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P01135

- TGFA_HUMAN

UniProt

P01135 - TGFA_HUMAN

Protein

Protransforming growth factor alpha

Gene

TGFA

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

    TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.

    GO - Molecular functioni

    1. epidermal growth factor receptor binding Source: UniProtKB
    2. growth factor activity Source: HGNC
    3. MAP kinase kinase activity Source: HGNC
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: HGNC
    2. angiogenesis Source: Ensembl
    3. cell proliferation Source: ProtInc
    4. epidermal growth factor receptor signaling pathway Source: Ensembl
    5. mammary gland alveolus development Source: Ensembl
    6. MAPK cascade Source: GOC
    7. negative regulation of apoptotic process Source: Ensembl
    8. positive regulation of cell division Source: UniProtKB-KW
    9. positive regulation of epidermal growth factor-activated receptor activity Source: HGNC
    10. positive regulation of epithelial cell proliferation Source: HGNC
    11. positive regulation of mitosis Source: HGNC
    12. response to drug Source: Ensembl
    13. wound healing Source: Ensembl

    Keywords - Molecular functioni

    Growth factor, Mitogen

    Enzyme and pathway databases

    SignaLinkiP01135.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protransforming growth factor alpha
    Cleaved into the following chain:
    Alternative name(s):
    EGF-like TGF
    Short name:
    ETGF
    TGF type 1
    Gene namesi
    Name:TGFA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11765. TGFA.

    Subcellular locationi

    GO - Cellular componenti

    1. basolateral plasma membrane Source: BHF-UCL
    2. cell surface Source: BHF-UCL
    3. cytoplasmic vesicle Source: BHF-UCL
    4. extracellular space Source: BHF-UCL
    5. integral component of membrane Source: UniProtKB-KW
    6. nucleus Source: Ensembl
    7. perinuclear region of cytoplasm Source: BHF-UCL
    8. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti1991. Cleft lip with or without cleft palate.
    2227. Hypodontia.
    99798. Oligodontia.
    PharmGKBiPA36480.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 160137Protransforming growth factor alphaPRO_0000302744Add
    BLAST
    Propeptidei24 – 3916Removed in mature formPRO_0000007752Add
    BLAST
    Chaini40 – 8950Transforming growth factor alphaPRO_0000007753Add
    BLAST
    Propeptidei90 – 16071Removed in mature formPRO_0000007754Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi47 ↔ 601 PublicationPROSITE-ProRule annotation
    Disulfide bondi55 ↔ 711 PublicationPROSITE-ProRule annotation
    Disulfide bondi73 ↔ 821 PublicationPROSITE-ProRule annotation
    Lipidationi153 – 1531S-palmitoyl cysteine1 Publication
    Lipidationi154 – 1541S-palmitoyl cysteine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    PRIDEiP01135.

    Miscellaneous databases

    PMAP-CutDBP01135.

    Expressioni

    Tissue specificityi

    Isoform 1, isoform 3 and isoform 4 are expressed in keratinocytes and tumor-derived cell lines.1 Publication

    Gene expression databases

    ArrayExpressiP01135.
    BgeeiP01135.
    CleanExiHS_TGFA.
    GenevestigatoriP01135.

    Organism-specific databases

    HPAiHPA042297.

    Interactioni

    Subunit structurei

    Interacts with the PDZ domains of MAGI3, SDCBP and SNTA1. The interaction with SDCBP, is required for the targeting to the cell surface. In the endoplasmic reticulum, in its immature form (i.e. with a prosegment and lacking full N-glycosylation), interacts with CNIH. In the Golgi apparatus, may form a complex with CNIH and GORASP2. Interacts (via cytoplasmic C-terminal domain) with NKD2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Magi3Q9EQJ94EBI-1034374,EBI-7455245From a different organism.

    Protein-protein interaction databases

    BioGridi112897. 6 interactions.
    DIPiDIP-5765N.
    IntActiP01135. 8 interactions.
    MINTiMINT-121235.
    STRINGi9606.ENSP00000295400.

    Structurei

    Secondary structure

    1
    160
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 453
    Helixi51 – 544
    Beta strandi58 – 636
    Turni64 – 674
    Beta strandi68 – 736
    Beta strandi77 – 793
    Beta strandi84 – 874

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GK5NMR-A83-89[»]
    1MOXX-ray2.50C/D40-89[»]
    1YUFNMR-A40-89[»]
    1YUGNMR-A40-89[»]
    2TGFNMR-A40-89[»]
    3E50X-ray2.30C/D40-89[»]
    3TGFNMR-A40-89[»]
    4TGFNMR-A40-89[»]
    ProteinModelPortaliP01135.
    SMRiP01135. Positions 40-89.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01135.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 9875ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini125 – 16036CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei99 – 12426HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 8341EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 EGF-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG41326.
    HOGENOMiHOG000013036.
    HOVERGENiHBG000330.
    InParanoidiP01135.
    KOiK08774.
    OMAiCHSETGC.
    OrthoDBiEOG7VQJGP.
    PhylomeDBiP01135.
    TreeFamiTF332938.

    Family and domain databases

    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR015497. EGF_rcpt_ligand.
    [Graphical view]
    PANTHERiPTHR10740. PTHR10740. 1 hit.
    SMARTiSM00181. EGF. 1 hit.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P01135-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVPSAGQLAL FALGIVLAAC QALENSTSPL SADPPVAAAV VSHFNDCPDS    50
    HTQFCFHGTC RFLVQEDKPA CVCHSGYVGA RCEHADLLAV VAASQKKQAI 100
    TALVVVSIVA LAVLIITCVL IHCCQVRKHC EWCRALICRH EKPSALLKGR 150
    TACCHSETVV 160
    Length:160
    Mass (Da):17,006
    Last modified:July 21, 1986 - v1
    Checksum:iD692184F9353DE47
    GO
    Isoform 2 (identifier: P01135-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         32-32: Missing.

    Show »
    Length:159
    Mass (Da):16,935
    Checksum:i41949AAD26D0BF65
    GO
    Isoform 3 (identifier: P01135-3) [UniParc]FASTAAdd to Basket

    Also known as: VaII

    The sequence of this isoform differs from the canonical sequence as follows:
         32-32: Missing.
         159-160: VV → ATLG

    Show »
    Length:161
    Mass (Da):17,079
    Checksum:i94BA72EB8AAD26D0
    GO
    Isoform 4 (identifier: P01135-4) [UniParc]FASTAAdd to Basket

    Also known as: VaI

    The sequence of this isoform differs from the canonical sequence as follows:
         159-160: VV → GCRLY

    Show »
    Length:163
    Mass (Da):17,400
    Checksum:i0E207CBAF8A84F93
    GO
    Isoform 5 (identifier: P01135-5) [UniParc]FASTAAdd to Basket

    Also known as: VaIM

    The sequence of this isoform differs from the canonical sequence as follows:
         32-32: Missing.
         159-160: VV → GCRLY

    Show »
    Length:162
    Mass (Da):17,329
    Checksum:iD4ABF94DFE2AAD26
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581G → A in AAA61157. (PubMed:2464748)Curated
    Sequence conflicti65 – 651Q → H in AAA61157. (PubMed:2464748)Curated
    Sequence conflicti159 – 1591V → L in AAA61157. (PubMed:2464748)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti109 – 1091V → M.
    Corresponds to variant rs11466259 [ dbSNP | Ensembl ].
    VAR_024271

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei32 – 321Missing in isoform 2, isoform 3 and isoform 5. 3 PublicationsVSP_038369
    Alternative sequencei159 – 1602VV → ATLG in isoform 3. 1 PublicationVSP_038370
    Alternative sequencei159 – 1602VV → GCRLY in isoform 4 and isoform 5. 1 PublicationVSP_038371

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03222 mRNA. Translation: AAA61159.1.
    M31172 mRNA. Translation: AAA61157.1.
    X70340 mRNA. Translation: CAA49806.1.
    AF123243
    , AF123238, AF123239, AF123240, AF123241, AF123242 Genomic DNA. Translation: AAF13491.1.
    AY325886
    , AY325885, AY326405, AY327131, AY327132, AY329368 Genomic DNA. Translation: AAP97822.2.
    AF149096 mRNA. Translation: AAF05089.1.
    AF149097 mRNA. Translation: AAF05090.1.
    AF149098 mRNA. Translation: AAF05091.1.
    BT006833 mRNA. Translation: AAP35479.1.
    AK290151 mRNA. Translation: BAF82840.1.
    AC005234 Genomic DNA. Translation: AAY14793.1.
    AC017084 Genomic DNA. Translation: AAY14705.1.
    CH471053 Genomic DNA. Translation: EAW99810.1.
    CH471053 Genomic DNA. Translation: EAW99812.1.
    BC005308 mRNA. Translation: AAH05308.1.
    M22440 Genomic DNA. Translation: AAA52530.1.
    AF075584, AF075583 Genomic DNA. Translation: AAD12238.1.
    CCDSiCCDS1905.1. [P01135-1]
    CCDS46316.1. [P01135-2]
    PIRiJN0876. WFHU1.
    RefSeqiNP_001093161.1. NM_001099691.2. [P01135-2]
    NP_003227.1. NM_003236.3. [P01135-1]
    UniGeneiHs.170009.
    Hs.628298.

    Genome annotation databases

    EnsembliENST00000295400; ENSP00000295400; ENSG00000163235. [P01135-1]
    ENST00000418333; ENSP00000404099; ENSG00000163235. [P01135-2]
    ENST00000445399; ENSP00000387493; ENSG00000163235. [P01135-3]
    GeneIDi7039.
    KEGGihsa:7039.
    UCSCiuc002sgs.4. human. [P01135-1]
    uc002sgt.4. human. [P01135-2]
    uc002sgu.3. human. [P01135-3]
    uc002sgv.3. human. [P01135-4]
    uc002sgw.3. human. [P01135-5]

    Polymorphism databases

    DMDMi135689.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03222 mRNA. Translation: AAA61159.1 .
    M31172 mRNA. Translation: AAA61157.1 .
    X70340 mRNA. Translation: CAA49806.1 .
    AF123243
    , AF123238 , AF123239 , AF123240 , AF123241 , AF123242 Genomic DNA. Translation: AAF13491.1 .
    AY325886
    , AY325885 , AY326405 , AY327131 , AY327132 , AY329368 Genomic DNA. Translation: AAP97822.2 .
    AF149096 mRNA. Translation: AAF05089.1 .
    AF149097 mRNA. Translation: AAF05090.1 .
    AF149098 mRNA. Translation: AAF05091.1 .
    BT006833 mRNA. Translation: AAP35479.1 .
    AK290151 mRNA. Translation: BAF82840.1 .
    AC005234 Genomic DNA. Translation: AAY14793.1 .
    AC017084 Genomic DNA. Translation: AAY14705.1 .
    CH471053 Genomic DNA. Translation: EAW99810.1 .
    CH471053 Genomic DNA. Translation: EAW99812.1 .
    BC005308 mRNA. Translation: AAH05308.1 .
    M22440 Genomic DNA. Translation: AAA52530.1 .
    AF075584 , AF075583 Genomic DNA. Translation: AAD12238.1 .
    CCDSi CCDS1905.1. [P01135-1 ]
    CCDS46316.1. [P01135-2 ]
    PIRi JN0876. WFHU1.
    RefSeqi NP_001093161.1. NM_001099691.2. [P01135-2 ]
    NP_003227.1. NM_003236.3. [P01135-1 ]
    UniGenei Hs.170009.
    Hs.628298.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GK5 NMR - A 83-89 [» ]
    1MOX X-ray 2.50 C/D 40-89 [» ]
    1YUF NMR - A 40-89 [» ]
    1YUG NMR - A 40-89 [» ]
    2TGF NMR - A 40-89 [» ]
    3E50 X-ray 2.30 C/D 40-89 [» ]
    3TGF NMR - A 40-89 [» ]
    4TGF NMR - A 40-89 [» ]
    ProteinModelPortali P01135.
    SMRi P01135. Positions 40-89.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112897. 6 interactions.
    DIPi DIP-5765N.
    IntActi P01135. 8 interactions.
    MINTi MINT-121235.
    STRINGi 9606.ENSP00000295400.

    Polymorphism databases

    DMDMi 135689.

    Proteomic databases

    PRIDEi P01135.

    Protocols and materials databases

    DNASUi 7039.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295400 ; ENSP00000295400 ; ENSG00000163235 . [P01135-1 ]
    ENST00000418333 ; ENSP00000404099 ; ENSG00000163235 . [P01135-2 ]
    ENST00000445399 ; ENSP00000387493 ; ENSG00000163235 . [P01135-3 ]
    GeneIDi 7039.
    KEGGi hsa:7039.
    UCSCi uc002sgs.4. human. [P01135-1 ]
    uc002sgt.4. human. [P01135-2 ]
    uc002sgu.3. human. [P01135-3 ]
    uc002sgv.3. human. [P01135-4 ]
    uc002sgw.3. human. [P01135-5 ]

    Organism-specific databases

    CTDi 7039.
    GeneCardsi GC02M070674.
    HGNCi HGNC:11765. TGFA.
    HPAi HPA042297.
    MIMi 190170. gene.
    neXtProti NX_P01135.
    Orphaneti 1991. Cleft lip with or without cleft palate.
    2227. Hypodontia.
    99798. Oligodontia.
    PharmGKBi PA36480.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41326.
    HOGENOMi HOG000013036.
    HOVERGENi HBG000330.
    InParanoidi P01135.
    KOi K08774.
    OMAi CHSETGC.
    OrthoDBi EOG7VQJGP.
    PhylomeDBi P01135.
    TreeFami TF332938.

    Enzyme and pathway databases

    SignaLinki P01135.

    Miscellaneous databases

    EvolutionaryTracei P01135.
    GeneWikii TGF_alpha.
    GenomeRNAii 7039.
    NextBioi 27501.
    PMAP-CutDB P01135.
    PROi P01135.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01135.
    Bgeei P01135.
    CleanExi HS_TGFA.
    Genevestigatori P01135.

    Family and domain databases

    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR015497. EGF_rcpt_ligand.
    [Graphical view ]
    PANTHERi PTHR10740. PTHR10740. 1 hit.
    SMARTi SM00181. EGF. 1 hit.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human transforming growth factor-alpha: precursor structure and expression in E. coli."
      Derynck R., Roberts A.B., Winkler M.E., Chen E.Y., Goeddel D.V.
      Cell 38:287-297(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A novel low molecular weight ribonucleic acid (RNA) related to transforming growth factor alpha messenger RNA."
      Jakowlew S.B., Kondaiah P., Dillard P.J., Sporn M.B., Roberts A.B.
      Mol. Endocrinol. 2:1056-1063(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Human transforming growth factor alpha: sequence analysis of the 4.5-kb and 1.6-kb mRNA species."
      Qian J.F., Lazar-Wesley E., Breugnot C., May E.
      Gene 132:291-296(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon.
    4. "Transforming growth factor-alpha: characterization of the BamHI, RsaI, and TaqI polymorphic regions."
      Qian J.F., Feingold J., Stoll C., May E.
      Am. J. Hum. Genet. 53:168-175(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Transforming growth factor-alpha (TGFA): genomic structure, boundary sequences, and mutation analysis in nonsyndromic cleft lip/palate and cleft palate only."
      Machida J., Yoshiura K., Funkhauser C.D., Natsume N., Kawai T., Murray J.C.
      Genomics 61:237-242(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Human keratinocytes and tumor-derived cell lines express alternatively spliced forms of transforming growth factor-alpha mRNA, encoding precursors lacking carboxyl-terminal valine residues."
      Xu X., Liao J., Creek K.E., Pirisi L.
      Oncogene 18:5554-5562(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), TISSUE SPECIFICITY.
    7. "Cloning of human full-length CDSs in BD Creator(TM) System Donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    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.
      , 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 1).
      Tissue: Thalamus.
    9. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Kidney.
    12. "The human transforming growth factor alpha promoter directs transcription initiation from a single site in the absence of a TATA sequence."
      Jakobovits E.B., Schlokat U., Vannice J.L., Derynck R., Levinson A.D.
      Mol. Cell. Biol. 8:5549-5554(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
    13. "TGFA: exon-intron structure and evaluation as a candidate gene for Alstrom syndrome."
      Collin G.B., Marshall J.D., Naggert J.K., Nishina P.M.
      Clin. Genet. 55:61-62(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
    14. "Characterization of disulfide bond position in proteins and sequence analysis of cystine-bridged peptides by tandem mass spectrometry."
      Bean M.F., Carr S.A.
      Anal. Biochem. 201:216-226(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    15. "Cysteines 153 and 154 of transmembrane transforming growth factor-alpha are palmitoylated and mediate cytoplasmic protein association."
      Shum L., Turck C.W., Derynck R.
      J. Biol. Chem. 271:28502-28508(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-153 AND CYS-154.
    16. "A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface."
      Fernandez-Larrea J., Merlos-Suarez A., Urena J.M., Baselga J., Arribas J.
      Mol. Cell 3:423-433(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNTA1 AND SDCBP.
    17. "Cornichon regulates transport and secretion of TGFalpha-related proteins in metazoan cells."
      Perez Castro C., Piscopo D., Nakagawa T., Derynck R.
      J. Cell Sci. 120:2454-2466(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNIH AND GORASP2.
    18. "EGF receptor-independent action of TGF-alpha protects Naked2 from AO7-mediated ubiquitylation and proteasomal degradation."
      Ding W., Li C., Hu T., Graves-Deal R., Fotia A.B., Weissman A.M., Coffey R.J.
      Proc. Natl. Acad. Sci. U.S.A. 105:13433-13438(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NKD2.
    19. "Solution structures of human transforming growth factor alpha derived from 1H NMR data."
      Kline T.P., Brown F.K., Brown S.C., Jeffs P.W., Kopple K.D., Mueller L.
      Biochemistry 29:7805-7813(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF TGF-ALPHA.
    20. "The solution structure of human transforming growth factor alpha."
      Harvey T.S., Wilkinson A.J., Tappin M.J., Cooke R.M., Campbell I.D.
      Eur. J. Biochem. 198:555-562(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF TGF-ALPHA.
    21. "Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints."
      Moy F.J., Li Y.C., Rauenbuehler P., Winkler M.E., Scheraga H.A., Montelione G.T.
      Biochemistry 32:7334-7353(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF TGF-ALPHA.

    Entry informationi

    Entry nameiTGFA_HUMAN
    AccessioniPrimary (citable) accession number: P01135
    Secondary accession number(s): A8K286
    , Q15577, Q53SK7, Q9BS56, Q9UEI3, Q9UKM1, Q9UKM2, Q9UKM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 159 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 2
      Human chromosome 2: 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