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P43404 (ZAP70_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase ZAP-70

EC=2.7.10.2
Alternative name(s):
70 kDa zeta-chain associated protein
Syk-related tyrosine kinase
Gene names
Name:Zap70
Synonyms:Srk, Zap-70
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length618 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. ZAP70 is also required for TCR-CD3Z internalization and degradation through interaction with the E3 ubiquitin-protein ligase CBL and adapter proteins SLA and SLA2. Thus, ZAP70 regulates both T-cell activation switch on and switch off by modulating TCR expression at the T-cell surface. During thymocyte development, ZAP70 promotes survival and cell-cycle progression of developing thymocytes before positive selection (when cells are still CD4/CD8 double negative). Additionally, ZAP70-dependent signaling pathway may also contribute to primary B-cells formation and activation through B-cell receptor (BCR). Ref.3 Ref.8 Ref.13 Ref.16

Catalytic activity

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

Enzyme regulation

Activated by phosphorylation at Tyr-492 in the activation loop.

Subunit structure

Interacts with CD3Z; this interaction docks ZAP70 at the stimulated TCR. Interacts with NFAM1. Interacts with adapter proteins SLA and SLA2; these interactions negatively regulates T-cell receptor signaling. Interacts with CBLB. Interacts with CBL; this interaction promotes ubiquitination, internalization and subsequent degradation of CD3Z. Identified in a complex with CBL and UBE2L3. Interacts with DEF6. Interacts (via SH2 domains) with RHOH; this interaction regulates ZAP70 subcellular localization. Interacts with FCRL3. Interacts with VAV1 By similarity. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein. Note: In quiescent T-lymphocytes, ZAP70 is cytoplasmic. Upon TCR activation, it is recruited at the plasma membrane by interacting with CD3Z. Colocalizes together with RHOH in the immunological synapse. RHOH is required for its proper localization to the cell membrane and cytoskeleton fractions in the thymocytes. Ref.3 Ref.15

Tissue specificity

Isoform 1 and isoform 2 are expressed in thymus, spleen and lymph nodes. Ref.3

Developmental stage

Isoform 2 is expressed in developing thymocytes from the CD44+CD25- stage up to mature T-cells. Isoform 1 is not expressed in thymocytes at the CD44+CD25- or CD44+CD25+ stages. Ref.3

Domain

Composed of 2 N-terminal SH2 domains and a C-terminal kinase domain. The tandem SH2 domains bind to the doubly phosphorylated tyrosine-based activation motif (ITAM) of CD247/CD3Z and the non-canonical phosphorylated tyrosine-based activation motif (TAM) of RHOH By similarity. The interdomain B located between the second SH2 and the kinase domain has been implicated in binding to other signaling molecules including CBL or VAV1. Thus, ZAP70 can also function as a scaffold by recruiting additional factors to the stimulated TCR complex By similarity. Ref.15

Post-translational modification

Phosphorylated on tyrosine residues upon T-cell antigen receptor (TCR) stimulation. Phosphorylation of Tyr-314 and Tyr-314 are essential for ZAP70 positive function on T-lymphocyte activation whereas Tyr-290 has a negative regulatory role. Within the C-terminal kinase domain, Tyr-491 and Tyr-492 are phosphorylated after TCR induction, Tyr-491 playing a negative regulatory role and Tyr-492 a positive. Tyr-492 is dephosphorylated by PTN22.

Disruption phenotype

Mice lack both CD4 and CD8 positive mature T-lymphocytes. Displays a complete block in B-Cell development at the pro-B cell stage in the absence of both SYK and ZAP70. Ref.8 Ref.13

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily.

Contains 1 protein kinase domain.

Contains 2 SH2 domains.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH2 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell receptor signaling pathway

Inferred from mutant phenotype Ref.2. Source: MGI

beta selection

Inferred from genetic interaction PubMed 9275205. Source: MGI

immune response

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from mutant phenotype Ref.8. Source: MGI

negative thymic T cell selection

Inferred from mutant phenotype Ref.8. Source: MGI

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 8798454. Source: MGI

positive regulation of T cell differentiation

Inferred from mutant phenotype Ref.2. Source: MGI

positive regulation of alpha-beta T cell differentiation

Inferred from mutant phenotype Ref.8Ref.2. Source: MGI

positive regulation of alpha-beta T cell proliferation

Inferred from genetic interaction PubMed 9275205. Source: MGI

positive regulation of calcium-mediated signaling

Inferred from mutant phenotype Ref.8Ref.2. Source: MGI

positive thymic T cell selection

Inferred from mutant phenotype Ref.8. Source: MGI

protein autophosphorylation

Inferred from direct assay PubMed 8798454. Source: MGI

protein phosphorylation

Inferred from direct assay PubMed 9169414. Source: MGI

thymic T cell selection

Inferred from mutant phenotype Ref.2. Source: MGI

   Cellular_componentT cell receptor complex

Inferred from sequence orthology PubMed 8176201. Source: MGI

cytoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 9182527. Source: MGI

immunological synapse

Inferred from direct assay Ref.15. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.15. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay PubMed 8798454. Source: MGI

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphotyrosine binding

Inferred from physical interaction Ref.1. Source: MGI

protein kinase activity

Inferred from direct assay PubMed 14738763. Source: MGI

protein tyrosine kinase activity

Inferred from direct assay PubMed 8798454PubMed 9169414. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P43404-1)

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.
Isoform 2 (identifier: P43404-2)

Also known as: TZK;

The sequence of this isoform differs from the canonical sequence as follows:
     1-306: Missing.
Isoform 3 (identifier: P43404-3)

Also known as: TZK-2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-309: Missing.
     310-360: DTSVYESPYS...VRQGVYRMRK → MAYGRVSGVS...MLSVASHLGR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 618618Tyrosine-protein kinase ZAP-70
PRO_0000088169

Regions

Domain10 – 10293SH2 1
Domain163 – 25492SH2 2
Domain337 – 597261Protein kinase
Nucleotide binding343 – 3519ATP By similarity
Region103 – 16260Interdomain A
Region255 – 33682Interdomain B

Sites

Active site4601Proton acceptor By similarity
Binding site3681ATP By similarity

Amino acid modifications

Modified residue2481Phosphotyrosine By similarity
Modified residue2871Phosphoserine By similarity
Modified residue2901Phosphotyrosine By similarity
Modified residue3141Phosphotyrosine; by LCK By similarity
Modified residue3181Phosphotyrosine By similarity
Modified residue4911Phosphotyrosine; by autocatalysis By similarity

Natural variations

Alternative sequence1 – 309309Missing in isoform 3.
VSP_031160
Alternative sequence1 – 306306Missing in isoform 2.
VSP_031159
Alternative sequence310 – 36051DTSVY…YRMRK → MAYGRVSGVSELSRVLYVPF PPPPFLSNPGVHDTRMYTQH AMLSVASHLGR in isoform 3.
VSP_031161
Natural variant4641R → C in ST; causes an absence of mature T-cells due to thymocyte development being arrested at the CD4+CD8+ stage. Ref.2

Experimental info

Sequence conflict1241R → C in AAA19250. Ref.1
Sequence conflict526 – 5294VTMW → GHHV in BAC67015. Ref.4
Sequence conflict5461E → Q in AAA19250. Ref.1
Sequence conflict5991L → P in AAA19250. Ref.1
Sequence conflict5991L → P in AAB36538. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 14, 2011. Version 3.
Checksum: 9E0D18B240B28392

FASTA61870,112
        10         20         30         40         50         60 
MPDPAAHLPF FYGSISRAEA EEHLKLAGMA DGLFLLRQCL RSLGGYVLSL VHDVRFHHFP 

        70         80         90        100        110        120 
IERQLNGTYA IAGGKAHCGP AELCQFYSQD PDGLPCNLRK PCNRPPGLEP QPGVFDCLRD 

       130        140        150        160        170        180 
AMVRDYVRQT WKLEGDALEQ AIISQAPQVE KLIATTAHER MPWYHSSLTR EEAERKLYSG 

       190        200        210        220        230        240 
QQTDGKFLLR PRKEQGTYAL SLVYGKTVYH YLISQDKAGK YCIPEGTKFD TLWQLVEYLK 

       250        260        270        280        290        300 
LKADGLIYRL KEVCPNSSAS AAVAAPTLPA HPSTFTQPQR RVDTLNSDGY TPEPARLASS 

       310        320        330        340        350        360 
TDKPRPMPMD TSVYESPYSD PEELKDKKLF LKRENLLVAD IELGCGNFGS VRQGVYRMRK 

       370        380        390        400        410        420 
KQIDVAIKVL KQGTEKADKD EMMREAQIMH QLDNPYIVRL IGVCQAEALM LVMEMAGGGP 

       430        440        450        460        470        480 
LHKFLLGKKE EIPVSNVAEL LHQVAMGMKY LEEKNFVHRD LAARNVLLVN RHYAKISDFG 

       490        500        510        520        530        540 
LSKALGADDS YYTARSAGKW PLKWYAPECI NFRKFSSRSD VWSYGVTMWE AFSYGQKPYK 

       550        560        570        580        590        600 
KMKGPEVLDF IKQGKRMECP PECPPEMYAL MSDCWIYKWE DRPDFLTVEQ RMRNYYYSLA 

       610 
SRAEGPPQCE QVAEAACG 

« Hide

Isoform 2 (TZK) [UniParc].

Checksum: 12CCA3AA2C3B1CF2
Show »

FASTA31235,883
Isoform 3 (TZK-2) [UniParc].

Checksum: D1A230395CA2AFE4
Show »

FASTA30935,255

References

« Hide 'large scale' references
[1]"Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: defining the nature of a signalling motif."
Gauen L.K.T., Zhu Y., Letourner F., Hu Q., Bolen J.B., Matis L.A., Klausner R.D., Shaw A.S.
Mol. Cell. Biol. 14:3729-3741(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Thymus.
[2]"A spontaneously arising mutation in the DLAARN motif of murine ZAP-70 abrogates kinase activity and arrests thymocyte development."
Wiest D.L., Ashe J.M., Howcroft T.K., Lee H.-M., Kemper D.M., Negishi I., Singer D.S., Singer A., Abe R.
Immunity 6:663-671(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ST CYS-464.
Strain: C57BL/6.
Tissue: Thymocyte.
[3]"Identification of a novel isoform of ZAP-70, truncated ZAP kinase."
Kuroyama H., Ikeda T., Kasai M., Yamasaki S., Tatsumi M., Utsuyama M., Saito T., Hirokawa K.
Biochem. Biophys. Res. Commun. 315:935-941(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: C57BL/6.
Tissue: Thymus.
[4]"Mouse TZK-2."
Ikeda T., Kuroyama H.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[5]"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. expand/collapse author list , 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] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Thymus.
[6]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[7]"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] (ISOFORM 1).
Strain: FVB/N.
Tissue: Salivary gland.
[8]"Essential role for ZAP-70 in both positive and negative selection of thymocytes."
Negishi I., Motoyama N., Nakayama K., Nakayama K., Senju S., Hatakeyama S., Zhang Q., Chan A.C., Loh D.Y.
Nature 376:435-438(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[9]"Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor signaling."
Sosinowski T., Pandey A., Dixit V.M., Weiss A.
J. Exp. Med. 191:463-474(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLA.
[10]"Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b."
Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T., Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M.
Nature 403:211-216(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBLB.
[11]"A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signaling."
Pandey A., Ibarrola N., Kratchmarova I., Fernandez M.M., Constantinescu S.N., Ohara O., Sawasdikosol S., Lodish H.F., Mann M.
J. Biol. Chem. 277:19131-19138(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLA2.
[12]"SWAP-70-like adapter of T cells, an adapter protein that regulates early TCR-initiated signaling in Th2 lineage cells."
Tanaka Y., Bi K., Kitamura R., Hong S., Altman Y., Matsumoto A., Tabata H., Lebedeva S., Bushway P.J., Altman A.
Immunity 18:403-414(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DEF6.
[13]"Unexpected requirement for ZAP-70 in pre-B cell development and allelic exclusion."
Schweighoffer E., Vanes L., Mathiot A., Nakamura T., Tybulewicz V.L.
Immunity 18:523-533(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[14]"NFAM1, an immunoreceptor tyrosine-based activation motif-bearing molecule that regulates B cell development and signaling."
Ohtsuka M., Arase H., Takeuchi A., Yamasaki S., Shiina R., Suenaga T., Sakurai D., Yokosuka T., Arase N., Iwashima M., Kitamura T., Moriya H., Saito T.
Proc. Natl. Acad. Sci. U.S.A. 101:8126-8131(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFAM1.
[15]"RhoH GTPase recruits and activates Zap70 required for T cell receptor signaling and thymocyte development."
Gu Y., Chae H.-D., Siefring J.E., Jasti A.C., Hildeman D.A., Williams D.A.
Nat. Immunol. 7:1182-1190(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RHOH, DOMAIN.
[16]"Distinct roles for Syk and ZAP-70 during early thymocyte development."
Palacios E.H., Weiss A.
J. Exp. Med. 204:1703-1715(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THYMOCYTE DEVELOPMENT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U04379 mRNA. Translation: AAA19250.1.
U77667 mRNA. Translation: AAB36538.1.
AB083210 mRNA. Translation: BAC43746.1.
AB084383 mRNA. Translation: BAC67015.1.
AK039883 mRNA. Translation: BAC30471.1.
AC084389 mRNA. No translation available.
BC029727 mRNA. Translation: AAH29727.1.
PIRI48914.
RefSeqNP_033565.2. NM_009539.3.
XP_006495959.1. XM_006495896.1.
UniGeneMm.8038.

3D structure databases

ProteinModelPortalP43404.
SMRP43404. Positions 1-605.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP43404. 3 interactions.
STRING10090.ENSMUSP00000027291.

Chemistry

ChEMBLCHEMBL2034801.

PTM databases

PhosphoSiteP43404.

Proteomic databases

PaxDbP43404.
PRIDEP43404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027291; ENSMUSP00000027291; ENSMUSG00000026117. [P43404-1]
GeneID22637.
KEGGmmu:22637.
UCSCuc007aqz.1. mouse. [P43404-1]

Organism-specific databases

CTD7535.
MGIMGI:99613. Zap70.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115195.
HOGENOMHOG000113264.
HOVERGENHBG001540.
InParanoidP43404.
KOK07360.
OMAMKGPEVI.
OrthoDBEOG7MWGWD.
TreeFamTF351629.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

BgeeP43404.
CleanExMM_ZAP70.
GenevestigatorP43404.

Family and domain databases

Gene3D1.10.930.10. 1 hit.
3.30.505.10. 2 hits.
InterProIPR011009. Kinase-like_dom.
IPR023420. Kinase_SYK/ZAP-70_inter-SH2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR012234. Tyr_kinase_non-rcpt_SYK/ZAP70.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PIRSFPIRSF000604. TyrPK_SYK. 1 hit.
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio303021.
PROP43404.
SOURCESearch...

Entry information

Entry nameZAP70_MOUSE
AccessionPrimary (citable) accession number: P43404
Secondary accession number(s): P97455, Q80VV2, Q8CHJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 14, 2011
Last modified: April 16, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot