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Tyrosine-protein kinase ZAP-70 (EC 2.7.10.2) (70 kDa zeta-chain associated protein) (Syk-related tyrosine kinase)

 ZAP70_MOUSE             Reviewed;         618 AA.
P43404; P97455; Q80VV2; Q8CHJ3;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 3.
20-JUN-2018, entry version 172.
RecName: Full=Tyrosine-protein kinase ZAP-70;
EC=2.7.10.2;
AltName: Full=70 kDa zeta-chain associated protein;
AltName: Full=Syk-related tyrosine kinase;
Name=Zap70; Synonyms=Srk, Zap-70;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Thymus;
PubMed=8196616; DOI=10.1128/MCB.14.6.3729;
Gauen L.K.T., Zhu Y., Letourner F., Hu Q., Bolen J.B., Matis L.A.,
Klausner R.D., Shaw A.S.;
"Interactions of p59fyn and ZAP-70 with T-cell receptor activation
motifs: defining the nature of a signalling motif.";
Mol. Cell. Biol. 14:3729-3741(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ST CYS-464.
STRAIN=C57BL/6J; TISSUE=Thymocyte;
PubMed=9208839; DOI=10.1016/S1074-7613(00)80442-2;
Wiest D.L., Ashe J.M., Howcroft T.K., Lee H.-M., Kemper D.M.,
Negishi I., Singer D.S., Singer A., Abe R.;
"A spontaneously arising mutation in the DLAARN motif of murine ZAP-70
abrogates kinase activity and arrests thymocyte development.";
Immunity 6:663-671(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=14985102; DOI=10.1016/j.bbrc.2004.01.127;
Kuroyama H., Ikeda T., Kasai M., Yamasaki S., Tatsumi M., Utsuyama M.,
Saito T., Hirokawa K.;
"Identification of a novel isoform of ZAP-70, truncated ZAP kinase.";
Biochem. Biophys. Res. Commun. 315:935-941(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Ikeda T., Kuroyama H.;
"Mouse TZK-2.";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=7630421; DOI=10.1038/376435a0;
Negishi I., Motoyama N., Nakayama K., Nakayama K., Senju S.,
Hatakeyama S., Zhang Q., Chan A.C., Loh D.Y.;
"Essential role for ZAP-70 in both positive and negative selection of
thymocytes.";
Nature 376:435-438(1995).
[9]
INTERACTION WITH SLA.
PubMed=10662792; DOI=10.1084/jem.191.3.463;
Sosinowski T., Pandey A., Dixit V.M., Weiss A.;
"Src-like adaptor protein (SLAP) is a negative regulator of T cell
receptor signaling.";
J. Exp. Med. 191:463-474(2000).
[10]
INTERACTION WITH CBLB.
PubMed=10646608; DOI=10.1038/35003228;
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.;
"Negative regulation of lymphocyte activation and autoimmunity by the
molecular adaptor Cbl-b.";
Nature 403:211-216(2000).
[11]
INTERACTION WITH SLA2.
PubMed=11891219; DOI=10.1074/jbc.M110318200;
Pandey A., Ibarrola N., Kratchmarova I., Fernandez M.M.,
Constantinescu S.N., Ohara O., Sawasdikosol S., Lodish H.F., Mann M.;
"A novel Src homology 2 domain-containing molecule, Src-like adapter
protein-2 (SLAP-2), which negatively regulates T cell receptor
signaling.";
J. Biol. Chem. 277:19131-19138(2002).
[12]
INTERACTION WITH DEF6.
PubMed=12648457; DOI=10.1016/S1074-7613(03)00054-2;
Tanaka Y., Bi K., Kitamura R., Hong S., Altman Y., Matsumoto A.,
Tabata H., Lebedeva S., Bushway P.J., Altman A.;
"SWAP-70-like adapter of T cells, an adapter protein that regulates
early TCR-initiated signaling in Th2 lineage cells.";
Immunity 18:403-414(2003).
[13]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12705855; DOI=10.1016/S1074-7613(03)00082-7;
Schweighoffer E., Vanes L., Mathiot A., Nakamura T., Tybulewicz V.L.;
"Unexpected requirement for ZAP-70 in pre-B cell development and
allelic exclusion.";
Immunity 18:523-533(2003).
[14]
INTERACTION WITH NFAM1.
PubMed=15143214; DOI=10.1073/pnas.0401119101;
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.;
"NFAM1, an immunoreceptor tyrosine-based activation motif-bearing
molecule that regulates B cell development and signaling.";
Proc. Natl. Acad. Sci. U.S.A. 101:8126-8131(2004).
[15]
SUBCELLULAR LOCATION, INTERACTION WITH RHOH, AND DOMAIN.
PubMed=17028588; DOI=10.1038/ni1396;
Gu Y., Chae H.-D., Siefring J.E., Jasti A.C., Hildeman D.A.,
Williams D.A.;
"RhoH GTPase recruits and activates Zap70 required for T cell receptor
signaling and thymocyte development.";
Nat. Immunol. 7:1182-1190(2006).
[16]
FUNCTION IN THYMOCYTE DEVELOPMENT.
PubMed=17606633; DOI=10.1084/jem.20070405;
Palacios E.H., Weiss A.;
"Distinct roles for Syk and ZAP-70 during early thymocyte
development.";
J. Exp. Med. 204:1703-1715(2007).
[17]
FUNCTION, INTERACTION WITH OTUD7B AND UBASH3B, UBIQUITINATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=26903241; DOI=10.1084/jem.20151426;
Hu H., Wang H., Xiao Y., Jin J., Chang J.H., Zou Q., Xie X., Cheng X.,
Sun S.C.;
"Otud7b facilitates T cell activation and inflammatory responses by
regulating Zap70 ubiquitination.";
J. Exp. Med. 213:399-414(2016).
-!- 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).
{ECO:0000269|PubMed:12705855, ECO:0000269|PubMed:14985102,
ECO:0000269|PubMed:17606633, ECO:0000269|PubMed:26903241,
ECO:0000269|PubMed:7630421}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Activated by phosphorylation at Tyr-492 in the
activation loop.
-!- SUBUNIT: Interacts with CD247/CD3Z; this interaction docks ZAP70
at the stimulated TCR (By similarity). Interacts with NFAM1
(PubMed:15143214). Interacts with adapter protein SLA; this
interaction negatively regulates T-cell receptor signaling
(PubMed:10662792). Interacts with VAV1 (By similarity). Interacts
with CBL; this interaction promotes ubiquitination,
internalization and subsequent degradation of CD247/CD3Z (By
similarity). Identified in a complex with CBL and UBE2L3 (By
similarity). Interacts with SHB (By similarity). Interacts with
adapter protein SLA2; this interaction negatively regulates T-cell
receptor signaling (PubMed:11891219). Interacts with CBLB
(PubMed:10646608). Interacts (via SH2 domains) with RHOH; this
interaction regulates ZAP70 subcellular localization
(PubMed:17028588). Interacts with DEF6 (PubMed:12648457).
Interacts (ubiquitinated form) with OTUD7B and UBASH3B
(PubMed:26903241). {ECO:0000250|UniProtKB:P43403,
ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10662792,
ECO:0000269|PubMed:11891219, ECO:0000269|PubMed:12648457,
ECO:0000269|PubMed:15143214, ECO:0000269|PubMed:17028588,
ECO:0000269|PubMed:26903241}.
-!- INTERACTION:
P24161:Cd247; NbExp=4; IntAct=EBI-3862932, EBI-7803400;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P43404-1; Sequence=Displayed;
Name=2; Synonyms=TZK;
IsoId=P43404-2; Sequence=VSP_031159;
Name=3; Synonyms=TZK-2;
IsoId=P43404-3; Sequence=VSP_031160, VSP_031161;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in
thymus, spleen and lymph nodes. {ECO:0000269|PubMed:14985102}.
-!- 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. {ECO:0000269|PubMed:14985102}.
-!- 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).
{ECO:0000250}.
-!- PTM: 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.
-!- PTM: Ubiquitinated in response to T cell activation.
Deubiquitinated by OTUD7B. {ECO:0000269|PubMed:26903241}.
-!- 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.
{ECO:0000269|PubMed:12705855, ECO:0000269|PubMed:7630421}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SYK/ZAP-70 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; U04379; AAA19250.1; -; mRNA.
EMBL; U77667; AAB36538.1; -; mRNA.
EMBL; AB083210; BAC43746.1; -; mRNA.
EMBL; AB084383; BAC67015.1; -; mRNA.
EMBL; AK039883; BAC30471.1; -; mRNA.
EMBL; AC084389; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC029727; AAH29727.1; -; mRNA.
CCDS; CCDS14888.1; -. [P43404-1]
PIR; I48914; I48914.
RefSeq; NP_001276541.1; NM_001289612.1. [P43404-2]
RefSeq; NP_001276694.1; NM_001289765.1. [P43404-1]
RefSeq; NP_033565.2; NM_009539.3. [P43404-1]
RefSeq; XP_006495959.1; XM_006495896.2. [P43404-1]
UniGene; Mm.8038; -.
ProteinModelPortal; P43404; -.
SMR; P43404; -.
BioGrid; 204628; 10.
IntAct; P43404; 39.
MINT; P43404; -.
STRING; 10090.ENSMUSP00000027291; -.
BindingDB; P43404; -.
ChEMBL; CHEMBL2034801; -.
iPTMnet; P43404; -.
PhosphoSitePlus; P43404; -.
EPD; P43404; -.
MaxQB; P43404; -.
PaxDb; P43404; -.
PRIDE; P43404; -.
Ensembl; ENSMUST00000027291; ENSMUSP00000027291; ENSMUSG00000026117. [P43404-1]
GeneID; 22637; -.
KEGG; mmu:22637; -.
UCSC; uc007aqz.2; mouse. [P43404-1]
UCSC; uc007arb.2; mouse. [P43404-3]
CTD; 7535; -.
MGI; MGI:99613; Zap70.
eggNOG; ENOG410IH0T; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000113264; -.
HOVERGEN; HBG001540; -.
InParanoid; P43404; -.
KO; K07360; -.
OMA; ADKDEMM; -.
OrthoDB; EOG091G07KU; -.
TreeFam; TF351629; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-MMU-202433; Generation of second messenger molecules.
PRO; PR:P43404; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026117; -.
CleanEx; MM_ZAP70; -.
ExpressionAtlas; P43404; baseline and differential.
Genevisible; P43404; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042101; C:T cell receptor complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; IDA:MGI.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0043366; P:beta selection; IGI:MGI.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0006955; P:immune response; ISO:MGI.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IMP:MGI.
GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IMP:MGI.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IGI:MGI.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IMP:MGI.
GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:MGI.
GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
GO; GO:0045061; P:thymic T cell selection; IMP:MGI.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd09938; SH2_N-SH2_Zap70_Syk_like; 1.
Gene3D; 1.10.930.10; -; 1.
Gene3D; 3.30.505.10; -; 2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR023420; Kinase_SYK/ZAP-70_inter-SH2_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR035838; SYK/ZAP-70_N_SH2.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR012234; Tyr_kinase_non-rcpt_SYK/ZAP70.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 2.
PIRSF; PIRSF000604; TyrPK_SYK; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 2.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF55550; SSF55550; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 2.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Immunity; Isopeptide bond; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; SH2 domain; Transferase;
Tyrosine-protein kinase; Ubl conjugation.
CHAIN 1 618 Tyrosine-protein kinase ZAP-70.
/FTId=PRO_0000088169.
DOMAIN 10 102 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 163 254 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 337 597 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 343 351 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 103 162 Interdomain A.
REGION 255 336 Interdomain B.
ACT_SITE 460 460 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 368 368 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 248 248 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43403}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000250|UniProtKB:P43403}.
MOD_RES 290 290 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43403}.
MOD_RES 314 314 Phosphotyrosine; by LCK.
{ECO:0000250|UniProtKB:P43403}.
MOD_RES 318 318 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43403}.
MOD_RES 491 491 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43403}.
MOD_RES 492 492 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43403}.
CROSSLNK 543 543 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P43403}.
VAR_SEQ 1 309 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_031160.
VAR_SEQ 1 306 Missing (in isoform 2).
{ECO:0000303|PubMed:14985102}.
/FTId=VSP_031159.
VAR_SEQ 310 360 DTSVYESPYSDPEELKDKKLFLKRENLLVADIELGCGNFGS
VRQGVYRMRK -> MAYGRVSGVSELSRVLYVPFPPPPFLS
NPGVHDTRMYTQHAMLSVASHLGR (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_031161.
VARIANT 464 464 R -> C (in ST; causes an absence of
mature T-cells due to thymocyte
development being arrested at the
CD4+CD8+ stage).
{ECO:0000269|PubMed:9208839}.
CONFLICT 124 124 R -> C (in Ref. 1; AAA19250).
{ECO:0000305}.
CONFLICT 526 529 VTMW -> GHHV (in Ref. 4; BAC67015).
{ECO:0000305}.
CONFLICT 546 546 E -> Q (in Ref. 1; AAA19250).
{ECO:0000305}.
CONFLICT 599 599 L -> P (in Ref. 1; AAA19250 and 2;
AAB36538). {ECO:0000305}.
SEQUENCE 618 AA; 70112 MW; 9E0D18B240B28392 CRC64;
MPDPAAHLPF FYGSISRAEA EEHLKLAGMA DGLFLLRQCL RSLGGYVLSL VHDVRFHHFP
IERQLNGTYA IAGGKAHCGP AELCQFYSQD PDGLPCNLRK PCNRPPGLEP QPGVFDCLRD
AMVRDYVRQT WKLEGDALEQ AIISQAPQVE KLIATTAHER MPWYHSSLTR EEAERKLYSG
QQTDGKFLLR PRKEQGTYAL SLVYGKTVYH YLISQDKAGK YCIPEGTKFD TLWQLVEYLK
LKADGLIYRL KEVCPNSSAS AAVAAPTLPA HPSTFTQPQR RVDTLNSDGY TPEPARLASS
TDKPRPMPMD TSVYESPYSD PEELKDKKLF LKRENLLVAD IELGCGNFGS VRQGVYRMRK
KQIDVAIKVL KQGTEKADKD EMMREAQIMH QLDNPYIVRL IGVCQAEALM LVMEMAGGGP
LHKFLLGKKE EIPVSNVAEL LHQVAMGMKY LEEKNFVHRD LAARNVLLVN RHYAKISDFG
LSKALGADDS YYTARSAGKW PLKWYAPECI NFRKFSSRSD VWSYGVTMWE AFSYGQKPYK
KMKGPEVLDF IKQGKRMECP PECPPEMYAL MSDCWIYKWE DRPDFLTVEQ RMRNYYYSLA
SRAEGPPQCE QVAEAACG


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