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Q8BSK8 (KS6B1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosomal protein S6 kinase beta-1

Short name=S6K-beta-1
Short name=S6K1
EC=2.7.11.1
Alternative name(s):
70 kDa ribosomal protein S6 kinase 1
Short name=P70S6K1
Short name=p70-S6K 1
Ribosomal protein S6 kinase I
Short name=S6K
p70 ribosomal S6 kinase alpha
Short name=p70 S6 kinase alpha
Short name=p70 S6K-alpha
Short name=p70 S6KA
Gene names
Name:Rps6kb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the preinitiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial RMP leading to dissociation of a RMP:PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B. May be involved in cytoskeletal rearrangement through binding to neurabin. Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR By similarity. Ref.5 Ref.6 Ref.7 Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activation requires multiple phosphorylation events on serine/threonine residues. Activation appears to be first mediated by phosphorylation of multiple sites in the autoinhibitory domain, which facilitates phosphorylation at Thr-412, disrupting the autoinhibitory mechanism and allowing phosphorylation of Thr-252 by PDPK1. The active conformation of the kinase is believed to be stabilized by a mechanism involving three conserved phosphorylation sites located in the kinase domain activation loop (Thr-252) and in the AGC-kinase C-terminal domain (Ser-394 in the middle of the tail/linker region and Thr-412 within a hydrophobic motif at its end). Activated by mTORC1; isoform AlphaI and isoform AlphaII are sensitive to rapamycin, which inhibits activating phosphorylation at Thr-412. Activated by PDPK1 By similarity.

Subunit structure

Interacts with PPP1R9A/neurabin-1 By similarity. Interacts with RPTOR. Interacts with IRS1. Interacts with EIF3B and EIF3C. Interacts with POLDIP3 and TRAF4 By similarity.

Subcellular location

Cytoplasm By similarity. Cell junctionsynapsesynaptosome By similarity. Mitochondrion outer membrane. Mitochondrion By similarity. Note: Colocalizes with URI1 at mitochondrion By similarity. Ref.6

Domain

The autoinhibitory domain is believed to block phosphorylation within the AGC-kinase C-terminal domain and the activation loop By similarity.

The TOS (TOR signaling) motif is essential for activation by mTORC1 By similarity.

Post-translational modification

Phosphorylation at Thr-412 is regulated by mTORC1. The phosphorylation at this site is maintained by an agonist-dependent autophosphorylation mechanism. Activated by phosphorylation at Thr-252 by PDPK1. Dephosphorylation by PPP1CC at Thr-412 in mitochondrion By similarity.

Disruption phenotype

Impairment of body growth. Lethal in combination with Rps6kb2 deficiency. Ref.7

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Translation regulation
   Cellular componentCell junction
Cytoplasm
Membrane
Mitochondrion
Mitochondrion outer membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative initiation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

TOR signaling

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

germ cell development

Inferred from direct assay PubMed 12140361. Source: MGI

long-term memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.6. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype Ref.6. Source: MGI

negative regulation of insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of skeletal muscle tissue growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of translational initiation

Inferred from electronic annotation. Source: Ensembl

protein kinase B signaling

Inferred from genetic interaction PubMed 15249583. Source: MGI

protein phosphorylation

Inferred from direct assay PubMed 15249583. Source: MGI

regulation of glucose import

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus involved in regulation of muscle adaptation

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to glucagon

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to heat

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to leucine

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

response to wounding

Inferred from electronic annotation. Source: Ensembl

skeletal muscle atrophy

Inferred from electronic annotation. Source: Ensembl

skeletal muscle contraction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay Ref.6. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptide binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 20657550. Source: IntAct

protein kinase activity

Inferred from direct assay PubMed 15249583. Source: MGI

protein serine/threonine/tyrosine kinase activity

Inferred from sequence orthology PubMed 22797923. Source: MGI

ribosomal protein S6 kinase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Mdm2P238042EBI-646423,EBI-641788

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Alpha I (identifier: Q8BSK8-1)

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.
Isoform Alpha II (identifier: Q8BSK8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 525525Ribosomal protein S6 kinase beta-1
PRO_0000024344

Regions

Domain91 – 352262Protein kinase
Domain353 – 42371AGC-kinase C-terminal
Nucleotide binding97 – 1059ATP By similarity
Region424 – 525102Autoinhibitory domain
Motif28 – 325TOS motif

Sites

Active site2181Proton acceptor By similarity
Binding site1231ATP By similarity

Amino acid modifications

Modified residue2521Phosphothreonine; by PDPK1 By similarity
Modified residue3941Phosphoserine By similarity
Modified residue4121Phosphothreonine; by MTOR, NEK6 and NEK7 By similarity
Modified residue4341Phosphoserine By similarity
Modified residue4411Phosphoserine By similarity
Modified residue4441Phosphothreonine By similarity
Modified residue4471Phosphoserine By similarity
Modified residue4521Phosphoserine By similarity
Modified residue5161N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 2323Missing in isoform Alpha II.
VSP_018840

Experimental info

Sequence conflict601G → E in BAC28000. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha I [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 5B3C09F6BB365EE2

FASTA52559,146
        10         20         30         40         50         60 
MRRRRRRDGF YLAPDFRHRE AEDMAGVFDI DLDQPEDAGS EDELEEGGQL NESMDHGGVG 

        70         80         90        100        110        120 
PYELGMEHCE KFEISETSVN RGPEKIRPEC FELLRVLGKG GYGKVFQVRK VTGANTGKIF 

       130        140        150        160        170        180 
AMKVLKKAMI VRNAKDTAHT KAERNILEEV KHPFIVDLIY AFQTGGKLYL ILEYLSGGEL 

       190        200        210        220        230        240 
FMQLEREGIF MEDTACFYLA EISMALGHLH QKGIIYRDLK PENIMLNHQG HVKLTDFGLC 

       250        260        270        280        290        300 
KESIHDGTVT HTFCGTIEYM APEILMRSGH NRAVDWWSLG ALMYDMLTGA PPFTGENRKK 

       310        320        330        340        350        360 
TIDKILKCKL NLPPYLTQEA RDLLKKLLKR NAASRLGAGP GDAGEVQAHP FFRHINWEEL 

       370        380        390        400        410        420 
LARKVEPPFK PLLQSEEDVS QFDSKFTRQT PVDSPDDSTL SESANQVFLG FTYVAPSVLE 

       430        440        450        460        470        480 
SVKEKFSFEP KIRSPRRFIG SPRTPVSPVK FSPGDFWGRG ASASTANPQT PVEYPMETSG 

       490        500        510        520 
IEQMDVTVSG EASAPLPIRQ PNSGPYKKQA FPMISKRPEH LRMNL 

« Hide

Isoform Alpha II [UniParc].

Checksum: 5AE6CF3FCAAE8B83
Show »

FASTA50256,157

References

« Hide 'large scale' references
[1]"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: C57BL/6J.
[2]"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.
[3]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].
[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].
Strain: Czech II.
Tissue: Mammary tumor.
[5]"Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase."
Wang X., Li W., Williams M., Terada N., Alessi D.R., Proud C.G.
EMBO J. 20:4370-4379(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF EEF2K.
[6]"p70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD."
Harada H., Andersen J.S., Mann M., Terada N., Korsmeyer S.J.
Proc. Natl. Acad. Sci. U.S.A. 98:9666-9670(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF BAD, FUNCTION IN APOPTOSIS REGULATION, SUBCELLULAR LOCATION.
[7]"S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-sensitive 5'-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway."
Pende M., Um S.H., Mieulet V., Sticker M., Goss V.L., Mestan J., Mueller M., Fumagalli S., Kozma S.C., Thomas G.
Mol. Cell. Biol. 24:3112-3124(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]"S6K directly phosphorylates IRS-1 on Ser-270 to promote insulin resistance in response to TNF-(alpha) signaling through IKK2."
Zhang J., Gao Z., Yin J., Quon M.J., Ye J.
J. Biol. Chem. 283:35375-35382(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF IRS1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK032724 mRNA. Translation: BAC28000.1.
AL604063 Genomic DNA. Translation: CAI25799.1.
CH466556 Genomic DNA. Translation: EDL15788.1.
BC038491 mRNA. Translation: AAH38491.1.
CCDSCCDS48875.1. [Q8BSK8-1]
RefSeqNP_001107806.1. NM_001114334.1. [Q8BSK8-1]
UniGeneMm.394280.
Mm.446624.
Mm.479484.

3D structure databases

ProteinModelPortalQ8BSK8.
SMRQ8BSK8. Positions 81-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215408. 10 interactions.
IntActQ8BSK8. 5 interactions.
MINTMINT-5092082.

Chemistry

ChEMBLCHEMBL5429.

PTM databases

PhosphoSiteQ8BSK8.

Proteomic databases

MaxQBQ8BSK8.
PaxDbQ8BSK8.
PRIDEQ8BSK8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000154617; ENSMUSP00000119715; ENSMUSG00000020516. [Q8BSK8-1]
GeneID72508.
KEGGmmu:72508.
UCSCuc007ksn.2. mouse. [Q8BSK8-1]

Organism-specific databases

CTD6198.
MGIMGI:1270849. Rps6kb1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000114960.
HOGENOMHOG000233033.
HOVERGENHBG108317.
InParanoidQ5SWG1.
KOK04688.
OMAANRMPAR.
OrthoDBEOG7B8S38.
TreeFamTF313438.

Gene expression databases

ArrayExpressQ8BSK8.
BgeeQ8BSK8.
CleanExMM_RPS6KB1.
GenevestigatorQ8BSK8.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016238. Ribosomal_S6_kinase.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000605. Ribsml_S6_kin_1. 1 hit.
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio336366.
PROQ8BSK8.
SOURCESearch...

Entry information

Entry nameKS6B1_MOUSE
AccessionPrimary (citable) accession number: Q8BSK8
Secondary accession number(s): Q5SWG1, Q8CHX0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 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

MGD cross-references

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