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Protein

Tyrosine-protein kinase Lyn

Gene

LYN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Mediates phosphorylation of the BCR-ABL fusion protein. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation.20 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation4 Publications

Enzyme regulationi

Subject to autoinhibition, mediated by intramolecular interactions between the SH2 domain and the C-terminal phosphotyrosine. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylated by CSK at Tyr-508; phosphorylation at Tyr-508 inhibits kinase activity. Kinase activity is modulated by dephosphorylation by PTPRC/CD45. Inhibited by Dasatinib, PP2, and SU6656.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei275ATPPROSITE-ProRule annotation1
Active sitei367Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi253 – 261ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • ephrin receptor binding Source: ARUK-UCL
  • gamma-tubulin binding Source: Ensembl
  • glycosphingolipid binding Source: Ensembl
  • integrin binding Source: Ensembl
  • ion channel binding Source: BHF-UCL
  • kinase activity Source: ARUK-UCL
  • non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  • phosphoprotein binding Source: Ensembl
  • phosphorylation-dependent protein binding Source: UniProtKB
  • platelet-derived growth factor receptor binding Source: Ensembl
  • protein tyrosine kinase activity Source: UniProtKB
  • receptor binding Source: GO_Central
  • SH3 domain binding Source: Ensembl
  • signal transducer, downstream of receptor, with protein tyrosine kinase activity Source: ProtInc
  • ubiquitin protein ligase binding Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase, Tyrosine-protein kinase
Biological processAdaptive immunity, Host-virus interaction, Immunity, Inflammatory response, Innate immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-114604 GPVI-mediated activation cascade
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-1433559 Regulation of KIT signaling
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-2029481 FCGR activation
R-HSA-210990 PECAM1 interactions
R-HSA-2454202 Fc epsilon receptor (FCERI) signaling
R-HSA-2682334 EPH-Ephrin signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-2871809 FCERI mediated Ca+2 mobilization
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-389356 CD28 co-stimulation
R-HSA-389513 CTLA4 inhibitory signaling
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-5621480 Dectin-2 family
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5690714 CD22 mediated BCR regulation
R-HSA-69231 Cyclin D associated events in G1
R-HSA-75892 Platelet Adhesion to exposed collagen
R-HSA-912631 Regulation of signaling by CBL
R-HSA-982772 Growth hormone receptor signaling
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers
SignaLinkiP07948
SIGNORiP07948

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Lyn (EC:2.7.10.2)
Alternative name(s):
Lck/Yes-related novel protein tyrosine kinase
V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
p53Lyn
p56Lyn
Gene namesi
Name:LYN
Synonyms:JTK8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000254087.7
HGNCiHGNC:6735 LYN
MIMi165120 gene
neXtProtiNX_P07948

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Constitutively phosphorylated and activated in cells from a number of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) patients. Mediates phosphorylation of the BCR-ABL fusion protein. Abnormally elevated expression levels or activation of LYN signaling may play a role in survival and proliferation of some types of cancer cells.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2G → A: Loss of localization to the cell membrane; when associated with A-3. 1 Publication1
Mutagenesisi3C → A: Loss of localization to the cell membrane; when associated with A-2. 1 Publication1
Mutagenesisi275K → A: Loss of activity and no effect on localization to the cell membrane. Abundant localization in the nucleus; when associated with A-2 and A-3. 4 Publications1
Mutagenesisi275K → L or R: Loss of kinase activity. 4 Publications1
Mutagenesisi346D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-353; A-498 and A-499. 1 Publication1
Mutagenesisi353E → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-498 and A-499. 1 Publication1
Mutagenesisi397Y → F: Strongly reduced kinase activity. 1 Publication1
Mutagenesisi498D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-499. 1 Publication1
Mutagenesisi499D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-498. 1 Publication1
Mutagenesisi508Y → F: Abolishes autoinhibition and thereby increases kinase activity. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi4067
OpenTargetsiENSG00000254087
PharmGKBiPA30498

Chemistry databases

ChEMBLiCHEMBL3905
DrugBankiDB06616 Bosutinib
DB09079 Nintedanib
DB08901 Ponatinib
GuidetoPHARMACOLOGYi2060

Polymorphism and mutation databases

BioMutaiLYN
DMDMi125480

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000881292 – 512Tyrosine-protein kinase LynAdd BLAST511

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1 Publication1
Lipidationi3S-palmitoyl cysteine1 Publication1
Modified residuei11PhosphoserineCombined sources1
Modified residuei13PhosphoserineCombined sources1
Modified residuei193Phosphotyrosine1 Publication1
Modified residuei228PhosphoserineCombined sources1
Modified residuei306PhosphotyrosineCombined sources1
Modified residuei316PhosphotyrosineCombined sources1
Modified residuei397Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei460Phosphotyrosine1 Publication1
Modified residuei473PhosphotyrosineCombined sources1
Modified residuei508Phosphotyrosine; by autocatalysis, CSK and MATKCombined sources3 Publications1

Post-translational modificationi

Ubiquitinated by CBL, leading to its degradation. Ubiquitination is SH3-dependent.2 Publications
Autophosphorylated. Phosphorylated on tyrosine residues in response to KIT signaling. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylation at Tyr-508 inhibits kinase activity. Phosphorylated at Tyr-508 by CSK. Dephosphorylated by PTPRC/CD45. Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A.7 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP07948
MaxQBiP07948
PaxDbiP07948
PeptideAtlasiP07948
PRIDEiP07948

2D gel databases

REPRODUCTION-2DPAGEiP07948

PTM databases

iPTMnetiP07948
PhosphoSitePlusiP07948
SwissPalmiP07948

Miscellaneous databases

PMAP-CutDBiP07948

Expressioni

Tissue specificityi

Detected in monocytes (at protein level). Detected in placenta, and in fetal brain, lung, liver and kidney. Widely expressed in a variety of organs, tissues, and cell types such as epidermoid, hematopoietic, and neuronal cells. Expressed in primary neuroblastoma tumors.2 Publications

Gene expression databases

BgeeiENSG00000254087
CleanExiHS_LYN
ExpressionAtlasiP07948 baseline and differential
GenevisibleiP07948 HS

Organism-specific databases

HPAiCAB004492
HPA001231

Interactioni

Subunit structurei

Interacts with TEC. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with LIME1 and with CD79A upon activation of the B-cell antigen receptor. Interacts with the B-cell receptor complex. Interacts with phosphorylated THEMIS2. Interacts with EPOR. Interacts with MS4A2/FCER1B. Interaction (via the SH2 and SH3 domains) with MUC1 is stimulated by IL7 and the subsequent phosphorylation increases the binding between MUC1 and CTNNB1/beta-catenin. Interacts with ADAM15. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with FASLG. Interacts with KIT. Interacts with HCLS1. Interacts with FCGR2B. Interacts with FCGR1A; the interaction may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts (via SH3 domain) with CBLC, PPP1R15A and PDE4A. Interacts with TGFB1I1. Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase; this interaction enhances phosphatidylinositol 3-kinase activity. Interacts with CSF2RB, the common subunit of the IL3, IL5 and CSF2 receptors. Interacts with PAG1; identified in a complex with PAG1 and STAT3. Interacts with ABL1. Interacts with PTPN6/SHP-1. Interacts (via SH3 domain) with SCIMP (via proline-rich region). Interacts with LPXN (via LD motif 3) and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via SH3-domain) with ANKRD54 (via ankyrin repeat region) in an activation-independent status of LYN. Forms a multiprotein complex with ANKRD54 and HCLS1. Interacts with Epstein-Barr virus LMP2A. Interacts with Herpes virus saimiri tyrosine kinase interacting protein (Tip). Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation. Interacts with CD36. Interacts with LYN (By similarity).By similarity29 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • ephrin receptor binding Source: ARUK-UCL
  • gamma-tubulin binding Source: Ensembl
  • integrin binding Source: Ensembl
  • ion channel binding Source: BHF-UCL
  • phosphoprotein binding Source: Ensembl
  • phosphorylation-dependent protein binding Source: UniProtKB
  • platelet-derived growth factor receptor binding Source: Ensembl
  • receptor binding Source: GO_Central
  • SH3 domain binding Source: Ensembl
  • ubiquitin protein ligase binding Source: Ensembl

Protein-protein interaction databases

BioGridi110245, 194 interactors
CORUMiP07948
DIPiDIP-1056N
ELMiP07948
IntActiP07948, 82 interactors
MINTiP07948
STRINGi9606.ENSP00000428924

Chemistry databases

BindingDBiP07948

Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi66 – 72Combined sources7
Beta strandi78 – 80Combined sources3
Beta strandi89 – 95Combined sources7
Beta strandi97 – 104Combined sources8
Turni105 – 107Combined sources3
Beta strandi110 – 114Combined sources5
Turni115 – 117Combined sources3
Beta strandi118 – 120Combined sources3
Helixi244 – 246Combined sources3
Beta strandi247 – 255Combined sources9
Beta strandi260 – 266Combined sources7
Turni267 – 269Combined sources3
Beta strandi270 – 277Combined sources8
Helixi284 – 296Combined sources13
Beta strandi305 – 309Combined sources5
Beta strandi311 – 320Combined sources10
Helixi327 – 332Combined sources6
Helixi334 – 338Combined sources5
Helixi341 – 360Combined sources20
Helixi370 – 372Combined sources3
Beta strandi373 – 375Combined sources3
Beta strandi381 – 383Combined sources3
Helixi407 – 409Combined sources3
Helixi412 – 417Combined sources6
Helixi422 – 437Combined sources16
Helixi449 – 457Combined sources9
Beta strandi466 – 468Combined sources3
Helixi470 – 479Combined sources10
Helixi484 – 486Combined sources3
Helixi490 – 501Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1FNMR-A61-123[»]
1WA7NMR-A61-123[»]
3A4OX-ray3.00X233-512[»]
5XY1X-ray2.70A239-512[»]
ProteinModelPortaliP07948
SMRiP07948
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07948

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 123SH3PROSITE-ProRule annotationAdd BLAST61
Domaini129 – 226SH2PROSITE-ProRule annotationAdd BLAST98
Domaini247 – 501Protein kinasePROSITE-ProRule annotationAdd BLAST255

Domaini

The protein kinase domain plays an important role in its localization in the cell membrane.1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00760000118938
HOGENOMiHOG000233858
HOVERGENiHBG008761
InParanoidiP07948
KOiK05854
OMAiWMAYYNN
OrthoDBiEOG091G0D46
PhylomeDBiP07948
TreeFamiTF351634

Family and domain databases

CDDicd10364 SH2_Src_Lyn, 1 hit
cd12004 SH3_Lyn, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR035852 Lyn_SH2
IPR035748 Lyn_SH3
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 1 hit
PS50002 SH3, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P07948-1) [UniParc]FASTAAdd to basket
Also known as: LYN A, p56lyn

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

        10         20         30         40         50
MGCIKSKGKD SLSDDGVDLK TQPVRNTERT IYVRDPTSNK QQRPVPESQL
60 70 80 90 100
LPGQRFQTKD PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW
110 120 130 140 150
KAKSLLTKKE GFIPSNYVAK LNTLETEEWF FKDITRKDAE RQLLAPGNSA
160 170 180 190 200
GAFLIRESET LKGSFSLSVR DFDPVHGDVI KHYKIRSLDN GGYYISPRIT
210 220 230 240 250
FPCISDMIKH YQKQADGLCR RLEKACISPK PQKPWDKDAW EIPRESIKLV
260 270 280 290 300
KRLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD
310 320 330 340 350
KLVRLYAVVT REEPIYIITE YMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ
360 370 380 390 400
IAEGMAYIER KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR
410 420 430 440 450
EGAKFPIKWT APEAINFGCF TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA
460 470 480 490 500
DVMTALSQGY RMPRVENCPD ELYDIMKMCW KEKAEERPTF DYLQSVLDDF
510
YTATEGQYQQ QP
Length:512
Mass (Da):58,574
Last modified:January 23, 2007 - v3
Checksum:i408D3D461204E378
GO
Isoform 2 (identifier: P07948-2) [UniParc]FASTAAdd to basket
Also known as: LYN B, p53lyn

The sequence of this isoform differs from the canonical sequence as follows:
     23-43: Missing.

Show »
Length:491
Mass (Da):56,033
Checksum:iD74E4074D4B0C92A
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041737385D → Y in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00500223 – 43Missing in isoform 2. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16038 mRNA Translation: AAA59540.1
M79321 mRNA Translation: AAB50019.1
BC075001 mRNA Translation: AAH75001.1
BC075002 mRNA Translation: AAH75002.1
BC126456 mRNA Translation: AAI26457.1
BC126458 mRNA Translation: AAI26459.1
CCDSiCCDS47859.1 [P07948-2]
CCDS6162.1 [P07948-1]
PIRiA26719 TVHULY
RefSeqiNP_001104567.1, NM_001111097.2 [P07948-2]
NP_002341.1, NM_002350.3 [P07948-1]
XP_016868905.1, XM_017013416.1 [P07948-2]
UniGeneiHs.491767
Hs.545418

Genome annotation databases

EnsembliENST00000519728; ENSP00000428924; ENSG00000254087 [P07948-1]
ENST00000520220; ENSP00000428424; ENSG00000254087 [P07948-2]
GeneIDi4067
KEGGihsa:4067
UCSCiuc003xsk.5 human [P07948-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiLYN_HUMAN
AccessioniPrimary (citable) accession number: P07948
Secondary accession number(s): A0AVQ5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 221 of the entry and version 3 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health