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P01135 (TGFA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protransforming growth factor alpha

Cleaved into the following chain:

  1. Transforming growth factor alpha
    Short name=TGF-alpha
    Alternative name(s):
    EGF-like TGF
    Short name=ETGF
    TGF type 1
Gene names
Name:TGFA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.16 Ref.17 Ref.18

Subcellular location

Transforming growth factor alpha: Secretedextracellular space.

Protransforming growth factor alpha: Cell membrane; Single-pass type I membrane protein.

Tissue specificity

Isoform 1, isoform 3 and isoform 4 are expressed in keratinocytes and tumor-derived cell lines. Ref.6

Sequence similarities

Contains 1 EGF-like domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainEGF-like domain
Signal
Transmembrane
Transmembrane helix
   Molecular functionGrowth factor
Mitogen
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from direct assay PubMed 11278323. Source: GOC

activation of MAPK activity

Inferred from direct assay PubMed 11278323. Source: HGNC

angiogenesis

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement PubMed 10861448. Source: ProtInc

epidermal growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

mammary gland alveolus development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of epidermal growth factor-activated receptor activity

Inferred from direct assay PubMed 11278323. Source: HGNC

positive regulation of epithelial cell proliferation

Inferred from direct assay PubMed 11278323. Source: HGNC

positive regulation of mitosis

Inferred from direct assay PubMed 11278323. Source: HGNC

response to drug

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasolateral plasma membrane

Inferred from direct assay PubMed 17553928. Source: BHF-UCL

cell surface

Inferred from direct assay PubMed 12743035. Source: BHF-UCL

cytoplasmic vesicle

Inferred from direct assay PubMed 15064403. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 12743035. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from direct assay PubMed 15064403. Source: BHF-UCL

plasma membrane

Non-traceable author statement PubMed 10918572. Source: ProtInc

   Molecular_functionMAP kinase kinase activity

Inferred from direct assay PubMed 11278323. Source: HGNC

epidermal growth factor receptor binding

Inferred from direct assay PubMed 11278323. Source: UniProtKB

growth factor activity

Inferred from direct assay PubMed 11278323. Source: HGNC

protein binding

Inferred from physical interaction Ref.18. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Magi3Q9EQJ94EBI-1034374,EBI-7455245From a different organism.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P01135-1)

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: P01135-2)

The sequence of this isoform differs from the canonical sequence as follows:
     32-32: Missing.
Isoform 3 (identifier: P01135-3)

Also known as: VaII;

The sequence of this isoform differs from the canonical sequence as follows:
     32-32: Missing.
     159-160: VV → ATLG
Isoform 4 (identifier: P01135-4)

Also known as: VaI;

The sequence of this isoform differs from the canonical sequence as follows:
     159-160: VV → GCRLY
Isoform 5 (identifier: P01135-5)

Also known as: VaIM;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 160137Protransforming growth factor alpha
PRO_0000302744
Propeptide24 – 3916Removed in mature form
PRO_0000007752
Chain40 – 8950Transforming growth factor alpha
PRO_0000007753
Propeptide90 – 16071Removed in mature form
PRO_0000007754

Regions

Topological domain24 – 9875Extracellular Potential
Transmembrane99 – 12426Helical; Potential
Topological domain125 – 16036Cytoplasmic Potential
Domain43 – 8341EGF-like

Amino acid modifications

Lipidation1531S-palmitoyl cysteine Ref.15
Lipidation1541S-palmitoyl cysteine Ref.15
Glycosylation251N-linked (GlcNAc...) Potential
Disulfide bond47 ↔ 60 Ref.14
Disulfide bond55 ↔ 71 Ref.14
Disulfide bond73 ↔ 82 Ref.14

Natural variations

Alternative sequence321Missing in isoform 2, isoform 3 and isoform 5.
VSP_038369
Alternative sequence159 – 1602VV → ATLG in isoform 3.
VSP_038370
Alternative sequence159 – 1602VV → GCRLY in isoform 4 and isoform 5.
VSP_038371
Natural variant1091V → M.
Corresponds to variant rs11466259 [ dbSNP | Ensembl ].
VAR_024271

Experimental info

Sequence conflict581G → A in AAA61157. Ref.2
Sequence conflict651Q → H in AAA61157. Ref.2
Sequence conflict1591V → L in AAA61157. Ref.2

Secondary structure

............. 160
Helix Strand Turn

Details...

Sequences

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

Last modified July 21, 1986. Version 1.
Checksum: D692184F9353DE47

FASTA16017,006
        10         20         30         40         50         60 
MVPSAGQLAL FALGIVLAAC QALENSTSPL SADPPVAAAV VSHFNDCPDS HTQFCFHGTC 

        70         80         90        100        110        120 
RFLVQEDKPA CVCHSGYVGA RCEHADLLAV VAASQKKQAI TALVVVSIVA LAVLIITCVL 

       130        140        150        160 
IHCCQVRKHC EWCRALICRH EKPSALLKGR TACCHSETVV 

« Hide

Isoform 2 [UniParc].

Checksum: 41949AAD26D0BF65
Show »

FASTA15916,935
Isoform 3 (VaII) [UniParc].

Checksum: 94BA72EB8AAD26D0
Show »

FASTA16117,079
Isoform 4 (VaI) [UniParc].

Checksum: 0E207CBAF8A84F93
Show »

FASTA16317,400
Isoform 5 (VaIM) [UniParc].

Checksum: D4ABF94DFE2AAD26
Show »

FASTA16217,329

References

« Hide 'large scale' references
[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. 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 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. expand/collapse author list , 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]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K03222 mRNA. Translation: AAA61159.1.
M31172 mRNA. Translation: AAA61157.1.
X70340 mRNA. Translation: CAA49806.1.
AF123243 expand/collapse EMBL AC list , AF123238, AF123239, AF123240, AF123241, AF123242 Genomic DNA. Translation: AAF13491.1.
AY325886 expand/collapse EMBL AC list , 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.
CCDSCCDS1905.1. [P01135-1]
CCDS46316.1. [P01135-2]
PIRWFHU1. JN0876.
RefSeqNP_001093161.1. NM_001099691.2. [P01135-2]
NP_003227.1. NM_003236.3. [P01135-1]
UniGeneHs.170009.
Hs.628298.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP01135.
SMRP01135. Positions 40-89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112897. 6 interactions.
DIPDIP-5765N.
IntActP01135. 6 interactions.
MINTMINT-121235.
STRING9606.ENSP00000295400.

Polymorphism databases

DMDM135689.

Proteomic databases

PRIDEP01135.

Protocols and materials databases

DNASU7039.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295400; ENSP00000295400; ENSG00000163235. [P01135-1]
ENST00000418333; ENSP00000404099; ENSG00000163235. [P01135-2]
ENST00000445399; ENSP00000387493; ENSG00000163235. [P01135-3]
ENST00000606814; ENSP00000475689; ENSG00000272517. [P01135-2]
ENST00000607651; ENSP00000475235; ENSG00000272517. [P01135-1]
ENST00000607808; ENSP00000475945; ENSG00000272517. [P01135-3]
GeneID7039.
KEGGhsa:7039.
UCSCuc002sgs.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

CTD7039.
GeneCardsGC02M070674.
HGNCHGNC:11765. TGFA.
HPAHPA042297.
MIM190170. gene.
neXtProtNX_P01135.
Orphanet1991. Cleft lip with or without cleft palate.
2227. Hypodontia.
99798. Oligodontia.
PharmGKBPA36480.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41326.
HOGENOMHOG000013036.
HOVERGENHBG000330.
InParanoidP01135.
KOK08774.
OMACHSETGC.
OrthoDBEOG7VQJGP.
PhylomeDBP01135.
TreeFamTF332938.

Enzyme and pathway databases

SignaLinkP01135.

Gene expression databases

ArrayExpressP01135.
BgeeP01135.
CleanExHS_TGFA.
GenevestigatorP01135.

Family and domain databases

InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR015497. EGF_rcpt_ligand.
[Graphical view]
PANTHERPTHR10740. PTHR10740. 1 hit.
SMARTSM00181. EGF. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01135.
GeneWikiTGF_alpha.
GenomeRNAi7039.
NextBio27501.
PMAP-CutDBP01135.
PROP01135.
SOURCESearch...

Entry information

Entry nameTGFA_HUMAN
AccessionPrimary (citable) accession number: P01135
Secondary accession number(s): A8K286 expand/collapse secondary AC list , Q15577, Q53SK7, Q9BS56, Q9UEI3, Q9UKM1, Q9UKM2, Q9UKM3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 158 of the entry and version 1 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

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 2

Human chromosome 2: entries, gene names and cross-references to MIM