EGF (англ. Epidermal growth factor) – білок, який кодується однойменним геном, розташованим у людей на короткому плечі 4-ї хромосоми. Довжина поліпептидного ланцюга білка становить 1 207 амінокислот, а молекулярна маса — 133 994.
EGF | |||||||||||||||||
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Ідентифікатори | |||||||||||||||||
Символи | EGF, HOMG4, URG, epidermal growth factor, epithelial growth factor | ||||||||||||||||
Зовнішні ІД | OMIM: 131530 MGI: 95290 HomoloGene: 1483 GeneCards: EGF | ||||||||||||||||
Пов'язані генетичні захворювання | |||||||||||||||||
renal hypomagnesemia 4 | |||||||||||||||||
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Шаблон експресії | |||||||||||||||||
Більше даних | |||||||||||||||||
Ортологи | |||||||||||||||||
Види | Людина | Миша | |||||||||||||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (мРНК) |
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RefSeq (білок) |
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Локус (UCSC) | Хр. 4: 109.91 – 110.01 Mb | Хр. 3: 129.47 – 129.55 Mb | |||||||||||||||
PubMed search | |||||||||||||||||
Вікідані | |||||||||||||||||
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10 | 20 | 30 | 40 | 50 | ||||
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MLLTLIILLP | VVSKFSFVSL | SAPQHWSCPE | GTLAGNGNST | CVGPAPFLIF | ||||
SHGNSIFRID | TEGTNYEQLV | VDAGVSVIMD | FHYNEKRIYW | VDLERQLLQR | ||||
VFLNGSRQER | VCNIEKNVSG | MAINWINEEV | IWSNQQEGII | TVTDMKGNNS | ||||
HILLSALKYP | ANVAVDPVER | FIFWSSEVAG | SLYRADLDGV | GVKALLETSE | ||||
KITAVSLDVL | DKRLFWIQYN | REGSNSLICS | CDYDGGSVHI | SKHPTQHNLF | ||||
AMSLFGDRIF | YSTWKMKTIW | IANKHTGKDM | VRINLHSSFV | PLGELKVVHP | ||||
LAQPKAEDDT | WEPEQKLCKL | RKGNCSSTVC | GQDLQSHLCM | CAEGYALSRD | ||||
RKYCEDVNEC | AFWNHGCTLG | CKNTPGSYYC | TCPVGFVLLP | DGKRCHQLVS | ||||
CPRNVSECSH | DCVLTSEGPL | CFCPEGSVLE | RDGKTCSGCS | SPDNGGCSQL | ||||
CVPLSPVSWE | CDCFPGYDLQ | LDEKSCAASG | PQPFLLFANS | QDIRHMHFDG | ||||
TDYGTLLSQQ | MGMVYALDHD | PVENKIYFAH | TALKWIERAN | MDGSQRERLI | ||||
EEGVDVPEGL | AVDWIGRRFY | WTDRGKSLIG | RSDLNGKRSK | IITKENISQP | ||||
RGIAVHPMAK | RLFWTDTGIN | PRIESSSLQG | LGRLVIASSD | LIWPSGITID | ||||
FLTDKLYWCD | AKQSVIEMAN | LDGSKRRRLT | QNDVGHPFAV | AVFEDYVWFS | ||||
DWAMPSVMRV | NKRTGKDRVR | LQGSMLKPSS | LVVVHPLAKP | GADPCLYQNG | ||||
GCEHICKKRL | GTAWCSCREG | FMKASDGKTC | LALDGHQLLA | GGEVDLKNQV | ||||
TPLDILSKTR | VSEDNITESQ | HMLVAEIMVS | DQDDCAPVGC | SMYARCISEG | ||||
EDATCQCLKG | FAGDGKLCSD | IDECEMGVPV | CPPASSKCIN | TEGGYVCRCS | ||||
EGYQGDGIHC | LDIDECQLGE | HSCGENASCT | NTEGGYTCMC | AGRLSEPGLI | ||||
CPDSTPPPHL | REDDHHYSVR | NSDSECPLSH | DGYCLHDGVC | MYIEALDKYA | ||||
CNCVVGYIGE | RCQYRDLKWW | ELRHAGHGQQ | QKVIVVAVCV | VVLVMLLLLS | ||||
LWGAHYYRTQ | KLLSKNPKNP | YEESSRDVRS | RRPADTEDGM | SSCPQPWFVV | ||||
IKEHQDLKNG | GQPVAGEDGQ | AADGSMQPTS | WRQEPQLCGM | GTEQGCWIPV | ||||
SSDKGSCPQV | MERSFHMPSY | GTQTLEGGVE | KPHSLLSANP | LWQQRALDPP | ||||
HQMELTQ |
Кодований геном білок за функцією належить до факторів росту. Задіяний у таких біологічних процесах як поліморфізм, альтернативний сплайсинг. Локалізований у мембрані.
Література
- The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 14: 2121—2127. 2004. PMID 15489334 DOI:10.1101/gr.2596504
- Furuya M., Akashi S., Hirayama K. (1989). The primary structure of human EGF produced by genetic engineering, studied by high-performance tandem mass spectrometry. Biochem. Biophys. Res. Commun. 163: 1100—1106. PMID 2789514 DOI:10.1016/0006-291X(89)92334-6
- Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G. (2011). Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD. Mol. Cell. Proteomics: —. PMID 22171320 DOI:10.1074/mcp.M111.013649
- Hommel U., Harvey T.S., Driscoll P.C., Campbell I.D. (1992). Human epidermal growth factor. High resolution solution structure and comparison with human transforming growth factor alpha. J. Mol. Biol. 227: 271—282. PMID 1522591 DOI:10.1016/0022-2836(92)90697-I
- Zettl M., Adrain C., Strisovsky K., Lastun V., Freeman M. (2011). Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling. Cell. 145: 79—91. PMID 21439629 DOI:10.1016/j.cell.2011.02.047
- Huang H.W., Mohan S.K., Yu C. (2010). The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin. Biochem. Biophys. Res. Commun. 402: 705—710. PMID 21029725 DOI:10.1016/j.bbrc.2010.10.089
Примітки
- Захворювання, генетично пов'язані з EGF переглянути/редагувати посилання на ВікіДаних.
- Human PubMed Reference:.
- Mouse PubMed Reference:.
- (англ.) . Архів оригіналу за 30 травня 2017. Процитовано 30 серпня 2017.
- (англ.) . Архів оригіналу за 31 серпня 2017. Процитовано 30 серпня 2017.
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EGF angl Epidermal growth factor bilok yakij koduyetsya odnojmennim genom roztashovanim u lyudej na korotkomu plechi 4 yi hromosomi Dovzhina polipeptidnogo lancyuga bilka stanovit 1 207 aminokislot a molekulyarna masa 133 994 EGFNayavni strukturiPDBPoshuk ortologiv PDBe RCSBSpisok kodiv PDB1IVO 1JL9 1NQL 1P9J 2KV4 3NJPIdentifikatoriSimvoliEGF HOMG4 URG epidermal growth factor epithelial growth factorZovnishni ID OMIM 131530 MGI 95290 HomoloGene 1483 GeneCards EGFPov yazani genetichni zahvoryuvannyarenal hypomagnesemia 4Ontologiya genaMolekulyarna funkciya calcium ion binding transmembrane receptor protein tyrosine kinase activator activity epidermal growth factor receptor binding Wnt protein binding GO 0001948 GO 0016582 protein binding growth factor activity Wnt activated receptor activity protein tyrosine kinase activity phosphatidylinositol 4 5 bisphosphate 3 kinase activityKlitinna komponenta integral component of membrane membrana receptor complex extracellular region lysosomal membrane ekzosoma platelet alpha granule lumen mizhklitinnij prostir clathrin coated vesicle membrane klitinna membranaBiologichnij proces negative regulation of epidermal growth factor receptor signaling pathway positive regulation of MAP kinase activity epidermal growth factor receptor signaling pathway regulation of protein localization to cell surface ERK1 and ERK2 cascade platelet degranulation regulation of calcium ion import mammary gland alveolus development MAPK cascade replikaciya DNK GO 0060469 GO 0009371 positive regulation of transcription DNA templated negative regulation of secretion positive regulation of hyaluronan biosynthetic process positive regulation of peptidyl threonine phosphorylation positive regulation of ubiquitin dependent protein catabolic process Angiogenez Wnt signaling pathway involved in dorsal ventral axis specification positive regulation of cell population proliferation positive regulation of peptidyl tyrosine phosphorylation positive regulation of cerebellar granule cell precursor proliferation canonical Wnt signaling pathway negative regulation of cholesterol efflux peptidyl tyrosine phosphorylation positive regulation of DNA binding positive regulation of phosphorylation positive regulation of mitotic nuclear division branching morphogenesis of an epithelial tube GO 0072468 signalna transdukciya regulation of peptidyl tyrosine phosphorylation ERBB2 signaling pathway phosphatidylinositol phosphate biosynthetic process positive regulation of protein tyrosine kinase activity activation of transmembrane receptor protein tyrosine kinase activity regulation of cell motility positive regulation of receptor internalization positive regulation of epidermal growth factor activated receptor activity membrane organization negative regulation of ERBB signaling pathway embryonic retina morphogenesis in camera type eye GO 1901313 positive regulation of gene expression positive regulation of cell migration positive regulation of protein kinase B signaling negative regulation of Notch signaling pathway regulation of receptor signaling pathway via JAK STAT positive regulation of canonical Wnt signaling pathway positive regulation of protein localization to early endosomeDzherela Amigo QuickGOShablon ekspresiyiBilshe danihOrtologiVidi Lyudina MishaEntrez1950 13645Ensembl ENSG00000138798 ENSMUSG00000028017UniProt P01133 P01132RefSeq mRNK NM 001178130 NM 001178131 NM 001963 NM 001357021NM 010113 NM 001310737 NM 001329594RefSeq bilok NP 001171601 NP 001171602 NP 001954 NP 001343950NP 001297666 NP 001316523 NP 034243Lokus UCSC Hr 4 109 91 110 01 MbHr 3 129 47 129 55 MbPubMed searchVikidaniDiv Red dlya lyudejDiv Red dlya mishejPoslidovnist aminokislot1020304050MLLTLIILLPVVSKFSFVSLSAPQHWSCPEGTLAGNGNSTCVGPAPFLIFSHGNSIFRIDTEGTNYEQLVVDAGVSVIMDFHYNEKRIYWVDLERQLLQRVFLNGSRQERVCNIEKNVSGMAINWINEEVIWSNQQEGIITVTDMKGNNSHILLSALKYPANVAVDPVERFIFWSSEVAGSLYRADLDGVGVKALLETSEKITAVSLDVLDKRLFWIQYNREGSNSLICSCDYDGGSVHISKHPTQHNLFAMSLFGDRIFYSTWKMKTIWIANKHTGKDMVRINLHSSFVPLGELKVVHPLAQPKAEDDTWEPEQKLCKLRKGNCSSTVCGQDLQSHLCMCAEGYALSRDRKYCEDVNECAFWNHGCTLGCKNTPGSYYCTCPVGFVLLPDGKRCHQLVSCPRNVSECSHDCVLTSEGPLCFCPEGSVLERDGKTCSGCSSPDNGGCSQLCVPLSPVSWECDCFPGYDLQLDEKSCAASGPQPFLLFANSQDIRHMHFDGTDYGTLLSQQMGMVYALDHDPVENKIYFAHTALKWIERANMDGSQRERLIEEGVDVPEGLAVDWIGRRFYWTDRGKSLIGRSDLNGKRSKIITKENISQPRGIAVHPMAKRLFWTDTGINPRIESSSLQGLGRLVIASSDLIWPSGITIDFLTDKLYWCDAKQSVIEMANLDGSKRRRLTQNDVGHPFAVAVFEDYVWFSDWAMPSVMRVNKRTGKDRVRLQGSMLKPSSLVVVHPLAKPGADPCLYQNGGCEHICKKRLGTAWCSCREGFMKASDGKTCLALDGHQLLAGGEVDLKNQVTPLDILSKTRVSEDNITESQHMLVAEIMVSDQDDCAPVGCSMYARCISEGEDATCQCLKGFAGDGKLCSDIDECEMGVPVCPPASSKCINTEGGYVCRCSEGYQGDGIHCLDIDECQLGEHSCGENASCTNTEGGYTCMCAGRLSEPGLICPDSTPPPHLREDDHHYSVRNSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELRHAGHGQQQKVIVVAVCVVVLVMLLLLSLWGAHYYRTQKLLSKNPKNPYEESSRDVRSRRPADTEDGMSSCPQPWFVVIKEHQDLKNGGQPVAGEDGQAADGSMQPTSWRQEPQLCGMGTEQGCWIPVSSDKGSCPQVMERSFHMPSYGTQTLEGGVEKPHSLLSANPLWQQRALDPPHQMELTQA Alanin C Cisteyin D Asparaginova kislota E Glutaminova kislota F Fenilalanin G Glicin H Gistidin I Izolejcin K Lizin L Lejcin M Metionin N Asparagin P Prolin Q Glutamin R Arginin S Serin T Treonin V Valin W Triptofan Y Tirozin Kodovanij genom bilok za funkciyeyu nalezhit do faktoriv rostu Zadiyanij u takih biologichnih procesah yak polimorfizm alternativnij splajsing Lokalizovanij u membrani LiteraturaThe status quality and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC Genome Res 14 2121 2127 2004 PMID 15489334 DOI 10 1101 gr 2596504 Furuya M Akashi S Hirayama K 1989 The primary structure of human EGF produced by genetic engineering studied by high performance tandem mass spectrometry Biochem Biophys Res Commun 163 1100 1106 PMID 2789514 DOI 10 1016 0006 291X 89 92334 6 Halim A Nilsson J Ruetschi U Hesse C Larson G 2011 Human urinary glycoproteomics attachment site specific analysis of N and O linked glycosylations by CID and ECD Mol Cell Proteomics PMID 22171320 DOI 10 1074 mcp M111 013649 Hommel U Harvey T S Driscoll P C Campbell I D 1992 Human epidermal growth factor High resolution solution structure and comparison with human transforming growth factor alpha J Mol Biol 227 271 282 PMID 1522591 DOI 10 1016 0022 2836 92 90697 I Zettl M Adrain C Strisovsky K Lastun V Freeman M 2011 Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling Cell 145 79 91 PMID 21439629 DOI 10 1016 j cell 2011 02 047 Huang H W Mohan S K Yu C 2010 The NMR solution structure of human epidermal growth factor hEGF at physiological pH and its interactions with suramin Biochem Biophys Res Commun 402 705 710 PMID 21029725 DOI 10 1016 j bbrc 2010 10 089PrimitkiZahvoryuvannya genetichno pov yazani z EGF pereglyanuti redaguvati posilannya na VikiDanih Human PubMed Reference Mouse PubMed Reference angl Arhiv originalu za 30 travnya 2017 Procitovano 30 serpnya 2017 angl Arhiv originalu za 31 serpnya 2017 Procitovano 30 serpnya 2017 Div takozhHromosoma 4Ce nezavershena stattya pro bilki Vi mozhete dopomogti proyektu vipravivshi abo dopisavshi yiyi