CD117

V-kit Hardi-Zakerman 4, homolog mačijeg sarkoma viralnog onkogena
V-kit Hardi-Zakerman 4, homolog mačijeg sarkoma viralnog onkogena
	PDB prikaz baziran na 1pkg.
Dostupne strukture
	1PKG, 1T45, 1T46, 2E9W, 2EC8, 2VIF, 3G0E, 3G0F
Identifikatori
Simboli	KIT; C-Kit; CD117; PBT; SCFR
Vanjski ID	OMIM: 164920 MGI: 96677 HomoloGene: 187 GeneCards: KIT Gene
EC broj	2.7.10.1
Ontologija gena
Molekularna funkcija	• vezivanje nukleotida; • vezivanje proteaza; • aktivnost proteinske tirozinske kinaze; • aktivnost transmembranskog receptora proteinske tirozinske kinaze; • aktivnost receptorskog signalnog proteina tirozinske kinaze; • receptorska aktivnost; • aktivnost faktora receptora stem ćelija; • proteinsko vezivanje; • ATP vezivanje; • citokinsko vezivanje; • aktivnost proteinske homodimerizacije; • vezivanje metalnog jona;
Celularna komponenta	• ekstracelularni prostor; • nukleus; • citoplazma; • ćelijska membrana; • spoljašnja strana ćelijske membrane; • integralno sa membranom;
Biološki proces	• aktivacija MAPK aktivnosti; • diferencijacija mijeloidnih progenitornih ćelija; • diferencijacija limfoidnih progenitornih ćelija; • glikosfingolipidni metabolički proces; • prenos signala; • signalni put transmembranskog receptora proteinske tirozinske kinaze; • kaskada intracelularne proteinske kinaze; • spermatogeneza; • razvoj spermatida; • pozitivna regulacija ćelijske proliferacije; • razvoj muških gonada; • respons na radijaciju; • pozitivna regulacija genske ekspresije; • pozitivna regulacija fosfolipaze C; • pozitivna regulacija kaskade fosfatidilinozitol 3-kinaze; • peptidil-tirozinska fosforilacija; • citokinom posredovani signalni put; • održavanje matičnih ćelija; • prenos signala fosforilacijom;
Ortolozi
Vrsta	Čovek
Entrez	3815
Ensembl	ENSG00000157404
UniProt	P10721
RefSeq (mRNA)	NM_000222.2
RefSeq (protein)	NP_000213.1
Lokacija (UCSC)	Chr 4:; 55.52 - 55.61 Mb
PubMed pretraga	[1]

Receptor faktora rasta mastocita/matičnih ćelija (engl. Mast/stem cell growth factor receptor - SCFR), takođe poznat kao proto-onkogen c-Kit ili tirozinska proteinska kinaza Kit ili CD117, je protein koji je kod ljudi kodiran KIT genom.^[1] Višestruke transkriptne varijante koje kodiraju različite izoforme ovog gena su poznate.^[2] KIT prvi opisao nemački biohemičar Aksel Ulrič 1987. kao ćelijski homolog mačijeg sarkomnog viralnog onkogena v-kit.^[3]

Interakcije

CD117 formira interakcije sa:

APS,^[4]
BCR,^[5]
CD63,^[6]
CD81,^[6]
CD9,^[6]
CRK,^[7]^[7]
CRKL,^[8]^[9]
DOK1,^[10]
FES,^[11]^[11]
GRB10,^[12]
Grb2,^[13]^[14]^[15]
KITLG,^[16]^[17]
LNK,^[18]
LYN,^[10]^[19]
MATK,^[20]^[21]
MPDZ,^[22]
PIK3R1,^[8]^[13]^[23]
PTPN11,^[24]^[25]
PTPN6,^[25]^[26]
STAT1,^[27]
SOCS1,^[13]
SOCS6,^[28]
SRC,^[29] i
TEC.^[30]
Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Reference

^ Andre C, Hampe A, Lachaume P, Martin E, Wang XP, Manus V, Hu WX, Galibert F (1997). „Sequence analysis of two genomic regions containing the KIT and the FMS receptor tyrosine kinase genes”. Genomics. 39 (2): 216—26. PMID 9027509. doi:10.1006/geno.1996.4482.
^ „Entrez Gene: KIT v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog”.
^ Yarden Y, Kuang WJ, Yang-Feng T, Coussens L, Munemitsu S, Dull TJ, Chen E, Schlessinger J, Francke U, Ullrich A (1987). „Human proto-oncogene c-kit: a new cell surface receptor tyrosine kinase for an unidentified ligand”. EMBO J. 6 (11): 3341—51. PMC 553789 . PMID 2448137.
^ Wollberg P, Lennartsson J, Gottfridsson E, Yoshimura A, Rönnstrand L (2003). „The adapter protein APS associates with the multifunctional docking sites Tyr-568 and Tyr-936 in c-Kit”. Biochem. J. 370 (Pt 3): 1033—8. PMC 1223215 . PMID 12444928. doi:10.1042/BJ20020716.
^ Hallek M, Danhauser-Riedl S, Herbst R, Warmuth M, Winkler A, Kolb HJ, Druker B, Griffin JD, Emmerich B, Ullrich A (1996). „Interaction of the receptor tyrosine kinase p145c-kit with the p210bcr/abl kinase in myeloid cells”. Br. J. Haematol. 94 (1): 5—16. PMID 8757502. doi:10.1046/j.1365-2141.1996.6102053.x.
^ ^а ^б ^в Anzai N, Lee Y, Youn BS, Fukuda S, Kim YJ, Mantel C, Akashi M, Broxmeyer HE (2002). „C-kit associated with the transmembrane 4 superfamily proteins constitutes a functionally distinct subunit in human hematopoietic progenitors”. Blood. 99 (12): 4413—21. PMID 12036870. doi:10.1182/blood.V99.12.4413.
^ ^а ^б Lennartsson J, Wernstedt C, Engström U, Hellman U, Rönnstrand L (2003). „Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk”. Exp. Cell Res. 288 (1): 110—8. PMID 12878163. doi:10.1016/S0014-4827(03)00206-4.
^ ^а ^б van Dijk TB, van Den Akker E, Amelsvoort MP, Mano H, Löwenberg B, von Lindern M (2000). „Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells”. Blood. 96 (10): 3406—13. PMID 11071635.
^ Sattler M, Salgia R, Shrikhande G, Verma S, Pisick E, Prasad KV, Griffin JD (1997). „Steel factor induces tyrosine phosphorylation of CRKL and binding of CRKL to a complex containing c-kit, phosphatidylinositol 3-kinase, and p120(CBL)”. J. Biol. Chem. 272 (15): 10248—53. PMID 9092574. doi:10.1074/jbc.272.15.10248.
^ ^а ^б Liang X, Wisniewski D, Strife A, Shivakrupa, Clarkson B, Resh MD (2002). „Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling”. J. Biol. Chem. 277 (16): 13732—8. PMID 11825908. doi:10.1074/jbc.M200277200.
^ ^а ^б Voisset E, Lopez S, Chaix A, Vita M, George C, Dubreuil P, De Sepulveda P (2010). „FES kinase participates in KIT-ligand induced chemotaxis”. Biochem. Biophys. Res. Commun. 393 (1): 174—8. PMID 20117079. doi:10.1016/j.bbrc.2010.01.116.
^ Jahn T, Seipel P, Urschel S, Peschel C, Duyster J (2002). „Role for the adaptor protein Grb10 in the activation of Akt”. Mol. Cell. Biol. 22 (4): 979—91. PMC 134632 . PMID 11809791. doi:10.1128/MCB.22.4.979-991.2002.
^ ^а ^б ^в De Sepulveda P, Okkenhaug K, Rose JL, Hawley RG, Dubreuil P, Rottapel R (1999). „Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation”. EMBO J. 18 (4): 904—15. PMC 1171183 . PMID 10022833. doi:10.1093/emboj/18.4.904.
^ Thömmes K, Lennartsson J, Carlberg M, Rönnstrand L (1999). „Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor”. Biochem. J. 341 ( Pt 1): 211—6. PMC 1220349 . PMID 10377264. doi:10.1042/0264-6021:3410211.
^ Feng GS, Ouyang YB, Hu DP, Shi ZQ, Gentz R, Ni J (1996). „Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway”. J. Biol. Chem. 271 (21): 12129—32. PMID 8647802. doi:10.1074/jbc.271.21.12129.
^ Lev S, Yarden Y, Givol D (1992). „A recombinant ectodomain of the receptor for the stem cell factor (SCF) retains ligand-induced receptor dimerization and antagonizes SCF-stimulated cellular responses”. J. Biol. Chem. 267 (15): 10866—73. PMID 1375232.
^ Blechman JM, Lev S, Brizzi MF, Leitner O, Pegoraro L, Givol D, Yarden Y (1993). „Soluble c-kit proteins and antireceptor monoclonal antibodies confine the binding site of the stem cell factor”. J. Biol. Chem. 268 (6): 4399—406. PMID 7680037.
^ Gueller S, Gery S, Nowak V, Liu L, Serve H, Koeffler HP (2008). „Adaptor protein Lnk associates with Tyr(568) in c-Kit”. Biochem. J. 415 (2): 241—5. PMID 18588518. doi:10.1042/BJ20080102.
^ Linnekin D, DeBerry CS, Mou S (1997). „Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells”. J. Biol. Chem. 272 (43): 27450—5. PMID 9341198. doi:10.1074/jbc.272.43.27450.
^ Jhun BH, Rivnay B, Price D, Avraham H (1995). „The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit”. J. Biol. Chem. 270 (16): 9661—6. PMID 7536744. doi:10.1074/jbc.270.16.9661.
^ Price DJ, Rivnay B, Fu Y, Jiang S, Avraham S, Avraham H (1997). „Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes”. J. Biol. Chem. 272 (9): 5915—20. PMID 9038210. doi:10.1074/jbc.272.9.5915.
^ Mancini A, Koch A, Stefan M, Niemann H, Tamura T (2000). „The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity”. FEBS Lett. 482 (1-2): 54—8. PMID 11018522. doi:10.1016/S0014-5793(00)02036-6.
^ Serve H, Hsu YC, Besmer P (1994). „Tyrosine residue 719 of the c-kit receptor is essential for binding of the P85 subunit of phosphatidylinositol (PI) 3-kinase and for c-kit-associated PI 3-kinase activity in COS-1 cells”. J. Biol. Chem. 269 (8): 6026—30. PMID 7509796.
^ Tauchi T, Feng GS, Marshall MS, Shen R, Mantel C, Pawson T, Broxmeyer HE (1994). „The ubiquitously expressed Syp phosphatase interacts with c-kit and Grb2 in hematopoietic cells”. J. Biol. Chem. 269 (40): 25206—11. PMID 7523381.
^ ^а ^б Kozlowski M, Larose L, Lee F, Le DM, Rottapel R, Siminovitch KA (1998). „SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain”. Mol. Cell. Biol. 18 (4): 2089—99. PMC 121439 . PMID 9528781.
^ Yi T, Ihle JN (1993). „Association of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligand”. Mol. Cell. Biol. 13 (6): 3350—8. PMC 359793 . PMID 7684496.
^ Deberry C, Mou S, Linnekin D (1997). „Stat1 associates with c-kit and is activated in response to stem cell factor”. Biochem. J. 327 ( Pt 1): 73—80. PMC 1218765 . PMID 9355737.
^ Bayle J, Letard S, Frank R, Dubreuil P, De Sepulveda P (2004). „Suppressor of cytokine signaling 6 associates with KIT and regulates KIT receptor signaling”. J. Biol. Chem. 279 (13): 12249—59. PMID 14707129. doi:10.1074/jbc.M313381200.
^ Lennartsson J, Blume-Jensen P, Hermanson M, Pontén E, Carlberg M, Rönnstrand L (1999). „Phosphorylation of Shc by Src family kinases is necessary for stem cell factor receptor/c-kit mediated activation of the Ras/MAP kinase pathway and c-fos induction”. Oncogene. 18 (40): 5546—53. PMID 10523831. doi:10.1038/sj.onc.1202929.
^ Tang B, Mano H, Yi T, Ihle JN (1994). „Tec kinase associates with c-kit and is tyrosine phosphorylated and activated following stem cell factor binding”. Mol. Cell. Biol. 14 (12): 8432—7. PMC 359382 . PMID 7526158.

Literatura

Lennartsson J, Rönnstrand L (2006). „The stem cell factor receptor/c-Kit as a drug target in cancer”. Curr. Cancer Drug Targ. 6 (1): 65—75. PMID 16475976. doi:10.2174/156800906775471725.
Rönnstrand L (2004). „Signal transduction via the stem cell factor receptor/c-Kit”. Cell. Mol. Life Sci. 61 (19–20): 2535—2548. PMID 15526160. doi:10.1007/s00018-004-4189-6.
Linnekin D (2000). „Early signaling pathways activated by c-Kit in hematopoietic cells”. Int. J. Biochem. Cell Biol. 31 (10): 1053—74. PMID 10582339. doi:10.1016/S1357-2725(99)00078-3.
Canonico B, Felici C, Papa S (2001). „CD117”. J. Biol. Regul. Homeost. Agents. 15 (1): 90—4. PMID 11388751.
Gupta R, Bain BJ, Knight CL (2002). „Cytogenetic and molecular genetic abnormalities in systemic mastocytosis”. Acta Haematol. 107 (2): 123—8. PMID 11919394. doi:10.1159/000046642.
Valent P; Ghannadan M; Hauswirth AW; et al. (2003). „Signal transduction-associated and cell activation-linked antigens expressed in human mast cells”. Int. J. Hematol. 75 (4): 357—62. PMID 12041664. doi:10.1007/BF02982124.
Sandberg AA, Bridge JA (2002). „Updates on the cytogenetics and molecular genetics of bone and soft tissue tumors. gastrointestinal stromal tumors”. Cancer Genet. Cytogenet. 135 (1): 1—22. PMID 12072198. doi:10.1016/S0165-4608(02)00546-0.
Kitamura Y, Hirotab S (2005). „Kit as a human oncogenic tyrosine kinase”. Cell. Mol. Life Sci. 61 (23): 2924—31. PMID 15583854. doi:10.1007/s00018-004-4273-y.
Larizza L, Magnani I, Beghini A (2005). „The Kasumi-1 cell line: a t(8;21)-kit mutant model for acute myeloid leukemia”. Leuk. Lymphoma. 46 (2): 247—55. PMID 15621809. doi:10.1080/10428190400007565.
Miettinen M, Lasota J (2006). „KIT (CD117): a review on expression in normal and neoplastic tissues, and mutations and their clinicopathologic correlation”. Appl. Immunohistochem. Mol. Morphol. 13 (3): 205—20. PMID 16082245.
Lasota J, Miettinen M (2007). „KIT and PDGFRA mutations in gastrointestinal stromal tumors (GISTs)”. Semin Diagn Pathol. 23 (2): 91—102. PMID 17193822. doi:10.1053/j.semdp.2006.08.006.
Patnaik MM, Tefferi A, Pardanani A (2007). „Kit: molecule of interest for the diagnosis and treatment of mastocytosis and other neoplastic disorders”. Current cancer drug targets. 7 (5): 492—503. PMID 17691909. doi:10.2174/156800907781386614.
Giebel LB, Strunk KM, Holmes SA, Spritz RA (1992). „Organization and nucleotide sequence of the human KIT (mast/stem cell growth factor receptor) proto-oncogene”. Oncogene. 7 (11): 2207—17. PMID 1279499.
Spritz RA, Droetto S, Fukushima Y (1992). „Deletion of the KIT and PDGFRA genes in a patient with piebaldism”. Am. J. Med. Genet. 44 (4): 492—5. PMID 1279971. doi:10.1002/ajmg.1320440422.
Spritz RA, Giebel LB, Holmes SA (1992). „Dominant negative and loss of function mutations of the c-kit (mast/stem cell growth factor receptor) proto-oncogene in human piebaldism”. Am. J. Hum. Genet. 50 (2): 261—9. PMC 1682440 . PMID 1370874.
Duronio V; Welham MJ; Abraham S; et al. (1992). „p21ras activation via hemopoietin receptors and c-kit requires tyrosine kinase activity but not tyrosine phosphorylation of p21ras GTPase-activating protein”. Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1587—91. PMC 48497 . PMID 1371879. doi:10.1073/pnas.89.5.1587.
André C; Martin E; Cornu F; et al. (1992). „Genomic organization of the human c-kit gene: evolution of the receptor tyrosine kinase subclass III”. Oncogene. 7 (4): 685—91. PMID 1373482.
Lev S, Yarden Y, Givol D (1992). „A recombinant ectodomain of the receptor for the stem cell factor (SCF) retains ligand-induced receptor dimerization and antagonizes SCF-stimulated cellular responses”. J. Biol. Chem. 267 (15): 10866—73. PMID 1375232.
Fleischman RA (1992). „Human piebald trait resulting from a dominant negative mutant allele of the c-kit membrane receptor gene”. J. Clin. Invest. 89 (6): 1713—7. PMC 295855 . PMID 1376329. doi:10.1172/JCI115772.
Vandenbark GR; deCastro CM; Taylor H; et al. (1992). „Cloning and structural analysis of the human c-kit gene”. Oncogene. 7 (7): 1259—66. PMID 1377810.
Alai M; Mui AL; Cutler RL; et al. (1992). „Steel factor stimulates the tyrosine phosphorylation of the proto-oncogene product, p95vav, in human hemopoietic cells”. J. Biol. Chem. 267 (25): 18021—5. PMID 1381360.
Ashman LK; Cambareri AC; To LB; et al. (1991). „Expression of the YB5.B8 antigen (c-kit proto-oncogene product) in normal human bone marrow”. Blood. 78 (1): 30—7. PMID 1712644.
Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Vidi još

Citokinski receptor

Spoljašnje veze

Proto-Oncogene+Proteins+c-kit на US National Library of Medicine Medical Subject Headings (MeSH)
C-kit receptor

[pmid9027509-1] Andre C, Hampe A, Lachaume P, Martin E, Wang XP, Manus V, Hu WX, Galibert F (1997). „Sequence analysis of two genomic regions containing the KIT and the FMS receptor tyrosine kinase genes”. Genomics. 39 (2): 216—26. PMID 9027509. doi:10.1006/geno.1996.4482.

[entrez-2] „Entrez Gene: KIT v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog”.

[pmid2448137-3] Yarden Y, Kuang WJ, Yang-Feng T, Coussens L, Munemitsu S, Dull TJ, Chen E, Schlessinger J, Francke U, Ullrich A (1987). „Human proto-oncogene c-kit: a new cell surface receptor tyrosine kinase for an unidentified ligand”. EMBO J. 6 (11): 3341—51. PMC 553789 . PMID 2448137.

[pmid12444928-4] Wollberg P, Lennartsson J, Gottfridsson E, Yoshimura A, Rönnstrand L (2003). „The adapter protein APS associates with the multifunctional docking sites Tyr-568 and Tyr-936 in c-Kit”. Biochem. J. 370 (Pt 3): 1033—8. PMC 1223215 . PMID 12444928. doi:10.1042/BJ20020716.

[pmid8757502-5] Hallek M, Danhauser-Riedl S, Herbst R, Warmuth M, Winkler A, Kolb HJ, Druker B, Griffin JD, Emmerich B, Ullrich A (1996). „Interaction of the receptor tyrosine kinase p145c-kit with the p210bcr/abl kinase in myeloid cells”. Br. J. Haematol. 94 (1): 5—16. PMID 8757502. doi:10.1046/j.1365-2141.1996.6102053.x.

[pmid12036870-6] а ^б ^в Anzai N, Lee Y, Youn BS, Fukuda S, Kim YJ, Mantel C, Akashi M, Broxmeyer HE (2002). „C-kit associated with the transmembrane 4 superfamily proteins constitutes a functionally distinct subunit in human hematopoietic progenitors”. Blood. 99 (12): 4413—21. PMID 12036870. doi:10.1182/blood.V99.12.4413.

[pmid12878163-7] а ^б Lennartsson J, Wernstedt C, Engström U, Hellman U, Rönnstrand L (2003). „Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk”. Exp. Cell Res. 288 (1): 110—8. PMID 12878163. doi:10.1016/S0014-4827(03)00206-4.

[pmid11071635-8] а ^б van Dijk TB, van Den Akker E, Amelsvoort MP, Mano H, Löwenberg B, von Lindern M (2000). „Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells”. Blood. 96 (10): 3406—13. PMID 11071635.

[pmid9092574-9] Sattler M, Salgia R, Shrikhande G, Verma S, Pisick E, Prasad KV, Griffin JD (1997). „Steel factor induces tyrosine phosphorylation of CRKL and binding of CRKL to a complex containing c-kit, phosphatidylinositol 3-kinase, and p120(CBL)”. J. Biol. Chem. 272 (15): 10248—53. PMID 9092574. doi:10.1074/jbc.272.15.10248.

[pmid11825908-10] а ^б Liang X, Wisniewski D, Strife A, Shivakrupa, Clarkson B, Resh MD (2002). „Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling”. J. Biol. Chem. 277 (16): 13732—8. PMID 11825908. doi:10.1074/jbc.M200277200.

[pmid20117079-11] а ^б Voisset E, Lopez S, Chaix A, Vita M, George C, Dubreuil P, De Sepulveda P (2010). „FES kinase participates in KIT-ligand induced chemotaxis”. Biochem. Biophys. Res. Commun. 393 (1): 174—8. PMID 20117079. doi:10.1016/j.bbrc.2010.01.116.

[pmid11809791-12] Jahn T, Seipel P, Urschel S, Peschel C, Duyster J (2002). „Role for the adaptor protein Grb10 in the activation of Akt”. Mol. Cell. Biol. 22 (4): 979—91. PMC 134632 . PMID 11809791. doi:10.1128/MCB.22.4.979-991.2002.

[pmid10022833-13] а ^б ^в De Sepulveda P, Okkenhaug K, Rose JL, Hawley RG, Dubreuil P, Rottapel R (1999). „Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation”. EMBO J. 18 (4): 904—15. PMC 1171183 . PMID 10022833. doi:10.1093/emboj/18.4.904.

[pmid10377264-14] Thömmes K, Lennartsson J, Carlberg M, Rönnstrand L (1999). „Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor”. Biochem. J. 341 ( Pt 1): 211—6. PMC 1220349 . PMID 10377264. doi:10.1042/0264-6021:3410211.

[pmid8647802-15] Feng GS, Ouyang YB, Hu DP, Shi ZQ, Gentz R, Ni J (1996). „Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway”. J. Biol. Chem. 271 (21): 12129—32. PMID 8647802. doi:10.1074/jbc.271.21.12129.

[pmid1375232-16] Lev S, Yarden Y, Givol D (1992). „A recombinant ectodomain of the receptor for the stem cell factor (SCF) retains ligand-induced receptor dimerization and antagonizes SCF-stimulated cellular responses”. J. Biol. Chem. 267 (15): 10866—73. PMID 1375232.

[pmid7680037-17] Blechman JM, Lev S, Brizzi MF, Leitner O, Pegoraro L, Givol D, Yarden Y (1993). „Soluble c-kit proteins and antireceptor monoclonal antibodies confine the binding site of the stem cell factor”. J. Biol. Chem. 268 (6): 4399—406. PMID 7680037.

[pmid18588518-18] Gueller S, Gery S, Nowak V, Liu L, Serve H, Koeffler HP (2008). „Adaptor protein Lnk associates with Tyr(568) in c-Kit”. Biochem. J. 415 (2): 241—5. PMID 18588518. doi:10.1042/BJ20080102.

[pmid9341198-19] Linnekin D, DeBerry CS, Mou S (1997). „Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells”. J. Biol. Chem. 272 (43): 27450—5. PMID 9341198. doi:10.1074/jbc.272.43.27450.

[pmid7536744-20] Jhun BH, Rivnay B, Price D, Avraham H (1995). „The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit”. J. Biol. Chem. 270 (16): 9661—6. PMID 7536744. doi:10.1074/jbc.270.16.9661.

[pmid9038210-21] Price DJ, Rivnay B, Fu Y, Jiang S, Avraham S, Avraham H (1997). „Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes”. J. Biol. Chem. 272 (9): 5915—20. PMID 9038210. doi:10.1074/jbc.272.9.5915.

[pmid11018522-22] Mancini A, Koch A, Stefan M, Niemann H, Tamura T (2000). „The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity”. FEBS Lett. 482 (1-2): 54—8. PMID 11018522. doi:10.1016/S0014-5793(00)02036-6.

[pmid7509796-23] Serve H, Hsu YC, Besmer P (1994). „Tyrosine residue 719 of the c-kit receptor is essential for binding of the P85 subunit of phosphatidylinositol (PI) 3-kinase and for c-kit-associated PI 3-kinase activity in COS-1 cells”. J. Biol. Chem. 269 (8): 6026—30. PMID 7509796.

[pmid7523381-24] Tauchi T, Feng GS, Marshall MS, Shen R, Mantel C, Pawson T, Broxmeyer HE (1994). „The ubiquitously expressed Syp phosphatase interacts with c-kit and Grb2 in hematopoietic cells”. J. Biol. Chem. 269 (40): 25206—11. PMID 7523381.

[pmid9528781-25] а ^б Kozlowski M, Larose L, Lee F, Le DM, Rottapel R, Siminovitch KA (1998). „SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain”. Mol. Cell. Biol. 18 (4): 2089—99. PMC 121439 . PMID 9528781.

[pmid7684496-26] Yi T, Ihle JN (1993). „Association of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligand”. Mol. Cell. Biol. 13 (6): 3350—8. PMC 359793 . PMID 7684496.

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[pmid14707129-28] Bayle J, Letard S, Frank R, Dubreuil P, De Sepulveda P (2004). „Suppressor of cytokine signaling 6 associates with KIT and regulates KIT receptor signaling”. J. Biol. Chem. 279 (13): 12249—59. PMID 14707129. doi:10.1074/jbc.M313381200.

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п р у Proteini: klasteri diferencijacije (vidi isto spisak ljudskih klastera diferencijacije)
1-50	CD1 (a-c, 1A, 1D, 1E) • CD2 • CD3 (γ, δ, ε) • CD4 • CD5 • CD6 • CD7 • CD8 (a) • CD9 • CD10 • CD11 (a, b, c) • CD13 • CD14 • CD15 • CD16 (A, B) • CD18 • CD19 • CD20 • CD21 • CD22 • CD23 • CD24 • CD25 • CD26 • CD27 • CD28 • CD29 • CD30 • CD31 • CD32 (A, B) • CD33 • CD34 • CD35 • CD36 • CD37 • CD38 • CD39 • CD40 • CD41 • CD42 (a, b, c, d) • CD43 • CD44 • CD45 • CD46 • CD47 • CD48 • CD49 (a, b, c, d, e, f) • CD50
51-100	CD51 • CD52 • CD53 • CD54 • CD55 • CD56 • CD57 • CD58 • CD59 • CD61 • CD62 (E, L, P) • CD63 • CD64 (A, B, C) • CD66 (a, b, c, d, e, f) • CD68 • CD69 • CD70 • CD71 • CD72 • CD73 • CD74 • CD78 • CD79 (a, b) • CD80 • CD81 • CD82 • CD83 • CD84 • CD85 (a, d, e, h, j, k) • CD86 • CD87 • CD88 • CD89 • CD90 • CD91- CD92 • CD93 • CD94 • CD95 • CD96 • CD97 • CD98 • CD99 • CD100
101-150	CD101 • CD102 • CD103 • CD104 • CD105 • CD106 • CD107 (a, b) • CD108 • CD109 • CD110 • CD111 • CD112 • CD113 • CD114 • CD115 • CD116 • CD117 • CD118 • CD119 • CD120 (a, b) • CD121 (a, b) • CD122 • CD123 • CD124 • CD125 • CD126 • CD127 • CD129 • CD130 • CD131 • CD132 • CD133 • CD134 • CD135 • CD136 • CD137 • CD138 • CD140b • CD141 • CD142 • CD143 • CD144 • CD146 • CD147 • CD148 • CD150
151-200	CD151 • CD152 • CD153 • CD154 • CD155 • CD156 (a, b, c) • CD157 • CD158 (a, d, e, i, k) • CD159 (a, c) • CD160 • CD161 • CD162 • CD163 • CD164 • CD166 • CD167 (a, b) • CD168 • CD169 • CD170 • CD171 • CD172 (a, b, g) • CD174 • CD177 • CD178 • CD179 (a, b) • CD181 • CD182 • CD183 • CD184 • CD185 • CD186 • CD191 • CD192 • CD193 • CD194 • CD195 • CD196 • CD197 • CDw198 • CDw199 • CD200
201-250	CD201 • CD202b • CD204 • CD205 • CD206 • CD207 • CD208 • CD209 • CDw210 (a, b) • CD212 • CD213a (1, 2) • CD217 • CD218 (a, b) • CD220 • CD221 • CD222 • CD223 • CD224 • CD225 • CD226 • CD227 • CD228 • CD229 • CD230 • CD233 • CD234 • CD235 (a, b) • CD236 • CD238 • CD239 • CD240CE • CD241 • CD243 • CD244 • CD246 • CD247- CD248 • CD249
251-300	CD252 • CD253 • CD254 • CD256 • CD257 • CD258 • CD261 • CD262 • CD264 • CD265 • CD266 • CD267 • CD268 • CD269 • CD271 • CD272 • CD273 • CD274 • CD275 • CD276 • CD278 • CD279 • CD280 • CD281 • CD282 • CD283 • CD284 • CD286 • CD288 • CD289 • CD290 • CD292 • CDw293 • CD294 • CD295 • CD297 • CD298 • CD299
301-350	CD300A • CD301 • CD302 • CD303 • CD304 • CD305 • CD306 • CD307 • CD309 • CD312 • CD314 • CD315 • CD316 • CD317 • CD318 • CD320 • CD321 • CD322 • CD324 • CD325 • CD326 • CD328 • CD329 • CD331 • CD332 • CD333 • CD334 • CD335 • CD336 • CD337 • CD338 • CD339 • CD340 • CD344 • CD349 • CD350

п р у Receptori: Receptori faktora rasta
Nervni faktori rasta	niski afinitet/p75 – visok afinitet Trk (TrkA, TrkB, TrkC) – Cilijarni neurotrofni faktor
Somatomedin	Insulinu-sličan faktor rasta 1 – Insulinu-sličan faktor rasta 2
CSF	Stem ćelijski faktor – Eritropoietin
TGF put	TGF-beta (1, 2) – Aktivin (1, 2) – Bone morfogenetski protein (1, 2)
Drugi	Hepatocitni faktor rasta – ErbB/Epidermalni faktor rasta – Fibroblast faktor rasta (1, 2, 3, 4) – Trombocit-izvedeni faktor rasta (A, B) – VEGF (1, 2, 3)
vidi isto Faktori rasta

п р у Enzimi
Teme	Aktivno mesto Alosterna regulacija Mesto vezivanja Katalitički perfektan enzim Koenzim Kofaktor Kooperativnost EC broj Enzimska kataliza Inhibicija enzima Enzimska kinetika Lajnviver—Berkov dijagram Mihaelis—Mentenina kinetika Spisak enzima
Tipovi	EC1 Oksidoreduktaze /spisak EC2 Transferaze /spisak EC3 Hidrolaze /spisak EC4 Lijaze /spisak EC5 Izomeraze /spisak EC6 Ligaze /spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6