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Q8C050 (KS6A5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. 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 alpha-5

Short name=S6K-alpha-5
EC=2.7.11.1
Alternative name(s):
90 kDa ribosomal protein S6 kinase 5
Nuclear mitogen- and stress-activated protein kinase 1
RSK-like protein kinase
Short name=RLSK
Gene names
Name:Rps6ka5
Synonyms:Msk1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length863 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.7

Cofactor

Magnesium By similarity. Ref.7

Enzyme regulation

Activated by phosphorylation at Ser-359, Thr-645 and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha, and by further autophosphorylation of Ser-211, Ser-375 and Ser-380 by the activated C-terminal kinase domain. The active N-terminal kinase domain finally phosphorylates downstream substrates, as well as Ser-814, Ser-816 and Ser-822 in its own C-terminal region.

Subunit structure

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells which transiently dissociates following mitogenic stimulation. Also associates with MAPK14/p38-alpha. Activated RPS6KA5 associates with and phosphorylates the NF-kappa-B p65 subunit RELA. Interacts with CREBBP and EP300 By similarity.

Subcellular location

Nucleus By similarity UniProtKB O75676.

Post-translational modification

Ser-375 and Thr-645 phosphorylation is required for kinase activity. Ser-375 and Ser-211 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-359, Thr-645 and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-814, Ser-816 and Ser-822 by the N-terminal kinase domain By similarity.

Ubiquitinated By similarity.

Miscellaneous

Enzyme activity requires the presence of both kinase domains By similarity. UniProtKB O75582

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 2 protein kinase domains.

Ontologies

Keywords
   Biological processInflammatory response
Stress response
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone H2A-S1 phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3-S10 phosphorylation

Inferred from sequence or structural similarity PubMed 12773393. Source: UniProtKB

histone H3-S28 phosphorylation

Inferred from sequence or structural similarity PubMed 12773393. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

interleukin-1-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of histone acetylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.7. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.7. Source: UniProtKB

response to external stimulus

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.7. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

protein serine/threonine kinase activity

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RaraP114162EBI-8391218,EBI-346736

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q8C050-1)

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 1 (identifier: Q8C050-2)

Also known as: 5;

The sequence of this isoform differs from the canonical sequence as follows:
     490-554: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 863863Ribosomal protein S6 kinase alpha-5
PRO_0000086208

Regions

Domain48 – 317270Protein kinase 1
Domain318 – 38669AGC-kinase C-terminal
Domain428 – 675248Protein kinase 2
Nucleotide binding54 – 629ATP By similarity UniProtKB Q15418
Nucleotide binding431 – 44010ATP By similarity

Sites

Active site1761Proton acceptor By similarity UniProtKB Q15418
Active site6081Proton acceptor By similarity UniProtKB Q15418
Binding site801ATP By similarity UniProtKB Q15418
Binding site4541ATP By similarity UniProtKB Q15418

Amino acid modifications

Modified residue2111Phosphoserine; by autocatalysis By similarity UniProtKB Q15418
Modified residue3591Phosphoserine; by MAPK1, MAPK3 and MAPK14 By similarity UniProtKB Q15418
Modified residue3751Phosphoserine; by autocatalysis By similarity UniProtKB Q15418
Modified residue3801Phosphoserine; by autocatalysis By similarity
Modified residue6451Phosphothreonine; by MAPK1, MAPK3 and MAPK14 By similarity
Modified residue7111Phosphoserine By similarity
Modified residue7211Phosphoserine By similarity
Modified residue7591Phosphoserine By similarity
Modified residue7641Phosphothreonine; by MAPK1, MAPK3 and MAPK14 By similarity
Modified residue8141Phosphoserine; by autocatalysis By similarity UniProtKB Q15418
Modified residue8161Phosphoserine; by autocatalysis By similarity
Modified residue8221Phosphoserine; by autocatalysis By similarity

Natural variations

Alternative sequence490 – 55465Missing in isoform 1.
VSP_050613

Experimental info

Sequence conflict2 – 1514EGEGG…AGTSG → GGRAAAAAARAPAE in AAQ24165. Ref.1
Sequence conflict1171H → N in BAC27809. Ref.2
Sequence conflict3761F → Y in BAC27809. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified October 24, 2003. Version 2.
Checksum: 7A3C76D4036EA3EA

FASTA86396,583
        10         20         30         40         50         60 
MEGEGGGSGG AGTSGDSGDG GEQLLTVKHE LRTANLTGHA EKVGIENFEL LKVLGTGAYG 

        70         80         90        100        110        120 
KVFLVRKISG HDAGKLYAMK VLKKATIVQK AKTTEHTRTE RQVLEHIRQS PFLVTLHYAF 

       130        140        150        160        170        180 
QTETKLHLIL DYINGGELFT HLSQRERFTE HEVQIYVGEI VLALEHLHKL GIIYRDIKLE 

       190        200        210        220        230        240 
NILLDSNGHV VLTDFGLSKE FVADETERAY SFCGTIEYMA PDIVRGGDSG HDKAVDWWSL 

       250        260        270        280        290        300 
GVLMYELLTG ASPFTVDGEK NSQAEISRRI LKSEPPYPQE MSTVAKDLLQ RLLMKDPKKR 

       310        320        330        340        350        360 
LGCGPRDAEE IKEHLFFEKI KWDDLAAKKV PAPFKPVIRD ELDVSNFAEE FTEMDPTYSP 

       370        380        390        400        410        420 
AALPQSSERL FQGYSFVAPS ILFKRNAAVI DPLQFHMGVD RPGVTNVARS AMMKDSPFYQ 

       430        440        450        460        470        480 
HYDLDLKDKP LGEGSFSICR KCVHKKTNQA FAVKIISKRM EANTQKEITA LKLCEGHPNI 

       490        500        510        520        530        540 
VKLHEVFHDQ VAASAQPPGQ VVLCSLLLLA LLFNRSLTRK PVTWTWLVHS TSQLPPLPPP 

       550        560        570        580        590        600 
MPEIVLFILL SDNGQLHTFL VMELLNGGEL FERIKRKKHF SETEASYIMR KLVSAVSHMH 

       610        620        630        640        650        660 
DVGVVHRDLK PENLLFTDEN DNLEIKVIDF GFARLKPPDN QPLKTPCFTL HYAAPELLTH 

       670        680        690        700        710        720 
NGYDESCDLW SLGVILYTML SGQVPFQSHD RSLTCTSAVE IMKKIKKGDF SFEGEAWKNV 

       730        740        750        760        770        780 
SQEAKDLIQG LLTVDPNKRL KMSGLRYNEW LQDGSQLSSN PLMTPDILGS SGAAVHTCVK 

       790        800        810        820        830        840 
ATFHAFNKYK REGFCLQNVD KAPLAKRRKM KRTSTSTETR SSSSESSRSS SSQSHGKTTP 

       850        860 
TKTLQPSNPT EGSNPDTLFQ FSD 

« Hide

Isoform 1 (5) [UniParc].

Checksum: 57AB12399BEF7B0E
Show »

FASTA79889,515

References

« Hide 'large scale' references
[1]"Cloning of mouse ribosomal protein S6 kinase, 90kDa, polypeptide 5 (RPS6KA5)."
Zhou G., Wang J., Xu W.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
[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] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Brain.
[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] (ISOFORM 1).
Tissue: Mammary gland.
[4]"Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1."
Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M., Ma W.-Y., Dong Z.
J. Biol. Chem. 276:33213-33219(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[5]"MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse epidermal JB6 cells."
Zhang Y., Liu G., Dong Z.
J. Biol. Chem. 276:42534-42542(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF STAT3.
[6]"MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts."
Wiggin G.R., Soloaga A., Foster J.M., Murray-Tait V., Cohen P., Arthur J.S.
Mol. Cell. Biol. 22:2871-2881(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1 AND ATF1.
[7]"Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)."
Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W., Haegeman G.
EMBO J. 22:1313-1324(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Mitogen and stress response kinase-1 (MSK1) mediates excitotoxic induced death of hippocampal neurones."
Hughes J.P., Staton P.C., Wilkinson M.G., Strijbos P.J., Skaper S.D., Arthur J.S., Reith A.D.
J. Neurochem. 86:25-32(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL DEATH.
[9]"MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2."
Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J., Nightingale K., Iborra F.J., Mahadevan L.C.
J. Cell Sci. 118:2247-2259(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[10]"ERK1/2 and p38-MAPK signalling pathways, through MSK1, are involved in NF-kappaB transactivation during oxidative stress in skeletal myoblasts."
Kefaloyianni E., Gaitanaki C., Beis I.
Cell. Signal. 18:2238-2251(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF RELA/NFKB3.
[11]"The kinases MSK1 and MSK2 are required for epidermal growth factor-induced, but not tumor necrosis factor-induced, histone H3 Ser10 phosphorylation."
Duncan E.A., Anest V., Cogswell P., Baldwin A.S.
J. Biol. Chem. 281:12521-12525(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[12]"The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor signaling."
Ananieva O., Darragh J., Johansen C., Carr J.M., McIlrath J., Park J.M., Wingate A., Monk C.E., Toth R., Santos S.G., Iversen L., Arthur J.S.
Nat. Immunol. 9:1028-1036(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1; ATF1 AND HISTONE H3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY341873 mRNA. Translation: AAQ24158.1.
AY341881 mRNA. Translation: AAQ24165.1.
AK032316 mRNA. Translation: BAC27809.1.
BC035298 mRNA. Translation: AAH35298.1.
RefSeqNP_705815.1. NM_153587.2.
XP_006516337.1. XM_006516274.1.
UniGeneMm.220417.
Mm.392855.

3D structure databases

ProteinModelPortalQ8C050.
SMRQ8C050. Positions 23-380, 414-793.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215759. 6 interactions.
IntActQ8C050. 2 interactions.
MINTMINT-4116279.
STRING10090.ENSMUSP00000042987.

PTM databases

PhosphoSiteQ8C050.

Proteomic databases

PaxDbQ8C050.
PRIDEQ8C050.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043599; ENSMUSP00000042987; ENSMUSG00000021180. [Q8C050-1]
GeneID73086.
KEGGmmu:73086.
UCSCuc007ost.1. mouse. [Q8C050-1]
uc007osu.1. mouse. [Q8C050-2]

Organism-specific databases

CTD9252.
MGIMGI:1920336. Rps6ka5.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110260.
HOGENOMHOG000233033.
HOVERGENHBG108317.
InParanoidQ8C050.
KOK04445.
OMAFQSHDKS.
OrthoDBEOG76HQ0Z.
PhylomeDBQ8C050.
TreeFamTF313438.

Gene expression databases

BgeeQ8C050.
CleanExMM_RPS6KA5.
GenevestigatorQ8C050.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016239. Ribosomal_S6_kinase_II.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 3 hits.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMSSF56112. SSF56112. 3 hits.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio337443.
PROQ8C050.
SOURCESearch...

Entry information

Entry nameKS6A5_MOUSE
AccessionPrimary (citable) accession number: Q8C050
Secondary accession number(s): Q8CI92
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 24, 2003
Last modified: April 16, 2014
This is version 120 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