KIT_MOUSE - dbPTM
KIT_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIT_MOUSE
UniProt AC P05532
Protein Name Mast/stem cell growth factor receptor Kit
Gene Name Kit
Organism Mus musculus (Mouse).
Sequence Length 979
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 MRGARGAWDLLCVLLVLLRGQTATSQPSASPGEPSPPSIHPAQSELIVEAGDTLSLTCIDPDFVRWTFKTYFNEMVENKKNEWIQEKAEATRTGTYTCSNSNGLTSSIYVFVRDPAKLFLVGLPLFGKEDSDALVRCPLTDPQVSNYSLIECDGKSLPTDLTFVPNPKAGITIKNVKRAYHRLCVRCAAQRDGTWLHSDKFTLKVRAAIKAIPVVSVPETSHLLKKGDTFTVVCTIKDVSTSVNSMWLKMNPQPQHIAQVKHNSWHRGDFNYERQETLTISSARVDDSGVFMCYANNTFGSANVTTTLKVVEKGFINISPVKNTTVFVTDGENVDLVVEYEAYPKPEHQQWIYMNRTSANKGKDYVKSDNKSNIRYVNQLRLTRLKGTEGGTYTFLVSNSDASASVTFNVYVNTKPEILTYDRLINGMLQCVAEGFPEPTIDWYFCTGAEQRCTTPVSPVDVQVQNVSVSPFGKLVVQSSIDSSVFRHNGTVECKASNDVGKSSAFFNFAFKGNNKEQIQAHTLFTPLLIGFVVAAGAMGIIVMVLTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSFIFSKQEEQAEAALYKNLLHSTEPSCDSSNEYMDMKPGVSYVVPTKTDKRRSARIDSYIERDVTPAIMEDDELALDLDDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFSCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMVSPEHAPAEMYDVMKTCWDADPLKRPTFKQVVQLIEKQISDSTKHIYSNLANCNPNPENPVVVDHSVRVNSVGSSASSTQPLLVHEDA
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
146N-linked_GlycosylationLTDPQVSNYSLIECD
CCCCCCCCCEEEEEC		31.40-
277PhosphorylationFNYERQETLTISSAR
CCCCEEEEEEEEEEE		22.3621183079
282PhosphorylationQETLTISSARVDDSG
EEEEEEEEEEECCCC		19.0822817900
296N-linked_GlycosylationGVFMCYANNTFGSAN
CEEEEEECCCCCCCC		22.9217255936
303N-linked_GlycosylationNNTFGSANVTTTLKV
CCCCCCCCEEEEEEE		33.1117255936
323N-linked_GlycosylationINISPVKNTTVFVTD
EEEECCCCEEEEEEC		41.01-
355N-linked_GlycosylationHQQWIYMNRTSANKG
HCCEEEEECCCCCCC		27.40-
370N-linked_GlycosylationKDYVKSDNKSNIRYV
CCCCCCCCCCCEEEE		57.66-
466N-linked_GlycosylationPVDVQVQNVSVSPFG
CCEEEEEEEEECCCC		29.22-
489N-linked_GlycosylationDSSVFRHNGTVECKA
CCCCCCCCCEEEEEE		43.50-
550PhosphorylationVMVLTYKYLQKPMYE
HHHHCHHHHCCCCEE		12.17-
556PhosphorylationKYLQKPMYEVQWKVV
HHHCCCCEEEEEEEE		22.83-
567PhosphorylationWKVVEEINGNNYVYI
EEEEEEECCCCEEEE		50.88N.N.
569PhosphorylationVVEEINGNNYVYIDP
EEEEECCCCEEEECC		31.97N.N.
571PhosphorylationEEINGNNYVYIDPTQ
EEECCCCEEEECCCC		9.9118753636
573PhosphorylationINGNNYVYIDPTQLP
ECCCCEEEECCCCCC		6.8318753636
580UbiquitinationYIDPTQLPYDHKWEF
EECCCCCCCCCCCCC		23.7627667366
581PhosphorylationIDPTQLPYDHKWEFP
ECCCCCCCCCCCCCC		38.99-
592UbiquitinationWEFPRNRLSFGKTLG
CCCCCCCCCCCCCCC		5.9327667366
596UbiquitinationRNRLSFGKTLGAGAF
CCCCCCCCCCCCCCC		38.2727667366
605UbiquitinationLGAGAFGKVVEATAY
CCCCCCHHHHHHHHH		36.33-
612PhosphorylationKVVEATAYGLIKSDA
HHHHHHHHHCCCCCH		14.22-
691PhosphorylationFLRRKRDSFIFSKQE
HHHHCCCCCCCCCHH		25.0326643407
695PhosphorylationKRDSFIFSKQEEQAE
CCCCCCCCCHHHHHH		28.7227180971
696UbiquitinationRDSFIFSKQEEQAEA
CCCCCCCCHHHHHHH		51.48-
702PhosphorylationSKQEEQAEAALYKNL
CCHHHHHHHHHHHHH		33.88N.N.
706PhosphorylationEQAEAALYKNLLHST
HHHHHHHHHHHHHCC		7.97N.N.
716PhosphorylationLLHSTEPSCDSSNEY
HHHCCCCCCCCCCCC		25.0719060867
719PhosphorylationSTEPSCDSSNEYMDM
CCCCCCCCCCCCCCC		39.1112393643
720PhosphorylationTEPSCDSSNEYMDMK
CCCCCCCCCCCCCCC		22.0426643407
723PhosphorylationSCDSSNEYMDMKPGV
CCCCCCCCCCCCCCE		11.5812393643
731PhosphorylationMDMKPGVSYVVPTKT
CCCCCCEEEEECCCC		20.3726643407
732PhosphorylationDMKPGVSYVVPTKTD
CCCCCEEEEECCCCC		11.7611090054
743PhosphorylationTKTDKRRSARIDSYI
CCCCCCHHHHHHHHH		26.40-
748PhosphorylationRRSARIDSYIERDVT
CHHHHHHHHHHCCCC		26.1627180971
749PhosphorylationRSARIDSYIERDVTP
HHHHHHHHHHCCCCC		11.7629472430
812UbiquitinationGRITKICDFGLARDI
CCHHEECCCCCCEEC		44.0927667366
821PhosphorylationGLARDIRNDSNYVVK
CCCEECCCCCCCEEE		58.35N.N.
823PhosphorylationARDIRNDSNYVVKGN
CEECCCCCCCEEECC		33.3426643407
824UbiquitinationRDIRNDSNYVVKGNA
EECCCCCCCEEECCC		36.1627667366
825PhosphorylationDIRNDSNYVVKGNAR
ECCCCCCCEEECCCC		15.57N.N.
828UbiquitinationNDSNYVVKGNARLPV
CCCCCEEECCCCCCC		36.0827667366
886AcetylationSKFYKMIKEGFRMVS
HHHHHHHHHCCCCCC		48.577626361
893PhosphorylationKEGFRMVSPEHAPAE
HHCCCCCCCCCCCHH		18.41-
902PhosphorylationEHAPAEMYDVMKTCW
CCCCHHHHHHHHHHC		9.26-
906AcetylationAEMYDVMKTCWDADP
HHHHHHHHHHCCCCC		40.147626371
912UbiquitinationMKTCWDADPLKRPTF
HHHHCCCCCCCCCCH		46.7427667366
924UbiquitinationPTFKQVVQLIEKQIS
CCHHHHHHHHHHHCC		37.5527667366
928UbiquitinationQVVQLIEKQISDSTK
HHHHHHHHHCCCCHH		46.0327667366
934PhosphorylationEKQISDSTKHIYSNL
HHHCCCCHHHHHHHH		31.4712374739
938PhosphorylationSDSTKHIYSNLANCN
CCCHHHHHHHHHCCC		7.39N.N.
939PhosphorylationDSTKHIYSNLANCNP
CCHHHHHHHHHCCCC		25.43-
962PhosphorylationDHSVRVNSVGSSASS
ECCEEECCCCCCCCC		25.6227180971
965PhosphorylationVRVNSVGSSASSTQP
EEECCCCCCCCCCCC		22.1526643407
966PhosphorylationRVNSVGSSASSTQPL
EECCCCCCCCCCCCE		26.6626643407
968PhosphorylationNSVGSSASSTQPLLV
CCCCCCCCCCCCEEE		35.5526643407
969PhosphorylationSVGSSASSTQPLLVH
CCCCCCCCCCCEEEE		30.6726643407
970PhosphorylationVGSSASSTQPLLVHE
CCCCCCCCCCEEEEC		31.5426643407
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
743SPhosphorylationKinasePRKCAP20444
Uniprot
748SPhosphorylationKinasePRKCAP20444
Uniprot
934YPhosphorylationKinaseFYNP39688
PhosphoELM
938YPhosphorylationKinaseFYNP39688
GPS
-KUbiquitinationE3 ubiquitin ligaseCblP22682
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIT_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOCS6_MOUSESocs6physical
14707129
FIZ1_MOUSEFiz1physical
10679268
MATK_MOUSEMatkphysical
10679268
P85A_MOUSEPik3r1physical
10679268
GRB2_MOUSEGrb2physical
10679268
VAV_MOUSEVav1physical
10679268
FES_MOUSEFesphysical
10679268
SH2B1_MOUSESh2b1physical
10679268
PLK1_MOUSEPlk1physical
10679268
STAP1_MOUSEStap1physical
10679268
P85B_MOUSEPik3r2physical
22378847
P85A_MOUSEPik3r1physical
22378847
PK3CA_MOUSEPik3caphysical
22378847
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIT_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural basis for stem cell factor-KIT signaling and activation ofclass III receptor tyrosine kinases.";
Liu H., Chen X., Focia P.J., He X.;
EMBO J. 26:891-901(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-314 IN COMPLEX WITHKITLG/SCF, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-296 AND ASN-303.

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