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P11798

- KCC2A_MOUSE

UniProt

P11798 - KCC2A_MOUSE

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Protein

Calcium/calmodulin-dependent protein kinase type II subunit alpha

Gene

Camk2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Autophosphorylation of Thr-286 allows the kinase to switch from a calmodulin-dependent to a calmodulin-independent state.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421ATPPROSITE-ProRule annotation
Active sitei135 – 1351Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 279ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: UniProtKB-EC
  3. glutamate receptor binding Source: MGI
  4. protein serine/threonine kinase activity Source: MGI

GO - Biological processi

  1. calcium ion transport Source: MGI
  2. G1/S transition of mitotic cell cycle Source: MGI
  3. peptidyl-serine phosphorylation Source: MGI
  4. positive regulation of calcium ion transport Source: MGI
  5. positive regulation of cardiac muscle cell apoptotic process Source: MGI
  6. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  7. protein autophosphorylation Source: MGI
  8. regulation of mitochondrial membrane permeability involved in apoptotic process Source: MGI
  9. regulation of neuronal synaptic plasticity Source: MGI
  10. regulation of neurotransmitter secretion Source: MGI
  11. response to ischemia Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17. 3474.
ReactomeiREACT_198244. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_198246. CREB phosphorylation through the activation of Ras.
REACT_198248. CREB phosphorylation through the activation of CaMKII.
REACT_198660. Interferon gamma signaling.
REACT_213550. HSF1-dependent transactivation.
REACT_221970. Ca2+ pathway.
REACT_258217. Unblocking of NMDA receptor, glutamate binding and activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type II subunit alpha (EC:2.7.11.17)
Short name:
CaM kinase II subunit alpha
Short name:
CaMK-II subunit alpha
Gene namesi
Name:Camk2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:88256. Camk2a.

Subcellular locationi

Isoform Alpha KAP : Cytoplasm Curated. Cell junctionsynapsepresynaptic cell membrane By similarity. Cell junctionsynapse By similarity
Note: Postsynaptic lipid rafts.By similarity

GO - Cellular componenti

  1. calcium- and calmodulin-dependent protein kinase complex Source: UniProtKB
  2. cell junction Source: UniProtKB-KW
  3. mitochondrion Source: GOC
  4. nucleus Source: Ensembl
  5. plasma membrane Source: UniProtKB-KW
  6. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Calcium/calmodulin-dependent protein kinase type II subunit alphaPRO_0000086092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphotyrosine1 Publication
Modified residuei286 – 2861Phosphothreonine; by autocatalysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP11798.
PaxDbiP11798.
PRIDEiP11798.

PTM databases

PhosphoSiteiP11798.

Expressioni

Tissue specificityi

Isoform Alpha CaMKII is expressed in brain while isoform Alpha KAP is expressed in skeletal muscle.

Gene expression databases

BgeeiP11798.
ExpressionAtlasiP11798. baseline and differential.
GenevestigatoriP11798.

Interactioni

Subunit structurei

CAMK2 is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Interacts with BAALC, MPDZ, SYN1, CAMK2N2 and SYNGAP1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Actn2Q9JI913EBI-400384,EBI-299169
Bag6Q9Z1R23EBI-400402,EBI-644645
Dlg4Q621083EBI-400384,EBI-300895
Grin2bQ009603EBI-400384,EBI-396905From a different organism.
Grin2bQ010976EBI-400384,EBI-400125
Lrrc7P705872EBI-400384,EBI-7798464From a different organism.

Protein-protein interaction databases

BioGridi198461. 6 interactions.
DIPiDIP-31593N.
IntActiP11798. 26 interactions.
MINTiMINT-136541.

Structurei

Secondary structure

1
478
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni338 – 3403Combined sources
Helixi341 – 36222Combined sources
Helixi366 – 3727Combined sources
Beta strandi373 – 3808Combined sources
Helixi382 – 3843Combined sources
Beta strandi389 – 3924Combined sources
Helixi393 – 4008Combined sources
Helixi404 – 4063Combined sources
Beta strandi410 – 42112Combined sources
Beta strandi423 – 43715Combined sources
Beta strandi445 – 45814Combined sources
Beta strandi461 – 47212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HKXX-ray2.65A/B/C/D/E/F/G/H/I/J/K/L/M/N336-478[»]
ProteinModelPortaliP11798.
SMRiP11798. Positions 7-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11798.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 271259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 30011Calmodulin-bindingAdd
BLAST
Regioni310 – 32011Interaction with BAALCBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiP11798.
KOiK04515.
OMAiDHQDEEN.
OrthoDBiEOG7ZD1VM.
TreeFamiTF315229.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Alpha CaMKII (identifier: P11798-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MATITCTRFT EEYQLFEELG KGAFSVVRRC VKVLAGQEYA AKIINTKKLS
60 70 80 90 100
ARDHQKLERE ARICRLLKHP NIVRLHDSIS EEGHHYLIFD LVTGGELFED
110 120 130 140 150
IVAREYYSEA DASHCIQQIL EAVLHCHQMG VVHRDLKPEN LLLASKLKGA
160 170 180 190 200
AVKLADFGLA IEVEGEQQAW FGFAGTPGYL SPEVLRKDPY GKPVDLWACG
210 220 230 240 250
VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV TPEAKDLINK
260 270 280 290 300
MLTINPSKRI TAAEALKHPW ISHRSTVASC MHRQETVDCL KKFNARRKLK
310 320 330 340 350
GAILTTMLAT RNFSGGKSGG NKKNDGVKES SESTNTTIED EDTKVRKQEI
360 370 380 390 400
IKVTEQLIEA ISNGDFESYT KMCDPGMTAF EPEALGNLVE GLDFHRFYFE
410 420 430 440 450
NLWSRNSKPV HTTILNPHIH LMGDESACIA YIRITQYLDA GGIPRTAQSE
460 470
ETRVWHRRDG KWQIVHFHRS GAPSVLPH
Length:478
Mass (Da):54,115
Last modified:January 23, 2007 - v2
Checksum:i306F416CCE9B5F62
GO
Isoform Alpha KAP (identifier: P11798-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-289: Missing.
     290-314: LKKFNARRKLKGAILTTMLATRNFS → MLLFLTLWALVPCLVLLTLYFLSST
     328-328: K → KKRKSSSSVQLM

Note: Has no kinase activity.

Show »
Length:200
Mass (Da):22,584
Checksum:i3FB8D6A5C891CBD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401A → P in CAA32946. (PubMed:2543961)Curated
Sequence conflicti169 – 1691A → R in CAA32946. (PubMed:2543961)Curated
Sequence conflicti228 – 2281G → R in CAA32946. (PubMed:2543961)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 289289Missing in isoform Alpha KAP. 1 PublicationVSP_004767Add
BLAST
Alternative sequencei290 – 31425LKKFN…TRNFS → MLLFLTLWALVPCLVLLTLY FLSST in isoform Alpha KAP. 1 PublicationVSP_004768Add
BLAST
Alternative sequencei328 – 3281K → KKRKSSSSVQLM in isoform Alpha KAP. 1 PublicationVSP_004769

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14836 mRNA. Translation: CAA32946.1.
X87142 mRNA. Translation: CAA60620.1.
AK083245 mRNA. Translation: BAC38829.1.
BC031745 mRNA. Translation: AAH31745.1.
CCDSiCCDS29276.1. [P11798-1]
CCDS29277.1. [P11798-2]
PIRiJC6083.
S04365.
RefSeqiNP_001273738.1. NM_001286809.1.
NP_033922.1. NM_009792.3. [P11798-2]
NP_803126.1. NM_177407.4. [P11798-1]
UniGeneiMm.131530.
Mm.446530.

Genome annotation databases

EnsembliENSMUST00000102888; ENSMUSP00000099952; ENSMUSG00000024617. [P11798-1]
ENSMUST00000115295; ENSMUSP00000110950; ENSMUSG00000024617. [P11798-2]
GeneIDi12322.
KEGGimmu:12322.
UCSCiuc008fbg.2. mouse. [P11798-1]
uc008fbh.2. mouse. [P11798-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14836 mRNA. Translation: CAA32946.1 .
X87142 mRNA. Translation: CAA60620.1 .
AK083245 mRNA. Translation: BAC38829.1 .
BC031745 mRNA. Translation: AAH31745.1 .
CCDSi CCDS29276.1. [P11798-1 ]
CCDS29277.1. [P11798-2 ]
PIRi JC6083.
S04365.
RefSeqi NP_001273738.1. NM_001286809.1.
NP_033922.1. NM_009792.3. [P11798-2 ]
NP_803126.1. NM_177407.4. [P11798-1 ]
UniGenei Mm.131530.
Mm.446530.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HKX X-ray 2.65 A/B/C/D/E/F/G/H/I/J/K/L/M/N 336-478 [» ]
ProteinModelPortali P11798.
SMRi P11798. Positions 7-474.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198461. 6 interactions.
DIPi DIP-31593N.
IntActi P11798. 26 interactions.
MINTi MINT-136541.

Chemistry

BindingDBi P11798.

PTM databases

PhosphoSitei P11798.

Proteomic databases

MaxQBi P11798.
PaxDbi P11798.
PRIDEi P11798.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102888 ; ENSMUSP00000099952 ; ENSMUSG00000024617 . [P11798-1 ]
ENSMUST00000115295 ; ENSMUSP00000110950 ; ENSMUSG00000024617 . [P11798-2 ]
GeneIDi 12322.
KEGGi mmu:12322.
UCSCi uc008fbg.2. mouse. [P11798-1 ]
uc008fbh.2. mouse. [P11798-2 ]

Organism-specific databases

CTDi 815.
MGIi MGI:88256. Camk2a.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118944.
HOGENOMi HOG000233016.
HOVERGENi HBG108055.
InParanoidi P11798.
KOi K04515.
OMAi DHQDEEN.
OrthoDBi EOG7ZD1VM.
TreeFami TF315229.

Enzyme and pathway databases

BRENDAi 2.7.11.17. 3474.
Reactomei REACT_198244. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_198246. CREB phosphorylation through the activation of Ras.
REACT_198248. CREB phosphorylation through the activation of CaMKII.
REACT_198660. Interferon gamma signaling.
REACT_213550. HSF1-dependent transactivation.
REACT_221970. Ca2+ pathway.
REACT_258217. Unblocking of NMDA receptor, glutamate binding and activation.

Miscellaneous databases

ChiTaRSi Camk2a. mouse.
EvolutionaryTracei P11798.
NextBioi 280898.
PROi P11798.
SOURCEi Search...

Gene expression databases

Bgeei P11798.
ExpressionAtlasi P11798. baseline and differential.
Genevestigatori P11798.

Family and domain databases

InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24347. PTHR24347. 1 hit.
Pfami PF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the cDNA for the alpha subunit of calmodulin kinase II from mouse brain."
    Hanley R.M., Payne M.E., Cruzalegui F., Christenson M.A., Means A.R.
    Nucleic Acids Res. 17:3992-3992(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
    Tissue: Brain.
  2. "An alternative, nonkinase product of the brain-specifically expressed Ca2+/calmodulin-dependent kinase II alpha isoform gene in skeletal muscle."
    Bayer K.-U., Loehler J., Harbers K.
    Mol. Cell. Biol. 16:29-36(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA KAP).
    Strain: BALB/c.
    Tissue: Skeletal muscle.
  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].
    Strain: C57BL/6J.
    Tissue: Hippocampus.
  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].
    Tissue: Eye.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 9-21; 33-42; 135-146; 260-267; 301-311; 329-344; 353-371; 397-405; 434-445 AND 470-478, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiKCC2A_MOUSE
AccessioniPrimary (citable) accession number: P11798
Secondary accession number(s): Q61284, Q6ZWN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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