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P10600

- TGFB3_HUMAN

UniProt

P10600 - TGFB3_HUMAN

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Protein

Transforming growth factor beta-3

Gene
TGFB3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in embryogenesis and cell differentiation.

GO - Molecular functioni

  1. identical protein binding Source: BHF-UCL
  2. protein binding Source: UniProtKB
  3. transforming growth factor beta binding Source: BHF-UCL
  4. type II transforming growth factor beta receptor binding Source: BHF-UCL
  5. type I transforming growth factor beta receptor binding Source: BHF-UCL

GO - Biological processi

  1. activation of MAPK activity Source: Ensembl
  2. aging Source: Ensembl
  3. blood coagulation Source: Reactome
  4. cell-cell junction organization Source: BHF-UCL
  5. cell growth Source: InterPro
  6. detection of hypoxia Source: BHF-UCL
  7. digestive tract development Source: Ensembl
  8. embryonic neurocranium morphogenesis Source: Ensembl
  9. extracellular matrix organization Source: Reactome
  10. face morphogenesis Source: BHF-UCL
  11. female pregnancy Source: Ensembl
  12. frontal suture morphogenesis Source: Ensembl
  13. inner ear development Source: Ensembl
  14. in utero embryonic development Source: BHF-UCL
  15. lung alveolus development Source: BHF-UCL
  16. mammary gland development Source: BHF-UCL
  17. menstrual cycle phase Source: BHF-UCL
  18. negative regulation of cell proliferation Source: BHF-UCL
  19. negative regulation of DNA replication Source: BHF-UCL
  20. negative regulation of macrophage cytokine production Source: DFLAT
  21. negative regulation of neuron apoptotic process Source: BHF-UCL
  22. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  23. odontogenesis Source: BHF-UCL
  24. ossification involved in bone remodeling Source: BHF-UCL
  25. palate development Source: BHF-UCL
  26. platelet activation Source: Reactome
  27. platelet degranulation Source: Reactome
  28. positive regulation of apoptotic process Source: BHF-UCL
  29. positive regulation of bone mineralization Source: BHF-UCL
  30. positive regulation of cell division Source: UniProtKB-KW
  31. positive regulation of collagen biosynthetic process Source: BHF-UCL
  32. positive regulation of DNA replication Source: BHF-UCL
  33. positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  34. positive regulation of filopodium assembly Source: BHF-UCL
  35. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  36. positive regulation of protein secretion Source: BHF-UCL
  37. positive regulation of SMAD protein import into nucleus Source: BHF-UCL
  38. positive regulation of transcription, DNA-templated Source: BHF-UCL
  39. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  40. response to estrogen Source: Ensembl
  41. response to hypoxia Source: BHF-UCL
  42. response to laminar fluid shear stress Source: Ensembl
  43. response to progesterone Source: BHF-UCL
  44. salivary gland morphogenesis Source: BHF-UCL
  45. SMAD protein import into nucleus Source: Ensembl
  46. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Mitogen

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.
REACT_163906. ECM proteoglycans.
SignaLinkiP10600.

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming growth factor beta-3
Short name:
TGF-beta-3
Cleaved into the following chain:
Gene namesi
Name:TGFB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:11769. TGFB3.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. extracellular matrix Source: BHF-UCL
  3. extracellular region Source: Reactome
  4. extracellular space Source: Ensembl
  5. neuronal cell body Source: Ensembl
  6. nucleus Source: Ensembl
  7. plasma membrane Source: BHF-UCL
  8. platelet alpha granule lumen Source: Reactome
  9. T-tubule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Arrhythmogenic right ventricular dysplasia, familial, 1 (ARVD1) [MIM:107970]: A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Rienhoff syndrome (RNHF) [MIM:615582]: A congenital syndrome characterized by abnormal development of several mesenchymal-derived tissues, including muscle and craniopalatofacial structures, accompanied by low muscle mass, growth retardation, distal arthrogryposis. Additional clinical features include arachnodactyly, pectus excavatum, pes planus, and hyperextensible large joints, as well as hypertelorism and bifid uvula. There is no evidence of vascular disease.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti409 – 4091C → Y in RNHF; hypomorphic mutation; results in impaired TGF-beta signaling. 1 Publication
VAR_070924

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

MIMi107970. phenotype.
615582. phenotype.
Orphaneti293899. Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
293888. Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
293910. Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
PharmGKBiPA36483.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed predictionAdd
BLAST
Chaini24 – 300277Latency-associated peptidePRO_0000033796Add
BLAST
Chaini301 – 412112Transforming growth factor beta-3PRO_0000033797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...) Reviewed prediction
Glycosylationi135 – 1351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi142 – 1421N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi307 ↔ 316
Disulfide bondi315 ↔ 378
Disulfide bondi344 ↔ 409
Disulfide bondi348 ↔ 411
Disulfide bondi377 – 377Interchain By similarity

Post-translational modificationi

The precursor is cleaved into mature TGF-beta-3 and LAP, which remains non-covalently linked to mature TGF-beta-3 rendering it inactive By similarity.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP10600.
PRIDEiP10600.

PTM databases

PhosphoSiteiP10600.

Miscellaneous databases

PMAP-CutDBP10600.

Expressioni

Gene expression databases

ArrayExpressiP10600.
BgeeiP10600.
CleanExiHS_TGFB3.
GenevestigatoriP10600.

Organism-specific databases

HPAiCAB018337.
HPA027923.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Interacts with ASPN.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TGFBR2P371738EBI-1033020,EBI-296151

Protein-protein interaction databases

BioGridi112901. 7 interactions.
DIPiDIP-5937N.
IntActiP10600. 6 interactions.
MINTiMINT-8177755.
STRINGi9606.ENSP00000238682.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi304 – 3096
Beta strandi314 – 3185
Beta strandi321 – 3233
Helixi324 – 3285
Beta strandi333 – 3353
Beta strandi337 – 3404
Beta strandi343 – 3464
Turni350 – 3534
Helixi357 – 36812
Helixi370 – 3723
Beta strandi377 – 3804
Beta strandi382 – 39211
Beta strandi395 – 40612
Beta strandi408 – 4125

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KTZX-ray2.15A301-412[»]
1TGJX-ray2.00A301-412[»]
1TGKX-ray3.30A301-412[»]
2PJYX-ray3.00A301-412[»]
3EO1X-ray3.10C/F/I/L301-412[»]
ProteinModelPortaliP10600.
SMRiP10600. Positions 24-412.

Miscellaneous databases

EvolutionaryTraceiP10600.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi261 – 2633Cell attachment site Reviewed prediction

Sequence similaritiesi

Belongs to the TGF-beta family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG269146.
HOGENOMiHOG000290198.
HOVERGENiHBG074115.
InParanoidiP10600.
KOiK13377.
OMAiPEPSVMT.
OrthoDBiEOG70GMFT.
PhylomeDBiP10600.
TreeFamiTF351793.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR016319. TGF-beta.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
IPR015618. Transform_grow_fac_b3.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PIRSFiPIRSF001787. TGF-beta. 1 hit.
PRINTSiPR01423. TGFBETA.
PR01426. TGFBETA3.
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10600-1 [UniParc]FASTAAdd to Basket

« Hide

MKMHLQRALV VLALLNFATV SLSLSTCTTL DFGHIKKKRV EAIRGQILSK    50
LRLTSPPEPT VMTHVPYQVL ALYNSTRELL EEMHGEREEG CTQENTESEY 100
YAKEIHKFDM IQGLAEHNEL AVCPKGITSK VFRFNVSSVE KNRTNLFRAE 150
FRVLRVPNPS SKRNEQRIEL FQILRPDEHI AKQRYIGGKN LPTRGTAEWL 200
SFDVTDTVRE WLLRRESNLG LEISIHCPCH TFQPNGDILE NIHEVMEIKF 250
KGVDNEDDHG RGDLGRLKKQ KDHHNPHLIL MMIPPHRLDN PGQGGQRKKR 300
ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY 350
LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ 400
LSNMVVKSCK CS 412
Length:412
Mass (Da):47,328
Last modified:July 1, 1989 - v1
Checksum:i3CAD3548D3AEA178
GO

Sequence cautioni

The sequence CAA33024.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601T → M.1 Publication
Corresponds to variant rs4252315 [ dbSNP | Ensembl ].
VAR_016315
Natural varianti409 – 4091C → Y in RNHF; hypomorphic mutation; results in impaired TGF-beta signaling. 1 Publication
VAR_070924

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03241 mRNA. Translation: AAA61161.1.
X14149 mRNA. Translation: CAA32362.1.
X14885
, X14886, X14887, X14888, X14889, X14890, X14891 Genomic DNA. Translation: CAA33024.1. Different initiation.
AY140241 Genomic DNA. Translation: AAM96819.1.
AY208161 Genomic DNA. Translation: AAO13495.1.
AF107885 Genomic DNA. Translation: AAC79727.1.
CCDSiCCDS9846.1.
PIRiA36169.
RefSeqiNP_003230.1. NM_003239.2.
XP_005268085.1. XM_005268028.1.
UniGeneiHs.592317.

Genome annotation databases

EnsembliENST00000238682; ENSP00000238682; ENSG00000119699.
GeneIDi7043.
KEGGihsa:7043.
UCSCiuc001xsc.2. human.

Polymorphism databases

DMDMi135684.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
SeattleSNPs
Wikipedia

TGF beta-3 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03241 mRNA. Translation: AAA61161.1 .
X14149 mRNA. Translation: CAA32362.1 .
X14885
, X14886 , X14887 , X14888 , X14889 , X14890 , X14891 Genomic DNA. Translation: CAA33024.1 . Different initiation.
AY140241 Genomic DNA. Translation: AAM96819.1 .
AY208161 Genomic DNA. Translation: AAO13495.1 .
AF107885 Genomic DNA. Translation: AAC79727.1 .
CCDSi CCDS9846.1.
PIRi A36169.
RefSeqi NP_003230.1. NM_003239.2.
XP_005268085.1. XM_005268028.1.
UniGenei Hs.592317.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KTZ X-ray 2.15 A 301-412 [» ]
1TGJ X-ray 2.00 A 301-412 [» ]
1TGK X-ray 3.30 A 301-412 [» ]
2PJY X-ray 3.00 A 301-412 [» ]
3EO1 X-ray 3.10 C/F/I/L 301-412 [» ]
ProteinModelPortali P10600.
SMRi P10600. Positions 24-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112901. 7 interactions.
DIPi DIP-5937N.
IntActi P10600. 6 interactions.
MINTi MINT-8177755.
STRINGi 9606.ENSP00000238682.

PTM databases

PhosphoSitei P10600.

Polymorphism databases

DMDMi 135684.

Proteomic databases

PaxDbi P10600.
PRIDEi P10600.

Protocols and materials databases

DNASUi 7043.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000238682 ; ENSP00000238682 ; ENSG00000119699 .
GeneIDi 7043.
KEGGi hsa:7043.
UCSCi uc001xsc.2. human.

Organism-specific databases

CTDi 7043.
GeneCardsi GC14M076424.
GeneReviewsi TGFB3.
HGNCi HGNC:11769. TGFB3.
HPAi CAB018337.
HPA027923.
MIMi 107970. phenotype.
190230. gene.
615582. phenotype.
neXtProti NX_P10600.
Orphaneti 293899. Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
293888. Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
293910. Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
PharmGKBi PA36483.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG269146.
HOGENOMi HOG000290198.
HOVERGENi HBG074115.
InParanoidi P10600.
KOi K13377.
OMAi PEPSVMT.
OrthoDBi EOG70GMFT.
PhylomeDBi P10600.
TreeFami TF351793.

Enzyme and pathway databases

Reactomei REACT_150331. Molecules associated with elastic fibres.
REACT_163906. ECM proteoglycans.
SignaLinki P10600.

Miscellaneous databases

ChiTaRSi TGFB3. human.
EvolutionaryTracei P10600.
GeneWikii Transforming_growth_factor,_beta_3.
GenomeRNAii 7043.
NextBioi 27521.
PMAP-CutDB P10600.
PROi P10600.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10600.
Bgeei P10600.
CleanExi HS_TGFB3.
Genevestigatori P10600.

Family and domain databases

Gene3Di 2.10.90.10. 1 hit.
InterProi IPR029034. Cystine-knot_cytokine.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR016319. TGF-beta.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
IPR015618. Transform_grow_fac_b3.
[Graphical view ]
PANTHERi PTHR11848. PTHR11848. 1 hit.
Pfami PF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view ]
PIRSFi PIRSF001787. TGF-beta. 1 hit.
PRINTSi PR01423. TGFBETA.
PR01426. TGFBETA3.
SMARTi SM00204. TGFB. 1 hit.
[Graphical view ]
SUPFAMi SSF57501. SSF57501. 1 hit.
PROSITEi PS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of another member of the transforming growth factor type beta gene family."
    ten Dijke P., Hansen P., Iwata K., Pieler C., Foulkes J.G.
    Proc. Natl. Acad. Sci. U.S.A. 85:4715-4719(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A new type of transforming growth factor-beta, TGF-beta 3."
    Derynck R., Lindquist P.B., Lee A., Wen D., Tamm J., Graycar J.L., Rhee L., Mason A.J., Miller D.A., Coffey R.J., Moses H.L., Chen E.Y.
    EMBO J. 7:3737-3743(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  3. "Complete genomic sequence of human transforming growth factor-beta 3."
    Madan A., Rowen L., Qin S., Dickhoff R., Shaffer T., James R., Abbasi N., Loretz C., Madan A., Dors M., Dahl T., Hall J., Lasky S., Hood L.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. NIEHS SNPs program
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. SeattleSNPs variation discovery resource
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-60.
  6. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Inhibition of translation of transforming growth factor-beta 3 mRNA by its 5' untranslated region."
    Arrick B.A., Lee A.L., Grendell R.L., Derynck R.
    Mol. Cell. Biol. 11:4306-4313(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-48.
  8. "Mechanisms for asporin function and regulation in articular cartilage."
    Nakajima M., Kizawa H., Saitoh M., Kou I., Miyazono K., Ikegawa S.
    J. Biol. Chem. 282:32185-32192(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ASPN.
  9. "The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding."
    Mittl P.R.E., Priestle J.P., Cox D.A., McMaster G., Cerletti N., Gruetter M.G.
    Protein Sci. 5:1261-1271(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 301-412.
  10. "Regulatory mutations in transforming growth factor-beta3 gene cause arrhythmogenic right ventricular cardiomyopathy type 1."
    Beffagna G., Occhi G., Nava A., Vitiello L., Ditadi A., Basso C., Bauce B., Carraro G., Thiene G., Towbin J.A., Danieli G.A., Rampazzo A.
    Cardiovasc. Res. 65:366-373(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ARVD1.
  11. "A mutation in TGFB3 associated with a syndrome of low muscle mass, growth retardation, distal arthrogryposis and clinical features overlapping with Marfan and Loeys-Dietz syndrome."
    Rienhoff H.Y. Jr., Yeo C.Y., Morissette R., Khrebtukova I., Melnick J., Luo S., Leng N., Kim Y.J., Schroth G., Westwick J., Vogel H., McDonnell N., Hall J.G., Whitman M.
    Am. J. Med. Genet. A 161A:2040-2046(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RNHF TYR-409, CHARACTERIZATION OF VARIANT RNHF TYR-409.

Entry informationi

Entry nameiTGFB3_HUMAN
AccessioniPrimary (citable) accession number: P10600
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 3, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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