PTK2 (англ. Protein tyrosine kinase 2) – білок, який кодується однойменним геном, розташованим у людей на короткому плечі 8-ї хромосоми. Довжина поліпептидного ланцюга білка становить 1 052 амінокислот, а молекулярна маса — 119 233.
PTK2 | |||||||||||||||||
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Ідентифікатори | |||||||||||||||||
Символи | PTK2, FADK, FAK, FAK1, FRNK, PPP1R71, p125FAK, pp125FAK, protein tyrosine kinase 2, Fak, Focal adhesion kinase, Dmel_CG10023, FAK65D, ptk2, DFAK, Fak56, DFak56, Dmel\CG10023, pFAK, CT28129, CG10023, Fak56D, DmFAK | ||||||||||||||||
Зовнішні ІД | OMIM: 600758 MGI: 95481 HomoloGene: 7314 GeneCards: PTK2 | ||||||||||||||||
Реагує на сполуку | |||||||||||||||||
defactinib, VS-4718 | |||||||||||||||||
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Шаблон експресії | |||||||||||||||||
37233/ 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) | н/д | Хр. 15: 73.21 – 73.42 Mb | |||||||||||||||
PubMed search | |||||||||||||||||
Вікідані | |||||||||||||||||
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10 | 20 | 30 | 40 | 50 | ||||
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MAAAYLDPNL | NHTPNSSTKT | HLGTGMERSP | GAMERVLKVF | HYFESNSEPT | ||||
TWASIIRHGD | ATDVRGIIQK | IVDSHKVKHV | ACYGFRLSHL | RSEEVHWLHV | ||||
DMGVSSVREK | YELAHPPEEW | KYELRIRYLP | KGFLNQFTED | KPTLNFFYQQ | ||||
VKSDYMLEIA | DQVDQEIALK | LGCLEIRRSY | WEMRGNALEK | KSNYEVLEKD | ||||
VGLKRFFPKS | LLDSVKAKTL | RKLIQQTFRQ | FANLNREESI | LKFFEILSPV | ||||
YRFDKECFKC | ALGSSWIISV | ELAIGPEEGI | SYLTDKGCNP | THLADFTQVQ | ||||
TIQYSNSEDK | DRKGMLQLKI | AGAPEPLTVT | APSLTIAENM | ADLIDGYCRL | ||||
VNGTSQSFII | RPQKEGERAL | PSIPKLANSE | KQGMRTHAVS | VSETDDYAEI | ||||
IDEEDTYTMP | STRDYEIQRE | RIELGRCIGE | GQFGDVHQGI | YMSPENPALA | ||||
VAIKTCKNCT | SDSVREKFLQ | EALTMRQFDH | PHIVKLIGVI | TENPVWIIME | ||||
LCTLGELRSF | LQVRKYSLDL | ASLILYAYQL | STALAYLESK | RFVHRDIAAR | ||||
NVLVSSNDCV | KLGDFGLSRY | MEDSTYYKAS | KGKLPIKWMA | PESINFRRFT | ||||
SASDVWMFGV | CMWEILMHGV | KPFQGVKNND | VIGRIENGER | LPMPPNCPPT | ||||
LYSLMTKCWA | YDPSRRPRFT | ELKAQLSTIL | EEEKAQQEER | MRMESRRQAT | ||||
VSWDSGGSDE | APPKPSRPGY | PSPRSSEGFY | PSPQHMVQTN | HYQVSGYPGS | ||||
HGITAMAGSI | YPGQASLLDQ | TDSWNHRPQE | IAMWQPNVED | STVLDLRGIG | ||||
QVLPTHLMEE | RLIRQQQEME | EDQRWLEKEE | RFLKPDVRLS | RGSIDREDGS | ||||
LQGPIGNQHI | YQPVGKPDPA | APPKKPPRPG | APGHLGSLAS | LSSPADSYNE | ||||
GVKLQPQEIS | PPPTANLDRS | NDKVYENVTG | LVKAVIEMSS | KIQPAPPEEY | ||||
VPMVKEVGLA | LRTLLATVDE | TIPLLPASTH | REIEMAQKLL | NSDLGELINK | ||||
MKLAQQYVMT | SLQQEYKKQM | LTAAHALAVD | AKNLLDVIDQ | ARLKMLGQTR | ||||
PH |
Кодований геном білок за функціями належить до трансфераз, кіназ, , тирозинових протеїнкіназ, фосфопротеїнів. Задіяний у таких біологічних процесах, як ангіогенез, ацетилювання, альтернативний сплайсинг. Білок має сайт для зв'язування з АТФ, нуклеотидами. Локалізований у клітинній мембрані, цитоплазмі, цитоскелеті, ядрі, мембрані, клітинних контактах.
Література
- Andre E., Becker-Andre M. (1993). Expression of an N-terminally truncated form of human focal adhesion kinase in brain. Biochem. Biophys. Res. Commun. 190: 140—147. PMID 8422239 DOI:10.1006/bbrc.1993.1022
- 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
- Miao H., Burnett E., Kinch M., Simon E., Wang B. (2000). Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation. Nat. Cell Biol. 2: 62—69. PMID 10655584 DOI:10.1038/35000008
- Relou I.A.M., Bax L.A.B., Van Rijn H.J.M., Akkerman J.-W.N. (2003). Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein. Biochem. J. 369: 407—416. PMID 12387730 DOI:10.1042/BJ20020410
- Xia H., Nho R.S., Kahm J., Kleidon J., Henke C.A. (2004). Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway. J. Biol. Chem. 279: 33024—33034. PMID 15166238 DOI:10.1074/jbc.M313265200
- Golubovskaya V.M., Finch R., Cance W.G. (2005). Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53. J. Biol. Chem. 280: 25008—25021. PMID 15855171 DOI:10.1074/jbc.M414172200
Примітки
- Сполуки, які фізично взаємодіють з Protein tyrosine kinase 2 переглянути/редагувати посилання на ВікіДаних.
- Human PubMed Reference:.
- Mouse PubMed Reference:.
- HUGO Gene Nomenclature Commitee, HGNC:9611 (англ.) . Процитовано 7 вересня 2017.
- (англ.) . Архів оригіналу за 18 вересня 2017. Процитовано 7 вересня 2017.
Див. також
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PTK2 angl Protein tyrosine kinase 2 bilok yakij koduyetsya odnojmennim genom roztashovanim u lyudej na korotkomu plechi 8 yi hromosomi Dovzhina polipeptidnogo lancyuga bilka stanovit 1 052 aminokislot a molekulyarna masa 119 233 PTK2Nayavni strukturiPDBPoshuk ortologiv H0YB16 PDBe H0YB16 RCSBSpisok kodiv PDB4Q9S 1K04 1K05 1MP8 1OW6 1OW7 1OW8 2ETM 2IJM 3B71 3BZ3 3PXK 3S9O 4EBV 4EBW 4GU6 4GU9 4I4E 4I4F 4K8A 4K9Y 4KAB 4KAO 4NY0IdentifikatoriSimvoliPTK2 FADK FAK FAK1 FRNK PPP1R71 p125FAK pp125FAK protein tyrosine kinase 2 Fak Focal adhesion kinase Dmel CG10023 FAK65D ptk2 DFAK Fak56 DFak56 Dmel CG10023 pFAK CT28129 CG10023 Fak56D DmFAKZovnishni ID OMIM 600758 MGI 95481 HomoloGene 7314 GeneCards PTK2Reaguye na spolukudefactinib VS 4718Ontologiya genaMolekulyarna funkciya SH2 domain binding kinase activity signaling receptor binding ATP binding protein kinase activity JUN kinase binding non membrane spanning protein tyrosine kinase activity transferase activity GO 0001948 GO 0016582 protein binding protein kinase binding nucleotide binding actin binding protein tyrosine kinase activity protein phosphatase bindingKlitinna komponenta citoplazma gialoplazma membrana focal adhesion extrinsic component of cytoplasmic side of plasma membrane centr organizaciyi mikrotrubochok citoskelet klitinne yadro stress fiber apical plasma membrane lamellipodium klitinna membrana cell cortex mizhklitinni kontakti dendritic spine Adgezivni kontaktiBiologichnij proces regulation of protein phosphorylation positive regulation of protein phosphorylation regulation of cell adhesion mediated by integrin placenta development vaskulogenez protein phosphorylation vascular endothelial growth factor receptor signaling pathway growth hormone receptor signaling pathway blood vessel development regulation of osteoblast differentiation Angiogenez transforming growth factor beta receptor signaling pathway cellular response to transforming growth factor beta stimulus positive regulation of protein kinase B signaling Fc gamma receptor signaling pathway involved in phagocytosis cell motility GO 0043087 GO 0032313 GO 0032319 GO 0032314 GO 0043088 regulation of GTPase activity signal complex assembly regulation of epithelial cell migration negative regulation of axonogenesis regulation of endothelial cell migration establishment of cell polarity regulation of focal adhesion assembly fosforilyuvannya netrin activated signaling pathway negative regulation of synapse assembly extracellular matrix organization negative regulation of apoptotic process neuron migration positive regulation of ubiquitin dependent protein catabolic process regulation of cell shape integrin mediated signaling pathway regulation of substrate adhesion dependent cell spreading negative regulation of organ growth microtubule cytoskeleton organization negative regulation of anoikis positive regulation of protein kinase activity negative regulation of cell cell adhesion positive regulation of cell migration ephrin receptor signaling pathway heart morphogenesis MAPK cascade axon guidance positive regulation of phosphatidylinositol 3 kinase activity multicellular organism development regulation of cell population proliferation positive regulation of cell population proliferation positive regulation of phosphatidylinositol 3 kinase signaling regulation of cytoskeleton organization endothelial cell migration central nervous system neuron axonogenesis vrodzhenij imunitet peptidyl tyrosine phosphorylation epidermal growth factor receptor signaling pathway protein autophosphorylation nuclear migration negative regulation of autophagy positive regulation of cardiac muscle hypertrophy peptidyl tyrosine autophosphorylation diferenciaciya klitin regulation of cell adhesionDzherela Amigo QuickGOShablon ekspresiyi37233 Bilshe danihOrtologiVidi Lyudina MishaEntrez5747 37233 5747 37233 14083Ensembl ENSG00000169398 FBgn0020440 ENSMUSG00000022607UniProt Q05397 P34152RefSeq mRNK NM 001199649 NM 005607 NM 153831 NM 001316342 NM 001144246NM 001144247 NM 001169736 NM 079069 NM 166352 NM 166353NM 001130409 NM 007982 NM 001358045 NM 001358046RefSeq bilok NP 001186578 NP 001303271 NP 005598 NP 722560 NP 001339623NP 001339624 NP 001339625 NP 001339626 NP 001339627 NP 001339628 NP 001339629 NP 001339630 NP 001339631 NP 001339632 NP 001339633 NP 001339634 NP 001339635 NP 001339636 NP 001339637 NP 001339638 NP 001339639 NP 001339640 NP 001339641 NP 001339642 NP 001339643 NP 001339644 NP 001339645 NP 001339646 NP 001339647 NP 001339648 NP 001339649 NP 001339650 NP 001339651 NP 001339652 NP 001339653 NP 001339654 NP 001339655 NP 001339656 NP 001339657 NP 001339658 NP 001339659 NP 001339660 NP 001339661 NP 001339662 NP 001339663 NP 001339664 NP 001339665 NP 001339666 NP 001339667 NP 001339668 NP 001339669 NP 001339670 NP 001339671 NP 001339672 NP 001339673 NP 001339674 NP 001339675 NP 001339676 NP 001339677 NP 001339678 NP 001339679 NP 001339680 NP 001339681NP 032008 NP 001344974 NP 001344975Lokus UCSC n dHr 15 73 21 73 42 MbPubMed searchVikidaniDiv Red dlya lyudejDiv Red dlya mishejPoslidovnist aminokislot1020304050MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPHA 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 funkciyami nalezhit do transferaz kinaz tirozinovih proteyinkinaz fosfoproteyiniv Zadiyanij u takih biologichnih procesah yak angiogenez acetilyuvannya alternativnij splajsing Bilok maye sajt dlya zv yazuvannya z ATF nukleotidami Lokalizovanij u klitinnij membrani citoplazmi citoskeleti yadri membrani klitinnih kontaktah LiteraturaAndre E Becker Andre M 1993 Expression of an N terminally truncated form of human focal adhesion kinase in brain Biochem Biophys Res Commun 190 140 147 PMID 8422239 DOI 10 1006 bbrc 1993 1022 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 Miao H Burnett E Kinch M Simon E Wang B 2000 Activation of EphA2 kinase suppresses integrin function and causes focal adhesion kinase dephosphorylation Nat Cell Biol 2 62 69 PMID 10655584 DOI 10 1038 35000008 Relou I A M Bax L A B Van Rijn H J M Akkerman J W N 2003 Site specific phosphorylation of platelet focal adhesion kinase by low density lipoprotein Biochem J 369 407 416 PMID 12387730 DOI 10 1042 BJ20020410 Xia H Nho R S Kahm J Kleidon J Henke C A 2004 Focal adhesion kinase is upstream of phosphatidylinositol 3 kinase Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway J Biol Chem 279 33024 33034 PMID 15166238 DOI 10 1074 jbc M313265200 Golubovskaya V M Finch R Cance W G 2005 Direct interaction of the N terminal domain of focal adhesion kinase with the N terminal transactivation domain of p53 J Biol Chem 280 25008 25021 PMID 15855171 DOI 10 1074 jbc M414172200PrimitkiSpoluki yaki fizichno vzayemodiyut z Protein tyrosine kinase 2 pereglyanuti redaguvati posilannya na VikiDanih Human PubMed Reference Mouse PubMed Reference HUGO Gene Nomenclature Commitee HGNC 9611 angl Procitovano 7 veresnya 2017 angl Arhiv originalu za 18 veresnya 2017 Procitovano 7 veresnya 2017 Div takozhHromosoma 8Ce nezavershena stattya pro bilki Vi mozhete dopomogti proyektu vipravivshi abo dopisavshi yiyi