KIT_HUMAN - dbPTM
KIT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIT_HUMAN
UniProt AC P10721
Protein Name Mast/stem cell growth factor receptor Kit
Gene Name KIT
Organism Homo sapiens (Human).
Sequence Length 976
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Cell membrane
Single-pass type I membrane protein.
Isoform 3: Cytoplasm. Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal region of th
Protein Description Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1..
Protein Sequence MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWEDYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDSSAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSVGSTASSSQPLLVHDDV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
130N-linked_GlycosylationSLYGKEDNDTLVRCP
HHCCCCCCCCEEECC		45.3016335952
145N-linked_GlycosylationLTDPEVTNYSLKGCQ
CCCHHHHCCCCCCCC		29.58UniProtKB CARBOHYD
147PhosphorylationDPEVTNYSLKGCQGK
CHHHHCCCCCCCCCC		26.1924719451
173SumoylationPKAGIMIKSVKRAYH
CCCCEEHHHHHHHHH		31.64-
173SumoylationPKAGIMIKSVKRAYH
CCCCEEHHHHHHHHH		31.64-
215PhosphorylationFKAVPVVSVSKASYL
CCCCCEEEEEHHEEE		22.40-
217PhosphorylationAVPVVSVSKASYLLR
CCCEEEEEHHEEEEC		18.26-
220PhosphorylationVVSVSKASYLLREGE
EEEEEHHEEEECCCC		21.7624719451
232PhosphorylationEGEEFTVTCTIKDVS
CCCCEEEEEEEEECC		10.81-
240PhosphorylationCTIKDVSSSVYSTWK
EEEEECCHHHHHEEE		24.54-
241PhosphorylationTIKDVSSSVYSTWKR
EEEECCHHHHHEEEC		19.98-
283N-linked_GlycosylationTISSARVNDSGVFMC
EEEECEECCCEEEEE		31.9817662946
293N-linked_GlycosylationGVFMCYANNTFGSAN
EEEEEEECCCCCCCC		22.9217662946
300N-linked_GlycosylationNNTFGSANVTTTLEV
CCCCCCCCEEEEEEE		33.1117662946
320N-linked_GlycosylationINIFPMINTTVFVND
EEEEEEECEEEEEEC		24.3617662946
352N-linked_GlycosylationHQQWIYMNRTFTDKW
HCCEEEEECCCCCCC		23.9117662946
354PhosphorylationQWIYMNRTFTDKWED
CEEEEECCCCCCCCC		26.3618491316
362PhosphorylationFTDKWEDYPKSENES
CCCCCCCCCCCCCCC		10.8818491316
367N-linked_GlycosylationEDYPKSENESNIRYV
CCCCCCCCCCCEEEE		66.1517662946
390PhosphorylationKGTEGGTYTFLVSNS
ECCCCEEEEEEEECC		9.9619053533
391PhosphorylationGTEGGTYTFLVSNSD
CCCCEEEEEEEECCC		15.4419053533
463N-linked_GlycosylationPVDVQTLNSSGPPFG
CEEEEECCCCCCCCC		37.20UniProtKB CARBOHYD
486N-linked_GlycosylationDSSAFKHNGTVECKA
CCCHHCCCCEEEEEE		48.71UniProtKB CARBOHYD
488PhosphorylationSAFKHNGTVECKAYN
CHHCCCCEEEEEEEC		20.60-
494PhosphorylationGTVECKAYNDVGKTS
CEEEEEEECCCCCEE		9.44-
545PhosphorylationIIVMILTYKYLQKPM
HHHHHHHHHHHCCCC		8.329528781
547PhosphorylationVMILTYKYLQKPMYE
HHHHHHHHHCCCCEE		12.179528781
553PhosphorylationKYLQKPMYEVQWKVV
HHHCCCCEEEEEEEE		22.8323401153
568PhosphorylationEEINGNNYVYIDPTQ
EEECCCCEEEECCCC		9.9123401153
570DephosphorylationINGNNYVYIDPTQLP
ECCCCEEEECCCCCC		6.839528781
570PhosphorylationINGNNYVYIDPTQLP
ECCCCEEEECCCCCC		6.8323401153
574PhosphorylationNYVYIDPTQLPYDHK
CEEEECCCCCCCCCC		38.7023401153
578PhosphorylationIDPTQLPYDHKWEFP
ECCCCCCCCCCCCCC		38.9923401153
607PhosphorylationFGKVVEATAYGLIKS
CHHHHHHHHHHCCCC		13.6030174305
609PhosphorylationKVVEATAYGLIKSDA
HHHHHHHHHCCCCCH		14.2225884760
614PhosphorylationTAYGLIKSDAAMTVA
HHHHCCCCCHHHHHH		26.0330174305
619PhosphorylationIKSDAAMTVAVKMLK
CCCCHHHHHHHHHHC		10.6930174305
628PhosphorylationAVKMLKPSAHLTERE
HHHHHCCCCCCHHHH		27.0830174305
632PhosphorylationLKPSAHLTEREALMS
HCCCCCCHHHHHHHH		24.1130174305
642UbiquitinationEALMSELKVLSYLGN
HHHHHHHHHHHHHCC		36.76-
703PhosphorylationDHAEAALYKNLLHSK
HHHHHHHHHHHHHCC		7.9726356563
718PhosphorylationESSCSDSTNEYMDMK
CCCCCCCCCHHCCCC		36.7419060867
721PhosphorylationCSDSTNEYMDMKPGV
CCCCCCHHCCCCCCC		10.6523401153
729PhosphorylationMDMKPGVSYVVPTKA
CCCCCCCEEEECCCC		20.3725884760
730PhosphorylationDMKPGVSYVVPTKAD
CCCCCCEEEECCCCC		11.767509796
735UbiquitinationVSYVVPTKADKRRSV
CEEEECCCCCCCCCE		48.82-
738UbiquitinationVVPTKADKRRSVRIG
EECCCCCCCCCEECC		55.35-
741PhosphorylationTKADKRRSVRIGSYI
CCCCCCCCEECCCEE		21.5622817900
746PhosphorylationRRSVRIGSYIERDVT
CCCEECCCEEECCCC		22.1423401153
747PhosphorylationRSVRIGSYIERDVTP
CCEECCCEEECCCCC		11.117509796
801PhosphorylationAARNILLTHGRITKI
HHHHHHHHCCCHHEE		20.88-
821PhosphorylationARDIKNDSNYVVKGN
CEECCCCCCCEEECC		39.1822817900
823PhosphorylationDIKNDSNYVVKGNAR
ECCCCCCCEEECCCC		15.5723401153
891PhosphorylationKEGFRMLSPEHAPAE
HHHHCCCCCCCCCHH		20.9222817900
900PhosphorylationEHAPAEMYDIMKTCW
CCCCHHHHHHHHHHC		8.2020147452
929PhosphorylationQLIEKQISESTNHIY
HHHHHHHHHCCCHHH		24.0128176486
931PhosphorylationIEKQISESTNHIYSN
HHHHHHHCCCHHHHH		27.9326356563
932PhosphorylationEKQISESTNHIYSNL
HHHHHHCCCHHHHHC		27.1128176486
936PhosphorylationSESTNHIYSNLANCS
HHCCCHHHHHCCCCC		5.5121082442
937PhosphorylationESTNHIYSNLANCSP
HCCCHHHHHCCCCCC		25.4326356563
943PhosphorylationYSNLANCSPNRQKPV
HHHCCCCCCCCCCCC		25.6423401153
954PhosphorylationQKPVVDHSVRINSVG
CCCCCCCEEEECCCC		14.5024702127
959PhosphorylationDHSVRINSVGSTASS
CCEEEECCCCCCCCC		26.0323401153
962PhosphorylationVRINSVGSTASSSQP
EEECCCCCCCCCCCC		20.7423401153
963PhosphorylationRINSVGSTASSSQPL
EECCCCCCCCCCCCE		25.3227732954
965PhosphorylationNSVGSTASSSQPLLV
CCCCCCCCCCCCEEE		30.5228450419
966PhosphorylationSVGSTASSSQPLLVH
CCCCCCCCCCCEEEE		30.4527732954
967PhosphorylationVGSTASSSQPLLVHD
CCCCCCCCCCEEEEC		33.0728450419
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
547YPhosphorylationKinaseKITP10721
PSP
553YPhosphorylationKinaseKITP10721
PSP
568YPhosphorylationKinaseKITP10721
PSP
570YPhosphorylationKinaseKITP10721
PSP
703YPhosphorylationKinaseKITP10721
PSP
721YPhosphorylationKinaseKITP10721
PSP
741SPhosphorylationKinaseKPCAP17252
PhosphoELM
746SPhosphorylationKinaseKPCAP17252
PhosphoELM
821SPhosphorylationKinasePRKCAP17252
GPS
823YPhosphorylationKinaseKITP10721
PSP
900YPhosphorylationKinaseSRCP05480
PSP
900YPhosphorylationKinaseSRC-FAMILY-GPS
900YPhosphorylationKinaseSRC_GROUP-PhosphoELM
900YPhosphorylationKinaseSRC64-PhosphoELM
936YPhosphorylationKinaseKITP10721
PSP
959SPhosphorylationKinasePRKCAP17252
GPS
-KUbiquitinationE3 ubiquitin ligaseSOCS6O14544
PMID:21030588
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:16780420
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIT_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of KIT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD9_HUMANCD9physical
12036870
CD63_HUMANCD63physical
12036870
CD81_HUMANCD81physical
12036870
GRB2_HUMANGRB2physical
10022833
P85A_HUMANPIK3R1physical
10022833
P85B_HUMANPIK3R2physical
10022833
SOCS1_HUMANSOCS1physical
10022833
CRKL_HUMANCRKLphysical
11071635
P85A_HUMANPIK3R1physical
11071635
PLCG1_HUMANPLCG1physical
11071635
SHIP1_HUMANINPP5Dphysical
11071635
YES_HUMANYES1physical
11071635
STAT1_HUMANSTAT1physical
9355737
CLH1_HUMANCLTCphysical
10477727
TEC_HUMANTECphysical
7526158
JAK2_HUMANJAK2physical
7527392
P85A_HUMANPIK3R1physical
7509796
SCF_HUMANKITLGphysical
1375232
GRB10_HUMANGRB10physical
11809791
PTN6_HUMANPTPN6physical
9528781
PTN11_HUMANPTPN11physical
9528781
MPDZ_HUMANMPDZphysical
11018522
MATK_HUMANMATKphysical
9038210
LYN_HUMANLYNphysical
9341198
SCF_HUMANKITLGphysical
7680037
PTPRO_HUMANPTPROphysical
10397721
GRB2_HUMANGRB2physical
17904548
CBL_HUMANCBLphysical
15315962
P85A_HUMANPIK3R1physical
17452978
GRB2_HUMANGRB2physical
17452978
SH2B2_MOUSESh2b2physical
12444928
P85A_HUMANPIK3R1physical
9233773
CRK_HUMANCRKphysical
9233773
IL7RA_HUMANIL7Rphysical
17554063
JAK3_HUMANJAK3physical
17554063
STA5B_HUMANSTAT5Bphysical
17554063
PK3CG_HUMANPIK3CGphysical
25241761
BCR_HUMANBCRphysical
25241761
CSF2R_HUMANCSF2RAphysical
25241761
P85A_HUMANPIK3R1physical
25241761
PLCG1_HUMANPLCG1physical
25241761
CBL_HUMANCBLphysical
25737303
ENPL_HUMANHSP90B1physical
25737303
KS6B1_HUMANRPS6KB1genetic
28319113
P53_HUMANTP53genetic
28319113
SMO_HUMANSMOgenetic
28319113
ILKAP_HUMANILKAPphysical
28065597
PTN20_HUMANPTPN20Bphysical
28065597
STYX_HUMANSTYXphysical
28065597
PK3CA_HUMANPIK3CAphysical
7691885
KIT_HUMANKITphysical
9949175
Drug and Disease Associations
Kegg Disease
H00003 Acute myeloid leukemia (AML)
H00023 Testicular cancer
H00170 Piebaldism
OMIM Disease
172800Piebald trait (PBT)
606764Gastrointestinal stromal tumor (GIST)
273300Testicular germ cell tumor (TGCT)
601626Leukemia, acute myelogenous (AML)
Kegg Drug
D01441 Imatinib mesilate (JAN); Imatinib mesylate (USAN); Gleevec (TN); Glivec (TN)
D03218 Axitinib (JAN/USAN); Inlyta (TN)
D03658 Dasatinib (INN)
D05029 Midostaurin (USAN/INN)
D05380 Pazopanib hydrochloride (JAN/USAN); Votrient (TN)
D05819 Semaxanib (USAN/INN)
D06005 Tandutinib (USAN/INN)
D06272 Sorafenib tosilate (JAN); Sorafenib tosylate (USAN); Nexavar (TN)
D06285 Vatalanib (USAN/INN)
D06402 Sunitinib malate (JAN/USAN); Sutent (TN)
D06413 Nilotinib hydrochloride hydrate (JAN); Tasigna (TN)
D06414 Dasatinib hydrate (JAN); Dasatinib (USAN); Sprycel (TN)
D06678 Motesanib; AMG 706
D08066 Imatinib (INN); Glamox (TN)
D08503 Toceranib (USAN)
D08524 Sorafenib (USAN/INN)
D08544 Toceranib phosphate (USAN)
D08552 Sunitinib (INN)
D08881 Cediranib (USAN/INN)
D08883 Cediranib maleate (JAN/USAN)
D08947 Motesanib phosphate (JAN); Motesanib diphosphate (USAN)
D08953 Nilotinib (USAN/INN)
D09864 Amuvatinib (USAN/INN)
D09865 Amuvatinib hydrochloride (USAN)
D10062 Cabozantinib (USAN)
D10095 Cabozantinib s-malate (USAN); Cometriq (TN)
D10229 Masitinib (INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIT_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural basis for activation of the receptor tyrosine kinase KITby stem cell factor.";
Yuzawa S., Opatowsky Y., Zhang Z., Mandiyan V., Lax I.,Schlessinger J.;
Cell 130:323-334(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-519 IN COMPLEX WITHKITLG/SCF, INTERACTION WITH KITLG/SCF, SUBUNIT, DISULFIDE BONDS,CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF ARG-381 ANDGLU-386, AND GLYCOSYLATION AT ASN-130; ASN-283; ASN-293; ASN-300;ASN-320; ASN-352 AND ASN-367.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-959, AND MASSSPECTROMETRY.
"Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk.";
Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L.;
Exp. Cell Res. 288:110-118(2003).
Cited for: PHOSPHORYLATION AT SER-891 AND TYR-900, PARTIAL PROTEIN SEQUENCE,INTERACTION WITH CRK AND PIK3R1, FUNCTION IN PHOSPHORYLATION OF CRK;AKT1 AND MAP KINASES, AND MASS SPECTROMETRY.
"Identification of the major phosphorylation sites for protein kinaseC in kit/stem cell factor receptor in vitro and in intact cells.";
Blume-Jensen P., Wernstedt C., Heldin C.H., Ronnstrand L.;
J. Biol. Chem. 270:14192-14200(1995).
Cited for: PHOSPHORYLATION AT SER-741; SER-746; SER-821 AND SER-959, ENZYMEREGULATION, PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS OF SER-741 ANDSER-746.
"Structural basis for c-KIT inhibition by the suppressor of cytokinesignaling 6 (SOCS6) ubiquitin ligase.";
Zadjali F., Pike A.C., Vesterlund M., Sun J., Wu C., Li S.S.,Ronnstrand L., Knapp S., Bullock A.N., Flores-Morales A.;
J. Biol. Chem. 286:480-490(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 564-574 IN COMPLEX WITHSOCS6, AND PHOSPHORYLATION AT TYR-568.
"Structure of a c-kit product complex reveals the basis for kinasetransactivation.";
Mol C.D., Lim K.B., Sridhar V., Zou H., Chien E.Y., Sang B.C.,Nowakowski J., Kassel D.B., Cronin C.N., McRee D.E.;
J. Biol. Chem. 278:31461-31464(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 549-931 IN COMPLEX WITH ADPAND MAGNESIUM IONS, SUBUNIT, AUTOPHOSPHORYLATION AT TYR-568 ANDTYR-570, AND MASS SPECTROMETRY.
"Function of activation loop tyrosine phosphorylation in the mechanismof c-Kit auto-activation and its implication in sunitinibresistance.";
DiNitto J.P., Deshmukh G.D., Zhang Y., Jacques S.L., Coli R.,Worrall J.W., Diehl W., English J.M., Wu J.C.;
J. Biochem. 147:601-609(2010).
Cited for: PHOSPHORYLATION AT TYR-547; TYR-553; TYR-703; TYR-721; TYR-730;TYR-823 AND TYR-900, MASS SPECTROMETRY, MUTAGENESIS OF TYR-823, ANDCHARACTERIZATION OF VARIANT HIS-816.
"The D816V mutation of c-Kit circumvents a requirement for Src familykinases in c-Kit signal transduction.";
Sun J., Pedersen M., Ronnstrand L.;
J. Biol. Chem. 284:11039-11047(2009).
Cited for: FUNCTION IN ACTIVATION OF SIGNALING PATHWAYS AND CELL SURVIVAL,FUNCTION IN PHOSPHORYLATION OF CBL, PHOSPHORYLATION AT TYR-568;TYR-703; TYR-721 AND TYR-936, UBIQUITINATION, SUBCELLULAR LOCATION,AND CHARACTERIZATION OF VARIANT VAL-816.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-936, AND MASSSPECTROMETRY.
"Identification of Tyr-703 and Tyr-936 as the primary associationsites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor.";
Thommes K., Lennartsson J., Carlberg M., Ronnstrand L.;
Biochem. J. 341:211-216(1999).
Cited for: INTERACTION WITH GRB2 AND GRB7, PARTIAL PROTEIN SEQUENCE,AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT TYR-703 AND TYR-936.
"Direct association of Csk homologous kinase (CHK) with thediphosphorylated site Tyr568/570 of the activated c-KIT inmegakaryocytes.";
Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.;
J. Biol. Chem. 272:5915-5920(1997).
Cited for: INTERACTION WITH PIK3R1; MATK/CHK; FYN AND SHC1, AND PHOSPHORYLATIONAT TYR-568; TYR-570 AND TYR-721.

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