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Protein

Tyrosine-protein kinase CSK

Gene

Csk

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

Functioni

Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK (By similarity).By similarity

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei222 – 2221ATPPROSITE-ProRule annotation
Active sitei314 – 3141Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi201 – 2099ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: HGNC
  • identical protein binding Source: MGI
  • non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  • protein tyrosine kinase activity Source: HGNC
  • receptor binding Source: GO_Central
  • transferase activity Source: HGNC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_306499. GAB1 signalosome.
REACT_309115. PD-1 signaling.
REACT_330010. Integrin alphaIIb beta3 signaling.
REACT_345471. Phosphorylation of CD3 and TCR zeta chains.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase CSK (EC:2.7.10.2)
Alternative name(s):
C-Src kinase
Protein-tyrosine kinase MPK-2
p50CSK
Gene namesi
Name:Csk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:88537. Csk.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: MGI
  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  • membrane raft Source: Ensembl
  • plasma membrane Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice die between day 9 and day 10 of gestation with several defects including a non-functional neural tube. SRC and FYN kinases show increased activity when CSK is missing.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 450449Tyrosine-protein kinase CSKPRO_0000088071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei184 – 1841PhosphotyrosineBy similarity
Modified residuei304 – 3041PhosphotyrosineBy similarity
Modified residuei364 – 3641Phosphoserine; by PKABy similarity
Modified residuei416 – 4161Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Phosphorylated at Ser-364 by PKA, leading to increased activity. Autophosphorylated (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41241.
PaxDbiP41241.
PRIDEiP41241.

PTM databases

PhosphoSiteiP41241.

Expressioni

Tissue specificityi

Ubiquitous, but most abundant in thymus and spleen, as well as in neonatal brain.

Gene expression databases

BgeeiP41241.
CleanExiMM_CSK.
GenevisibleiP41241. MM.

Interactioni

Subunit structurei

Homodimer (via SH3-domain) (By similarity). Interacts with PTPN22 (PubMed:8890164). Interacts with phosphorylated SIT1, PAG1, LIME1 and TGFB1I1; these interactions serve to recruit CSK to the membrane where it can phosphorylate and inhibit Src-family kinases (PubMed:9858471, PubMed:12218089, PubMed:12612075, PubMed:16166631). Interacts with SRCIN1 (By similarity). Interacts with RHOH (By similarity). Interacts (via SH2 domain) with SCIMP (By similarity).By similarity5 Publications

Protein-protein interaction databases

BioGridi198936. 9 interactions.
IntActiP41241. 6 interactions.
MINTiMINT-1345201.
STRINGi10090.ENSMUSP00000034863.

Structurei

Secondary structure

1
450
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 186Combined sources
Beta strandi35 – 417Combined sources
Beta strandi43 – 519Combined sources
Beta strandi57 – 615Combined sources
Helixi62 – 643Combined sources
Beta strandi65 – 673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JEGNMR-A1-83[»]
ProteinModelPortaliP41241.
SMRiP41241. Positions 4-450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41241.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 7062SH3PROSITE-ProRule annotationAdd
BLAST
Domaini82 – 17190SH2PROSITE-ProRule annotationAdd
BLAST
Domaini195 – 449255Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 7062Interaction with PTPN221 PublicationAdd
BLAST

Domaini

The architecture of this protein is similar to that of Src-family kinases (SFKs) with one N-terminal SH3 domain, one SH2 domain, and a C-terminal kinase domain.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP41241.
KOiK05728.
OMAiTRDPNWY.
OrthoDBiEOG7SV0V5.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P41241-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAIQAAWPS GTECIAKYNF HGTAEQDLPF CKGDVLTIVA VTKDPNWYKA
60 70 80 90 100
KNKVGREGII PANYVQKREG VKAGTKLSLM PWFHGKITRE QAERLLYPPE
110 120 130 140 150
TGLFLVREST NYPGDYTLCV SCEGKVEHYR IMYHASKLSI DEEVYFENLM
160 170 180 190 200
QLVEHYTTDA DGLCTRLIKP KVMEGTVAAQ DEFYRSGWAL NMKELKLLQT
210 220 230 240 250
IGKGEFGDVM LGDYRGNKVA VKCIKNDATA QAFLAEASVM TQLRHSNLVQ
260 270 280 290 300
LLGVIVEEKG GLYIVTEYMA KGSLVDYLRS RGRSVLGGDC LLKFSLDVCE
310 320 330 340 350
AMEYLEGNNF VHRDLAARNV LVSEDNVAKV SDFGLTKEAS STQDTGKLPV
360 370 380 390 400
KWTAPEALRE KKFSTKSDVW SFGILLWEIY SFGRVPYPRI PLKDVVPRVE
410 420 430 440 450
KGYKMDAPDG CPPAVYEVMK NCWHLDAATR PTFLQLREQL EHIKTHELHL
Length:450
Mass (Da):50,716
Last modified:July 27, 2011 - v2
Checksum:iE8D3EC9357B86277
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti299 – 2991C → L in AAA18766 (PubMed:7511815).Curated
Sequence conflicti417 – 4171E → D in AAA18766 (PubMed:7511815).Curated
Sequence conflicti423 – 4231W → S in AAA18766 (PubMed:7511815).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05247 mRNA. Translation: AAA18766.1.
AY902339 Genomic DNA. Translation: AAX90624.1.
AK156058 mRNA. Translation: BAE33565.1.
AK170815 mRNA. Translation: BAE42047.1.
BC018394 mRNA. Translation: AAH18394.1.
BC052006 mRNA. Translation: AAH52006.2.
X57242 mRNA. Translation: CAA40518.1.
CCDSiCCDS23228.1.
PIRiI48929.
RefSeqiNP_001291690.1. NM_001304761.1.
NP_031809.2. NM_007783.3.
XP_006510864.1. XM_006510801.2.
XP_006510865.1. XM_006510802.2.
UniGeneiMm.21974.

Genome annotation databases

EnsembliENSMUST00000034863; ENSMUSP00000034863; ENSMUSG00000032312.
GeneIDi12988.
KEGGimmu:12988.
UCSCiuc009pvk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05247 mRNA. Translation: AAA18766.1.
AY902339 Genomic DNA. Translation: AAX90624.1.
AK156058 mRNA. Translation: BAE33565.1.
AK170815 mRNA. Translation: BAE42047.1.
BC018394 mRNA. Translation: AAH18394.1.
BC052006 mRNA. Translation: AAH52006.2.
X57242 mRNA. Translation: CAA40518.1.
CCDSiCCDS23228.1.
PIRiI48929.
RefSeqiNP_001291690.1. NM_001304761.1.
NP_031809.2. NM_007783.3.
XP_006510864.1. XM_006510801.2.
XP_006510865.1. XM_006510802.2.
UniGeneiMm.21974.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JEGNMR-A1-83[»]
ProteinModelPortaliP41241.
SMRiP41241. Positions 4-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198936. 9 interactions.
IntActiP41241. 6 interactions.
MINTiMINT-1345201.
STRINGi10090.ENSMUSP00000034863.

PTM databases

PhosphoSiteiP41241.

Proteomic databases

MaxQBiP41241.
PaxDbiP41241.
PRIDEiP41241.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034863; ENSMUSP00000034863; ENSMUSG00000032312.
GeneIDi12988.
KEGGimmu:12988.
UCSCiuc009pvk.2. mouse.

Organism-specific databases

CTDi1445.
MGIiMGI:88537. Csk.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP41241.
KOiK05728.
OMAiTRDPNWY.
OrthoDBiEOG7SV0V5.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_306499. GAB1 signalosome.
REACT_309115. PD-1 signaling.
REACT_330010. Integrin alphaIIb beta3 signaling.
REACT_345471. Phosphorylation of CD3 and TCR zeta chains.

Miscellaneous databases

EvolutionaryTraceiP41241.
NextBioi282780.
PROiP41241.
SOURCEiSearch...

Gene expression databases

BgeeiP41241.
CleanExiMM_CSK.
GenevisibleiP41241. MM.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ctk: a protein-tyrosine kinase related to Csk that defines an enzyme family."
    Klages S., Adam D., Class K., Fargnoli J., Bolen J.B., Penhallow R.C.
    Proc. Natl. Acad. Sci. U.S.A. 91:2597-2601(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Characterization of quantitative trait loci influencing growth and adiposity using congenic mouse strains."
    Farber C.R., Corva P.M., Medrano J.F.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CAST/Ei.
    Tissue: Brain.
  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: NOD.
    Tissue: Spleen.
  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: C57BL/6 and FVB/N.
    Tissue: Brain and Colon.
  5. "An Eph-related receptor protein tyrosine kinase gene segmentally expressed in the developing mouse hindbrain."
    Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A., Wilkinson D.G., Charnay P.
    Oncogene 7:2499-2506(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 316-367.
    Strain: C57BL/6.
    Tissue: Embryonic brain.
  6. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 338-347, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  7. "Disruption of the csk gene, encoding a negative regulator of Src family tyrosine kinases, leads to neural tube defects and embryonic lethality in mice."
    Imamoto A., Soriano P.
    Cell 73:1117-1124(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. "Association of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cells."
    Cloutier J.-F., Veillette A.
    EMBO J. 15:4909-4918(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPN22.
  9. "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin."
    Thomas S.M., Hagel M., Turner C.E.
    J. Cell Sci. 112:181-190(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  10. "Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells."
    Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.
    J. Immunol. 169:2813-2817(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAG1.
  11. "Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor."
    Davidson D., Bakinowski M., Thomas M.L., Horejsi V., Veillette A.
    Mol. Cell. Biol. 23:2017-2028(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAG1.
  12. "Cbp deficiency alters Csk localization in lipid rafts but does not affect T-cell development."
    Xu S., Huo J., Tan J.E.-L., Lam K.-P.
    Mol. Cell. Biol. 25:8486-8495(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAG1, SUBCELLULAR LOCATION.
  13. "A novel, specific interaction involving the Csk SH3 domain and its natural ligand."
    Ghose R., Shekhtman A., Goger M.J., Ji H., Cowburn D.
    Nat. Struct. Biol. 8:998-1004(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-83.

Entry informationi

Entry nameiCSK_MOUSE
AccessioniPrimary (citable) accession number: P41241
Secondary accession number(s): Q03143, Q80WU4, Q8VCW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 158 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.