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P41241

- CSK_MOUSE

UniProt

P41241 - CSK_MOUSE

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Protein

Tyrosine-protein kinase CSK

Gene

Csk

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. ATP binding Source: HGNC
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  3. protein tyrosine kinase activity Source: HGNC
  4. transferase activity Source: HGNC

GO - Biological processi

  1. adherens junction organization Source: Ensembl
  2. brain development Source: Ensembl
  3. cellular response to peptide hormone stimulus Source: Ensembl
  4. immune system process Source: UniProtKB-KW
  5. intracellular signal transduction Source: HGNC
  6. negative regulation of bone resorption Source: Ensembl
  7. negative regulation of cell proliferation Source: MGI
  8. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
  9. negative regulation of Golgi to plasma membrane protein transport Source: Ensembl
  10. negative regulation of interleukin-6 production Source: Ensembl
  11. negative regulation of kinase activity Source: Ensembl
  12. negative regulation of low-density lipoprotein particle clearance Source: Ensembl
  13. negative regulation of phagocytosis Source: Ensembl
  14. oligodendrocyte differentiation Source: Ensembl
  15. peptidyl-tyrosine phosphorylation Source: GOC
  16. positive regulation of MAP kinase activity Source: Ensembl
  17. protein autophosphorylation Source: Ensembl
  18. protein phosphorylation Source: HGNC
  19. regulation of Fc receptor mediated stimulatory signaling pathway Source: Ensembl
  20. regulation of T cell activation Source: HGNC
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_206286. GAB1 signalosome.
REACT_216080. 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: Chromosome 9

Organism-specific databases

MGIiMGI:88537. Csk.

Subcellular locationi

Cytoplasm 1 Publication. Cell membrane 1 Publication
Note: Mainly cytoplasmic, also present in lipid rafts.

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. cytoplasm Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: Ensembl
  4. membrane raft Source: Ensembl
  5. 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

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.
GenevestigatoriP41241.

Interactioni

Subunit structurei

Homodimer (via SH3-domain). Interacts with PTPN8. 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. Interacts with SRCIN1. Interacts with RHOH. Interacts (via SH2 domain) with SCIMP By similarity.By similarity

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 PTPN8Add
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.
OMAiERLLCPP.
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:
EMBL
GenBank
DDBJ
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_031809.2. NM_007783.2.
XP_006510864.1. XM_006510801.1.
XP_006510865.1. XM_006510802.1.
XP_006510866.1. XM_006510803.1.
UniGeneiMm.21974.

Genome annotation databases

EnsembliENSMUST00000034863; ENSMUSP00000034863; ENSMUSG00000032312.
GeneIDi12988.
KEGGimmu:12988.
UCSCiuc009pvk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS23228.1.
PIRi I48929.
RefSeqi NP_031809.2. NM_007783.2.
XP_006510864.1. XM_006510801.1.
XP_006510865.1. XM_006510802.1.
XP_006510866.1. XM_006510803.1.
UniGenei Mm.21974.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JEG NMR - A 1-83 [» ]
ProteinModelPortali P41241.
SMRi P41241. Positions 4-450.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198936. 9 interactions.
IntActi P41241. 6 interactions.
MINTi MINT-1345201.

Chemistry

BindingDBi P41241.

PTM databases

PhosphoSitei P41241.

Proteomic databases

MaxQBi P41241.
PaxDbi P41241.
PRIDEi P41241.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034863 ; ENSMUSP00000034863 ; ENSMUSG00000032312 .
GeneIDi 12988.
KEGGi mmu:12988.
UCSCi uc009pvk.1. mouse.

Organism-specific databases

CTDi 1445.
MGIi MGI:88537. Csk.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119011.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi P41241.
KOi K05728.
OMAi ERLLCPP.
OrthoDBi EOG7SV0V5.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_206286. GAB1 signalosome.
REACT_216080. Phosphorylation of CD3 and TCR zeta chains.

Miscellaneous databases

EvolutionaryTracei P41241.
NextBioi 282780.
PROi P41241.
SOURCEi Search...

Gene expression databases

Bgeei P41241.
CleanExi MM_CSK.
Genevestigatori P41241.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. 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 ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. 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 ]
ProtoNeti Search...

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 PTPN8.
  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: October 29, 2014
This is version 149 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