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P43403

- ZAP70_HUMAN

UniProt

P43403 - ZAP70_HUMAN

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Protein
Tyrosine-protein kinase ZAP-70
Gene
ZAP70, SRK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 CD247/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-CD247/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).6 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 Publication

Enzyme regulationi

Activated by phosphorylation at Tyr-493 in the activation loop. Inhibited by staurosporine.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei369 – 3691ATP
Active sitei461 – 4611Proton acceptor2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi345 – 3528ATP

GO - Molecular functioni

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

GO - Biological processi

  1. B cell activation Source: UniProtKB
  2. T cell activation Source: UniProtKB
  3. T cell aggregation Source: UniProtKB
  4. T cell differentiation Source: UniProtKB
  5. T cell migration Source: UniProtKB
  6. T cell receptor signaling pathway Source: UniProtKB
  7. adaptive immune response Source: UniProtKB
  8. beta selection Source: Ensembl
  9. immune response Source: UniProtKB
  10. intracellular signal transduction Source: UniProtKB
  11. negative thymic T cell selection Source: Ensembl
  12. peptidyl-tyrosine phosphorylation Source: MGI
  13. positive regulation of T cell differentiation Source: MGI
  14. positive regulation of alpha-beta T cell differentiation Source: Ensembl
  15. positive regulation of alpha-beta T cell proliferation Source: Ensembl
  16. positive regulation of calcium-mediated signaling Source: Ensembl
  17. positive thymic T cell selection Source: MGI
  18. protein autophosphorylation Source: Ensembl
  19. protein phosphorylation Source: UniProtKB
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. 2681.
ReactomeiREACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
SignaLinkiP43403.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ZAP70
Synonyms:SRK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:12858. ZAP70.

Subcellular locationi

Cytoplasm. Cell membrane; Peripheral membrane protein
Note: In quiescent T-lymphocytes, it is cytoplasmic. Upon TCR activation, it is recruited at the plasma membrane by interacting with CD247/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 By similarity.1 Publication

GO - Cellular componenti

  1. T cell receptor complex Source: MGI
  2. cytoplasm Source: HGNC
  3. cytosol Source: Reactome
  4. immunological synapse Source: Ensembl
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Selective T-cell defect (STCD) [MIM:269840]: A form of severe combined immunodeficiency characterized by a selective absence of CD8+ T-cells.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti337 – 3371L → R in STCD. 1 Publication
VAR_065623
Natural varianti465 – 4651R → C in STCD. 1 Publication
VAR_065624
Natural varianti465 – 4651R → H in STCD. 1 Publication
VAR_015538
Natural varianti507 – 5071A → V in STCD. 1 Publication
VAR_065625
Natural varianti518 – 5181S → R in STCD. 1 Publication
VAR_006351
Natural varianti541 – 5411K → KLEQ in STCD.
VAR_038688
Natural varianti564 – 5641C → R in STCD. 1 Publication
VAR_065626

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311W → A: Increased constitutive kinase activity. 1 Publication
Mutagenesisi133 – 1331L → A: Increased constitutive kinase activity. 1 Publication
Mutagenesisi141 – 1411A → E: Increased constitutive kinase activity. 1 Publication
Mutagenesisi144 – 1441S → A: Increased kinase activity after activation by LCK. 1 Publication
Mutagenesisi145 – 1451Q → A: Increased kinase activity after activation by LCK. 1 Publication
Mutagenesisi147 – 1471P → A: Increased kinase activity after activation by LCK. 1 Publication
Mutagenesisi292 – 2921Y → F: Induces constitutive TCR stimulation-independent NFAT induction. 1 Publication
Mutagenesisi314 – 3141V → A: Increased constitutive kinase activity.
Mutagenesisi315 – 3151Y → A: Increased constitutive kinase activity; when associated with F-319. 4 Publications
Mutagenesisi315 – 3151Y → F: Increased constitutive kinase activity; when associated with F-319. About 75% loss of CD247/CD3Z-binding in stimulated TCR and complete loss of VAV1 interaction. 4 Publications
Mutagenesisi319 – 3191Y → A: Increased constitutive kinase activity; when associated with F-315. 2 Publications
Mutagenesisi319 – 3191Y → F: Increased constitutive kinase activity; when associated with F-315. About 80% loss of TCR-induced NFAT activation. 2 Publications
Mutagenesisi461 – 4611D → N: Abolishes kinase activity. 1 Publication
Mutagenesisi479 – 4791D → N: Abolishes kinase activity. 1 Publication
Mutagenesisi492 – 4921Y → F: Increases kinase activity. 1 Publication
Mutagenesisi493 – 4931Y → F: Impairs kinase activity. 1 Publication
Mutagenesisi597 – 5971Y → A: Increased kinase activity after activation by LCK. 1 Publication
Mutagenesisi598 – 5981Y → A: Increased kinase activity after activation by LCK. 1 Publication

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

MIMi269840. phenotype.
Orphaneti911. Combined immunodeficiency due to ZAP70 deficiency.
PharmGKBiPA37447.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Tyrosine-protein kinase ZAP-70
PRO_0000088168Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481Phosphotyrosine1 Publication
Modified residuei289 – 2891Phosphoserine1 Publication
Modified residuei292 – 2921Phosphotyrosine2 Publications
Modified residuei315 – 3151Phosphotyrosine; by LCK1 Publication
Modified residuei319 – 3191Phosphotyrosine1 Publication
Modified residuei492 – 4921Phosphotyrosine
Modified residuei603 – 6031N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues upon T-cell antigen receptor (TCR) stimulation. Phosphorylation of Tyr-315 and Tyr-319 are essential for ZAP70 positive function on T-lymphocyte activation whereas Tyr-292 has a negative regulatory role. Within the C-terminal kinase domain, Tyr-492 and Tyr-493 are phosphorylated after TCR induction, Tyr-492 playing a negative regulatory role and Tyr-493 a positive. Tyr-493 is dephosphorylated by PTN22.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP43403.
PaxDbiP43403.
PRIDEiP43403.

PTM databases

PhosphoSiteiP43403.

Miscellaneous databases

PMAP-CutDBP43403.

Expressioni

Tissue specificityi

Expressed in T- and natural killer cells. Also present in early thymocytes and pro/pre B-cells.3 Publications

Gene expression databases

ArrayExpressiP43403.
BgeeiP43403.
CleanExiHS_ZAP70.
GenevestigatoriP43403.

Organism-specific databases

HPAiCAB002625.
HPA003134.

Interactioni

Subunit structurei

Interacts with NFAM1. Interacts with adapter proteins SLA and SLA2; these interactions negatively regulates T-cell receptor signaling. Interacts with CBLB By similarity. Interacts with DEF6. Interacts (via SH2 domains) with RHOH; this interaction regulates ZAP70 subcellular localization By similarity. Interacts with FCRL3. Interacts with VAV1. Interacts with CD247/CD3Z; this interaction docks ZAP70 at the stimulated TCR. Interacts with CBL; this interaction promotes ubiquitination, internalization and subsequent degradation of CD247/CD3Z. Identified in a complex with CBL and UBE2L3.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CD247P2096322EBI-1211276,EBI-1165705
CD3EP077663EBI-1211276,EBI-1211297
KITP107212EBI-1211276,EBI-1379503
LCKP062392EBI-1211276,EBI-1348
METP085812EBI-1211276,EBI-1039152
PTPN22Q9Y2R24EBI-1211276,EBI-1211241
Ubash3bQ8BGG710EBI-1211276,EBI-8846415From a different organism.

Protein-protein interaction databases

BioGridi113367. 49 interactions.
DIPiDIP-38781N.
IntActiP43403. 19 interactions.
MINTiMINT-110540.
STRINGi9606.ENSP00000264972.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 74
Beta strandi11 – 144
Helixi17 – 2610
Beta strandi34 – 385
Beta strandi40 – 423
Beta strandi46 – 527
Beta strandi55 – 639
Beta strandi69 – 713
Beta strandi77 – 793
Helixi80 – 8910
Beta strandi94 – 963
Helixi114 – 13118
Helixi135 – 15622
Helixi157 – 1604
Helixi170 – 1789
Turni179 – 1813
Beta strandi186 – 1916
Beta strandi197 – 2048
Beta strandi207 – 2159
Beta strandi221 – 2233
Beta strandi229 – 2313
Helixi232 – 24110
Beta strandi246 – 2483
Helixi309 – 3113
Beta strandi316 – 3205
Helixi322 – 3265
Helixi334 – 3363
Beta strandi337 – 3459
Beta strandi350 – 3578
Beta strandi364 – 3718
Helixi377 – 39216
Beta strandi401 – 41515
Helixi422 – 4265
Turni430 – 4323
Helixi435 – 45420
Helixi464 – 4663
Beta strandi467 – 4715
Beta strandi474 – 4774
Turni482 – 4854
Helixi503 – 5053
Helixi508 – 5136
Helixi518 – 53316
Turni534 – 5363
Turni539 – 5424
Helixi546 – 5538
Helixi566 – 5749
Helixi580 – 5823
Helixi586 – 60116

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FBVX-ray2.90B289-297[»]
1M61X-ray2.50A1-256[»]
1U59X-ray2.30A327-606[»]
2CBLX-ray2.10B286-297[»]
2OQ1X-ray1.90A3-256[»]
2OZOX-ray2.60A1-606[»]
2Y1NX-ray2.00B/D286-297[»]
3ZNIX-ray2.21B/F/J/N286-297[»]
4A4BX-ray2.79B286-297[»]
4A4CX-ray2.70B286-297[»]
4K2RX-ray3.00A1-606[»]
ProteinModelPortaliP43403.
SMRiP43403. Positions 1-609.

Miscellaneous databases

EvolutionaryTraceiP43403.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 10293SH2 1
Add
BLAST
Domaini163 – 25492SH2 2
Add
BLAST
Domaini338 – 600263Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni103 – 16260Interdomain A
Add
BLAST
Regioni255 – 33783Interdomain B
Add
BLAST

Domaini

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 contains 3 tyrosines (Tyr-292, Tyr-315, Tyr-319) that are phosphorylated following TCR activation. These sites have 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.1 Publication

Sequence similaritiesi

Contains 2 SH2 domains.

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000113264.
HOVERGENiHBG001540.
InParanoidiP43403.
KOiK07360.
OMAiMKGPEVI.
OrthoDBiEOG7MWGWD.
PhylomeDBiP43403.
TreeFamiTF351629.

Family and domain databases

Gene3Di1.10.930.10. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR011009. 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]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PIRSFiPIRSF000604. TyrPK_SYK. 1 hit.
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P43403-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MPDPAAHLPF FYGSISRAEA EEHLKLAGMA DGLFLLRQCL RSLGGYVLSL    50
VHDVRFHHFP IERQLNGTYA IAGGKAHCGP AELCEFYSRD PDGLPCNLRK 100
PCNRPSGLEP QPGVFDCLRD AMVRDYVRQT WKLEGEALEQ AIISQAPQVE 150
KLIATTAHER MPWYHSSLTR EEAERKLYSG AQTDGKFLLR PRKEQGTYAL 200
SLIYGKTVYH YLISQDKAGK YCIPEGTKFD TLWQLVEYLK LKADGLIYCL 250
KEACPNSSAS NASGAAAPTL PAHPSTLTHP QRRIDTLNSD GYTPEPARIT 300
SPDKPRPMPM DTSVYESPYS DPEELKDKKL FLKRDNLLIA DIELGCGNFG 350
SVRQGVYRMR KKQIDVAIKV LKQGTEKADT EEMMREAQIM HQLDNPYIVR 400
LIGVCQAEAL MLVMEMAGGG PLHKFLVGKR EEIPVSNVAE LLHQVSMGMK 450
YLEEKNFVHR DLAARNVLLV NRHYAKISDF GLSKALGADD SYYTARSAGK 500
WPLKWYAPEC INFRKFSSRS DVWSYGVTMW EALSYGQKPY KKMKGPEVMA 550
FIEQGKRMEC PPECPPELYA LMSDCWIYKW EDRPDFLTVE QRMRACYYSL 600
ASKVEGPPGS TQKAEAACA 619
Length:619
Mass (Da):69,872
Last modified:November 1, 1995 - v1
Checksum:iD1E1A8EC66FA116F
GO
Isoform 2 (identifier: P43403-2) [UniParc]FASTAAdd to Basket

Also known as: TZK

The sequence of this isoform differs from the canonical sequence as follows:
     1-307: Missing.

Show »
Length:312
Mass (Da):35,647
Checksum:iB1D7A63A61D63215
GO
Isoform 3 (identifier: P43403-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-126: Missing.
     127-134: VRQTWKLE → MRLGPRWK

Note: No experimental confirmation available.

Show »
Length:493
Mass (Da):55,873
Checksum:i14F1841C3F898EEF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti175 – 1751R → L.1 Publication
Corresponds to variant rs55964305 [ dbSNP | Ensembl ].
VAR_041846
Natural varianti191 – 1911P → L.1 Publication
Corresponds to variant rs56403250 [ dbSNP | Ensembl ].
VAR_041847
Natural varianti337 – 3371L → R in STCD. 1 Publication
VAR_065623
Natural varianti448 – 4481G → E in a head and neck squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_041848
Natural varianti465 – 4651R → C in STCD. 1 Publication
VAR_065624
Natural varianti465 – 4651R → H in STCD. 1 Publication
VAR_015538
Natural varianti507 – 5071A → V in STCD. 1 Publication
VAR_065625
Natural varianti518 – 5181S → R in STCD. 1 Publication
VAR_006351
Natural varianti523 – 5231W → L.1 Publication
Corresponds to variant rs56189815 [ dbSNP | Ensembl ].
VAR_041849
Natural varianti541 – 5411K → KLEQ in STCD.
VAR_038688
Natural varianti564 – 5641C → R in STCD. 1 Publication
VAR_065626

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 307307Missing in isoform 2.
VSP_031156Add
BLAST
Alternative sequencei1 – 126126Missing in isoform 3.
VSP_031157Add
BLAST
Alternative sequencei127 – 1348VRQTWKLE → MRLGPRWK in isoform 3.
VSP_031158

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L05148 mRNA. No translation available.
AB083211 mRNA. Translation: BAC43747.1.
AC016699 Genomic DNA. Translation: AAX93187.1.
BC039039 mRNA. Translation: AAH39039.1.
BC053878 mRNA. Translation: AAH53878.1.
CCDSiCCDS33254.1. [P43403-1]
CCDS33255.1. [P43403-2]
PIRiA44266.
A49955.
RefSeqiNP_001070.2. NM_001079.3. [P43403-1]
NP_997402.1. NM_207519.1. [P43403-2]
XP_006712792.1. XM_006712729.1. [P43403-2]
UniGeneiHs.234569.

Genome annotation databases

EnsembliENST00000264972; ENSP00000264972; ENSG00000115085. [P43403-1]
ENST00000442208; ENSP00000411141; ENSG00000115085. [P43403-3]
ENST00000451498; ENSP00000400475; ENSG00000115085. [P43403-2]
GeneIDi7535.
KEGGihsa:7535.
UCSCiuc002syd.1. human. [P43403-1]
uc002sye.1. human. [P43403-3]

Polymorphism databases

DMDMi1177044.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

ZAP70base

ZAP70 mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L05148 mRNA. No translation available.
AB083211 mRNA. Translation: BAC43747.1 .
AC016699 Genomic DNA. Translation: AAX93187.1 .
BC039039 mRNA. Translation: AAH39039.1 .
BC053878 mRNA. Translation: AAH53878.1 .
CCDSi CCDS33254.1. [P43403-1 ]
CCDS33255.1. [P43403-2 ]
PIRi A44266.
A49955.
RefSeqi NP_001070.2. NM_001079.3. [P43403-1 ]
NP_997402.1. NM_207519.1. [P43403-2 ]
XP_006712792.1. XM_006712729.1. [P43403-2 ]
UniGenei Hs.234569.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FBV X-ray 2.90 B 289-297 [» ]
1M61 X-ray 2.50 A 1-256 [» ]
1U59 X-ray 2.30 A 327-606 [» ]
2CBL X-ray 2.10 B 286-297 [» ]
2OQ1 X-ray 1.90 A 3-256 [» ]
2OZO X-ray 2.60 A 1-606 [» ]
2Y1N X-ray 2.00 B/D 286-297 [» ]
3ZNI X-ray 2.21 B/F/J/N 286-297 [» ]
4A4B X-ray 2.79 B 286-297 [» ]
4A4C X-ray 2.70 B 286-297 [» ]
4K2R X-ray 3.00 A 1-606 [» ]
ProteinModelPortali P43403.
SMRi P43403. Positions 1-609.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113367. 49 interactions.
DIPi DIP-38781N.
IntActi P43403. 19 interactions.
MINTi MINT-110540.
STRINGi 9606.ENSP00000264972.

Chemistry

BindingDBi P43403.
ChEMBLi CHEMBL2803.
GuidetoPHARMACOLOGYi 2285.

PTM databases

PhosphoSitei P43403.

Polymorphism databases

DMDMi 1177044.

Proteomic databases

MaxQBi P43403.
PaxDbi P43403.
PRIDEi P43403.

Protocols and materials databases

DNASUi 7535.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264972 ; ENSP00000264972 ; ENSG00000115085 . [P43403-1 ]
ENST00000442208 ; ENSP00000411141 ; ENSG00000115085 . [P43403-3 ]
ENST00000451498 ; ENSP00000400475 ; ENSG00000115085 . [P43403-2 ]
GeneIDi 7535.
KEGGi hsa:7535.
UCSCi uc002syd.1. human. [P43403-1 ]
uc002sye.1. human. [P43403-3 ]

Organism-specific databases

CTDi 7535.
GeneCardsi GC02P098331.
GeneReviewsi ZAP70.
HGNCi HGNC:12858. ZAP70.
HPAi CAB002625.
HPA003134.
MIMi 176947. gene.
269840. phenotype.
neXtProti NX_P43403.
Orphaneti 911. Combined immunodeficiency due to ZAP70 deficiency.
PharmGKBi PA37447.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000113264.
HOVERGENi HBG001540.
InParanoidi P43403.
KOi K07360.
OMAi MKGPEVI.
OrthoDBi EOG7MWGWD.
PhylomeDBi P43403.
TreeFami TF351629.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
SignaLinki P43403.

Miscellaneous databases

EvolutionaryTracei P43403.
GeneWikii ZAP70.
GenomeRNAii 7535.
NextBioi 29481.
PMAP-CutDB P43403.
PROi P43403.
SOURCEi Search...

Gene expression databases

ArrayExpressi P43403.
Bgeei P43403.
CleanExi HS_ZAP70.
Genevestigatori P43403.

Family and domain databases

Gene3Di 1.10.930.10. 1 hit.
3.30.505.10. 2 hits.
InterProi IPR011009. 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 ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view ]
PIRSFi PIRSF000604. TyrPK_SYK. 1 hit.
PRINTSi PR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 2 hits.
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. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain."
    Chan A.C., Iwashima M., Turck C.W., Weiss A.
    Cell 71:649-662(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CD3Z, TISSUE SPECIFICITY, PHOSPHORYLATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Leukocyte.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 3).
    Tissue: Blood and Brain.
  5. "Defective T cell receptor signaling and CD8+ thymic selection in humans lacking zap-70 kinase."
    Arpaia E., Shahar M., Dadi H., Cohen A., Roifman C.M.
    Cell 76:947-958(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 521-547, VARIANT STCD LEU-GLU-GLN-541 INS, FUNCTION.
    Tissue: Lymphoid tissue.
  6. "ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity."
    Isakov N., Wange R.L., Burgess W.H., Watts J.D., Aebersold R., Samelson L.E.
    J. Exp. Med. 181:375-380(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF TAM-BINDING.
  7. "Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function."
    Chan A.C., Dalton M., Johnson R., Kong G.H., Wang T., Thoma R., Kurosaki T.
    EMBO J. 14:2499-2508(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-492 AND TYR-493.
  8. "Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function."
    Bubeck Wardenburg J., Fu C., Jackman J.K., Flotow H., Wilkinson S.E., Williams D.H., Johnson R., Kong G., Chan A.C., Findell P.R.
    J. Biol. Chem. 271:19641-19644(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF LCP2.
  9. "Enhancement of lymphocyte responsiveness by a gain-of-function mutation of ZAP-70."
    Zhao Q., Weiss A.
    Mol. Cell. Biol. 16:6765-6774(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-292, MUTAGENESIS OF TYR-292.
  10. "The Vav binding site (Y315) in ZAP-70 is critical for antigen receptor-mediated signal transduction."
    Wu J., Zhao Q., Kurosaki T., Weiss A.
    J. Exp. Med. 185:1877-1882(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VAV1, MUTAGENESIS OF TYR-315.
  11. "In vivo association of CD5 with tyrosine-phosphorylated ZAP-70 and p21 phospho-zeta molecules in human CD3+ thymocytes."
    Gary-Gouy H., Lang V., Sarun S., Boumsell L., Bismuth G.
    J. Immunol. 159:3739-3747(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. "LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation."
    Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.
    Cell 92:83-92(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF LAT.
  13. "ZAP-70 association with T cell receptor zeta (TCRzeta): fluorescence imaging of dynamic changes upon cellular stimulation."
    Sloan-Lancaster J., Presley J., Ellenberg J., Yamazaki T., Lippincott-Schwartz J., Samelson L.E.
    J. Cell Biol. 143:613-624(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "Tyrosine 319, a newly identified phosphorylation site of ZAP-70, plays a critical role in T cell antigen receptor signaling."
    Di Bartolo V., Mege D., Germain V., Pelosi M., Dufour E., Michel F., Magistrelli G., Isacchi A., Acuto O.
    J. Biol. Chem. 274:6285-6294(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-315 AND TYR-319, MUTAGENESIS OF TYR-315 AND TYR-319.
  15. "SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling."
    Tang J., Sawasdikosol S., Chang J.-H., Burakoff S.J.
    Proc. Natl. Acad. Sci. U.S.A. 96:9775-9780(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBL AND SLA.
  16. "Cbl promotes ubiquitination of the T cell receptor zeta through an adaptor function of Zap-70."
    Wang H.Y., Altman Y., Fang D., Elly C., Dai Y., Shao Y., Liu Y.C.
    J. Biol. Chem. 276:26004-26011(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CD3Z UBIQUITINATION.
  17. "SPAP2, an Ig family receptor containing both ITIMs and ITAMs."
    Xu M.-J., Zhao R., Cao H., Zhao Z.J.
    Biochem. Biophys. Res. Commun. 293:1037-1046(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCRL3.
  18. "Tyrosine 315 determines optimal recruitment of ZAP-70 to the T cell antigen receptor."
    Di Bartolo V., Malissen M., Dufour E., Sechet E., Malissen B., Acuto O.
    Eur. J. Immunol. 32:568-575(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-315.
  19. "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."
    Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.
    Eur. J. Biochem. 269:3279-3288(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHB.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  22. "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.
  23. "T cell activation-induced CrkII binding to the Zap70 protein tyrosine kinase is mediated by Lck-dependent phosphorylation of Zap70 tyrosine 315."
    Gelkop S., Gish G.D., Babichev Y., Pawson T., Isakov N.
    J. Immunol. 175:8123-8132(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY LCK.
  24. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "ZAP-70 expression in normal pro/pre B cells, mature B cells, and in B-cell acute lymphoblastic leukemia."
    Crespo M., Villamor N., Gine E., Muntanola A., Colomer D., Marafioti T., Jones M., Camos M., Campo E., Montserrat E., Bosch F.
    Clin. Cancer Res. 12:726-734(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  26. Cited for: DEPHOSPHORYLATION BY PTN22.
  27. Cited for: REVIEW ON FUNCTION.
  28. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  29. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. Cited for: FUNCTION, DOMAIN.
  31. "Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor."
    Hatada M.H., Lu X., Laird E.R., Green J., Morgenstern J.P., Lou M., Marr C.S., Phillips T.B., Ram M.K., Theriault K., Zoller M.J., Karas L.K.
    Nature 377:32-38(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-256 IN COMPLEX WITH CD247, INTERACTION WITH CD247.
  32. "Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase."
    Meng W., Sawasdikosol S., Burakoff S.J., Eck M.J.
    Nature 398:84-90(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 286-297 IN COMPLEX WITH CBL, INTERACTION WITH CBL.
  33. "Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases."
    Zheng N., Wang P., Jeffrey P.D., Pavletich N.P.
    Cell 102:533-539(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 289-297 IN COMPLEX WITH CBL AND UBE2L3.
  34. "Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather than a tandem."
    Folmer R.H., Geschwindner S., Xue Y.
    Biochemistry 41:14176-14184(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-256.
  35. "The three-dimensional structure of the ZAP-70 kinase domain in complex with staurosporine: implications for the design of selective inhibitors."
    Jin L., Pluskey S., Petrella E.C., Cantin S.M., Gorga J.C., Rynkiewicz M.J., Pandey P., Strickler J.E., Babine R.E., Weaver D.T., Seidl K.J.
    J. Biol. Chem. 279:42818-42825(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 327-606 IN COMPLEX WITH STAUROSPORINE, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-479, ENZYME REGULATION.
  36. "Structural basis for the inhibition of tyrosine kinase activity of ZAP-70."
    Deindl S., Kadlecek T.A., Brdicka T., Cao X., Weiss A., Kuriyan J.
    Cell 129:735-746(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-606 OF MUTANT ASN-461 IN COMPLEX WITH MAGNESIUM AND ATP ANALOG, ACTIVE SITE, MUTAGENESIS OF TRP-131; LEU-133; ALA-141; SER-144; GLN-145; PRO-147; TYR-315; TYR-319; ASP-461; TYR-597 AND TYR-598.
  37. "ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency."
    Chan A.C., Kadlecek T.A., Elder M.E., Filipovich A.H., Kuo W.-L., Iwashima M., Parslow T.G., Weiss A.
    Science 264:1599-1601(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT STCD ARG-518.
  38. "Specific immunoglobulin E responses in ZAP-70-deficient patients are mediated by Syk-dependent T-cell receptor signalling."
    Toyabe S., Watanabe A., Harada W., Karasawa T., Uchiyama M.
    Immunology 103:164-171(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT STCD HIS-465.
  39. "Distinct T cell developmental consequences in humans and mice expressing identical mutations in the DLAARN motif of ZAP-70."
    Elder M.E., Skoda-Smith S., Kadlecek T.A., Wang F., Wu J., Weiss A.
    J. Immunol. 166:656-661(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT STCD CYS-465.
  40. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-175; LEU-191; GLU-448 AND LEU-523.
  41. "Clinical heterogeneity can hamper the diagnosis of patients with ZAP70 deficiency."
    Turul T., Tezcan I., Artac H., de Bruin-Versteeg S., Barendregt B.H., Reisli I., Sanal O., van Dongen J.J., van der Burg M.
    Eur. J. Pediatr. 168:87-93(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS STCD ARG-337; VAL-507 AND ARG-564.

Entry informationi

Entry nameiZAP70_HUMAN
AccessioniPrimary (citable) accession number: P43403
Secondary accession number(s): A6NFP4
, Q6PIA4, Q8IXD6, Q9UBS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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