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P37173 (TGFR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TGF-beta receptor type-2

Short name=TGFR-2
EC=2.7.11.30
Alternative name(s):
TGF-beta type II receptor
Transforming growth factor-beta receptor type II
Short name=TGF-beta receptor type II
Short name=TbetaR-II
Gene names
Name:TGFBR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. Ref.11

Catalytic activity

ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Homodimer. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The respective affinity of TGFRB1 and TGFRB2 for the ligands may modulate the kinetics of assembly of the receptor and may explain the different biological activities of TGFB1, TGFB2 and TGFB3. Interacts with DAXX. Interacts with TCTEX1D4. Interacts with ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor. Interacts with and is activated by SCUBE3; this interaction does not affect TGFB1-binding to TGFBR2. Interacts with VPS39; this interaction is independent of the receptor kinase activity and of the presence of TGF-beta. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.1.

Post-translational modification

Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.

Involvement in disease

Hereditary non-polyposis colorectal cancer 6 (HNPCC6) [MIM:614331]: An autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra-colonic tumors of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, HNPCC is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC' or 'incomplete HNPCC' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25

Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Loeys-Dietz syndrome 1B (LDS1B) [MIM:610168]: An aortic aneurysm syndrome with widespread systemic involvement. The disorder is characterized by arterial tortuosity and aneurysms, craniosynostosis, hypertelorism, and bifid uvula or cleft palate. Other findings include exotropy, micrognathia and retrognathia, structural brain abnormalities, intellectual deficit, congenital heart disease, translucent skin, joint hyperlaxity and aneurysm with dissection throughout the arterial tree.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.32 Ref.36 Ref.37 Ref.38 Ref.39

Loeys-Dietz syndrome 2B (LDS2B) [MIM:610380]: An aortic aneurysm syndrome with widespread systemic involvement. Physical findings include diffuse arterial aneurysms and dissections, prominent joint laxity, easy bruising, wide and atrophic scars, velvety and translucent skin with easily visible veins, spontaneous rupture of the spleen or bowel, and catastrophic complications of pregnancy, including rupture of the gravid uterus and the arteries, either during pregnancy or in the immediate postpartum period. Loeys-Dietz syndrome type 2 is characterized by the absence of craniofacial abnormalities with the exception of bifid uvula that can be present in some patients.
Note: The disease is caused by mutations affecting the gene represented in this entry. TGFBR2 mutations Cys-460 and His-460 have been reported to be associated with thoracic aortic aneurysms and dissection (TAAD). This phenotype, also known as thoracic aortic aneurysms type 3 (AAT3), is distinguised from LDS2B by having aneurysms restricted to thoracic aorta. As individuals carrying these mutations also exhibit descending aortic disease and aneurysms of other arteries (Ref.30), they have been considered as LDS2B by the OMIM resource. Ref.29 Ref.30 Ref.35

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Differentiation
Growth regulation
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAortic aneurysm
Disease mutation
Hereditary nonpolyposis colorectal cancer
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of protein kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

aging

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from direct assay PubMed 17471240. Source: UniProtKB

blood vessel development

Traceable author statement PubMed 10092230. Source: BHF-UCL

brain development

Inferred from sequence or structural similarity. Source: BHF-UCL

bronchus morphogenesis

Inferred from electronic annotation. Source: Ensembl

cartilage development

Inferred from electronic annotation. Source: Ensembl

common-partner SMAD protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

digestive tract development

Inferred from electronic annotation. Source: Ensembl

embryo implantation

Inferred from electronic annotation. Source: Ensembl

embryonic cranial skeleton morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

embryonic hemopoiesis

Inferred from sequence or structural similarity. Source: BHF-UCL

gastrulation

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from sequence or structural similarity. Source: BHF-UCL

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

lens development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

lens fiber cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

lung lobe morphogenesis

Inferred from electronic annotation. Source: Ensembl

mammary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

myeloid dendritic cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

organ regeneration

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from sequence or structural similarity. Source: BHF-UCL

pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 18453574PubMed 11157754. Source: BHF-UCL

patterning of blood vessels

Inferred from sequence or structural similarity. Source: BHF-UCL

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 12015308. Source: BHF-UCL

peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 12015308. Source: BHF-UCL

positive regulation of B cell tolerance induction

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of NK T cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of T cell tolerance induction

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell proliferation

Traceable author statement PubMed 7761852. Source: ProtInc

positive regulation of epithelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of mesenchymal cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of reactive oxygen species metabolic process

Inferred from mutant phenotype PubMed 20160708. Source: BHF-UCL

positive regulation of skeletal muscle tissue regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of tolerance induction to self antigen

Inferred from sequence or structural similarity. Source: BHF-UCL

protein phosphorylation

Inferred from direct assay PubMed 12015308. Source: BHF-UCL

receptor-mediated endocytosis

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

response to cholesterol

Inferred from direct assay PubMed 17878231. Source: BHF-UCL

response to drug

Inferred from direct assay PubMed 17878231. Source: BHF-UCL

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

trachea formation

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 18453574. Source: BHF-UCL

vasculogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcaveola

Inferred from direct assay PubMed 17878231. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

external side of plasma membrane

Inferred from direct assay PubMed 18453574. Source: BHF-UCL

integral component of membrane

Inferred from direct assay PubMed 7852346. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 8774881. Source: BHF-UCL

transforming growth factor beta receptor homodimeric complex

Inferred by curator PubMed 1326540. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

SMAD binding

Inferred from direct assay PubMed 11157754PubMed 18453574PubMed 11157754. Source: BHF-UCL

glycosaminoglycan binding

Inferred from direct assay PubMed 7852346. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 11157754PubMed 11157754. Source: BHF-UCL

receptor signaling protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

transforming growth factor beta binding

Inferred from direct assay Ref.23PubMed 18453574PubMed 7852346PubMed 11157754. Source: BHF-UCL

transforming growth factor beta receptor activity, type II

Inferred from electronic annotation. Source: InterPro

transforming growth factor beta-activated receptor activity

Inferred from direct assay PubMed 18453574PubMed 7852346. Source: BHF-UCL

transmembrane receptor protein serine/threonine kinase activity

Inferred from direct assay PubMed 12015308. Source: BHF-UCL

type I transforming growth factor beta receptor binding

Inferred from direct assay PubMed 11157754. Source: BHF-UCL

type III transforming growth factor beta receptor binding

Inferred from direct assay PubMed 11157754. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P37173-1)

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.
Isoform 2 (identifier: P37173-2)

The sequence of this isoform differs from the canonical sequence as follows:
     31-32: SV → SDVEMEAQKDEIICPSCNRTAHPLRHI

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.10
Chain23 – 567545TGF-beta receptor type-2
PRO_0000024426

Regions

Topological domain23 – 166144Extracellular Potential
Transmembrane167 – 18721Helical; Potential
Topological domain188 – 567380Cytoplasmic Potential
Domain244 – 544301Protein kinase
Nucleotide binding250 – 2589ATP By similarity

Sites

Active site3791Proton acceptor By similarity
Binding site2771ATP By similarity

Amino acid modifications

Modified residue5481Phosphoserine Ref.17
Modified residue5531Phosphoserine By similarity
Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 84 Ref.23 Ref.24
Disulfide bond54 ↔ 71 Ref.23 Ref.24
Disulfide bond61 ↔ 67 Ref.23 Ref.24
Disulfide bond77 ↔ 101 Ref.23 Ref.24
Disulfide bond121 ↔ 136 Ref.23 Ref.24
Disulfide bond138 ↔ 143 Ref.23 Ref.24

Natural variations

Alternative sequence31 – 322SV → SDVEMEAQKDEIICPSCNRT AHPLRHI in isoform 2.
VSP_012157
Natural variant361M → V. Ref.7
Corresponds to variant rs17025864 [ dbSNP | Ensembl ].
VAR_020510
Natural variant611C → R in a gastric adenocarcinoma sample; somatic mutation. Ref.34
VAR_041414
Natural variant731I → V in a colorectal cancer sample; somatic mutation. Ref.33
VAR_036070
Natural variant1911V → I. Ref.28 Ref.34
Corresponds to variant rs56105708 [ dbSNP | Ensembl ].
VAR_017606
Natural variant3061Q → HE in LDS1B.
VAR_066723
Natural variant3081L → P in LDS1B and LDS2B; has a negative effect on TGF-beta signaling. Ref.29 Ref.37
Corresponds to variant rs28934568 [ dbSNP | Ensembl ].
VAR_022351
Natural variant3151T → M in HNPCC6. Ref.25 Ref.34
Corresponds to variant rs34833812 [ dbSNP | Ensembl ].
VAR_008156
Natural variant3281H → Y in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.34
VAR_041415
Natural variant3361Y → N in LDS1B. Ref.31
VAR_022352
Natural variant3551A → P in LDS1B. Ref.31
VAR_022353
Natural variant3571G → W in LDS1B. Ref.31
VAR_022354
Natural variant3731M → I. Ref.34
Corresponds to variant rs35719192 [ dbSNP | Ensembl ].
VAR_041416
Natural variant3771H → R in LDS1B. Ref.38
VAR_066724
Natural variant3871V → M in a breast tumor. Ref.27 Ref.34
Corresponds to variant rs35766612 [ dbSNP | Ensembl ].
VAR_022355
Natural variant4351N → S in a breast tumor; signaling of TGF-beta significantly inhibited. Ref.27
VAR_022356
Natural variant4391V → A. Ref.1 Ref.4 Ref.5 Ref.6
Corresponds to variant rs1050833 [ dbSNP | Ensembl ].
VAR_028063
Natural variant4461D → N in LDS1B. Ref.32
VAR_066725
Natural variant4471V → A in a breast tumor; signaling of TGF-beta significantly inhibited. Ref.27
VAR_022357
Natural variant4491S → F in LDS1B and LDS2B; has a negative effect on TGF-beta signaling. Ref.29 Ref.38
VAR_022358
Natural variant4521L → M in a breast tumor; signaling of TGF-beta significantly inhibited. Ref.27
VAR_022359
Natural variant4571M → K in LDS1B. Ref.36
VAR_066726
Natural variant4601R → C in LDS2B. Ref.30
VAR_029760
Natural variant4601R → H in LDS2B. Ref.30
VAR_029761
Natural variant4901N → S in a gastric adenocarcinoma sample; somatic mutation. Ref.34
VAR_041417
Natural variant5091G → V in LDS1B. Ref.39
VAR_066727
Natural variant5101I → F in LDS1B. Ref.39
VAR_066728
Natural variant5101I → S in LDS2B. Ref.35
VAR_066729
Natural variant5141C → R in LDS1B. Ref.38
VAR_066730
Natural variant5211W → R in LDS1B. Ref.37
VAR_066731
Natural variant5261E → Q in esophageal cancer. Ref.26
VAR_015816
Natural variant5281R → C in LDS1B. Ref.31
VAR_022360
Natural variant5281R → H in LDS1B. Ref.31 Ref.33
VAR_022361
Natural variant5371R → C in LDS2B; has a negative effect on TGF-beta signaling. Ref.29
Corresponds to variant rs28934869 [ dbSNP | Ensembl ].
VAR_022362

Experimental info

Mutagenesis2771K → R: Abolishes kinase activity, TGF-beta signaling and interaction with DAXX. Ref.14
Sequence conflict3811K → N in BAA09332. Ref.6

Secondary structure

................................ 567
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: C541DA751FFBDBEB

FASTA56764,568
        10         20         30         40         50         60 
MGRGLLRGLW PLHIVLWTRI ASTIPPHVQK SVNNDMIVTD NNGAVKFPQL CKFCDVRFST 

        70         80         90        100        110        120 
CDNQKSCMSN CSITSICEKP QEVCVAVWRK NDENITLETV CHDPKLPYHD FILEDAASPK 

       130        140        150        160        170        180 
CIMKEKKKPG ETFFMCSCSS DECNDNIIFS EEYNTSNPDL LLVIFQVTGI SLLPPLGVAI 

       190        200        210        220        230        240 
SVIIIFYCYR VNRQQKLSST WETGKTRKLM EFSEHCAIIL EDDRSDISST CANNINHNTE 

       250        260        270        280        290        300 
LLPIELDTLV GKGRFAEVYK AKLKQNTSEQ FETVAVKIFP YEEYASWKTE KDIFSDINLK 

       310        320        330        340        350        360 
HENILQFLTA EERKTELGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRKL GSSLARGIAH 

       370        380        390        400        410        420 
LHSDHTPCGR PKMPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPTLSV DDLANSGQVG 

       430        440        450        460        470        480 
TARYMAPEVL ESRMNLENVE SFKQTDVYSM ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE 

       490        500        510        520        530        540 
HPCVESMKDN VLRDRGRPEI PSFWLNHQGI QMVCETLTEC WDHDPEARLT AQCVAERFSE 

       550        560 
LEHLDRLSGR SCSEEKIPED GSLNTTK 

« Hide

Isoform 2 [UniParc].

Checksum: 8ADCBA70F95E1CBB
Show »

FASTA59267,457

References

« Hide 'large scale' references
[1]"Expression cloning of the TGF-beta type II receptor, a functional transmembrane serine/threonine kinase."
Lin H.Y., Wang X.-F., Ng-Eaton E., Weinberg R.A., Lodish H.F.
Cell 68:775-785(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-439, SUBCELLULAR LOCATION.
Tissue: Liver.
[2]Erratum
Lin H.Y., Wang X.-F., Ng-Eaton E., Weinberg R.A., Lodish H.F.
Cell 70:1069-1069(1992) [PubMed] [Europe PMC] [Abstract]
[3]"A cDNA encoding the human transforming growth factor beta receptor suppresses the growth defect of a yeast mutant."
Nikawa J.
Gene 149:367-372(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Glial cell.
[4]"The genomic structure of the gene encoding the human transforming growth factor beta type II receptor (TGF-beta RII)."
Takenoshita S., Hagiwara K., Nagashima M., Gemma A., Bennett W.P., Harris C.C.
Genomics 36:341-344(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT ALA-439.
[5]"Genomic structure of the transforming growth factor beta type II receptor gene and its mutations in hereditary nonpolyposis colorectal cancers."
Lu S.-L., Zhang W.C., Akiyama Y., Nomizu T., Yuasa Y.
Cancer Res. 56:4595-4598(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT ALA-439.
[6]"Cloning of a cDNA encoding the human transforming growth factor-beta type II receptor: heterogeneity of the mRNA."
Ogasa H., Noma T., Murata H., Kawai S., Nakazawa A.
Gene 181:185-190(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-439.
Tissue: Liver.
[7]NIEHS SNPs program
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-36.
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Placenta.
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-37.
[11]"GS domain mutations that constitutively activate T beta R-I, the downstream signaling component in the TGF-beta receptor complex."
Wieser R., Wrana J.L., Massague J.
EMBO J. 14:2199-2208(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TGFBR1.
[12]"SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor."
Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.
Cell 95:779-791(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZFYVE9.
[13]"Oligomeric structure of type I and type II transforming growth factor beta receptors: homodimers form in the ER and persist at the plasma membrane."
Gilboa L., Wells R.G., Lodish H.F., Henis Y.I.
J. Cell Biol. 140:767-777(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION.
[14]"TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation."
Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A.
Nat. Cell Biol. 3:708-714(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAXX, MUTAGENESIS OF LYS-277.
[15]"TLP, a novel modulator of TGF-beta signaling, has opposite effects on Smad2- and Smad3-dependent signaling."
Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S., McNally J.G., Roberts A.B.
EMBO J. 22:4465-4477(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VPS39.
[16]"Identification of Tctex2beta, a novel dynein light chain family member that interacts with different transforming growth factor-beta receptors."
Meng Q.-J., Lux A., Holloschi A., Li J., Hughes J.M.X., Foerg T., McCarthy J.E.G., Heagerty A.M., Kioschis P., Hafner M., Garland J.M.
J. Biol. Chem. 281:37069-37080(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TCTEX1D4.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"SCUBE3 is an endogenous TGF-beta receptor ligand and regulates the epithelial-mesenchymal transition in lung cancer."
Wu Y.Y., Peck K., Chang Y.L., Pan S.H., Cheng Y.F., Lin J.C., Yang R.B., Hong T.M., Yang P.C.
Oncogene 30:3682-3693(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCUBE3.
[20]"Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex."
Hart P.J., Deep S., Taylor A.B., Shu Z., Hinck C.S., Hinck A.P.
Nat. Struct. Biol. 9:203-208(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 38-159 IN COMPLEX WITH TGF-BETA3.
[21]"The 1.1 A crystal structure of human TGF-beta type II receptor ligand binding domain."
Boesen C.C., Radaev S., Motyka S.A., Patamawenu A., Sun P.D.
Structure 10:913-919(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 49-159.
[22]"Solution structure and backbone dynamics of the TGFbeta type II receptor extracellular domain."
Deep S., Walker K.P. III, Shu Z., Hinck A.P.
Biochemistry 42:10126-10139(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 38-159.
[23]"Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding."
Groppe J., Hinck C.S., Samavarchi-Tehrani P., Zubieta C., Schuermann J.P., Taylor A.B., Schwarz P.M., Wrana J.L., Hinck A.P.
Mol. Cell 29:157-168(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 43-149 IN COMPLEX WITH TGFBR1 AND TGFB3, DISULFIDE BONDS.
[24]"Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily."
Radaev S., Zou Z., Huang T., Lafer E.M., Hinck A.P., Sun P.D.
J. Biol. Chem. 285:14806-14814(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 38-153 IN COMPLEX WITH TGFBR1 AND TGFB1, RECEPTOR AFFINITY FOR LIGANDS, DISULFIDE BONDS.
[25]"HNPCC associated with germline mutation in the TGF-beta type II receptor gene."
Lu S.-L., Kawabata M., Imamura T., Akiyama Y., Nomizu T., Miyazono K., Yuasa Y.
Nat. Genet. 19:17-18(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC6 MET-315.
[26]"A dominant negative mutation of transforming growth factor-beta receptor type II gene in microsatellite stable oesophageal carcinoma."
Tanaka S., Mori M., Mafune K., Ohno S., Sugimachi K.
Br. J. Cancer 82:1557-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ESOPHAGEAL CANCER GLN-526.
[27]"Inhibiting mutations in the transforming growth factor beta type 2 receptor in recurrent human breast cancer."
Luecke C.D., Philpott A., Metcalfe J.C., Thompson A.M., Hughes-Davies L., Kemp P.R., Hesketh R.
Cancer Res. 61:482-485(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BREAST TUMOR MET-387; SER-435; ALA-447 AND MET-452, CHARACTERIZATION OF VARIANTS BREAST TUMOR SER-435; ALA-447 AND MET-452.
[28]"A catalog of 106 single-nucleotide polymorphisms (SNPs) and 11 other types of variations in genes for transforming growth factor-beta1 (TGF-beta1) and its signaling pathway."
Watanabe Y., Kinoshita A., Yamada T., Ohta T., Kishino T., Matsumoto N., Ishikawa M., Niikawa N., Yoshiura K.
J. Hum. Genet. 47:478-483(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ILE-191.
[29]"Heterozygous TGFBR2 mutations in Marfan syndrome."
Mizuguchi T., Collod-Beroud G., Akiyama T., Abifadel M., Harada N., Morisaki T., Allard D., Varret M., Claustres M., Morisaki H., Ihara M., Kinoshita A., Yoshiura K., Junien C., Kajii T., Jondeau G., Ohta T., Kishino T. expand/collapse author list , Furukawa Y., Nakamura Y., Niikawa N., Boileau C., Matsumoto N.
Nat. Genet. 36:855-860(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LDS2B PRO-308; PHE-449 AND CYS-537, CHARACTERIZATION OF VARIANTS LDS2B PRO-308; PHE-449 AND CYS-537.
[30]"Mutations in transforming growth factor-beta receptor type II cause familial thoracic aortic aneurysms and dissections."
Pannu H., Fadulu V.T., Chang J., Lafont A., Hasham S.N., Sparks E., Giampietro P.F., Zaleski C., Estrera A.L., Safi H.J., Shete S., Willing M.C., Raman C.S., Milewicz D.M.
Circulation 112:513-520(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LDS2B CYS-460 AND HIS-460.
[31]"A syndrome of altered cardiovascular, craniofacial, neurocognitive and skeletal development caused by mutations in TGFBR1 or TGFBR2."
Loeys B.L., Chen J., Neptune E.R., Judge D.P., Podowski M., Holm T., Meyers J., Leitch C.C., Katsanis N., Sharifi N., Xu F.L., Myers L.A., Spevak P.J., Cameron D.E., De Backer J.F., Hellemans J., Chen Y., Davis E.C. expand/collapse author list , Webb C.L., Kress W., Coucke P.J., Rifkin D.B., De Paepe A.M., Dietz H.C.
Nat. Genet. 37:275-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LDS1B ASN-336; PRO-355; TRP-357; HIS-528 AND CYS-528.
[32]"Two novel and one known mutation of the TGFBR2 gene in Marfan syndrome not associated with FBN1 gene defects."
Disabella E., Grasso M., Marziliano N., Ansaldi S., Lucchelli C., Porcu E., Tagliani M., Pilotto A., Diegoli M., Lanzarini L., Malattia C., Pelliccia A., Ficcadenti A., Gabrielli O., Arbustini E.
Eur. J. Hum. Genet. 14:34-38(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LDS1B ASN-446.
[33]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-73 AND HIS-528.
[34]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-61; ILE-191; MET-315; TYR-328; ILE-373; MET-387 AND SER-490.
[35]"Loeys-Dietz syndrome type I and type II: clinical findings and novel mutations in two Italian patients."
Drera B., Ritelli M., Zoppi N., Wischmeijer A., Gnoli M., Fattori R., Calzavara-Pinton P.G., Barlati S., Colombi M.
Orphanet J. Rare Dis. 4:24-24(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LDS2B SER-510.
[36]"Progressive aortic root and pulmonary artery aneurysms in a neonate with Loeys-Dietz syndrome type 1B."
Muramatsu Y., Kosho T., Magota M., Yokotsuka T., Ito M., Yasuda A., Kito O., Suzuki C., Nagata Y., Kawai S., Ikoma M., Hatano T., Nakayama M., Kawamura R., Wakui K., Morisaki H., Morisaki T., Fukushima Y.
Am. J. Med. Genet. A 152:417-421(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LDS1B LYS-457.
[37]"Germline TGF-beta receptor mutations and skeletal fragility: a report on two patients with Loeys-Dietz syndrome."
Kirmani S., Tebben P.J., Lteif A.N., Gordon D., Clarke B.L., Hefferan T.E., Yaszemski M.J., McGrann P.S., Lindor N.M., Ellison J.W.
Am. J. Med. Genet. A 152:1016-1019(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LDS1B PRO-308 AND ARG-521.
[38]"Clinical features and genetic analysis of Korean patients with Loeys-Dietz syndrome."
Yang J.H., Ki C.S., Han H., Song B.G., Jang S.Y., Chung T.Y., Sung K., Lee H.J., Kim D.K.
J. Hum. Genet. 57:52-56(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LDS1B GLN-306 DELINS HIS-GLU; ARG-377; PHE-449 AND ARG-514.
[39]"A sporadic case of Loeys-Dietz syndrome type I with two novel mutations of the TGFBR2 gene."
Ha J.S., Kim Y.H.
Korean J. Pediatr. 54:272-275(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LDS1B VAL-509 AND PHE-510.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M85079 mRNA. Translation: AAA61164.1.
D28131 mRNA. Translation: BAA05673.1.
U52246 expand/collapse EMBL AC list , U52240, U52241, U52242, U52244, U52245 Genomic DNA. Translation: AAB17553.1.
U69152 expand/collapse EMBL AC list , U69146, U69147, U69148, U69149, U69150, U69151 Genomic DNA. Translation: AAB40916.1.
D50683 mRNA. Translation: BAA09332.1.
AY675319 Genomic DNA. Translation: AAT70724.1.
AK300383 mRNA. Translation: BAG62117.1.
CH471055 Genomic DNA. Translation: EAW64412.1.
CCDSCCDS2648.1. [P37173-1]
CCDS33727.1. [P37173-2]
PIRA42100.
RefSeqNP_001020018.1. NM_001024847.2. [P37173-2]
NP_003233.4. NM_003242.5. [P37173-1]
UniGeneHs.604277.
Hs.82028.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KTZX-ray2.15B38-159[»]
1M9ZX-ray1.05A49-159[»]
1PLONMR-A38-159[»]
2PJYX-ray3.00B42-149[»]
3KFDX-ray3.00E/F/G/H38-153[»]
ProteinModelPortalP37173.
SMRP37173. Positions 48-153, 244-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112906. 45 interactions.
DIPDIP-5939N.
IntActP37173. 17 interactions.
MINTMINT-206666.
STRING9606.ENSP00000351905.

Chemistry

BindingDBP37173.
ChEMBLCHEMBL4267.
GuidetoPHARMACOLOGY1795.

PTM databases

PhosphoSiteP37173.

Polymorphism databases

DMDM116242818.

Proteomic databases

MaxQBP37173.
PaxDbP37173.
PRIDEP37173.

Protocols and materials databases

DNASU7048.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295754; ENSP00000295754; ENSG00000163513. [P37173-1]
ENST00000359013; ENSP00000351905; ENSG00000163513. [P37173-2]
GeneID7048.
KEGGhsa:7048.
UCSCuc003ceo.3. human. [P37173-1]

Organism-specific databases

CTD7048.
GeneCardsGC03P030623.
GeneReviewsTGFBR2.
H-InvDBHIX0024332.
HGNCHGNC:11773. TGFBR2.
MIM133239. phenotype.
190182. gene.
610168. phenotype.
610380. phenotype.
614331. phenotype.
neXtProtNX_P37173.
Orphanet91387. Familial thoracic aortic aneurysm and aortic dissection.
144. Hereditary nonpolyposis colon cancer.
60030. Loeys-Dietz syndrome.
284973. Marfan syndrome type 2.
PharmGKBPA36486.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231495.
HOVERGENHBG104975.
KOK04388.
OMAWETSKPR.
OrthoDBEOG7JHM5B.
PhylomeDBP37173.
TreeFamTF314724.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkP37173.

Gene expression databases

ArrayExpressP37173.
BgeeP37173.
CleanExHS_TGFBR2.
GenevestigatorP37173.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR000333. TGFB_receptor.
IPR017194. Transform_growth_fac-b_typ-2.
IPR015013. Transforming_GF_b_rcpt_2_ecto.
[Graphical view]
PANTHERPTHR23255. PTHR23255. 1 hit.
PfamPF08917. ecTbetaR2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF037393. TGFRII. 1 hit.
PRINTSPR00653. ACTIVIN2R.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTGFBR2. human.
EvolutionaryTraceP37173.
GeneWikiTGF_beta_receptor_2.
GenomeRNAi7048.
NextBio27541.
PROP37173.
SOURCESearch...

Entry information

Entry nameTGFR2_HUMAN
AccessionPrimary (citable) accession number: P37173
Secondary accession number(s): B4DTV5 expand/collapse secondary AC list , Q15580, Q6DKT6, Q99474
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM