in adult spleen, liver, testis, heart, brain and lung.

Post-translational modification

RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylation of Ser-204 plays a role in the necroptotic function of RIPK3. Phosphorylation at Ser-232 is required for binding MLKL.

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.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Necrosis
   Cellular componentCell membrane
Cytoplasm
Membrane
Mitochondrion
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processI-kappaB kinase/NF-kappaB signaling

Inferred from direct assay Ref.1. Source: MGI

NIK/NF-kappaB signaling

Inferred from direct assay Ref.1. Source: GOC

T cell differentiation in thymus

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

T cell homeostasis

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

activation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

amyloid fibril formation

Inferred from sequence or structural similarity. Source: UniProtKB

lymph node development

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

necroptotic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway

Inferred from direct assay Ref.1. Source: MGI

positive regulation of ligase activity

Inferred from direct assay PubMed 19498109. Source: MGI

positive regulation of necroptotic process

Inferred from mutant phenotype PubMed 21052097PubMed 22265414. Source: UniProtKB

positive regulation of oxidoreductase activity

Inferred from direct assay PubMed 19498109. Source: MGI

positive regulation of protein deacetylation

Inferred from genetic interaction PubMed 23201684. Source: MGI

positive regulation of reactive oxygen species metabolic process

Inferred from mutant phenotype PubMed 21052097. Source: UniProtKB

positive regulation of transferase activity

Inferred from genetic interaction PubMed 19498109. Source: MGI

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

regulation of T cell mediated cytotoxicity

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

regulation of activated T cell proliferation

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

regulation of activation-induced cell death of T cells

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

regulation of adaptive immune response

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

regulation of interferon-gamma production

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

regulation of reactive oxygen species metabolic process

Inferred from mutant phenotype PubMed 21052097. Source: MGI

spleen development

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

thymus development

Inferred from genetic interaction PubMed 21876153. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular

Inferred from direct assay Ref.1. Source: MGI

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

ripoptosome

Inferred from direct assay PubMed 23201684. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

NF-kappaB-inducing kinase activity

Inferred from direct assay Ref.1. Source: MGI

protein kinase activity

Inferred from direct assay Ref.1. Source: MGI

protein serine/threonine kinase activity

Inferred from direct assay Ref.11Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DAXXQ9UER72EBI-2367423,EBI-77321From a different organism.
Ripk1Q608557EBI-2367423,EBI-529119

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Receptor-interacting serine/threonine-protein kinase 3
PRO_0000086611

Regions

Domain22 – 292271Protein kinase
Nucleotide binding28 – 369ATP By similarity
Motif440 – 46122RIP homotypic interaction motif (RHIM)
Compositional bias352 – 43887Pro-rich

Sites

Active site1431Proton acceptor Probable
Binding site511ATP Probable

Amino acid modifications

Modified residue21Phosphoserine Ref.12
Modified residue1651Phosphoserine Ref.12
Modified residue1711Phosphoserine; by autocatalysis Potential
Modified residue2041Phosphoserine; by autocatalysis By similarity
Modified residue2311Phosphothreonine Ref.12
Modified residue2321Phosphoserine Ref.12
Modified residue2571Phosphothreonine Ref.12
Modified residue3041Phosphoserine Ref.12
Modified residue3261Phosphoserine Ref.12
Modified residue3381Phosphothreonine Ref.12
Modified residue3531Phosphoserine Ref.12
Modified residue3691Phosphoserine Ref.12
Modified residue3801Phosphoserine Ref.12
Modified residue3921Phosphothreonine Ref.12

Experimental info

Mutagenesis511K → A: Complete loss of induced necrosis.
Mutagenesis1111C → A: No effect. Ref.13
Mutagenesis1431D → N: Abolishes kinase activity and ability to mediate necroptosis. No autophosphorylation. Ref.1 Ref.11
Mutagenesis2301K → A: Slightly affects interaction with MLKL; when associated with A-236. Affects interaction with MLKL; when associated with A-232 and A-236. Ref.13
Mutagenesis2311T → A: Abolishes ability to mediate necroptosis. Ref.12
Mutagenesis2321S → A: Abolishes ability to mediate necroptosis. Affects interaction with MLKL; when associated with A-230 and A-236. Ref.9 Ref.12 Ref.13
Mutagenesis2361E → A: Slightly affects interaction with MLKL; when associated with A-230. Affects interaction with MLKL; when associated with A-230 and A-232. Ref.13
Mutagenesis459 – 4624PPRT → AAAA: Complete loss of induced necrosis.
Sequence conflict1361N → D in AAF03133. Ref.1
Sequence conflict1361N → D in BAE32636. Ref.2
Sequence conflict1981D → K in AAF03133. Ref.1
Sequence conflict1981D → K in BAE32636. Ref.2
Sequence conflict1981D → N in AAH29210. Ref.5
Sequence conflict2831D → G in BAE32636. Ref.2
Sequence conflict4711D → G in BAE32636. Ref.2

Secondary structure

.................................................. 486
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9QZL0 [UniParc].

Last modified February 19, 2014. Version 2.
Checksum: 31C5EEE77F55778B

FASTA48653,322
        10         20         30         40         50         60 
MSSVKLWPTG ASAVPLVSRE ELKKLEFVGK GGFGVVFRAH HRTWNHDVAV KIVNSKKISW 

        70         80         90        100        110        120 
EVKAMVNLRN ENVLLLLGVT EDLQWDFVSG QALVTRFMEN GSLAGLLQPE CPRPWPLLCR 

       130        140        150        160        170        180 
LLQEVVLGMC YLHSLNPPLL HRDLKPSNIL LDPELHAKLA DFGLSTFQGG SQSGSGSGSG 

       190        200        210        220        230        240 
SRDSGGTLAY LDPELLFDVN LKASKASDVY SFGILVWAVL AGREAELVDK TSLIRETVCD 

       250        260        270        280        290        300 
RQSRPPLTEL PPGSPETPGL EKLKELMIHC WGSQSENRPS FQDCEPKTNE VYNLVKDKVD 

       310        320        330        340        350        360 
AAVSEVKHYL SQHRSSGRNL SAREPSQRGT EMDCPRETMV SKMLDRLHLE EPSGPVPGKC 

       370        380        390        400        410        420 
PERQAQDTSV GPATPARTSS DPVAGTPQIP HTLPFRGTTP GPVFTETPGP HPQRNQGDGR 

       430        440        450        460        470        480 
HGTPWYPWTP PNPMTGPPAL VFNNCSEVQI GNYNSLVAPP RTTASSSAKY DQAQFGRGRG 


WQPFHK 

« Hide

References

« Hide 'large scale' references
[1]"Mouse receptor interacting protein 3 does not contain a caspase-recruiting or a death domain but induces apoptosis and activates NF-kappaB."
Pazdernik N.J., Donner D.B., Goebl M.G., Harrington M.A.
Mol. Cell. Biol. 19:6500-6508(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACTIVE SITE, MUTAGENESIS OF ASP-143.
Tissue: Embryo.
[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. expand/collapse author list , 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].
Strain: NOD.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Czech II.
Tissue: Mammary tumor.
[6]"Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1."
Upton J.W., Kaiser W.J., Mocarski E.S.
J. Biol. Chem. 283:16966-16970(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MURID HERPESVIRUS 1 VIRAL INHIBITOR OF RIP ACTIVATION.
[7]"DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB."
Rebsamen M., Heinz L.X., Meylan E., Michallet M.C., Schroder K., Hofmann K., Vazquez J., Benedict C.A., Tschopp J.
EMBO Rep. 10:916-922(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ZBP1.
[8]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase."
Sun L., Wang H., Wang Z., He S., Chen S., Liao D., Wang L., Yan J., Liu W., Lei X., Wang X.
Cell 148:213-227(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-232.
[10]"Toll-like receptor 3-mediated necrosis via TRIF, RIP3, and MLKL."
Kaiser W.J., Sridharan H., Huang C., Mandal P., Upton J.W., Gough P.J., Sehon C.A., Marquis R.W., Bertin J., Mocarski E.S.
J. Biol. Chem. 288:31268-31279(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism."
Murphy J.M., Czabotar P.E., Hildebrand J.M., Lucet I.S., Zhang J.G., Alvarez-Diaz S., Lewis R., Lalaoui N., Metcalf D., Webb A.I., Young S.N., Varghese L.N., Tannahill G.M., Hatchell E.C., Majewski I.J., Okamoto T., Dobson R.C., Hilton D.J. expand/collapse author list , Babon J.J., Nicola N.A., Strasser A., Silke J., Alexander W.S.
Immunity 39:443-453(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-143, INTERACTION WITH MLKL.
[12]"Diverse sequence determinants control human and mouse receptor interacting protein 3 (RIP3) and mixed lineage kinase domain-like (MLKL) interaction in necroptotic signaling."
Chen W., Zhou Z., Li L., Zhong C.Q., Zheng X., Wu X., Zhang Y., Ma H., Huang D., Li W., Xia Z., Han J.
J. Biol. Chem. 288:16247-16261(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-2; SER-165; THR-231; SER-232; THR-257; SER-304; SER-326; THR-338; SER-353; SER-369; SER-380 AND THR-392, INTERACTION WITH MLKL, MUTAGENESIS OF THR-231 AND SER-232.
[13]"Structural insights into RIP3-mediated necroptotic signaling."
Xie T., Peng W., Yan C., Wu J., Gong X., Shi Y.
Cell Rep. 5:70-78(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-313 OF MUTANT ALA-111 IN COMPLEX WITH MLKL, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-111; LYS-230; SER-232 AND GLU-236.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF178953 mRNA. Translation: AAF03133.1.
AK154505 mRNA. Translation: BAE32636.1.
AC098877 Genomic DNA. No translation available.
CH466535 Genomic DNA. Translation: EDL36236.1.
BC029210 mRNA. Translation: AAH29210.1.
RefSeqNP_064339.2. NM_019955.2.
UniGeneMm.46612.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4M66X-ray2.40A/B1-313[»]
4M69X-ray2.50A1-313[»]
ProteinModelPortalQ9QZL0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-54883N.
IntActQ9QZL0. 15 interactions.
STRING10090.ENSMUSP00000022830.

PTM databases

PhosphoSiteQ9QZL0.

Proteomic databases

PaxDbQ9QZL0.
PRIDEQ9QZL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022830; ENSMUSP00000022830; ENSMUSG00000022221.
GeneID56532.
KEGGmmu:56532.
UCSCuc007uav.2. mouse.

Organism-specific databases

CTD11035.
MGIMGI:2154952. Ripk3.

Phylogenomic databases

eggNOGNOG274817.
GeneTreeENSGT00550000074536.
HOGENOMHOG000035101.
HOVERGENHBG062538.
InParanoidQ9QZL0.
PhylomeDBQ9QZL0.

Gene expression databases

CleanExMM_RIPK3.
GenevestigatorQ9QZL0.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR025735. RHIM_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF12721. RHIM. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio312886.
PROQ9QZL0.
SOURCESearch...

Entry information

Entry nameRIPK3_MOUSE
AccessionPrimary (citable) accession number: Q9QZL0
Secondary accession number(s): G3X8V8, Q3U3Z9, Q8K2Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: February 19, 2014
Last modified: April 16, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot