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TGFA_HUMAN
ID   TGFA_HUMAN              Reviewed;         160 AA.
AC   P01135; A8K286; Q15577; Q53SK7; Q9BS56; Q9UEI3; Q9UKM1; Q9UKM2; Q9UKM3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 218.
DE   RecName: Full=Protransforming growth factor alpha;
DE   Contains:
DE     RecName: Full=Transforming growth factor alpha;
DE              Short=TGF-alpha;
DE     AltName: Full=EGF-like TGF;
DE              Short=ETGF;
DE     AltName: Full=TGF type 1;
DE   Flags: Precursor;
GN   Name=TGFA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=6088071; DOI=10.1016/0092-8674(84)90550-6;
RA   Derynck R., Roberts A.B., Winkler M.E., Chen E.Y., Goeddel D.V.;
RT   "Human transforming growth factor-alpha: precursor structure and expression
RT   in E. coli.";
RL   Cell 38:287-297(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2464748; DOI=10.1210/mend-2-11-1056;
RA   Jakowlew S.B., Kondaiah P., Dillard P.J., Sporn M.B., Roberts A.B.;
RT   "A novel low molecular weight ribonucleic acid (RNA) related to
RT   transforming growth factor alpha messenger RNA.";
RL   Mol. Endocrinol. 2:1056-1063(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
RX   PubMed=8224876; DOI=10.1016/0378-1119(93)90210-t;
RA   Qian J.F., Lazar-Wesley E., Breugnot C., May E.;
RT   "Human transforming growth factor alpha: sequence analysis of the 4.5-kb
RT   and 1.6-kb mRNA species.";
RL   Gene 132:291-296(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8100397;
RA   Qian J.F., Feingold J., Stoll C., May E.;
RT   "Transforming growth factor-alpha: characterization of the BamHI, RsaI, and
RT   TaqI polymorphic regions.";
RL   Am. J. Hum. Genet. 53:168-175(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10552925; DOI=10.1006/geno.1999.5962;
RA   Machida J., Yoshiura K., Funkhauser C.D., Natsume N., Kawai T.,
RA   Murray J.C.;
RT   "Transforming growth factor-alpha (TGFA): genomic structure, boundary
RT   sequences, and mutation analysis in nonsyndromic cleft lip/palate and cleft
RT   palate only.";
RL   Genomics 61:237-242(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), AND TISSUE SPECIFICITY.
RX   PubMed=10523832; DOI=10.1038/sj.onc.1203091;
RA   Xu X., Liao J., Creek K.E., Pirisi L.;
RT   "Human keratinocytes and tumor-derived cell lines express alternatively
RT   spliced forms of transforming growth factor-alpha mRNA, encoding precursors
RT   lacking carboxyl-terminal valine residues.";
RL   Oncogene 18:5554-5562(1999).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) System Donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RX   PubMed=2907605; DOI=10.1128/mcb.8.12.5549-5554.1988;
RA   Jakobovits E.B., Schlokat U., Vannice J.L., Derynck R., Levinson A.D.;
RT   "The human transforming growth factor alpha promoter directs transcription
RT   initiation from a single site in the absence of a TATA sequence.";
RL   Mol. Cell. Biol. 8:5549-5554(1988).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RX   PubMed=10066034; DOI=10.1034/j.1399-0004.1999.550111.x;
RA   Collin G.B., Marshall J.D., Naggert J.K., Nishina P.M.;
RT   "TGFA: exon-intron structure and evaluation as a candidate gene for Alstrom
RT   syndrome.";
RL   Clin. Genet. 55:61-62(1999).
RN   [14]
RP   DISULFIDE BONDS.
RX   PubMed=1632509; DOI=10.1016/0003-2697(92)90331-z;
RA   Bean M.F., Carr S.A.;
RT   "Characterization of disulfide bond position in proteins and sequence
RT   analysis of cystine-bridged peptides by tandem mass spectrometry.";
RL   Anal. Biochem. 201:216-226(1992).
RN   [15]
RP   PALMITOYLATION AT CYS-153 AND CYS-154.
RX   PubMed=8910478; DOI=10.1074/jbc.271.45.28502;
RA   Shum L., Turck C.W., Derynck R.;
RT   "Cysteines 153 and 154 of transmembrane transforming growth factor-alpha
RT   are palmitoylated and mediate cytoplasmic protein association.";
RL   J. Biol. Chem. 271:28502-28508(1996).
RN   [16]
RP   INTERACTION WITH SNTA1 AND SDCBP.
RX   PubMed=10230395; DOI=10.1016/s1097-2765(00)80470-0;
RA   Fernandez-Larrea J., Merlos-Suarez A., Urena J.M., Baselga J., Arribas J.;
RT   "A role for a PDZ protein in the early secretory pathway for the targeting
RT   of proTGF-alpha to the cell surface.";
RL   Mol. Cell 3:423-433(1999).
RN   [17]
RP   INTERACTION WITH CNIH AND GORASP2.
RX   PubMed=17607000; DOI=10.1242/jcs.004200;
RA   Perez Castro C., Piscopo D., Nakagawa T., Derynck R.;
RT   "Cornichon regulates transport and secretion of TGFalpha-related proteins
RT   in metazoan cells.";
RL   J. Cell Sci. 120:2454-2466(2007).
RN   [18]
RP   INTERACTION WITH NKD2.
RX   PubMed=18757723; DOI=10.1073/pnas.0806298105;
RA   Ding W., Li C., Hu T., Graves-Deal R., Fotia A.B., Weissman A.M.,
RA   Coffey R.J.;
RT   "EGF receptor-independent action of TGF-alpha protects Naked2 from AO7-
RT   mediated ubiquitylation and proteasomal degradation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:13433-13438(2008).
RN   [19]
RP   STRUCTURE BY NMR OF TGF-ALPHA.
RX   PubMed=2261437; DOI=10.1021/bi00486a005;
RA   Kline T.P., Brown F.K., Brown S.C., Jeffs P.W., Kopple K.D., Mueller L.;
RT   "Solution structures of human transforming growth factor alpha derived from
RT   1H NMR data.";
RL   Biochemistry 29:7805-7813(1990).
RN   [20]
RP   STRUCTURE BY NMR OF TGF-ALPHA.
RX   PubMed=2050136; DOI=10.1111/j.1432-1033.1991.tb16050.x;
RA   Harvey T.S., Wilkinson A.J., Tappin M.J., Cooke R.M., Campbell I.D.;
RT   "The solution structure of human transforming growth factor alpha.";
RL   Eur. J. Biochem. 198:555-562(1991).
RN   [21]
RP   STRUCTURE BY NMR OF TGF-ALPHA.
RX   PubMed=8338831; DOI=10.1021/bi00080a003;
RA   Moy F.J., Li Y.C., Rauenbuehler P., Winkler M.E., Scheraga H.A.,
RA   Montelione G.T.;
RT   "Solution structure of human type-alpha transforming growth factor
RT   determined by heteronuclear NMR spectroscopy and refined by energy
RT   minimization with restraints.";
RL   Biochemistry 32:7334-7353(1993).
CC   -!- FUNCTION: TGF alpha is a mitogenic polypeptide that is able to bind to
CC       the EGF receptor/EGFR and to act synergistically with TGF beta to
CC       promote anchorage-independent cell proliferation in soft agar.
CC   -!- SUBUNIT: Interacts with the PDZ domains of MAGI3, SDCBP and SNTA1. The
CC       interaction with SDCBP, is required for the targeting to the cell
CC       surface. In the endoplasmic reticulum, in its immature form (i.e. with
CC       a prosegment and lacking full N-glycosylation), interacts with CNIH. In
CC       the Golgi apparatus, may form a complex with CNIH and GORASP2.
CC       Interacts (via cytoplasmic C-terminal domain) with NKD2.
CC       {ECO:0000269|PubMed:10230395, ECO:0000269|PubMed:17607000,
CC       ECO:0000269|PubMed:18757723}.
CC   -!- INTERACTION:
CC       P01135; P00533: EGFR; NbExp=4; IntAct=EBI-1034374, EBI-297353;
CC       P01135; Q969F2: NKD2; NbExp=3; IntAct=EBI-1034374, EBI-1538629;
CC       P01135; O43765: SGTA; NbExp=3; IntAct=EBI-1034374, EBI-347996;
CC       P01135; Q9EQJ9: Magi3; Xeno; NbExp=4; IntAct=EBI-1034374, EBI-7455245;
CC       P01135-2; O95214: LEPROTL1; NbExp=3; IntAct=EBI-12367411, EBI-750776;
CC       P01135-2; O43765: SGTA; NbExp=6; IntAct=EBI-12367411, EBI-347996;
CC   -!- SUBCELLULAR LOCATION: [Transforming growth factor alpha]: Secreted,
CC       extracellular space.
CC   -!- SUBCELLULAR LOCATION: [Protransforming growth factor alpha]: Cell
CC       membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=P01135-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P01135-2; Sequence=VSP_038369;
CC       Name=3; Synonyms=VaII;
CC         IsoId=P01135-3; Sequence=VSP_038369, VSP_038370;
CC       Name=4; Synonyms=VaI;
CC         IsoId=P01135-4; Sequence=VSP_038371;
CC       Name=5; Synonyms=VaIM;
CC         IsoId=P01135-5; Sequence=VSP_038369, VSP_038371;
CC   -!- TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 4 are expressed in
CC       keratinocytes and tumor-derived cell lines.
CC       {ECO:0000269|PubMed:10523832}.
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DR   EMBL; K03222; AAA61159.1; -; mRNA.
DR   EMBL; M31172; AAA61157.1; -; mRNA.
DR   EMBL; X70340; CAA49806.1; -; mRNA.
DR   EMBL; AF123243; AAF13491.1; -; Genomic_DNA.
DR   EMBL; AF123238; AAF13491.1; JOINED; Genomic_DNA.
DR   EMBL; AF123239; AAF13491.1; JOINED; Genomic_DNA.
DR   EMBL; AF123240; AAF13491.1; JOINED; Genomic_DNA.
DR   EMBL; AF123241; AAF13491.1; JOINED; Genomic_DNA.
DR   EMBL; AF123242; AAF13491.1; JOINED; Genomic_DNA.
DR   EMBL; AY325886; AAP97822.2; -; Genomic_DNA.
DR   EMBL; AY325885; AAP97822.2; JOINED; Genomic_DNA.
DR   EMBL; AY326405; AAP97822.2; JOINED; Genomic_DNA.
DR   EMBL; AY327131; AAP97822.2; JOINED; Genomic_DNA.
DR   EMBL; AY327132; AAP97822.2; JOINED; Genomic_DNA.
DR   EMBL; AY329368; AAP97822.2; JOINED; Genomic_DNA.
DR   EMBL; AF149096; AAF05089.1; -; mRNA.
DR   EMBL; AF149097; AAF05090.1; -; mRNA.
DR   EMBL; AF149098; AAF05091.1; -; mRNA.
DR   EMBL; BT006833; AAP35479.1; -; mRNA.
DR   EMBL; AK290151; BAF82840.1; -; mRNA.
DR   EMBL; AC005234; AAY14793.1; -; Genomic_DNA.
DR   EMBL; AC017084; AAY14705.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAW99810.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAW99812.1; -; Genomic_DNA.
DR   EMBL; BC005308; AAH05308.1; -; mRNA.
DR   EMBL; M22440; AAA52530.1; -; Genomic_DNA.
DR   EMBL; AF075584; AAD12238.1; -; Genomic_DNA.
DR   EMBL; AF075583; AAD12238.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS1905.1; -. [P01135-1]
DR   CCDS; CCDS46316.1; -. [P01135-2]
DR   PIR; JN0876; WFHU1.
DR   RefSeq; NP_001093161.1; NM_001099691.2. [P01135-2]
DR   RefSeq; NP_001295087.1; NM_001308158.1.
DR   RefSeq; NP_001295088.1; NM_001308159.1.
DR   RefSeq; NP_003227.1; NM_003236.3. [P01135-1]
DR   PDB; 1GK5; NMR; -; A=83-89.
DR   PDB; 1MOX; X-ray; 2.50 A; C/D=40-89.
DR   PDB; 1YUF; NMR; -; A=40-89.
DR   PDB; 1YUG; NMR; -; A=40-89.
DR   PDB; 2TGF; NMR; -; A=40-89.
DR   PDB; 3E50; X-ray; 2.30 A; C/D=40-89.
DR   PDB; 3TGF; NMR; -; A=40-89.
DR   PDB; 4TGF; NMR; -; A=40-89.
DR   PDB; 5KN5; X-ray; 2.80 A; C/F=49-88.
DR   PDB; 7SZ5; EM; 3.60 A; C/D=40-89.
DR   PDB; 7SZ7; EM; 3.40 A; C/D=40-89.
DR   PDBsum; 1GK5; -.
DR   PDBsum; 1MOX; -.
DR   PDBsum; 1YUF; -.
DR   PDBsum; 1YUG; -.
DR   PDBsum; 2TGF; -.
DR   PDBsum; 3E50; -.
DR   PDBsum; 3TGF; -.
DR   PDBsum; 4TGF; -.
DR   PDBsum; 5KN5; -.
DR   PDBsum; 7SZ5; -.
DR   PDBsum; 7SZ7; -.
DR   AlphaFoldDB; P01135; -.
DR   BMRB; P01135; -.
DR   SMR; P01135; -.
DR   BioGRID; 112897; 83.
DR   DIP; DIP-5765N; -.
DR   IntAct; P01135; 10.
DR   MINT; P01135; -.
DR   STRING; 9606.ENSP00000295400; -.
DR   ChEMBL; CHEMBL4662938; -.
DR   GlyGen; P01135; 1 site.
DR   SwissPalm; P01135; -.
DR   BioMuta; TGFA; -.
DR   DMDM; 135689; -.
DR   MassIVE; P01135; -.
DR   PaxDb; P01135; -.
DR   PeptideAtlas; P01135; -.
DR   PRIDE; P01135; -.
DR   ProteomicsDB; 51332; -. [P01135-1]
DR   ProteomicsDB; 51333; -. [P01135-2]
DR   ProteomicsDB; 51334; -. [P01135-3]
DR   ProteomicsDB; 51335; -. [P01135-4]
DR   ProteomicsDB; 51336; -. [P01135-5]
DR   ABCD; P01135; 10 sequenced antibodies.
DR   Antibodypedia; 16331; 1379 antibodies from 39 providers.
DR   DNASU; 7039; -.
DR   Ensembl; ENST00000295400.11; ENSP00000295400.6; ENSG00000163235.16. [P01135-1]
DR   Ensembl; ENST00000418333.6; ENSP00000404099.2; ENSG00000163235.16. [P01135-2]
DR   Ensembl; ENST00000445399.5; ENSP00000387493.1; ENSG00000163235.16. [P01135-3]
DR   GeneID; 7039; -.
DR   KEGG; hsa:7039; -.
DR   MANE-Select; ENST00000295400.11; ENSP00000295400.6; NM_003236.4; NP_003227.1.
DR   UCSC; uc002sgs.4; human. [P01135-1]
DR   CTD; 7039; -.
DR   DisGeNET; 7039; -.
DR   GeneCards; TGFA; -.
DR   HGNC; HGNC:11765; TGFA.
DR   HPA; ENSG00000163235; Tissue enhanced (brain).
DR   MalaCards; TGFA; -.
DR   MIM; 190170; gene.
DR   neXtProt; NX_P01135; -.
DR   OpenTargets; ENSG00000163235; -.
DR   Orphanet; 2227; NON RARE IN EUROPE: Hypodontia.
DR   Orphanet; 99798; Oligodontia.
DR   PharmGKB; PA36480; -.
DR   VEuPathDB; HostDB:ENSG00000163235; -.
DR   eggNOG; ENOG502S1CF; Eukaryota.
DR   GeneTree; ENSGT00940000160058; -.
DR   HOGENOM; CLU_109645_1_0_1; -.
DR   InParanoid; P01135; -.
DR   OMA; SACCHSE; -.
DR   OrthoDB; 1401257at2759; -.
DR   PhylomeDB; P01135; -.
DR   TreeFam; TF332938; -.
DR   PathwayCommons; P01135; -.
DR   Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-HSA-177929; Signaling by EGFR.
DR   Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
DR   Reactome; R-HSA-180292; GAB1 signalosome.
DR   Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
DR   Reactome; R-HSA-182971; EGFR downregulation.
DR   Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR   Reactome; R-HSA-212718; EGFR interacts with phospholipase C-gamma.
DR   Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR   Reactome; R-HSA-5638303; Inhibition of Signaling by Overexpressed EGFR.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR   Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR   Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR   SignaLink; P01135; -.
DR   SIGNOR; P01135; -.
DR   BioGRID-ORCS; 7039; 4 hits in 1079 CRISPR screens.
DR   ChiTaRS; TGFA; human.
DR   EvolutionaryTrace; P01135; -.
DR   GeneWiki; TGF_alpha; -.
DR   GenomeRNAi; 7039; -.
DR   Pharos; P01135; Tbio.
DR   PRO; PR:P01135; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P01135; protein.
DR   Bgee; ENSG00000163235; Expressed in esophagus squamous epithelium and 174 other tissues.
DR   ExpressionAtlas; P01135; baseline and differential.
DR   Genevisible; P01135; HS.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; IDA:HGNC-UCL.
DR   GO; GO:0048018; F:receptor ligand activity; IDA:MGI.
DR   GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IDA:MGI.
DR   GO; GO:0072574; P:hepatocyte proliferation; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; TAS:GO_Central.
DR   GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IDA:HGNC-UCL.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:HGNC-UCL.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:HGNC-UCL.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:HGNC-UCL.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   IDEAL; IID00290; -.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR015497; EGF_rcpt_ligand.
DR   PANTHER; PTHR10740; PTHR10740; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Growth factor; Lipoprotein; Membrane;
KW   Mitogen; Palmitate; Reference proteome; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..160
FT                   /note="Protransforming growth factor alpha"
FT                   /id="PRO_0000302744"
FT   PROPEP          24..39
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000007752"
FT   CHAIN           40..89
FT                   /note="Transforming growth factor alpha"
FT                   /id="PRO_0000007753"
FT   PROPEP          90..160
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000007754"
FT   TOPO_DOM        24..98
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..160
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..83
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   LIPID           153
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:8910478"
FT   LIPID           154
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:8910478"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000269|PubMed:1632509"
FT   DISULFID        55..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000269|PubMed:1632509"
FT   DISULFID        73..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000269|PubMed:1632509"
FT   VAR_SEQ         32
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10523832,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|Ref.7"
FT                   /id="VSP_038369"
FT   VAR_SEQ         159..160
FT                   /note="VV -> ATLG (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10523832"
FT                   /id="VSP_038370"
FT   VAR_SEQ         159..160
FT                   /note="VV -> GCRLY (in isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10523832"
FT                   /id="VSP_038371"
FT   VARIANT         109
FT                   /note="V -> M (in dbSNP:rs11466259)"
FT                   /id="VAR_024271"
FT   CONFLICT        58
FT                   /note="G -> A (in Ref. 2; AAA61157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="Q -> H (in Ref. 2; AAA61157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="V -> L (in Ref. 2; AAA61157)"
FT                   /evidence="ECO:0000305"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:1MOX"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:1YUF"
FT   STRAND          58..63
FT                   /evidence="ECO:0007829|PDB:1MOX"
FT   TURN            64..67
FT                   /evidence="ECO:0007829|PDB:1MOX"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:1MOX"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:1MOX"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:5KN5"
SQ   SEQUENCE   160 AA;  17006 MW;  D692184F9353DE47 CRC64;
     MVPSAGQLAL FALGIVLAAC QALENSTSPL SADPPVAAAV VSHFNDCPDS HTQFCFHGTC
     RFLVQEDKPA CVCHSGYVGA RCEHADLLAV VAASQKKQAI TALVVVSIVA LAVLIITCVL
     IHCCQVRKHC EWCRALICRH EKPSALLKGR TACCHSETVV
 
 
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