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Q9Z2B5

- E2AK3_MOUSE

UniProt

Q9Z2B5 - E2AK3_MOUSE

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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

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 kinase activity Source: MGI
  4. 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
Complete GO annotation...

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

Enzyme and pathway databases

ReactomeiREACT_243361. PERK regulates gene expression.

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 510482LumenalSequence AnalysisAdd
BLAST
Transmembranei511 – 53121HelicalSequence AnalysisAdd
BLAST
Topological domaini532 – 1114583CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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

MaxQBiQ9Z2B5.
PaxDbiQ9Z2B5.
PRIDEiQ9Z2B5.

PTM databases

PhosphoSiteiQ9Z2B5.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

By ER stress.

Gene expression databases

BgeeiQ9Z2B5.
ExpressionAtlasiQ9Z2B5. baseline and differential.
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 – 5885Combined sources
Beta strandi589 – 5968Combined sources
Beta strandi601 – 6088Combined sources
Turni609 – 6113Combined sources
Beta strandi614 – 6218Combined sources
Turni625 – 6273Combined sources
Helixi628 – 63912Combined sources
Beta strandi650 – 6567Combined sources
Helixi661 – 6677Combined sources
Beta strandi881 – 8877Combined sources
Helixi894 – 8996Combined sources
Helixi904 – 9063Combined sources
Helixi909 – 92820Combined sources
Helixi938 – 9403Combined sources
Beta strandi941 – 9433Combined sources
Beta strandi949 – 9513Combined sources
Helixi986 – 9883Combined sources
Helixi991 – 9955Combined sources
Helixi1002 – 101615Combined sources
Helixi1022 – 103312Combined sources
Helixi1039 – 10446Combined sources
Helixi1046 – 105611Combined sources
Helixi1060 – 10623Combined sources
Helixi1066 – 10716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QD2X-ray2.81B583-1078[»]
ProteinModelPortaliQ9Z2B5.
SMRiQ9Z2B5. Positions 302-335, 583-668, 826-1103.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MERATRPGPR ALLLLLFLLL GCAAGISAVA PARSLLAPAS ETVFGLGAAA
60 70 80 90 100
APTSAARVPA VATAEVTVED AEALPAAAGE PESRATEPDD DVELRPRGRS
110 120 130 140 150
LVIISTLDGR IAALDAENDG KKQWDLDVGS GSLVSSSLSK PEVFGNKMII
160 170 180 190 200
PSLDGDLFQW DRDRESMEAV PFTVESLLES SYKFGDDVVL VGGKSLITYG
210 220 230 240 250
LSAYSGKLRY ICSALGCRRW DSDEMEEEED ILLLQRTQKT VRAVGPRSGS
260 270 280 290 300
EKWNFSVGHF ELRYIPDMET RAGFIESTFK PGGNKEDSKI ISDVEEQEAT
310 320 330 340 350
MLDTVIKVSV ADWKVMAFSR KGGRLEWEYQ FCTPIASAWL VRDGKVIPIS
360 370 380 390 400
LFDDTSYTAS EEALGDEEDI VEAARGATEN SVYLGMYRGQ LYLQSSVRVS
410 420 430 440 450
EKFPTSPKAL ESVNGENAII PLPTIKWKPL IHSPSRTPVL VGSDEFDKCL
460 470 480 490 500
SNDKYSHEEY SNGALSILQY PYDNGYYLPY YKRERNKRST QITVRFLDSP
510 520 530 540 550
HYSKNIRKKD PILLLHWWKE IFGTILLCIV ATTFIVRRLF HPQPHRQRKE
560 570 580 590 600
SETQCQTESK YDSVSADVSD NSWNDMKYSG YVSRYLTDFE PIQCMGRGGF
610 620 630 640 650
GVVFEAKNKV DDCNYAIKRI RLPNRELARE KVMREVKALA KLEHPGIVRY
660 670 680 690 700
FNAWLETPPE KWQEEMDEIW LKDESTDWPL SSPSPMDAPS VKIRRMDPFS
710 720 730 740 750
TKEQIEVIAP SPERSRSFSV GISCGQTSSS ESQFSPLEFS GTDCGDNSDS
760 770 780 790 800
ADAAYNLQDS CLTDCEDVED GTVDGNDEGH SFELCPSEAS PYTRSREGTS
810 820 830 840 850
SSIVFEDSGC GNASSKEEPR GNRLHDGNHY VNKLTDLKCS SSRSSSEATT
860 870 880 890 900
LSTSPTRPTT LSLDFTKNTV GQLQPSSPKV YLYIQMQLCR KENLKDWMNR
910 920 930 940 950
RCSLEDREHG VCLHIFLQIA EAVEFLHSKG LMHRDLKPSN IFFTMDDVVK
960 970 980 990 1000
VGDFGLVTAM DQDEEEQTVL TPMPAYATHT GQVGTKLYMS PEQIHGNNYS
1010 1020 1030 1040 1050
HKVDIFSLGL ILFELLYPFS TQMERVRILT DVRNLKFPLL FTQKYPQEHM
1060 1070 1080 1090 1100
MVQDMLSPSP TERPEATDII ENAIFENLEF PGKTVLRQRS RSMSSSGTKH
1110
SRQPSCSYSP LPGN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QD2 X-ray 2.81 B 583-1078 [» ]
ProteinModelPortali Q9Z2B5.
SMRi Q9Z2B5. Positions 302-335, 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

MaxQBi Q9Z2B5.
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.

Enzyme and pathway databases

Reactomei REACT_243361. PERK regulates gene expression.

Miscellaneous databases

PROi Q9Z2B5.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z2B5.
ExpressionAtlasi Q9Z2B5. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 138 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