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Q9Z2B5

- E2AK3_MOUSE

UniProt

Q9Z2B5 - E2AK3_MOUSE

Protein

Eukaryotic translation initiation factor 2-alpha kinase 3

Gene

Eif2ak3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Perturbation in protein folding in the endoplasmic reticulum (ER) promotes reversible dissociation from HSPA5/BIP and oligomerization, resulting in transautophosphorylation and kinase activity induction.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei618 – 6181ATP
    Active sitei935 – 9351Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi595 – 6039ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. eukaryotic translation initiation factor 2alpha kinase activity Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein kinase activity Source: MGI
    5. protein serine/threonine kinase activity Source: MGI

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    2. bone mineralization Source: MGI
    3. calcium-mediated signaling Source: MGI
    4. chondrocyte development Source: MGI
    5. endocrine pancreas development Source: UniProtKB
    6. endoplasmic reticulum organization Source: MGI
    7. endoplasmic reticulum unfolded protein response Source: UniProtKB
    8. ER overload response Source: UniProtKB
    9. fat cell differentiation Source: MGI
    10. insulin-like growth factor receptor signaling pathway Source: MGI
    11. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: MGI
    12. lactation Source: MGI
    13. negative regulation of apoptotic process Source: MGI
    14. negative regulation of gene expression Source: MGI
    15. negative regulation of myelination Source: MGI
    16. negative regulation of translation Source: MGI
    17. ossification Source: UniProtKB
    18. pancreas development Source: MGI
    19. positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: MGI
    20. positive regulation of protein binding Source: MGI
    21. positive regulation of signal transduction Source: MGI
    22. protein autophosphorylation Source: UniProtKB
    23. protein homooligomerization Source: UniProtKB
    24. protein phosphorylation Source: MGI
    25. regulation of fatty acid metabolic process Source: MGI
    26. skeletal system development Source: MGI
    27. SREBP signaling pathway Source: MGI
    28. translation Source: MGI

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Stress response, Translation regulation, Unfolded protein response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 2-alpha kinase 3 (EC:2.7.11.1)
    Alternative name(s):
    PRKR-like endoplasmic reticulum kinase
    Pancreatic eIF2-alpha kinase
    Gene namesi
    Name:Eif2ak3
    Synonyms:Pek, Perk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1341830. Eif2ak3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. endoplasmic reticulum Source: MGI
    3. endoplasmic reticulum membrane Source: MGI
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi618 – 6181K → A: Loss of activity and autophosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 11141086Eukaryotic translation initiation factor 2-alpha kinase 3PRO_0000024323Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi254 – 2541N-linked (GlcNAc...)
    Modified residuei615 – 6151PhosphotyrosineBy similarity
    Modified residuei711 – 7111PhosphoserineBy similarity
    Modified residuei980 – 9801Phosphothreonine1 Publication
    Modified residuei1092 – 10921PhosphoserineBy similarity

    Post-translational modificationi

    Autophosphorylated. Phosphorylated at Tyr-615 following endoplasmic reticulum stress, leading to activate its tyrosine-protein kinase activity. Dephosphorylated by PTPN1/TP1B, leading to inactivate its enzyme activity By similarity. Oligomerization of the N-terminal ER luminal domain by ER stress promotes PERK trans-autophosphorylation of the C-terminal cytoplasmic kinase domain at multiple residues including Thr-980 on the kinase activation loop.By similarity1 Publication
    N-glycosylated.
    ADP-ribosylated by PARP16 upon ER stress, which increases kinase activity.By similarity

    Keywords - PTMi

    ADP-ribosylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ9Z2B5.
    PRIDEiQ9Z2B5.

    PTM databases

    PhosphoSiteiQ9Z2B5.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Inductioni

    By ER stress.

    Gene expression databases

    ArrayExpressiQ9Z2B5.
    BgeeiQ9Z2B5.
    GenevestigatoriQ9Z2B5.

    Interactioni

    Subunit structurei

    Forms dimers with HSPA5/BIP in resting cells. Oligomerizes in ER-stressed cells. Interacts with DNAJC3 and MFN2.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279585EBI-1226344,EBI-6904269From a different organism.
    EIF2S1P051984EBI-1226344,EBI-1056162From a different organism.
    Mfn2Q80U632EBI-1226344,EBI-8437663

    Protein-protein interaction databases

    IntActiQ9Z2B5. 3 interactions.
    STRINGi10090.ENSMUSP00000034093.

    Structurei

    Secondary structure

    1
    1114
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi584 – 5885
    Beta strandi589 – 5968
    Beta strandi601 – 6088
    Turni609 – 6113
    Beta strandi614 – 6218
    Turni625 – 6273
    Helixi628 – 63912
    Beta strandi650 – 6567
    Helixi661 – 6677
    Beta strandi881 – 8877
    Helixi894 – 8996
    Helixi904 – 9063
    Helixi909 – 92820
    Helixi938 – 9403
    Beta strandi941 – 9433
    Beta strandi949 – 9513
    Helixi986 – 9883
    Helixi991 – 9955
    Helixi1002 – 101615
    Helixi1022 – 103312
    Helixi1039 – 10446
    Helixi1046 – 105611
    Helixi1060 – 10623
    Helixi1066 – 10716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QD2X-ray2.81B583-1078[»]
    ProteinModelPortaliQ9Z2B5.
    SMRiQ9Z2B5. Positions 99-213, 583-668, 826-1103.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 510482LumenalSequence AnalysisAdd
    BLAST
    Topological domaini532 – 1114583CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei511 – 53121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini589 – 1075487Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi48 – 514Poly-Ala
    Compositional biasi224 – 2296Poly-Glu

    Domaini

    The lumenal domain senses perturbations in protein folding in the ER, probably through reversible interaction with HSPA5/BIP.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00530000062984.
    HOGENOMiHOG000112308.
    HOVERGENiHBG051431.
    InParanoidiQ9Z2B5.
    PhylomeDBiQ9Z2B5.

    Family and domain databases

    Gene3Di2.140.10.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 2 hits.
    [Graphical view]
    SUPFAMiSSF50998. SSF50998. 2 hits.
    SSF56112. SSF56112. 2 hits.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Z2B5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERATRPGPR ALLLLLFLLL GCAAGISAVA PARSLLAPAS ETVFGLGAAA     50
    APTSAARVPA VATAEVTVED AEALPAAAGE PESRATEPDD DVELRPRGRS 100
    LVIISTLDGR IAALDAENDG KKQWDLDVGS GSLVSSSLSK PEVFGNKMII 150
    PSLDGDLFQW DRDRESMEAV PFTVESLLES SYKFGDDVVL VGGKSLITYG 200
    LSAYSGKLRY ICSALGCRRW DSDEMEEEED ILLLQRTQKT VRAVGPRSGS 250
    EKWNFSVGHF ELRYIPDMET RAGFIESTFK PGGNKEDSKI ISDVEEQEAT 300
    MLDTVIKVSV ADWKVMAFSR KGGRLEWEYQ FCTPIASAWL VRDGKVIPIS 350
    LFDDTSYTAS EEALGDEEDI VEAARGATEN SVYLGMYRGQ LYLQSSVRVS 400
    EKFPTSPKAL ESVNGENAII PLPTIKWKPL IHSPSRTPVL VGSDEFDKCL 450
    SNDKYSHEEY SNGALSILQY PYDNGYYLPY YKRERNKRST QITVRFLDSP 500
    HYSKNIRKKD PILLLHWWKE IFGTILLCIV ATTFIVRRLF HPQPHRQRKE 550
    SETQCQTESK YDSVSADVSD NSWNDMKYSG YVSRYLTDFE PIQCMGRGGF 600
    GVVFEAKNKV DDCNYAIKRI RLPNRELARE KVMREVKALA KLEHPGIVRY 650
    FNAWLETPPE KWQEEMDEIW LKDESTDWPL SSPSPMDAPS VKIRRMDPFS 700
    TKEQIEVIAP SPERSRSFSV GISCGQTSSS ESQFSPLEFS GTDCGDNSDS 750
    ADAAYNLQDS CLTDCEDVED GTVDGNDEGH SFELCPSEAS PYTRSREGTS 800
    SSIVFEDSGC GNASSKEEPR GNRLHDGNHY VNKLTDLKCS SSRSSSEATT 850
    LSTSPTRPTT LSLDFTKNTV GQLQPSSPKV YLYIQMQLCR KENLKDWMNR 900
    RCSLEDREHG VCLHIFLQIA EAVEFLHSKG LMHRDLKPSN IFFTMDDVVK 950
    VGDFGLVTAM DQDEEEQTVL TPMPAYATHT GQVGTKLYMS PEQIHGNNYS 1000
    HKVDIFSLGL ILFELLYPFS TQMERVRILT DVRNLKFPLL FTQKYPQEHM 1050
    MVQDMLSPSP TERPEATDII ENAIFENLEF PGKTVLRQRS RSMSSSGTKH 1100
    SRQPSCSYSP LPGN 1114
    Length:1,114
    Mass (Da):124,682
    Last modified:May 1, 1999 - v1
    Checksum:i65A47D6C0DD2E046
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 15210VFGNKMIIPS → GTHKTSSKEC in BAB26908. (PubMed:16141072)Curated
    Sequence conflicti826 – 8261Missing in BAB22655. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076681 mRNA. Translation: AAD03337.1.
    AK010397 mRNA. Translation: BAB26908.1.
    AK003226 mRNA. Translation: BAB22655.1.
    CCDSiCCDS20223.1.
    PIRiT14351.
    UniGeneiMm.247167.

    Genome annotation databases

    EnsembliENSMUST00000162950; ENSMUSP00000123759; ENSMUSG00000031668.
    UCSCiuc009cgc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076681 mRNA. Translation: AAD03337.1 .
    AK010397 mRNA. Translation: BAB26908.1 .
    AK003226 mRNA. Translation: BAB22655.1 .
    CCDSi CCDS20223.1.
    PIRi T14351.
    UniGenei Mm.247167.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QD2 X-ray 2.81 B 583-1078 [» ]
    ProteinModelPortali Q9Z2B5.
    SMRi Q9Z2B5. Positions 99-213, 583-668, 826-1103.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9Z2B5. 3 interactions.
    STRINGi 10090.ENSMUSP00000034093.

    PTM databases

    PhosphoSitei Q9Z2B5.

    Proteomic databases

    PaxDbi Q9Z2B5.
    PRIDEi Q9Z2B5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000162950 ; ENSMUSP00000123759 ; ENSMUSG00000031668 .
    UCSCi uc009cgc.1. mouse.

    Organism-specific databases

    MGIi MGI:1341830. Eif2ak3.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00530000062984.
    HOGENOMi HOG000112308.
    HOVERGENi HBG051431.
    InParanoidi Q9Z2B5.
    PhylomeDBi Q9Z2B5.

    Miscellaneous databases

    PROi Q9Z2B5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z2B5.
    Bgeei Q9Z2B5.
    Genevestigatori Q9Z2B5.

    Family and domain databases

    Gene3Di 2.140.10.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50998. SSF50998. 2 hits.
    SSF56112. SSF56112. 2 hits.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase."
      Harding H.P., Zhang Y., Ron D.
      Nature 397:271-274(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-618.
      Strain: NIH Swiss.
      Tissue: Fibroblast.
    2. Erratum
      Harding H.P., Zhang Y., Ron D.
      Nature 398:90-90(1999)
    3. "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 1-152 AND 769-1114.
      Strain: C57BL/6J.
    4. "Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response."
      Bertolotti A., Zhang Y., Hendershot L.M., Harding H.P., Ron D.
      Nat. Cell Biol. 2:326-332(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    5. "PERK mediates cell-cycle exit during the mammalian unfolded protein response."
      Brewer J.W., Diehl J.A.
      Proc. Natl. Acad. Sci. U.S.A. 97:12625-12630(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK."
      Yan W., Frank C.L., Korth M.J., Sopher B.L., Novoa I., Ron D., Katze M.G.
      Proc. Natl. Acad. Sci. U.S.A. 99:15920-15925(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAJC3.
    7. Cited for: FUNCTION, INTERACTION WITH MFN2.
    8. "The structure of the PERK kinase domain suggests the mechanism for its activation."
      Cui W., Li J., Ron D., Sha B.
      Acta Crystallogr. D 67:423-428(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 583-701 AND 867-1078, SUBUNIT, PHOSPHORYLATION AT THR-980.

    Entry informationi

    Entry nameiE2AK3_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2B5
    Secondary accession number(s): Q9CTK8, Q9CWT5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3