SCF_HUMAN - dbPTM
SCF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCF_HUMAN
UniProt AC P21583
Protein Name Kit ligand
Gene Name KITLG
Organism Homo sapiens (Human).
Sequence Length 273
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Cytoplasm . Cytoplasm, cytoskeleton. Cell membrane
Single-pass type I membrane protein. Cell projection, lamellipodium . Cell projection, filopodium .
Soluble KIT ligand: Secret
Protein Description Ligand for the receptor-type protein-tyrosine kinase KIT. 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. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins..
Protein Sequence MKKTQTWILTCIYLQLLLFNPLVKTEGICRNRVTNNVKDVTKLVANLPKDYMITLKYVPGMDVLPSHCWISEMVVQLSDSLTDLLDKFSNISEGLSNYSIIDKLVNIVDDLVECVKENSSKDLKKSFKSPEPRLFTPEEFFRIFNRSIDAFKDFVVASETSDCVVSSTLSPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKAKNPPGDSSLHWAAMALPALFSLIIGFAFGALYWKKRQPSLTRAVENIQINEEDNEISMLQEKEREFQEV
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
6Phosphorylation--MKKTQTWILTCIY
--CCHHHHHHHHHHH		21.5027174698
10PhosphorylationKTQTWILTCIYLQLL
HHHHHHHHHHHHHHH		6.4227174698
13PhosphorylationTWILTCIYLQLLLFN
HHHHHHHHHHHHHHC		7.1927174698
27SulfoxidationNPLVKTEGICRNRVT
CHHHCCCCHHCCCCC		29.548762148
34PhosphorylationGICRNRVTNNVKDVT
CHHCCCCCCCHHHHH		20.1728060719
36SulfoxidationCRNRVTNNVKDVTKL
HCCCCCCCHHHHHHH		32.618762148
48SulfoxidationTKLVANLPKDYMITL
HHHHHCCCCCEEEEE		27.558762148
90N-linked_GlycosylationDLLDKFSNISEGLSN
HHHHHHCCCCHHHCC		44.961381905
90N-linked_GlycosylationDLLDKFSNISEGLSN
HHHHHHCCCCHHHCC		44.961381905
118N-linked_GlycosylationLVECVKENSSKDLKK
HHHHHHHCCCHHHHH		45.961381905
118N-linked_GlycosylationLVECVKENSSKDLKK
HHHHHHHCCCHHHHH		45.961381905
126PhosphorylationSSKDLKKSFKSPEPR
CCHHHHHHCCCCCCC		36.0030108239
128UbiquitinationKDLKKSFKSPEPRLF
HHHHHHCCCCCCCCC		72.67-
128 (in isoform 2)Ubiquitination-72.67-
129PhosphorylationDLKKSFKSPEPRLFT
HHHHHCCCCCCCCCC		32.2730108239
136PhosphorylationSPEPRLFTPEEFFRI
CCCCCCCCHHHHHHH		34.0930108239
145N-linked_GlycosylationEEFFRIFNRSIDAFK
HHHHHHHHHHHHHHH		34.121381905
145N-linked_GlycosylationEEFFRIFNRSIDAFK
HHHHHHHHHHHHHHH		34.121381905
146 (in isoform 3)Ubiquitination-25.0021906983
152UbiquitinationNRSIDAFKDFVVASE
HHHHHHHHCCEEEEC		52.56-
159SulfoxidationKDFVVASETSDCVVS
HCCEEEECCCCCEEE		42.468762148
167O-linked_GlycosylationTSDCVVSSTLSPEKD
CCCCEEECCCCCCCC		23.041381905
168O-linked_GlycosylationSDCVVSSTLSPEKDS
CCCEEECCCCCCCCC		24.611381905
180O-linked_GlycosylationKDSRVSVTKPFMLPP
CCCCCEECCCCCCCH		26.031381905
181UbiquitinationDSRVSVTKPFMLPPV
CCCCEECCCCCCCHH		33.8221906983
181 (in isoform 1)Ubiquitination-33.8221906983
195N-linked_GlycosylationVAASSLRNDSSSSNR
HHHHHHCCCCCCCCC		59.83UniProtKB CARBOHYD
231 (in isoform 3)Ubiquitination-9.2121906983
238 (in isoform 2)Ubiquitination-25.2321906983
243PhosphorylationYWKKRQPSLTRAVEN
HHHHHCCCHHHHHHH		33.7523312004
261PhosphorylationNEEDNEISMLQEKER
CCCCCCHHHHHHHHH		13.7825841592
266UbiquitinationEISMLQEKEREFQEV
CHHHHHHHHHHHHCC		49.462190698
266 (in isoform 1)Ubiquitination-49.4621906983
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

Oops, there are no upstream regulatory protein records of SCF_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
90NGlycosylation

1381905
90NGlycosylation

1381905
97NGlycosylation

1381905
97NGlycosylation

1381905
118NGlycosylation

1381905
118NGlycosylation

1381905
145NGlycosylation

1381905
145NGlycosylation

1381905
167SGlycosylation

1381905
167SGlycosylation

1381905
168TGlycosylation

1381905
168TGlycosylation

1381905
180TGlycosylation

1381905
180TGlycosylation

1381905
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 SCF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SCF_HUMANKITLGphysical
8626683
SCF_HUMANKITLGphysical
10884405
AT8B2_HUMANATP8B2physical
26186194
PIGU_HUMANPIGUphysical
26186194
KLD10_HUMANKLHDC10physical
26186194
FLT3L_HUMANFLT3LGphysical
25241761
KLD10_HUMANKLHDC10physical
28514442
AT8B2_HUMANATP8B2physical
28514442
S22AI_HUMANSLC22A18physical
28514442
Drug and Disease Associations
Kegg Disease
H00884 Familial progressive hyperpigmentation
OMIM Disease
145250Hyperpigmentation with or without hypopigmentation, familial progressive (FPHH)
Kegg Drug
D02937 Ancestim (genetical recombination) (JAN); Ancestim (USAN/INN); Stemgen (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SCF_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Post-translational processing of membrane-associated recombinanthuman stem cell factor expressed in Chinese hamster ovary cells.";
Lu H.S., Clogston C.L., Wypych J., Parker V.P., Lee T.D., Swiderek K.,Baltera R.F. Jr., Patel A.C., Chang D.C., Brankow D.W., Liu X.-D.,Ogden S.G., Karkare S.B., Hu S.S., Zsebo K.M., Langley K.E.;
Arch. Biochem. Biophys. 298:150-158(1992).
Cited for: PROTEIN SEQUENCE OF 26-40; 64-79; 87-102; 110-149 AND 154-190 (ISOFORM1), DISULFIDE BONDS, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, ANDGLYCOSYLATION AT ASN-90; ASN-118; ASN-145; SER-167; THR-168 ANDTHR-180.
O-linked Glycosylation
ReferencePubMed
"Post-translational processing of membrane-associated recombinanthuman stem cell factor expressed in Chinese hamster ovary cells.";
Lu H.S., Clogston C.L., Wypych J., Parker V.P., Lee T.D., Swiderek K.,Baltera R.F. Jr., Patel A.C., Chang D.C., Brankow D.W., Liu X.-D.,Ogden S.G., Karkare S.B., Hu S.S., Zsebo K.M., Langley K.E.;
Arch. Biochem. Biophys. 298:150-158(1992).
Cited for: PROTEIN SEQUENCE OF 26-40; 64-79; 87-102; 110-149 AND 154-190 (ISOFORM1), DISULFIDE BONDS, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, ANDGLYCOSYLATION AT ASN-90; ASN-118; ASN-145; SER-167; THR-168 ANDTHR-180.

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