Protein

Tyrosine-protein phosphatase non-receptor type 11

Gene

PTPN11

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Positively regulates MAPK signal transduction pathway (PubMed:28074573). Dephosphorylates GAB1, ARHGAP35 and EGFR (PubMed:28074573). Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulatation of its RhoA binding activity. Dephosphorylates CDC73 (PubMed:26742426).5 Publications

Catalytic activityⁱ

Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate.PROSITE-ProRule annotation3 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	429	SubstrateBy similarity	1
Active siteⁱ	463	Phosphocysteine intermediate	1
Binding siteⁱ	510	SubstrateBy similarity	1

GO - Molecular functionⁱ

1-phosphatidylinositol-3-kinase activity Source: Reactome
cell adhesion molecule binding Source: Ensembl
D1 dopamine receptor binding Source: Ensembl
insulin receptor binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 7493946
insulin receptor substrate binding Source: Ensembl
non-membrane spanning protein tyrosine phosphatase activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 10655584
peptide hormone receptor binding Source: Ensembl
phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
phospholipase binding Source: Ensembl
phosphoprotein phosphatase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 15133037
phosphotyrosine residue binding
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 12051764
protein domain specific binding Source: Ensembl
protein kinase binding Source: ARUK-UCL
protein tyrosine phosphatase activity
Source: UniProtKB
Inferred from direct assayⁱ
receptor tyrosine kinase binding Source: Ensembl
SH3/SH2 adaptor activity
Source: BHF-UCL
Inferred from physical interactionⁱ
- 7493946

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

abortive mitotic cell cycle Source: Ensembl
activation of MAPK activity Source: Ensembl
atrioventricular canal development
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 12058348
axon guidance Source: Reactome
Bergmann glial cell differentiation Source: Ensembl
brain development
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 11704759
cellular response to cytokine stimulus Source: Reactome
cellular response to epidermal growth factor stimulus
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 28074573
cellular response to mechanical stimulus Source: Ensembl
cerebellar cortex formation Source: Ensembl
cytokine-mediated signaling pathway Source: Reactome
DNA damage checkpoint Source: Ensembl
ephrin receptor signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 10655584
epidermal growth factor receptor signaling pathway Source: Reactome
ERBB signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 15133037
face morphogenesis
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 11704759
fibroblast growth factor receptor signaling pathway Source: Reactome
genitalia development
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 12058348
glucose homeostasis Source: Ensembl
heart development
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 12058348
homeostasis of number of cells within a tissue Source: Ensembl
hormone-mediated signaling pathway Source: Ensembl
hormone metabolic process Source: Ensembl
inner ear development
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 12058348
integrin-mediated signaling pathway Source: Ensembl
interleukin-6-mediated signaling pathway Source: Reactome
intestinal epithelial cell migration Source: Ensembl
leukocyte migration Source: Reactome
megakaryocyte development Source: Ensembl
microvillus organization Source: Ensembl
multicellular organismal reproductive process Source: Ensembl
multicellular organism growth Source: Ensembl
negative regulation of cell adhesion mediated by integrin Source: Ensembl
negative regulation of cortisol secretion Source: Ensembl
negative regulation of growth hormone secretion Source: Ensembl
negative regulation of insulin secretion Source: Ensembl
neurotrophin TRK receptor signaling pathway Source: Ensembl
organ growth Source: Ensembl
peptidyl-tyrosine dephosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 15133037
platelet activation Source: Reactome
platelet-derived growth factor receptor signaling pathway Source: Ensembl
platelet formation Source: Ensembl
positive regulation of ERK1 and ERK2 cascade
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 28074573
positive regulation of glucose import
Source: BHF-UCL
Inferred from direct assayⁱ
- 7493946
positive regulation of hormone secretion Source: Ensembl
positive regulation of insulin receptor signaling pathway
Source: BHF-UCL
Inferred from direct assayⁱ
- 7493946
positive regulation of interferon-beta production Source: ARUK-UCL
positive regulation of interleukin-6 production Source: ARUK-UCL
positive regulation of mitotic cell cycle Source: Ensembl
positive regulation of protein kinase B signaling Source: Reactome
positive regulation of tumor necrosis factor production Source: ARUK-UCL
regulation of cell adhesion mediated by integrin
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 10655584
regulation of multicellular organism growth Source: Ensembl
regulation of protein complex assembly
Source: BHF-UCL
Inferred from direct assayⁱ
- 7493946
regulation of protein export from nucleus Source: Ensembl
regulation of type I interferon-mediated signaling pathway Source: Reactome
T cell costimulation Source: Reactome
triglyceride metabolic process Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protein phosphatase

Molecular function

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAⁱ	3.1.3.48 2681
Reactomeⁱ	R-HSA-1059683 Interleukin-6 signaling R-HSA-109704 PI3K Cascade R-HSA-110056 MAPK3 (ERK1) activation R-HSA-112411 MAPK1 (ERK2) activation R-HSA-114604 GPVI-mediated activation cascade R-HSA-1170546 Prolactin receptor signaling R-HSA-1257604 PIP3 activates AKT signaling R-HSA-1295596 Spry regulation of FGF signaling R-HSA-1433557 Signaling by SCF-KIT R-HSA-180292 GAB1 signalosome R-HSA-186763 Downstream signal transduction R-HSA-210990 PECAM1 interactions R-HSA-210993 Tie2 Signaling R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer R-HSA-2586552 Signaling by Leptin R-HSA-388841 Costimulation by the CD28 family R-HSA-389513 CTLA4 inhibitory signaling R-HSA-389948 PD-1 signaling R-HSA-391160 Signal regulatory protein family interactions R-HSA-418886 Netrin mediated repulsion signals R-HSA-432142 Platelet sensitization by LDL R-HSA-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling R-HSA-5654689 PI-3K cascade:FGFR1 R-HSA-5654693 FRS-mediated FGFR1 signaling R-HSA-5654695 PI-3K cascade:FGFR2 R-HSA-5654700 FRS-mediated FGFR2 signaling R-HSA-5654706 FRS-mediated FGFR3 signaling R-HSA-5654710 PI-3K cascade:FGFR3 R-HSA-5654712 FRS-mediated FGFR4 signaling R-HSA-5654720 PI-3K cascade:FGFR4 R-HSA-5654726 Negative regulation of FGFR1 signaling R-HSA-5654727 Negative regulation of FGFR2 signaling R-HSA-5654732 Negative regulation of FGFR3 signaling R-HSA-5654733 Negative regulation of FGFR4 signaling R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling R-HSA-877312 Regulation of IFNG signaling R-HSA-8853659 RET signaling R-HSA-8854691 Interleukin-20 family signaling R-HSA-8865999 MET activates PTPN11 R-HSA-8934593 Regulation of RUNX1 Expression and Activity R-HSA-9008059 Interleukin-37 signaling R-HSA-9028731 Activated NTRK2 signals through FRS2 and FRS3 R-HSA-909733 Interferon alpha/beta signaling R-HSA-912694 Regulation of IFNA signaling R-HSA-936964 Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
SignaLinkⁱ	Q06124
SIGNORⁱ	Q06124

Protein family/group databases

MoonDBⁱ	Q06124 Predicted

MoonDBⁱ

Q06124 Predicted

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Tyrosine-protein phosphatase non-receptor type 11 (EC:3.1.3.482 Publications) Alternative name(s): Protein-tyrosine phosphatase 1D Short name: PTP-1D Protein-tyrosine phosphatase 2C Short name: PTP-2C SH-PTP2 Short name: SHP-2 Short name: Shp2 SH-PTP3
Gene namesⁱ	Name:PTPN11 Synonyms:PTP2C, SHPTP2
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 12

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000179295.16
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9644 PTPN11
MIMⁱ	176876 gene
neXtProtⁱ	NX_Q06124

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

LEOPARD syndrome 1 (LPRD1)10 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_027188	279	Y → S in LPRD1. 2 PublicationsCorresponds to variant dbSNP:rs121918456EnsemblClinVar.	1
Natural variantⁱVAR_027190	465	A → T in LPRD1. 1 PublicationCorresponds to variant dbSNP:rs121918468Ensembl.	1
Natural variantⁱVAR_027191	468	G → A in LPRD1. 2 PublicationsCorresponds to variant dbSNP:rs121918469Ensembl.	1
Natural variantⁱVAR_015621	472	T → M in LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 5 PublicationsCorresponds to variant dbSNP:rs121918457Ensembl.	1
Natural variantⁱVAR_027192	502	R → L in LPRD1. 1 PublicationCorresponds to variant dbSNP:rs397507542Ensembl.	1
Natural variantⁱVAR_027193	502	R → W in LPRD1; reduced phosphatase activity. 2 PublicationsCorresponds to variant dbSNP:rs397507541Ensembl.	1
Natural variantⁱVAR_027194	510	Q → P in LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 4 PublicationsCorresponds to variant dbSNP:rs397509345Ensembl.	1
Natural variantⁱVAR_027196	514	Q → P in LPRD1. 1 PublicationCorresponds to variant dbSNP:rs121918470Ensembl.	1

Noonan syndrome 1 (NS1)15 Publications

The disease is caused by mutations affecting the gene represented in this entry. Mutations in PTPN11 account for more than 50% of the cases.

Disease descriptionA form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. Some patients with NS1 develop multiple giant cell lesions of the jaw or other bony or soft tissues, which are classified as pigmented villonodular synovitis (PVNS) when occurring in the jaw or joints.

Leukemia, juvenile myelomonocytic (JMML)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_015991	61	D → V in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs121918461EnsemblClinVar.	1
Natural variantⁱVAR_015992	61	D → Y in JMML. 1 PublicationCorresponds to variant dbSNP:rs397507510EnsemblClinVar.	1
Natural variantⁱVAR_015993	69	E → K in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs397507511EnsemblClinVar.	1
Natural variantⁱVAR_015996	72	A → T in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918453EnsemblClinVar.	1
Natural variantⁱVAR_015997	72	A → V in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918454EnsemblClinVar.	1
Natural variantⁱVAR_015998	76	E → A in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.	1
Natural variantⁱVAR_015999	76	E → G in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.	1
Natural variantⁱVAR_016000	76	E → K in JMML; increases protein tyrosine phosphatase activity against CDC73. 2 PublicationsCorresponds to variant dbSNP:rs121918464EnsemblClinVar.	1
Natural variantⁱVAR_016001	76	E → V in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.	1
Natural variantⁱVAR_016002	507	G → A in JMML. 1 PublicationCorresponds to variant dbSNP:rs397507546Ensembl.	1

Metachondromatosis (MC)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA skeletal disorder with radiologic features of both multiple exostoses and Ollier disease, characterized by the presence of exostoses, commonly of the bones of the hands and feet, and enchondromas of the metaphyses of long bones and iliac crest.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	463	C → S: Abolishes phosphatase activity. 1 Publication		1

Keywords - Diseaseⁱ

Deafness, Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5781
GeneReviewsⁱ	PTPN11
MalaCards human disease database More...MalaCardsⁱ	PTPN11
MIMⁱ	151100 phenotype 156250 phenotype 163950 phenotype 607785 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000179295
Orphanetⁱ	86834 Juvenile myelomonocytic leukemia 2499 Metachondromatosis 648 Noonan syndrome 500 Noonan syndrome with multiple lentigines
PharmGKBⁱ	PA33986

Chemistry databases

ChEMBLⁱ	CHEMBL3864
Drug and drug target database More...DrugBankⁱ	DB02779 Dodecane-Trimethylamine

Polymorphism and mutation databases

BioMutaⁱ	PTPN11
DMDMⁱ	84028248

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000094767	2 – 597	Tyrosine-protein phosphatase non-receptor type 11Add BLAST		596

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylthreonineCombined sources	1
Modified residueⁱ	62	PhosphotyrosineCombined sources	1
Modified residueⁱ	66	PhosphotyrosineBy similarity	1
Modified residueⁱ	546	Phosphotyrosine; by PDGFRBy similarity	1
Modified residueⁱ	584	Phosphotyrosine; by PDGFRCombined sources	1

Post-translational modificationⁱ

Phosphorylated on Tyr-546 and Tyr-584 upon receptor protein tyrosine kinase activation; which creates a binding site for GRB2 and other SH2-containing proteins. Phosphorylated upon activation of the receptor-type kinase FLT3. Phosphorylated upon activation of the receptor-type kinase PDGFRA (By similarity). Phosphorylated by activated PDGFRB.By similarity4 Publications

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	Q06124
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q06124
PaxDbⁱ	Q06124
PeptideAtlas More...PeptideAtlasⁱ	Q06124
PRIDEⁱ	Q06124
ProteomicsDBⁱ	58414 58415 [Q06124-2] 58416 [Q06124-3]
TopDownProteomicsⁱ	Q06124-2 [Q06124-2]

PTM databases

DEPODⁱ	Q06124
iPTMnetⁱ	Q06124
PhosphoSitePlusⁱ	Q06124

Expressionⁱ

Tissue specificityⁱ

Widely expressed, with highest levels in heart, brain, and skeletal muscle.3 Publications

Gene expression databases

Bgeeⁱ	ENSG00000179295 Expressed in 242 organ(s), highest expression level in substantia nigra
CleanExⁱ	HS_PTPN11
ExpressionAtlasⁱ	Q06124 baseline and differential
Genevisibleⁱ	Q06124 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB005377

HPAⁱ

CAB005377

Interactionⁱ

Subunit structureⁱ

Interacts with phosphorylated LIME1 and BCAR3. Interacts with SHB and INPP5D/SHIP1 (By similarity). Interacts with MILR1 (tyrosine-phosphorylated). Interacts with FLT1 (tyrosine-phosphorylated), FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-phosphorylated), KIT and GRB2. Interacts with PDGFRA (tyrosine phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) (By similarity). Interacts with PTPNS1 and CD84. Interacts with phosphorylated SIT1 and MPZL1. Interacts with FCRL4, FCRL6 and ANKHD1. Interacts with KIR2DL1; the interaction is enhanced by ARRB2. Interacts with GAB2. Interacts with TERT; the interaction retains TERT in the nucleus. Interacts with PECAM1 and FER. Interacts with EPHA2 (activated); participates in PTK2/FAK1 dephosphorylation in EPHA2 downstream signaling. Interacts with ROS1; mediates PTPN11 phosphorylation. Interacts with PDGFRB (tyrosine phosphorylated); this interaction increases the PTPN11 phosphatase activity. Interacts with GAREM1 isoform 1 (tyrosine phosphorylated); the interaction increases MAPK/ERK activity and does not affect the GRB2/SOS complex formation. Interacts with CDC73 (PubMed:26742426). Interacts with CEACAM1 (via cytoplasmic domain); this interaction depends on the monomer/dimer equilibrium and is phosphorylation-dependent (By similarity). Interacts with MPIG6B (via ITIM motif) (PubMed:23112346). Interacts with SIGLEC10 (By similarity). Interacts with FCRL3 (via phosphorylated ITIM motifs) (PubMed:11162587, PubMed:19843936).By similarity27 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
AR	P10275	12	EBI-297779,EBI-608057
CCKBR	P32239	5	EBI-297779,EBI-1753137
CD244	Q9BZW8	5	EBI-297779,EBI-1580565
CD33	P20138	5	EBI-297779,EBI-3906571
DDR1	Q08345	4	EBI-297779,EBI-711879
EEF1A1	P68105	2	EBI-297779,EBI-7645934	From Oryctolagus cuniculus.
EEF1A2	Q71V39	2	EBI-297779,EBI-7645815	From Oryctolagus cuniculus.
ERBB2	P04626	2	EBI-297779,EBI-641062
FLT1	P17948	2	EBI-297779,EBI-1026718
GAB1	Q13480	39	EBI-297779,EBI-517684
GAB2	Q9UQC2	4	EBI-297779,EBI-975200
GRB2	P62993	6	EBI-297779,EBI-401755
IGF1R	P08069	3	EBI-297779,EBI-475981
INSR	P06213	2	EBI-297779,EBI-475899
IRS1	P35568	3	EBI-297779,EBI-517592
Irs1	P35570	3	EBI-297779,EBI-520230	From Rattus norvegicus.
KIR2DL3	P43628	4	EBI-297779,EBI-8632435
KIT	P10721	29	EBI-297779,EBI-1379503
MET	P08581	13	EBI-297779,EBI-1039152
MPZL1	O95297	4	EBI-297779,EBI-963338
PDCD1	Q15116	3	EBI-297779,EBI-4314328
PDGFRB	P09619	8	EBI-297779,EBI-641237
PECAM1	P16284	7	EBI-297779,EBI-716404
PXN	P49023	3	EBI-297779,EBI-702209
RPIA	P49247	4	EBI-297779,EBI-744831
Sirpa	P97710	3	EBI-297779,EBI-7945080	From Rattus norvegicus.
TRIM32	Q13049	3	EBI-297779,EBI-742790

GO - Molecular functionⁱ

cell adhesion molecule binding Source: Ensembl
D1 dopamine receptor binding Source: Ensembl
insulin receptor binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 7493946
insulin receptor substrate binding Source: Ensembl
peptide hormone receptor binding Source: Ensembl
phospholipase binding Source: Ensembl
phosphotyrosine residue binding
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 12051764
protein domain specific binding Source: Ensembl
protein kinase binding Source: ARUK-UCL
receptor tyrosine kinase binding Source: Ensembl
SH3/SH2 adaptor activity
Source: BHF-UCL
Inferred from physical interactionⁱ
- 7493946

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	111745, 172 interactors
CORUMⁱ	Q06124
Database of interacting proteins More...DIPⁱ	DIP-516N
ELMⁱ	Q06124
IntActⁱ	Q06124, 72 interactors
Molecular INTeraction database More...MINTⁱ	Q06124
STRINGⁱ	9606.ENSP00000340944

Chemistry databases

BindingDBⁱ	Q06124

BindingDBⁱ

Q06124

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	4 – 6	Combined sources	3
Helixⁱ	13 – 23	Combined sources	11
Beta strandⁱ	28 – 33	Combined sources	6
Beta strandⁱ	35 – 37	Combined sources	3
Beta strandⁱ	41 – 47	Combined sources	7
Beta strandⁱ	50 – 57	Combined sources	8
Beta strandⁱ	59 – 61	Combined sources	3
Beta strandⁱ	63 – 65	Combined sources	3
Beta strandⁱ	70 – 73	Combined sources	4
Helixⁱ	74 – 82	Combined sources	9
Beta strandⁱ	83 – 85	Combined sources	3
Beta strandⁱ	87 – 90	Combined sources	4
Beta strandⁱ	91 – 93	Combined sources	3
Helixⁱ	107 – 109	Combined sources	3
Beta strandⁱ	113 – 116	Combined sources	4
Helixⁱ	119 – 129	Combined sources	11
Beta strandⁱ	134 – 139	Combined sources	6
Beta strandⁱ	141 – 143	Combined sources	3
Beta strandⁱ	147 – 153	Combined sources	7
Beta strandⁱ	154 – 156	Combined sources	3
Beta strandⁱ	166 – 175	Combined sources	10
Beta strandⁱ	178 – 184	Combined sources	7
Beta strandⁱ	187 – 189	Combined sources	3
Helixⁱ	190 – 199	Combined sources	10
Beta strandⁱ	202 – 204	Combined sources	3
Turnⁱ	205 – 207	Combined sources	3
Beta strandⁱ	208 – 210	Combined sources	3
Beta strandⁱ	218 – 222	Combined sources	5
Helixⁱ	223 – 225	Combined sources	3
Helixⁱ	226 – 234	Combined sources	9
Helixⁱ	251 – 253	Combined sources	3
Helixⁱ	256 – 258	Combined sources	3
Helixⁱ	259 – 262	Combined sources	4
Helixⁱ	266 – 269	Combined sources	4
Helixⁱ	271 – 276	Combined sources	6
Beta strandⁱ	277 – 279	Combined sources	3
Helixⁱ	286 – 288	Combined sources	3
Beta strandⁱ	289 – 291	Combined sources	3
Beta strandⁱ	304 – 310	Combined sources	7
Beta strandⁱ	319 – 321	Combined sources	3
Helixⁱ	323 – 325	Combined sources	3
Beta strandⁱ	327 – 331	Combined sources	5
Helixⁱ	335 – 337	Combined sources	3
Helixⁱ	338 – 347	Combined sources	10
Beta strandⁱ	352 – 355	Combined sources	4
Beta strandⁱ	359 – 361	Combined sources	3
Beta strandⁱ	364 – 366	Combined sources	3
Beta strandⁱ	376 – 380	Combined sources	5
Beta strandⁱ	383 – 392	Combined sources	10
Beta strandⁱ	394 – 405	Combined sources	12
Helixⁱ	413 – 415	Combined sources	3
Beta strandⁱ	417 – 424	Combined sources	8
Beta strandⁱ	429 – 431	Combined sources	3
Beta strandⁱ	434 – 436	Combined sources	3
Helixⁱ	437 – 451	Combined sources	15
Beta strandⁱ	459 – 467	Combined sources	9
Helixⁱ	468 – 486	Combined sources	19
Beta strandⁱ	488 – 492	Combined sources	5
Helixⁱ	494 – 502	Combined sources	9
Helixⁱ	512 – 528	Combined sources	17
Beta strandⁱ	585 – 589	Combined sources	5

Show more details

3D structure databases

ProteinModelPortalⁱ	Q06124
SMRⁱ	Q06124
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q06124

EvolutionaryTraceⁱ

Q06124

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	6 – 102	SH2 1PROSITE-ProRule annotationAdd BLAST	97
Domainⁱ	112 – 216	SH2 2PROSITE-ProRule annotationAdd BLAST	105
Domainⁱ	247 – 521	Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST	275

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	463 – 469	Substrate bindingBy similarity		7

Domainⁱ

The SH2 domains repress phosphatase activity. Binding of these domains to phosphotyrosine-containing proteins relieves this auto-inhibition, possibly by inducing a conformational change in the enzyme.

Sequence similaritiesⁱ

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily.Curated

Keywords - Domainⁱ

Repeat, SH2 domain

Phylogenomic databases

eggNOGⁱ	KOG0790 Eukaryota COG5599 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00920000148980
HOGENOMⁱ	HOG000273907
HOVERGENⁱ	HBG000223
InParanoidⁱ	Q06124
KEGG Orthology (KO) More...KOⁱ	K07293
OMAⁱ	KEYGAMR
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0VZ3
PhylomeDBⁱ	Q06124
TreeFamⁱ	TF351632

Family and domain databases

Gene3Dⁱ	3.30.505.10, 2 hits 3.90.190.10, 1 hit
InterProⁱ	View protein in InterPro IPR029021 Prot-tyrosine_phosphatase-like IPR000242 PTPase_domain IPR000980 SH2 IPR036860 SH2_dom_sf IPR016130 Tyr_Pase_AS IPR003595 Tyr_Pase_cat IPR012152 Tyr_Pase_non-rcpt_typ-6/11 IPR000387 TYR_PHOSPHATASE_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00017 SH2, 2 hits PF00102 Y_phosphatase, 1 hit
PIRSFⁱ	PIRSF000929 Tyr-Ptase_nr_6, 1 hit
PRINTSⁱ	PR00700 PRTYPHPHTASE PR00401 SH2DOMAIN
SMARTⁱ	View protein in SMART SM00194 PTPc, 1 hit SM00404 PTPc_motif, 1 hit SM00252 SH2, 2 hits
SUPFAMⁱ	SSF52799 SSF52799, 1 hit SSF55550 SSF55550, 2 hits
PROSITEⁱ	View protein in PROSITE PS50001 SH2, 2 hits PS00383 TYR_PHOSPHATASE_1, 1 hit PS50056 TYR_PHOSPHATASE_2, 1 hit PS50055 TYR_PHOSPHATASE_PTP, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q06124-1) [UniParc]FASTA Add to basket

Also known as: PTP2Ci

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.

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        10         20         30         40         50
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA 
        60         70         80         90        100
VTHIKIQNTG DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY 
       110        120        130        140        150
PLNCADPTSE RWFHGHLSGK EAEKLLTEKG KHGSFLVRES QSHPGDFVLS 
       160        170        180        190        200
VRTGDDKGES NDGKSKVTHV MIRCQELKYD VGGGERFDSL TDLVEHYKKN 
       210        220        230        240        250
PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT DKVKQGFWEE 
       260        270        280        290        300
FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP 
       310        320        330        340        350
VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS 
       360        370        380        390        400
RVIVMTTKEV ERGKSKCVKY WPDEYALKEY GVMRVRNVKE SAAHDYTLRE 
       410        420        430        440        450
LKLSKVGQAL LQGNTERTVW QYHFRTWPDH GVPSDPGGVL DFLEEVHHKQ 
       460        470        480        490        500
ESIMDAGPVV VHCSAGIGRT GTFIVIDILI DIIREKGVDC DIDVPKTIQM 
       510        520        530        540        550
VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK RKGHEYTNIK 
       560        570        580        590 
YSLADQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQKSFR

Length:597

Mass (Da):68,436

Last modified:December 20, 2005 - v2

Checksum:ⁱ37E8BFC7ECA2D03F

Isoform 2 (identifier: Q06124-2) [UniParc]FASTA Add to basket

Also known as: PTP2C

The sequence of this isoform differs from the canonical sequence as follows:
408-411: Missing.

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        10         20         30         40         50
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA 
        60         70         80         90        100
VTHIKIQNTG DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY 
       110        120        130        140        150
PLNCADPTSE RWFHGHLSGK EAEKLLTEKG KHGSFLVRES QSHPGDFVLS 
       160        170        180        190        200
VRTGDDKGES NDGKSKVTHV MIRCQELKYD VGGGERFDSL TDLVEHYKKN 
       210        220        230        240        250
PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT DKVKQGFWEE 
       260        270        280        290        300
FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP 
       310        320        330        340        350
VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS 
       360        370        380        390        400
RVIVMTTKEV ERGKSKCVKY WPDEYALKEY GVMRVRNVKE SAAHDYTLRE 
       410        420        430        440        450
LKLSKVGQGN TERTVWQYHF RTWPDHGVPS DPGGVLDFLE EVHHKQESIM 
       460        470        480        490        500
DAGPVVVHCS AGIGRTGTFI VIDILIDIIR EKGVDCDIDV PKTIQMVRSQ 
       510        520        530        540        550
RSGMVQTEAQ YRFIYMAVQH YIETLQRRIE EEQKSKRKGH EYTNIKYSLA 
       560        570        580        590 
DQTSGDQSPL PPCTPTPPCA EMREDSARVY ENVGLMQQQK SFR

Show »

Length:593

Mass (Da):68,011

Checksum:ⁱ9CDBEFFA5E6CCB45

Isoform 3 (identifier: Q06124-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
     408-411: Missing.
     464-464: S → R
     465-597: Missing.

« Hide

        10         20         30         40         50
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA 
        60         70         80         90        100
VTHIKIQNTG DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY 
       110        120        130        140        150
PLNCADPTSE RWFHGHLSGK EAEKLLTEKG KHGSFLVRES QSHPGDFVLS 
       160        170        180        190        200
VRTGDDKGES NDGKSKVTHV MIRCQELKYD VGGGERFDSL TDLVEHYKKN 
       210        220        230        240        250
PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT DKVKQGFWEE 
       260        270        280        290        300
FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP 
       310        320        330        340        350
VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS 
       360        370        380        390        400
RVIVMTTKEV ERGKSKCVKY WPDEYALKEY GVMRVRNVKE SAAHDYTLRE 
       410        420        430        440        450
LKLSKVGQGN TERTVWQYHF RTWPDHGVPS DPGGVLDFLE EVHHKQESIM 
       460
DAGPVVVHCR

Show »

Length:460

Mass (Da):52,828

Checksum:ⁱEB8E1553B37F1CC0

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A0U1RRI0	A0A0U1RRI0_HUMAN	Tyrosine-protein phosphatase non-re... Tyrosine-protein phosphatase non-receptor type 11	PTPN11	196	Annotation score:
H0YF12	H0YF12_HUMAN	Tyrosine-protein phosphatase non-re... Tyrosine-protein phosphatase non-receptor type 11	PTPN11	108	Annotation score:
A0A1W2PPU4	A0A1W2PPU4_HUMAN	Tyrosine-protein phosphatase non-re... Tyrosine-protein phosphatase non-receptor type 11	PTPN11	216	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	539	S → R in BAA02740 (PubMed:8216283).Curated		1
Sequence conflictⁱ	552	S → P in BAA02740 (PubMed:8216283).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_027183	2	T → I in NS1. 1 PublicationCorresponds to variant dbSNP:rs267606990EnsemblClinVar.	1
Natural variantⁱVAR_015601	42	T → A in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507501EnsemblClinVar.	1
Natural variantⁱVAR_027184	58	N → K in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507506EnsemblClinVar.	1
Natural variantⁱVAR_066060	59	T → A in NS1. 1 PublicationCorresponds to variant dbSNP:rs886043790EnsemblClinVar.	1
Natural variantⁱVAR_015602	60	G → A in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507509EnsemblClinVar.	1
Natural variantⁱVAR_015990	60	G → V in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs397507509EnsemblClinVar.	1
Natural variantⁱVAR_015603	61	D → G in NS1. 4 PublicationsCorresponds to variant dbSNP:rs121918461EnsemblClinVar.	1
Natural variantⁱVAR_015604	61	D → N in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507510EnsemblClinVar.	1
Natural variantⁱVAR_015991	61	D → V in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs121918461EnsemblClinVar.	1
Natural variantⁱVAR_015992	61	D → Y in JMML. 1 PublicationCorresponds to variant dbSNP:rs397507510EnsemblClinVar.	1
Natural variantⁱVAR_015605	62	Y → D in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 PublicationsCorresponds to variant dbSNP:rs121918460EnsemblClinVar.	1
Natural variantⁱVAR_015606	63	Y → C in NS1. 6 PublicationsCorresponds to variant dbSNP:rs121918459EnsemblClinVar.	1
Natural variantⁱVAR_015993	69	E → K in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs397507511EnsemblClinVar.	1
Natural variantⁱVAR_027185	69	E → Q in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507511EnsemblClinVar.	1
Natural variantⁱVAR_015994	71	F → K in acute myeloid leukemia; requires 2 nucleotide substitutions. 1 Publication	1
Natural variantⁱVAR_015995	71	F → L in myelodysplastic syndrome. 2 PublicationsCorresponds to variant dbSNP:rs397507512EnsemblClinVar.	1
Natural variantⁱVAR_015607	72	A → G in NS1. 3 PublicationsCorresponds to variant dbSNP:rs121918454EnsemblClinVar.	1
Natural variantⁱVAR_015608	72	A → S in NS1. 3 PublicationsCorresponds to variant dbSNP:rs121918453EnsemblClinVar.	1
Natural variantⁱVAR_015996	72	A → T in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918453EnsemblClinVar.	1
Natural variantⁱVAR_015997	72	A → V in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918454EnsemblClinVar.	1
Natural variantⁱVAR_015609	73	T → I in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 PublicationsCorresponds to variant dbSNP:rs121918462EnsemblClinVar.	1
Natural variantⁱVAR_015998	76	E → A in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.	1
Natural variantⁱVAR_015610	76	E → D in NS1. 3 PublicationsCorresponds to variant dbSNP:rs397507514EnsemblClinVar.	1
Natural variantⁱVAR_015999	76	E → G in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.	1
Natural variantⁱVAR_016000	76	E → K in JMML; increases protein tyrosine phosphatase activity against CDC73. 2 PublicationsCorresponds to variant dbSNP:rs121918464EnsemblClinVar.	1
Natural variantⁱVAR_016001	76	E → V in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.	1
Natural variantⁱVAR_027186	79	Q → P in NS1. 1 Publication	1
Natural variantⁱVAR_015611	79	Q → R in NS1. 4 PublicationsCorresponds to variant dbSNP:rs121918466EnsemblClinVar.	1
Natural variantⁱVAR_015612	106	D → A in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507517EnsemblClinVar.	1
Natural variantⁱVAR_015613	139	E → D in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507520EnsemblClinVar.	1
Natural variantⁱVAR_027187	256	Q → R in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507523EnsemblClinVar.	1
Natural variantⁱVAR_078101	261	L → F in NS1; increases MAPK signaling; increases protein tyrosine phosphatase activity; changed substrate selectivity for GAB1. 1 PublicationCorresponds to variant dbSNP:rs397507525EnsemblClinVar.	1
Natural variantⁱVAR_078102	261	L → H in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 PublicationCorresponds to variant dbSNP:rs765642157Ensembl.	1
Natural variantⁱVAR_078103	262	L → F in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 Publication	1
Natural variantⁱVAR_078104	262	L → R in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 PublicationCorresponds to variant dbSNP:rs397507526EnsemblClinVar.	1
Natural variantⁱVAR_078105	265	R → Q in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 PublicationCorresponds to variant dbSNP:rs376607329EnsemblClinVar.	1
Natural variantⁱVAR_015614	279	Y → C in NS1 and LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 7 PublicationsCorresponds to variant dbSNP:rs121918456EnsemblClinVar.	1
Natural variantⁱVAR_027188	279	Y → S in LPRD1. 2 PublicationsCorresponds to variant dbSNP:rs121918456EnsemblClinVar.	1
Natural variantⁱVAR_015615	282	I → V in NS1. 3 PublicationsCorresponds to variant dbSNP:rs397507529EnsemblClinVar.	1
Natural variantⁱVAR_015617	285	F → L in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507531EnsemblClinVar.	1
Natural variantⁱVAR_015616	285	F → S in NS1. 2 PublicationsCorresponds to variant dbSNP:rs121918463EnsemblClinVar.	1
Natural variantⁱVAR_015619	308	N → D in NS1; common mutation. 5 PublicationsCorresponds to variant dbSNP:rs28933386EnsemblClinVar.	1
Natural variantⁱVAR_015618	308	N → S in NS1; some patients also manifest giant cell lesions of bone and soft tissue. 2 PublicationsCorresponds to variant dbSNP:rs121918455EnsemblClinVar.	1
Natural variantⁱVAR_015620	309	I → V in NS1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs201787206EnsemblClinVar.	1
Natural variantⁱVAR_027189	415	T → M in NS1. 1 PublicationCorresponds to variant dbSNP:rs121918467Ensembl.	1
Natural variantⁱVAR_027190	465	A → T in LPRD1. 1 PublicationCorresponds to variant dbSNP:rs121918468Ensembl.	1
Natural variantⁱVAR_027191	468	G → A in LPRD1. 2 PublicationsCorresponds to variant dbSNP:rs121918469Ensembl.	1
Natural variantⁱVAR_015621	472	T → M in LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 5 PublicationsCorresponds to variant dbSNP:rs121918457Ensembl.	1
Natural variantⁱVAR_071706	495	P → S in NS1; increased phosphatase activity. 1 PublicationCorresponds to variant dbSNP:rs397507539Ensembl.	1
Natural variantⁱVAR_027192	502	R → L in LPRD1. 1 PublicationCorresponds to variant dbSNP:rs397507542Ensembl.	1
Natural variantⁱVAR_027193	502	R → W in LPRD1; reduced phosphatase activity. 2 PublicationsCorresponds to variant dbSNP:rs397507541Ensembl.	1
Natural variantⁱVAR_015622	505	R → K in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507543Ensembl.	1
Natural variantⁱVAR_015623	506	S → T in NS1. 2 PublicationsCorresponds to variant dbSNP:rs121918458Ensembl.	1
Natural variantⁱVAR_016002	507	G → A in JMML. 1 PublicationCorresponds to variant dbSNP:rs397507546Ensembl.	1
Natural variantⁱVAR_016003	507	G → R in NS1 and JMML; JMML patient also shows growth retardation and pulmonic stenosis. 2 PublicationsCorresponds to variant dbSNP:rs397507545Ensembl.	1
Natural variantⁱVAR_015624	508	M → V in NS1. 3 Publications

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UniProtKB - Q06124 (PTN11_HUMAN)

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Tyrosine-protein phosphatase non-receptor type 11

PTPN11

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

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Cytosol

Mitochondrion

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

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Functionⁱ

GO - Molecular functionⁱ

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Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ