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P43405

- KSYK_HUMAN

UniProt

P43405 - KSYK_HUMAN

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Protein

Tyrosine-protein kinase SYK

Gene
SYK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development. Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. It also phosphorylates and activates PLCG1 and the PKC signaling pathway. It also phosphorylates BTK and regulates its activity in B-cell antigen receptor (BCR)-coupled signaling. Beside its function downstream of BCR plays also a role in T-cell receptor signaling. Plays also a crucial role in the innate immune response to fungal, bacterial and viral pathogens. It is for instance activated by the membrane lectin CLEC7A. Upon stimulation by fungal proteins, CLEC7A together with SYK activates immune cells inducing the production of ROS. Also activates the inflammasome and NF-kappa-B-mediated transcription of chemokines and cytokines in presence of pathogens. Regulates neutrophil degranulation and phagocytosis through activation of the MAPK signaling cascade. Also mediates the activation of dendritic cells by cell necrosis stimuli. Also involved in mast cells activation. Also functions downstream of receptors mediating cell adhesion. Relays for instance, integrin-mediated neutrophils and macrophages activation and P-selectin receptor/SELPG-mediated recruitment of leukocytes to inflammatory loci. Plays also a role in non-immune processes. It is for instance involved in vascular development where it may regulate blood and lymphatic vascular separation. It is also required for osteoclast development and function. Functions in the activation of platelets by collagen, mediating PLCG2 phosphorylation and activation. May be coupled to the collagen receptor by the ITAM domain-containing FCER1G. Also activated by the membrane lectin CLEC1B that is required for activation of platelets by PDPN/podoplanin. Involved in platelet adhesion being activated by ITGB3 engaged by fibrinogen.6 Publications

Catalytic activityi

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

Enzyme regulationi

Autoinhibited. Intramolecular binding of the interdomains A and B (also called linker region) to parts of the catalytic domain keep the catalytic center in an inactive conformation. The phosphorylation of the interdomains or the binding of the SH2 domains with dually phosphorylated ITAM domains on transmembrane proteins disrupt those intramolecular interactions allowing the kinase domain to adopt an active conformation. The phosphorylation of SYK and of the ITAM domains which is responsible for SYK activation is essentially mediated by SRC subfamily kinases, like LYN, upon transmembrane receptors engagement. May also be negatively regulated by PTPN6 through dephosphorylation. Downstream signaling adapters and intermediates like BLNK or RHOH may mediate positive and/or negative feedback regulation. Negatively regulated by CBL and CBLB through ubiquitination and probable degradation. Phosphorylates SH3BP2 which in turn may regulate SYK through LYN By similarity.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei402 – 4021ATP By similarity
Active sitei494 – 4941Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi377 – 3859ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. integrin binding Source: UniProtKB
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein kinase activity Source: UniProtKB
  6. protein tyrosine kinase activity Source: Reactome
  7. receptor signaling protein tyrosine kinase activity Source: Ensembl

GO - Biological processi

  1. activation of JUN kinase activity Source: Ensembl
  2. adaptive immune response Source: UniProtKB
  3. angiogenesis Source: UniProtKB-KW
  4. B cell receptor signaling pathway Source: UniProtKB
  5. beta selection Source: Ensembl
  6. blood coagulation Source: Reactome
  7. blood vessel morphogenesis Source: UniProtKB
  8. cell proliferation Source: ProtInc
  9. cellular response to molecule of fungal origin Source: UniProtKB
  10. defense response to bacterium Source: UniProtKB
  11. enzyme linked receptor protein signaling pathway Source: Ensembl
  12. Fc-epsilon receptor signaling pathway Source: Reactome
  13. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  14. innate immune response Source: UniProtKB
  15. integrin-mediated signaling pathway Source: UniProtKB
  16. leukocyte activation involved in immune response Source: UniProtKB
  17. leukocyte cell-cell adhesion Source: UniProtKB
  18. leukotriene biosynthetic process Source: Ensembl
  19. lymph vessel development Source: UniProtKB
  20. macrophage activation involved in immune response Source: UniProtKB
  21. neutrophil activation involved in immune response Source: UniProtKB
  22. neutrophil chemotaxis Source: UniProtKB
  23. organ morphogenesis Source: ProtInc
  24. platelet activation Source: Reactome
  25. positive regulation of alpha-beta T cell differentiation Source: Ensembl
  26. positive regulation of alpha-beta T cell proliferation Source: Ensembl
  27. positive regulation of B cell differentiation Source: Ensembl
  28. positive regulation of bone resorption Source: UniProtKB
  29. positive regulation of calcium-mediated signaling Source: Ensembl
  30. positive regulation of cell adhesion mediated by integrin Source: UniProtKB
  31. positive regulation of cytokine secretion Source: Ensembl
  32. positive regulation of gamma-delta T cell differentiation Source: Ensembl
  33. positive regulation of granulocyte macrophage colony-stimulating factor biosynthetic process Source: Ensembl
  34. positive regulation of interleukin-3 biosynthetic process Source: Ensembl
  35. positive regulation of mast cell degranulation Source: Ensembl
  36. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  37. protein autophosphorylation Source: Ensembl
  38. protein phosphorylation Source: UniProtKB
  39. regulation of arachidonic acid secretion Source: UniProtKB
  40. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  41. regulation of neutrophil degranulation Source: UniProtKB
  42. regulation of phagocytosis Source: UniProtKB
  43. regulation of platelet activation Source: UniProtKB
  44. regulation of platelet aggregation Source: UniProtKB
  45. regulation of superoxide anion generation Source: UniProtKB
  46. serotonin secretion by platelet Source: UniProtKB
  47. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Angiogenesis, Host-virus interaction, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_147814. DAP12 signaling.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_160274. FCGR activation.
REACT_163701. FCERI mediated MAPK activation.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_163936. Fc epsilon receptor (FCERI) signaling.
REACT_1695. GPVI-mediated activation cascade.
REACT_23787. Regulation of signaling by CBL.
REACT_27283. Interleukin-2 signaling.
SignaLinkiP43405.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase SYK (EC:2.7.10.2)
Alternative name(s):
Spleen tyrosine kinase
p72-Syk
Gene namesi
Name:SYK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:11491. SYK.

Subcellular locationi

Cell membrane Inferred. Cytoplasmcytosol Inferred

GO - Cellular componenti

  1. B cell receptor complex Source: Ensembl
  2. cytosol Source: UniProtKB
  3. early phagosome Source: UniProtKB
  4. plasma membrane Source: Reactome
  5. T cell receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi297 – 2971S → A: Abolishes YWHAG binding. 1 Publication
Mutagenesisi630 – 6301Y → F: Loss of interaction with BLNK. 1 Publication

Organism-specific databases

PharmGKBiPA36273.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 635635Tyrosine-protein kinase SYKPRO_0000088165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Phosphotyrosine2 Publications
Modified residuei44 – 441Phosphoserine1 Publication
Modified residuei47 – 471Phosphotyrosine1 Publication
Modified residuei131 – 1311Phosphotyrosine1 Publication
Modified residuei202 – 2021Phosphoserine1 Publication
Modified residuei256 – 2561Phosphothreonine1 Publication
Modified residuei295 – 2951Phosphoserine1 Publication
Modified residuei296 – 2961Phosphotyrosine1 Publication
Modified residuei297 – 2971Phosphoserine1 Publication
Modified residuei316 – 3161Phosphoserine1 Publication
Modified residuei317 – 3171Phosphothreonine1 Publication
Modified residuei319 – 3191Phosphoserine1 Publication
Modified residuei323 – 3231Phosphotyrosine; by LYN2 Publications
Modified residuei345 – 3451Phosphothreonine1 Publication
Modified residuei348 – 3481Phosphotyrosine1 Publication
Modified residuei350 – 3501Phosphoserine1 Publication
Modified residuei352 – 3521Phosphotyrosine1 Publication
Modified residuei364 – 3641Phosphotyrosine1 Publication
Modified residuei379 – 3791Phosphoserine1 Publication
Modified residuei384 – 3841Phosphothreonine1 Publication
Modified residuei484 – 4841Phosphotyrosine1 Publication
Modified residuei507 – 5071Phosphotyrosine1 Publication
Modified residuei525 – 5251Phosphotyrosine; by autocatalysis1 Publication
Modified residuei526 – 5261Phosphotyrosine1 Publication
Modified residuei530 – 5301Phosphothreonine1 Publication
Modified residuei546 – 5461Phosphotyrosine By similarity
Modified residuei579 – 5791Phosphoserine1 Publication
Modified residuei582 – 5821Phosphothreonine1 Publication
Modified residuei629 – 6291Phosphotyrosine1 Publication
Modified residuei630 – 6301Phosphotyrosine2 Publications
Modified residuei631 – 6311Phosphotyrosine1 Publication

Post-translational modificationi

Ubiquitinated by CBLB after BCR activation; which promotes proteasomal degradation By similarity.
Autophosphorylated. Phosphorylated on tyrosine residues by LYN following receptors engagement. Phosphorylation on Tyr-323 creates a binding site for CBL, an adapter protein that serves as a negative regulator of BCR-stimulated calcium ion signaling. Phosphorylation at Tyr-348 creates a binding site for VAV1. Phosphorylation on Tyr-348 and Tyr-352 enhances the phosphorylation and activation of phospholipase C-gamma and the early phase of calcium ion mobilization via a phosphoinositide 3-kinase-independent pathway By similarity. Phosphorylation on Ser-297 is very common, it peaks 5 minutes after BCR stimulation, and creates a binding site for YWHAG. Phosphorylation at Tyr-630 creates a binding site for BLNK. Dephosphorylated by PTPN6.4 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP43405.
PaxDbiP43405.
PeptideAtlasiP43405.
PRIDEiP43405.

PTM databases

PhosphoSiteiP43405.

Expressioni

Tissue specificityi

Widely expressed in hematopoietic cells (at protein level). Within the B-cells compartment it is for instance expressed for pro-B-cells to plasma cells.1 Publication

Gene expression databases

BgeeiP43405.
CleanExiHS_SYK.
GenevestigatoriP43405.

Organism-specific databases

HPAiCAB007773.
HPA001384.

Interactioni

Subunit structurei

Interacts with LYN; phosphorylates SYK By similarity. Interacts with RHOH (phosphorylated); regulates mast cells activation By similarity. Interacts with NFAM1 (phosphorylated); probably involved in BCR signaling By similarity. Interacts with VAV1 (via SH2 domain); phosphorylates VAV1 upon BCR activation. Interacts with GAB2 (phosphorylated); probably involved in IgE Fc receptor signaling By similarity. Interacts (via its SH2 domains) with CD79A (via its phosphorylated ITAM domain); the interaction stimulates SYK autophosphorylation and activation By similarity. Interacts with FCRL3. Interacts (via SH2 domains) with FCER1G (via ITAM domain); activates SYK and mediates neutrophils and macrophages integrin-mediated activation By similarity. Interacts with ITGB2 and FGR; involved in ITGB2 downstream signaling By similarity. Interacts with ITGB3; upon activation by ITGB3 promotes platelet adhesion. Interacts (via SH2 domains) with TYROBP (via ITAM domain); involved in neutrophils and macrophages integrin-mediated activation By similarity. Interacts with MSN and SELPLG; mediates the selectin-dependent activation of SYK by SELPLG. Interacts with BLNK (via SH2 domain). Interacts (via the second SH2 domain) with USP25 (via C-terminus); phosphorylates USP25 and regulates USP25 intracellular levels. Interacts (via SH2 domains) with CLEC1B (dimer). Interacts with CLEC7A; participates in leukocyte activation in presence of fungal pathogens. Interacts (phosphorylated) with SLA; may regulate SYK through CBL recruitment. Interacts with YWHAG; attenuates BCR-induced membrane translocation and activation of SYK. Interacts with Epstein-Barr virus LMP2A. Interacts (via SH2 domains) with GCSAM; the interaction increases after B-cell receptor stimulation, resulting in enhanced SYK autophosphorylation and activity.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBLP226812EBI-78302,EBI-518228
CD22P202734EBI-78302,EBI-78277
CD37P110493EBI-78302,EBI-6139068
CD3EP077666EBI-78302,EBI-1211297
EGFRP005336EBI-78302,EBI-297353
ERBB2P046267EBI-78302,EBI-641062
ERBB3P218606EBI-78302,EBI-720706
FCER1GP302732EBI-78302,EBI-515289
GAB1Q134804EBI-78302,EBI-517684
LCKP062397EBI-78302,EBI-1348
METP085813EBI-78302,EBI-1039152
PLCG1P191744EBI-78302,EBI-79387
UBASH3BQ8TF422EBI-78302,EBI-1380492

Protein-protein interaction databases

BioGridi112717. 95 interactions.
DIPiDIP-253N.
IntActiP43405. 34 interactions.
MINTiMINT-148486.
STRINGi9606.ENSP00000364898.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3110
Beta strandi38 – 436
Beta strandi47 – 493
Beta strandi51 – 577
Beta strandi60 – 689
Beta strandi74 – 763
Beta strandi82 – 843
Helixi85 – 928
Beta strandi99 – 1013
Helixi119 – 13618
Helixi140 – 15819
Helixi163 – 1653
Beta strandi169 – 1724
Helixi175 – 1839
Beta strandi184 – 1863
Beta strandi187 – 1893
Beta strandi192 – 20110
Beta strandi203 – 2097
Beta strandi212 – 2209
Beta strandi221 – 2244
Beta strandi226 – 2283
Beta strandi229 – 2313
Beta strandi234 – 2363
Helixi237 – 2448
Beta strandi251 – 2533
Helixi342 – 3443
Helixi346 – 3483
Helixi351 – 3533
Beta strandi361 – 3644
Helixi367 – 3693
Beta strandi370 – 3723
Beta strandi376 – 3794
Beta strandi381 – 39111
Beta strandi393 – 40311
Helixi406 – 4094
Helixi412 – 42514
Beta strandi435 – 44915
Helixi456 – 4627
Helixi468 – 48720
Helixi497 – 4993
Beta strandi500 – 5045
Beta strandi507 – 5104
Helixi515 – 5184
Beta strandi524 – 5274
Helixi536 – 5383
Helixi541 – 5466
Beta strandi548 – 5503
Helixi551 – 56616
Turni567 – 5693
Turni572 – 5754
Helixi578 – 5869
Beta strandi589 – 5913
Helixi599 – 60810
Turni613 – 6153
Helixi619 – 63517

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A81X-ray3.00A/C/E/G/I/K9-262[»]
1CSYNMR-A163-265[»]
1CSZNMR-A163-265[»]
1XBAX-ray2.00A356-635[»]
1XBBX-ray1.57A356-635[»]
1XBCX-ray2.00A356-635[»]
3BUWX-ray1.45A/C317-329[»]
3EMGX-ray2.60A349-635[»]
3FQEX-ray2.50A356-635[»]
3FQHX-ray2.26A/B356-635[»]
3FQSX-ray2.10A356-635[»]
3SRVX-ray1.95A/B360-635[»]
3TUBX-ray2.23A343-635[»]
3TUCX-ray2.10A343-635[»]
3TUDX-ray2.33A343-635[»]
3VF8X-ray2.08A343-635[»]
3VF9X-ray2.30A343-635[»]
4DFLX-ray1.98A363-635[»]
4DFNX-ray2.48A363-635[»]
4F4PX-ray2.37A365-635[»]
4FL1X-ray1.79A356-635[»]
4FL2X-ray2.19A1-635[»]
4FL3X-ray1.90A1-635[»]
4FYNX-ray2.32A356-635[»]
4FYOX-ray1.40A356-635[»]
4FZ6X-ray1.85A356-635[»]
4FZ7X-ray1.75A356-635[»]
4GFGX-ray2.35A356-635[»]
4I0RX-ray2.10A356-635[»]
4I0SX-ray1.98A356-635[»]
4I0TX-ray1.70A356-635[»]
4PUZX-ray2.08A/B356-635[»]
4PV0X-ray2.00A363-635[»]
4PX6X-ray1.60A356-635[»]
ProteinModelPortaliP43405.
SMRiP43405. Positions 9-265, 330-635.

Miscellaneous databases

EvolutionaryTraceiP43405.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 10793SH2 1Add
BLAST
Domaini168 – 25992SH2 2Add
BLAST
Domaini371 – 631261Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 16760Interdomain AAdd
BLAST
Regioni260 – 370111Interdomain BAdd
BLAST

Domaini

The SH2 domains mediate the interaction of SYK with the phosphorylated ITAM domains of transmembrane proteins. Some proteins like CLEC1B have a partial ITAM domain (also called hemITAM) containing a single YxxL motif. The interaction with SYK requires CLEC1B homodimerization.1 Publication

Sequence similaritiesi

Contains 2 SH2 domains.

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000113264.
HOVERGENiHBG001540.
InParanoidiP43405.
KOiK05855.
OMAiKGYYQMK.
OrthoDBiEOG7MWGWD.
PhylomeDBiP43405.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P43405-1) [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

MASSGMADSA NHLPFFFGNI TREEAEDYLV QGGMSDGLYL LRQSRNYLGG    50
FALSVAHGRK AHHYTIEREL NGTYAIAGGR THASPADLCH YHSQESDGLV 100
CLLKKPFNRP QGVQPKTGPF EDLKENLIRE YVKQTWNLQG QALEQAIISQ 150
KPQLEKLIAT TAHEKMPWFH GKISREESEQ IVLIGSKTNG KFLIRARDNN 200
GSYALCLLHE GKVLHYRIDK DKTGKLSIPE GKKFDTLWQL VEHYSYKADG 250
LLRVLTVPCQ KIGTQGNVNF GGRPQLPGSH PATWSAGGII SRIKSYSFPK 300
PGHRKSSPAQ GNRQESTVSF NPYEPELAPW AADKGPQREA LPMDTEVYES 350
PYADPEEIRP KEVYLDRKLL TLEDKELGSG NFGTVKKGYY QMKKVVKTVA 400
VKILKNEAND PALKDELLAE ANVMQQLDNP YIVRMIGICE AESWMLVMEM 450
AELGPLNKYL QQNRHVKDKN IIELVHQVSM GMKYLEESNF VHRDLAARNV 500
LLVTQHYAKI SDFGLSKALR ADENYYKAQT HGKWPVKWYA PECINYYKFS 550
SKSDVWSFGV LMWEAFSYGQ KPYRGMKGSE VTAMLEKGER MGCPAGCPRE 600
MYDLMNLCWT YDVENRPGFA AVELRLRNYY YDVVN 635
Length:635
Mass (Da):72,066
Last modified:November 1, 1995 - v1
Checksum:iEAA6BDE65881FC68
GO
Isoform Short (identifier: P43405-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     283-305: Missing.

Show »
Length:612
Mass (Da):69,510
Checksum:i1D4FD24C6C9F5C53
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451R → H.
Corresponds to variant rs16906862 [ dbSNP | Ensembl ].
VAR_033838

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei283 – 30523Missing in isoform Short. VSP_005010Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191P → A in CAA51970. 1 Publication
Sequence conflicti250 – 2501G → P in CAA51970. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z29630 mRNA. Translation: CAA82737.1.
L28824 mRNA. Translation: AAA36526.1.
AL354862 Genomic DNA. No translation available.
BC001645 mRNA. Translation: AAH01645.1.
BC011399 mRNA. Translation: AAH11399.1.
BC002962 mRNA. Translation: AAH02962.1.
X73568 mRNA. Translation: CAA51970.1.
CCDSiCCDS47992.1. [P43405-2]
CCDS6688.1. [P43405-1]
PIRiA53596.
RefSeqiNP_001128524.1. NM_001135052.3. [P43405-2]
NP_001167638.1. NM_001174167.2. [P43405-1]
NP_001167639.1. NM_001174168.2. [P43405-2]
NP_003168.2. NM_003177.6. [P43405-1]
XP_005252204.1. XM_005252147.2. [P43405-1]
UniGeneiHs.371720.

Genome annotation databases

EnsembliENST00000375746; ENSP00000364898; ENSG00000165025. [P43405-1]
ENST00000375747; ENSP00000364899; ENSG00000165025. [P43405-2]
ENST00000375751; ENSP00000364904; ENSG00000165025. [P43405-2]
ENST00000375754; ENSP00000364907; ENSG00000165025. [P43405-1]
GeneIDi6850.
KEGGihsa:6850.
UCSCiuc004aqz.3. human. [P43405-1]
uc004ara.3. human. [P43405-2]

Polymorphism databases

DMDMi1174527.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z29630 mRNA. Translation: CAA82737.1 .
L28824 mRNA. Translation: AAA36526.1 .
AL354862 Genomic DNA. No translation available.
BC001645 mRNA. Translation: AAH01645.1 .
BC011399 mRNA. Translation: AAH11399.1 .
BC002962 mRNA. Translation: AAH02962.1 .
X73568 mRNA. Translation: CAA51970.1 .
CCDSi CCDS47992.1. [P43405-2 ]
CCDS6688.1. [P43405-1 ]
PIRi A53596.
RefSeqi NP_001128524.1. NM_001135052.3. [P43405-2 ]
NP_001167638.1. NM_001174167.2. [P43405-1 ]
NP_001167639.1. NM_001174168.2. [P43405-2 ]
NP_003168.2. NM_003177.6. [P43405-1 ]
XP_005252204.1. XM_005252147.2. [P43405-1 ]
UniGenei Hs.371720.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A81 X-ray 3.00 A/C/E/G/I/K 9-262 [» ]
1CSY NMR - A 163-265 [» ]
1CSZ NMR - A 163-265 [» ]
1XBA X-ray 2.00 A 356-635 [» ]
1XBB X-ray 1.57 A 356-635 [» ]
1XBC X-ray 2.00 A 356-635 [» ]
3BUW X-ray 1.45 A/C 317-329 [» ]
3EMG X-ray 2.60 A 349-635 [» ]
3FQE X-ray 2.50 A 356-635 [» ]
3FQH X-ray 2.26 A/B 356-635 [» ]
3FQS X-ray 2.10 A 356-635 [» ]
3SRV X-ray 1.95 A/B 360-635 [» ]
3TUB X-ray 2.23 A 343-635 [» ]
3TUC X-ray 2.10 A 343-635 [» ]
3TUD X-ray 2.33 A 343-635 [» ]
3VF8 X-ray 2.08 A 343-635 [» ]
3VF9 X-ray 2.30 A 343-635 [» ]
4DFL X-ray 1.98 A 363-635 [» ]
4DFN X-ray 2.48 A 363-635 [» ]
4F4P X-ray 2.37 A 365-635 [» ]
4FL1 X-ray 1.79 A 356-635 [» ]
4FL2 X-ray 2.19 A 1-635 [» ]
4FL3 X-ray 1.90 A 1-635 [» ]
4FYN X-ray 2.32 A 356-635 [» ]
4FYO X-ray 1.40 A 356-635 [» ]
4FZ6 X-ray 1.85 A 356-635 [» ]
4FZ7 X-ray 1.75 A 356-635 [» ]
4GFG X-ray 2.35 A 356-635 [» ]
4I0R X-ray 2.10 A 356-635 [» ]
4I0S X-ray 1.98 A 356-635 [» ]
4I0T X-ray 1.70 A 356-635 [» ]
4PUZ X-ray 2.08 A/B 356-635 [» ]
4PV0 X-ray 2.00 A 363-635 [» ]
4PX6 X-ray 1.60 A 356-635 [» ]
ProteinModelPortali P43405.
SMRi P43405. Positions 9-265, 330-635.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112717. 95 interactions.
DIPi DIP-253N.
IntActi P43405. 34 interactions.
MINTi MINT-148486.
STRINGi 9606.ENSP00000364898.

Chemistry

BindingDBi P43405.
ChEMBLi CHEMBL2599.
GuidetoPHARMACOLOGYi 2230.

PTM databases

PhosphoSitei P43405.

Polymorphism databases

DMDMi 1174527.

Proteomic databases

MaxQBi P43405.
PaxDbi P43405.
PeptideAtlasi P43405.
PRIDEi P43405.

Protocols and materials databases

DNASUi 6850.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375746 ; ENSP00000364898 ; ENSG00000165025 . [P43405-1 ]
ENST00000375747 ; ENSP00000364899 ; ENSG00000165025 . [P43405-2 ]
ENST00000375751 ; ENSP00000364904 ; ENSG00000165025 . [P43405-2 ]
ENST00000375754 ; ENSP00000364907 ; ENSG00000165025 . [P43405-1 ]
GeneIDi 6850.
KEGGi hsa:6850.
UCSCi uc004aqz.3. human. [P43405-1 ]
uc004ara.3. human. [P43405-2 ]

Organism-specific databases

CTDi 6850.
GeneCardsi GC09P093564.
HGNCi HGNC:11491. SYK.
HPAi CAB007773.
HPA001384.
MIMi 600085. gene.
neXtProti NX_P43405.
PharmGKBi PA36273.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000113264.
HOVERGENi HBG001540.
InParanoidi P43405.
KOi K05855.
OMAi KGYYQMK.
OrthoDBi EOG7MWGWD.
PhylomeDBi P43405.
TreeFami TF351629.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_147814. DAP12 signaling.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_160274. FCGR activation.
REACT_163701. FCERI mediated MAPK activation.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_163936. Fc epsilon receptor (FCERI) signaling.
REACT_1695. GPVI-mediated activation cascade.
REACT_23787. Regulation of signaling by CBL.
REACT_27283. Interleukin-2 signaling.
SignaLinki P43405.

Miscellaneous databases

EvolutionaryTracei P43405.
GeneWikii Syk.
GenomeRNAii 6850.
NextBioi 26739.
PROi P43405.
SOURCEi Search...

Gene expression databases

Bgeei P43405.
CleanExi HS_SYK.
Genevestigatori P43405.

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. "Cloning of the cDNA for the deleted syk kinase homologous to ZAP-70 from human basophilic leukemia cell line (KU812)."
    Yagi S., Suzuki K., Hasegawa A., Okumura K., Ra C.
    Biochem. Biophys. Res. Commun. 200:28-34(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning of human Syk. A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex."
    Law C.-L., Sidorenko S.P., Chandran K.A., Draves K.E., Chan A.C., Weiss A., Edelhoff S., Disteche C.M., Clark E.A.
    J. Biol. Chem. 269:12310-12319(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AUTOPHOSPHORYLATION.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [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 LONG AND SHORT).
    Tissue: Eye and Lymph.
  5. "Molecular cloning of the human homologue to the pig protein-tyrosine kinase syk."
    Mueller B., Cooper L., Terhorst C.
    Immunogenetics 39:359-362(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-635.
    Tissue: Tonsil.
  6. "Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases."
    Miller C.L., Burkhardt A.L., Lee J.H., Stealey B., Longnecker R., Bolen J.B., Kieff E.
    Immunity 2:155-166(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A.
  7. "Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product."
    Deckert M., Tartare-Deckert S., Couture C., Mustelin T., Altman A.
    Immunity 5:591-604(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VAV1.
  8. "Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk."
    Law C.L., Chandran K.A., Sidorenko S.P., Clark E.A.
    Mol. Cell. Biol. 16:1305-1315(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG1, INTERACTION WITH PLCG1.
  9. "Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases."
    Deckert M., Elly C., Altman A., Liu Y.C.
    J. Biol. Chem. 273:8867-8874(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CBL, INTERACTION WITH CBL.
  10. "Cbl-mediated negative regulation of the Syk tyrosine kinase. A critical role for Cbl phosphotyrosine-binding domain binding to Syk phosphotyrosine 323."
    Lupher M.L. Jr., Rao N., Lill N.L., Andoniou C.E., Miyake S., Clark E.A., Druker B., Band H.
    J. Biol. Chem. 273:35273-35281(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH CBL.
  11. "Dephosphorylation of ZAP-70 and inhibition of T cell activation by activated SHP1."
    Brockdorff J., Williams S., Couture C., Mustelin T.
    Eur. J. Immunol. 29:2539-2550(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN6, ENZYME REGULATION.
  12. "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 SLA.
  13. "Molecular cloning and characterization of SPAP1, an inhibitory receptor."
    Xu M.-J., Zhao R., Zhao Z.J.
    Biochem. Biophys. Res. Commun. 280:768-775(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCRL3.
  14. "BLNK: molecular scaffolding through 'cis'-mediated organization of signaling proteins."
    Chiu C.W., Dalton M., Ishiai M., Kurosaki T., Chan A.C.
    EMBO J. 21:6461-6472(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN B-CELL RECEPTOR SIGNALING PATHWAY, FUNCTION IN PHOSPHORYLATION OF BLNK.
  15. "ITAM-based interaction of ERM proteins with Syk mediates signaling by the leukocyte adhesion receptor PSGL-1."
    Urzainqui A., Serrador J.M., Viedma F., Yanez-Mo M., Rodriguez A., Corbi A.L., Alonso-Lebrero J.L., Luque A., Deckert M., Vazquez J., Sanchez-Madrid F.
    Immunity 17:401-412(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL ADHESION, INTERACTION WITH SELPLG AND MSN.
  16. "Coordinate interactions of Csk, Src, and Syk kinases with [alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton."
    Obergfell A., Eto K., Mocsai A., Buensuceso C., Moores S.L., Brugge J.S., Lowell C.A., Shattil S.J.
    J. Cell Biol. 157:265-275(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITGB3.
  17. "Association of the Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD (SLP-76) with the p85 subunit of phosphoinositide 3-kinase."
    Shim E.K., Moon C.S., Lee G.Y., Ha Y.J., Chae S.K., Lee J.R.
    FEBS Lett. 575:35-40(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF LCP2.
  18. "The kinase Syk as an adaptor controlling sustained calcium signalling and B-cell development."
    Kulathu Y., Hobeika E., Turchinovich G., Reth M.
    EMBO J. 27:1333-1344(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BLNK, ENZYME REGULATION, MUTAGENESIS OF TYR-630, PHOSPHORYLATION AT TYR-630.
  19. Cited for: ENZYME REGULATION.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. Cited for: INTERACTION WITH CLEC1B.
  24. "Functional interaction between the ubiquitin-specific protease 25 and the SYK tyrosine kinase."
    Cholay M., Reverdy C., Benarous R., Colland F., Daviet L.
    Exp. Cell Res. 316:667-675(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP25, FUNCTION.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Complex phosphorylation dynamics control the composition of the Syk interactome in B cells."
    Bohnenberger H., Oellerich T., Engelke M., Hsiao H.H., Urlaub H., Wienands J.
    Eur. J. Immunol. 41:1550-1562(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-28; SER-44; TYR-47; TYR-131; SER-202; THR-256; SER-295; TYR-296; SER-297; SER-316; THR-317; SER-319; TYR-323; THR-345; TYR-348; SER-350; TYR-352; TYR-364; SER-379; THR-384; TYR-484; TYR-507; TYR-525; TYR-526; THR-530; SER-579; THR-582; TYR-629; TYR-630 AND TYR-631, INTERACTION WITH YWHAG, MUTAGENESIS OF SER-297.
    Tissue: B-cell.
  27. Cited for: INTERACTION WITH GCSAM.
  28. "Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptide."
    Narula S.S., Yuan R.W., Adams S.E., Green O.M., Green J., Philips T.B., Zydowsky L.D., Botfield M.C., Hatada M., Laird E.R., Zoller M.J., Karas J.L., Dalgarno D.C.
    Structure 3:1061-1073(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 163-265.
  29. "Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide."
    Fuetterer K., Wong J., Grucza R.A., Chan A.C., Waksman G.
    J. Mol. Biol. 281:523-537(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF SH2 DOMAINS IN COMPLEX WITH CD3E PHOSPHORYLATED ITAM DOMAIN.

Entry informationi

Entry nameiKSYK_HUMAN
AccessioniPrimary (citable) accession number: P43405
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 171 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 9
    Human chromosome 9: 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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