P01135 (TGFA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	160 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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: Secreted › extracellular 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 component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	EGF-like domain Signal Transmembrane Transmembrane helix
Molecular function	Growth factor Mitogen
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: Compara cell proliferation Traceable author statement PubMed 10861448. Source: ProtInc epidermal growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara mammary gland alveolus development Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara 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: Compara wound healing Inferred from electronic annotation. Source: Compara
Cellular_component	basolateral 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from direct assay PubMed 15064403. Source: BHF-UCL
Molecular_function	MAP 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
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Chain

24 – 160

137

Protransforming growth factor alpha

PRO_0000302744

Propeptide

24 – 39

16

Removed in mature form

PRO_0000007752

Chain

40 – 89

50

Transforming growth factor alpha

PRO_0000007753

Propeptide

90 – 160

71

Removed in mature form

PRO_0000007754

Regions

Topological domain

24 – 98

75

Extracellular Potential

Transmembrane

99 – 124

26

Helical; Potential

Topological domain

125 – 160

36

Cytoplasmic Potential

Domain

43 – 83

41

EGF-like

Amino acid modifications

Lipidation

153

1

S-palmitoyl cysteine Ref.15

Lipidation

154

1

S-palmitoyl cysteine Ref.15

Glycosylation

25

1

N-linked (GlcNAc...) Potential

Disulfide bond

47 ↔ 60

Ref.14

Disulfide bond

55 ↔ 71

Ref.14

Disulfide bond

73 ↔ 82

Ref.14

Natural variations

Alternative sequence

32

1

Missing in isoform 2, isoform 3 and isoform 5.

VSP_038369

Alternative sequence

159 – 160

2

VV → ATLG in isoform 3.

VSP_038370

Alternative sequence

159 – 160

2

VV → GCRLY in isoform 4 and isoform 5.

VSP_038371

Natural variant

109

1

V → M.
Corresponds to variant rs11466259 [ dbSNP | Ensembl ].

VAR_024271

Experimental info

Sequence conflict

58

1

G → A in AAA61157. Ref.2

Sequence conflict

65

1

Q → H in AAA61157. Ref.2

Sequence conflict

159

1

V → L in AAA61157. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

160

Helix Strand Turn

Details...

Beta strand

43 – 45

3

Helix

51 – 54

4

Beta strand

58 – 63

6

Turn

64 – 67

4

Beta strand

68 – 73

6

Beta strand

77 – 79

3

Beta strand

84 – 87

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: D692184F9353DE47	FASTA	160	17,006
	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
	Isoform 2 [UniParc]. Checksum: 41949AAD26D0BF65	FASTA	159	16,935
	10 20 30 40 50 60 MVPSAGQLAL FALGIVLAAC QALENSTSPL SDPPVAAAVV SHFNDCPDSH TQFCFHGTCR 70 80 90 100 110 120 FLVQEDKPAC VCHSGYVGAR CEHADLLAVV AASQKKQAIT ALVVVSIVAL AVLIITCVLI 130 140 150 HCCQVRKHCE WCRALICRHE KPSALLKGRT ACCHSETVV
	Isoform 3 (VaII) [UniParc]. Checksum: 94BA72EB8AAD26D0	FASTA	161	17,079
	10 20 30 40 50 60 MVPSAGQLAL FALGIVLAAC QALENSTSPL SDPPVAAAVV SHFNDCPDSH TQFCFHGTCR 70 80 90 100 110 120 FLVQEDKPAC VCHSGYVGAR CEHADLLAVV AASQKKQAIT ALVVVSIVAL AVLIITCVLI 130 140 150 160 HCCQVRKHCE WCRALICRHE KPSALLKGRT ACCHSETATL G
	Isoform 4 (VaI) [UniParc]. Checksum: 0E207CBAF8A84F93	FASTA	163	17,400
	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 TACCHSETGC RLY
	Isoform 5 (VaIM) [UniParc]. Checksum: D4ABF94DFE2AAD26	FASTA	162	17,329
	10 20 30 40 50 60 MVPSAGQLAL FALGIVLAAC QALENSTSPL SDPPVAAAVV SHFNDCPDSH TQFCFHGTCR 70 80 90 100 110 120 FLVQEDKPAC VCHSGYVGAR CEHADLLAVV AASQKKQAIT ALVVVSIVAL AVLIITCVLI 130 140 150 160 HCCQVRKHCE WCRALICRHE KPSALLKGRT ACCHSETGCR LY

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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 , 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.

IPI

IPI00465177.
IPI00856067.
IPI00872280.
IPI00926333.
IPI00954043.

PIR

WFHU1. JN0876.

RefSeq

NP_001093161.1. NM_001099691.2.
NP_003227.1. NM_003236.3.

UniGene

Hs.170009.
Hs.628298.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P01135.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5765N.

IntAct

P01135. 2 interactions.

MINT

MINT-121235.

STRING

9606.ENSP00000295400.

Polymorphism databases

DMDM

135689.

Proteomic databases

PRIDE

P01135.

Protocols and materials databases

DNASU

7039.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295400; ENSP00000295400; ENSG00000163235.
ENST00000418333; ENSP00000404099; ENSG00000163235.
ENST00000445399; ENSP00000387493; ENSG00000163235.

GeneID

7039.

KEGG

hsa:7039.

UCSC

uc002sgs.4. human.
uc002sgt.4. human.
uc002sgu.3. human.
uc002sgw.3. human.

Organism-specific databases

CTD

7039.

GeneCards

GC02M070674.

HGNC

HGNC:11765. TGFA.

HPA

HPA042297.

MIM

190170. gene.

neXtProt

NX_P01135.

Orphanet

1991. Cleft lip with or without cleft palate.

PharmGKB

PA36480.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41326.

HOGENOM

HOG000013036.

HOVERGEN

HBG000330.

InParanoid

P01135.

KO

K08774.

OMA

IGARCEH.

OrthoDB

EOG4SN1PX.

PhylomeDB

P01135.

Enzyme and pathway databases

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.

Gene expression databases

ArrayExpress

P01135.

Bgee

P01135.

CleanEx

HS_TGFA.

Genevestigator

P01135.

GermOnline

ENSG00000163235. Homo sapiens.

Family and domain databases

InterPro

IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR015497. EGF_rcpt_ligand.
[Graphical view]

PANTHER

PTHR10740. PTHR10740. 1 hit.

SMART

SM00181. EGF. 1 hit.
[Graphical view]

PROSITE

PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P01135.

GenomeRNAi

7039.

NextBio

27501.

PMAP-CutDB

P01135.

SOURCE

Search...

Entry information

Entry name

TGFA_HUMAN

Accession

Primary (citable) accession number: P01135
Secondary accession number(s): A8K286 , 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:	May 1, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.