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P01135

- TGFA_HUMAN

UniProt

P01135 - TGFA_HUMAN

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Protein

Protransforming growth factor alpha

Gene

TGFA

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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP01135.
CleanExiHS_TGFA.
ExpressionAtlasiP01135. baseline and differential.
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
EGFRP005332EBI-1034374,EBI-297353
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.
GeneTreeiENSGT00730000110951.
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

        10         20         30         40         50
MVPSAGQLAL FALGIVLAAC QALENSTSPL SADPPVAAAV VSHFNDCPDS
60 70 80 90 100
HTQFCFHGTC RFLVQEDKPA CVCHSGYVGA RCEHADLLAV VAASQKKQAI
110 120 130 140 150
TALVVVSIVA LAVLIITCVL IHCCQVRKHC EWCRALICRH EKPSALLKGR
160
TACCHSETVV
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.
GeneTreei ENSGT00730000110951.
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

Bgeei P01135.
CleanExi HS_TGFA.
ExpressionAtlasi P01135. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 160 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