P43404 (ZAP70_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	618 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Co-localizes 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 process	Adaptive immunity Immunity
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH2 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T 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: Compara 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 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
Cellular_component	T cell receptor complex Inferred from sequence orthology PubMed 8176201. Source: MGI cytosol Inferred from direct assay PubMed 9182527. Source: MGI immunological synapse Inferred from direct assay Ref.15. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay PubMed 8798454. Source: MGI non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 618	618	Tyrosine-protein kinase ZAP-70		PRO_0000088169
Regions
	Domain	10 – 102	93	SH2 1
	Domain	163 – 254	92	SH2 2
	Domain	337 – 597	261	Protein kinase
	Nucleotide binding	343 – 351	9	ATP By similarity
	Region	103 – 162	60	Interdomain A
	Region	255 – 336	82	Interdomain B
Sites
	Active site	460	1	Proton acceptor By similarity
	Binding site	368	1	ATP By similarity
Amino acid modifications
	Modified residue	248	1	Phosphotyrosine By similarity
	Modified residue	287	1	Phosphoserine By similarity
	Modified residue	290	1	Phosphotyrosine By similarity
	Modified residue	314	1	Phosphotyrosine; by LCK By similarity
	Modified residue	318	1	Phosphotyrosine By similarity
	Modified residue	491	1	Phosphotyrosine; by autocatalysis By similarity
Natural variations
	Alternative sequence	1 – 309	309	Missing in isoform 3.		VSP_031160
	Alternative sequence	1 – 306	306	Missing in isoform 2.		VSP_031159
	Alternative sequence	310 – 360	51	DTSVY…YRMRK → MAYGRVSGVSELSRVLYVPF PPPPFLSNPGVHDTRMYTQH AMLSVASHLGR in isoform 3.		VSP_031161
	Natural variant	464	1	R → 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 conflict	124	1	R → C in AAA19250. Ref.1
	Sequence conflict	526 – 529	4	VTMW → GHHV in BAC67015. Ref.4
	Sequence conflict	546	1	E → Q in AAA19250. Ref.1
	Sequence conflict	599	1	L → P in AAA19250. Ref.1
	Sequence conflict	599	1	L → P in AAB36538. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 14, 2011. Version 3. Checksum: 9E0D18B240B28392	FASTA	618	70,112
	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
	Isoform 2 (TZK) [UniParc]. Checksum: 12CCA3AA2C3B1CF2	FASTA	312	35,883
	10 20 30 40 50 60 MPMDTSVYES PYSDPEELKD KKLFLKRENL LVADIELGCG NFGSVRQGVY RMRKKQIDVA 70 80 90 100 110 120 IKVLKQGTEK ADKDEMMREA QIMHQLDNPY IVRLIGVCQA EALMLVMEMA GGGPLHKFLL 130 140 150 160 170 180 GKKEEIPVSN VAELLHQVAM GMKYLEEKNF VHRDLAARNV LLVNRHYAKI SDFGLSKALG 190 200 210 220 230 240 ADDSYYTARS AGKWPLKWYA PECINFRKFS SRSDVWSYGV TMWEAFSYGQ KPYKKMKGPE 250 260 270 280 290 300 VLDFIKQGKR MECPPECPPE MYALMSDCWI YKWEDRPDFL TVEQRMRNYY YSLASRAEGP 310 PQCEQVAEAA CG
	Isoform 3 (TZK-2) [UniParc]. Checksum: D1A230395CA2AFE4	FASTA	309	35,255
	10 20 30 40 50 60 MAYGRVSGVS ELSRVLYVPF PPPPFLSNPG VHDTRMYTQH AMLSVASHLG RKQIDVAIKV 70 80 90 100 110 120 LKQGTEKADK DEMMREAQIM HQLDNPYIVR LIGVCQAEAL MLVMEMAGGG PLHKFLLGKK 130 140 150 160 170 180 EEIPVSNVAE LLHQVAMGMK YLEEKNFVHR DLAARNVLLV NRHYAKISDF GLSKALGADD 190 200 210 220 230 240 SYYTARSAGK WPLKWYAPEC INFRKFSSRS DVWSYGVTMW EAFSYGQKPY KKMKGPEVLD 250 260 270 280 290 300 FIKQGKRMEC PPECPPEMYA LMSDCWIYKW EDRPDFLTVE QRMRNYYYSL ASRAEGPPQC EQVAEAACG

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00331216. IPI00403592. IPI00885341.
PIR	I48914.
RefSeq	NP_033565.2. NM_009539.2.
UniGene	Mm.8038.
3D structure databases
ProteinModelPortal	P43404.
SMR	P43404. Positions 1-605.
ModBase	Search...
Protein-protein interaction databases
IntAct	P43404. 1 interaction.
STRING	10090.ENSMUSP00000027291.
PTM databases
PhosphoSite	P43404.
Proteomic databases
PaxDb	P43404.
PRIDE	P43404.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027291; ENSMUSP00000027291; ENSMUSG00000026117.
GeneID	22637.
KEGG	mmu:22637.
UCSC	uc007aqz.1. mouse. uc007ara.1. mouse. uc007arb.1. mouse.
Organism-specific databases
CTD	7535.
MGI	MGI:99613. Zap70.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00620000087791.
HOGENOM	HOG000113264.
HOVERGEN	HBG001540.
InParanoid	P43404.
KO	K07360.
OMA	PAHPSTF.
OrthoDB	EOG4NZTSX.
Enzyme and pathway databases
BRENDA	2.7.10.2. 3474.
Gene expression databases
Bgee	P43404.
CleanEx	MM_ZAP70.
Genevestigator	P43404.
GermOnline	ENSMUSG00000026117. Mus musculus.
Family and domain databases
Gene3D	1.10.930.10. 1 hit. 3.30.505.10. 2 hits.
InterPro	IPR011009. Kinase-like_dom. IPR023420. Kinase_SYK/ZAP-70_inter-SH2. IPR000719. Prot_kinase_cat_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]
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 2 hits. [Graphical view]
PIRSF	PIRSF000604. TyrPK_SYK. 1 hit.
PRINTS	PR00401. SH2DOMAIN. PR00109. TYRKINASE.
SMART	SM00252. SH2. 2 hits. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50001. SH2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	303021.
SOURCE	Search...

Entry information

Entry name

ZAP70_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program