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P21583 (SCF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kit ligand
Alternative name(s):
Mast cell growth factor
Short name=MGF
Stem cell factor
Short name=SCF
c-Kit ligand

Cleaved into the following chain:

  1. Soluble KIT ligand
    Short name=sKITLG
Gene names
Name:KITLG
Synonyms:MGF, SCF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homodimer, non-covalently linked Probable. Heterotetramer with KIT, binding two KIT molecules; thereby mediates KIT dimerization and subsequent activation by autophosphorylation.

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.9.

Isoform 2: Cell membrane; Single-pass type I membrane protein By similarity. Cytoplasmcytoskeleton By similarity Ref.9.

Soluble KIT ligand: Secreted Ref.9.

Developmental stage

Acts in the early stages of hematopoiesis.

Post-translational modification

A soluble form (sKITLG) is produced by proteolytic processing of isoform 1 in the extracellular domain.

Found in two differentially glycosylated forms, LMW-SCF and HMW-SCF. LMW-SCF is fully N-glycosylated at Asn-145, partially N-glycosylated at Asn-90, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97 or Asn-118. HMW-SCF is N-glycosylated at Asn-118, Asn-90 and Asn-145, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97. Ref.9

A soluble form exists as a cleavage product of the extracellular domain.

Polymorphism

Genetic variants in KITLG define the skin/hair/eye pigmentation variation locus 7 (SHEP7) [MIM:611664]. Hair, eye and skin pigmentation are among the most visible examples of human phenotypic variation, with a broad normal range that is subject to substantial geographic stratification. In the case of skin, individuals tend to have lighter pigmentation with increasing distance from the equator. By contrast, the majority of variation in human eye and hair color is found among individuals of European ancestry, with most other human populations fixed for brown eyes and black hair.

Involvement in disease

Familial progressive hyperpigmentation (FPH) [MIM:145250]: A disorder characterized by hyperpigmented patches in the skin, present in early infancy and increasing in size and number with age.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

Sequence similarities

Belongs to the SCF family.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionGrowth factor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

ectopic germ cell programmed cell death

Inferred from electronic annotation. Source: Ensembl

embryonic hemopoiesis

Inferred from direct assay PubMed 21149635. Source: DFLAT

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

male gonad development

Inferred from expression pattern PubMed 17848411. Source: UniProtKB

negative regulation of mast cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

neural crest cell migration

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of DNA replication

Inferred from direct assay PubMed 9722506. Source: BHF-UCL

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of Ras protein signal transduction

Inferred from electronic annotation. Source: Ensembl

positive regulation of mast cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of melanocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of myeloid leukocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Non-traceable author statement Ref.3. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.17. Source: IntAct

stem cell factor receptor binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KITP107212EBI-1379527,EBI-1379503

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P21583-1)

Also known as: SCF248;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P21583-2)

Also known as: SCF220;

The sequence of this isoform differs from the canonical sequence as follows:
     174-202: DSRVSVTKPFMLPPVAASSLRNDSSSSNR → G
Isoform 3 (identifier: P21583-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.
     36-43: NVKDVTKL → MPSCLAAQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.9
Chain26 – 273248Kit ligand
PRO_0000031913
Chain26 – 190165Soluble KIT ligand
PRO_0000403391

Regions

Topological domain26 – 214189Extracellular Potential
Transmembrane215 – 23723Helical; Potential
Topological domain238 – 27336Cytoplasmic Potential

Sites

Site971Not glycosylated

Amino acid modifications

Glycosylation901N-linked (GlcNAc...); partial Ref.9
Glycosylation1181N-linked (GlcNAc...); partial Ref.9
Glycosylation1451N-linked (GlcNAc...) Ref.9
Glycosylation1671O-linked (GalNAc...) Ref.9
Glycosylation1681O-linked (GalNAc...) Ref.9
Glycosylation1801O-linked (GalNAc...) Ref.9
Glycosylation1951N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 114 Ref.9 Ref.15 Ref.16 Ref.17
Disulfide bond68 ↔ 163 Ref.9 Ref.15 Ref.16 Ref.17

Natural variations

Alternative sequence1 – 3535Missing in isoform 3.
VSP_032762
Alternative sequence36 – 438NVKDVTKL → MPSCLAAQ in isoform 3.
VSP_032763
Alternative sequence174 – 20229DSRVS…SSSNR → G in isoform 2.
VSP_006022
Natural variant361N → S in FPH; gain-of-function mutation; sKITLG reveales that the mutant Ser-36 sKITLG increases the content of the melanin by 109% compared with the wild-type sKITLG; tyrosinase activity is significantly increased by the mutant sKITLG compared to wild-type control. Ref.18
VAR_063237
Natural variant541T → A.
Corresponds to variant rs3741457 [ dbSNP | Ensembl ].
VAR_042652
Natural variant2101D → Y.
Corresponds to variant rs41283112 [ dbSNP | Ensembl ].
VAR_063238
Natural variant2321F → Y.
Corresponds to variant rs12721563 [ dbSNP | Ensembl ].
VAR_042653

Experimental info

Sequence conflict551L → S in AAD22048. Ref.3
Sequence conflict551L → S in AAK92486. Ref.4
Sequence conflict1281K → R in AAD22048. Ref.3
Sequence conflict1281K → R in AAK92486. Ref.4
Sequence conflict1341L → F in AAD22048. Ref.3
Sequence conflict1341L → F in AAK92486. Ref.4

Secondary structure

.......................... 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SCF248) [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 19FD362CB59C6607

FASTA27330,899
        10         20         30         40         50         60 
MKKTQTWILT CIYLQLLLFN PLVKTEGICR NRVTNNVKDV TKLVANLPKD YMITLKYVPG 

        70         80         90        100        110        120 
MDVLPSHCWI SEMVVQLSDS LTDLLDKFSN ISEGLSNYSI IDKLVNIVDD LVECVKENSS 

       130        140        150        160        170        180 
KDLKKSFKSP EPRLFTPEEF FRIFNRSIDA FKDFVVASET SDCVVSSTLS PEKDSRVSVT 

       190        200        210        220        230        240 
KPFMLPPVAA SSLRNDSSSS NRKAKNPPGD SSLHWAAMAL PALFSLIIGF AFGALYWKKR 

       250        260        270 
QPSLTRAVEN IQINEEDNEI SMLQEKEREF QEV 

« Hide

Isoform 2 (SCF220) [UniParc].

Checksum: 937AEA64456DF4FA
Show »

FASTA24527,867
Isoform 3 [UniParc].

Checksum: 7D6B1E487BE3709B
Show »

FASTA23826,667

References

« Hide 'large scale' references
[1]"Primary structure and functional expression of rat and human stem cell factor DNAs."
Martin F.H., Suggs S.V., Langley K.E., Lu H.S., Ting J., Okino K.H., Morris C.F., McNiece I.K., Jacobsen F.W., Mendiaz E.A., Birkett N.C., Smith K.A., Johnson M.J., Parker V.P., Flores J.C., Patel A.C., Fisher E.F., Erjavec H.O. expand/collapse author list , Herrera C.J., Wypych J., Sachdev R.K., Pope J.A., Leslie I., Wen D., Lin C.-H., Cupples R.L., Zsebo K.M.
Cell 63:203-211(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Alternate splicing of mRNAs encoding human mast cell growth factor and localization of the gene to chromosome 12q22-q24."
Anderson D.M., Williams D.E., Tushinski R., Gimpel S., Eisenman J., Cannizzaro L.A., Aronson M., Croce C.M., Huebner K., Cosman D.
Cell Growth Differ. 2:373-378(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Parathyroid hormone-regulated production of stem cell factor in human osteoblasts and osteoblast-like cells."
Blair H.C., Julian B.A., Cao X., Jordan S.E., Dong S.S.
Biochem. Biophys. Res. Commun. 255:778-784(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]Han C., Peng X., Yuan J., Qiang B.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Tongue and Trachea.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Amygdala.
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Colon.
[9]"Post-translational processing of membrane-associated recombinant human 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-40; 64-79; 87-102; 110-149 AND 154-190 (ISOFORM 1), DISULFIDE BONDS, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, GLYCOSYLATION AT ASN-90; ASN-118; ASN-145; SER-167; THR-168 AND THR-180.
[10]"Expression of two types of kit ligand mRNAs in human tumor cells."
Toyota M., Hinoda Y., Itoh F., Tsujisaki M., Imai K., Yachi A.
Int. J. Hematol. 55:301-304(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 167-248 (ISOFORM 2).
[11]"Stem cell factor/c-kit system in spermatogenesis."
Mauduit C., Hamamah S., Benahmed M.
Hum. Reprod. Update 5:535-545(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"Signal transduction via the stem cell factor receptor/c-Kit."
Ronnstrand L.
Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Normal and oncogenic forms of the receptor tyrosine kinase kit."
Lennartsson J., Jelacic T., Linnekin D., Shivakrupa R.
Stem Cells 23:16-43(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[14]"Genetic determinants of hair, eye and skin pigmentation in Europeans."
Sulem P., Gudbjartsson D.F., Stacey S.N., Helgason A., Rafnar T., Magnusson K.P., Manolescu A., Karason A., Palsson A., Thorleifsson G., Jakobsdottir M., Steinberg S., Palsson S., Jonasson F., Sigurgeirsson B., Thorisdottir K., Ragnarsson R., Benediktsdottir K.R. expand/collapse author list , Aben K.K., Kiemeney L.A., Olafsson J.H., Gulcher J., Kong A., Thorsteinsdottir U., Stefansson K.
Nat. Genet. 39:1443-1452(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SHEP7.
[15]"Structure of the active core of human stem cell factor and analysis of binding to its receptor kit."
Jiang X., Gurel O., Mendiaz E.A., Stearns G.W., Clogston C.L., Lu H.S., Osslund T.D., Syed R.S., Langley K.E., Hendrickson W.A.
EMBO J. 19:3192-3203(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), DISULFIDE BONDS.
[16]"Crystal structure of human stem cell factor: implication for stem cell factor receptor dimerization and activation."
Zhang Z., Zhang R., Joachimiak A., Schlessinger J., Kong X.P.
Proc. Natl. Acad. Sci. U.S.A. 97:7732-7737(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-166, DISULFIDE BONDS.
[17]"Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor."
Yuzawa S., Opatowsky Y., Zhang Z., Mandiyan V., Lax I., Schlessinger J.
Cell 130:323-334(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 26-166 IN COMPLEX WITH KIT, DISULFIDE BONDS.
[18]"Gain-of-function mutation of KIT ligand on melanin synthesis causes familial progressive hyperpigmentation."
Wang Z.-Q., Si L., Tang Q., Lin D., Fu Z., Zhang J., Cui B., Zhu Y., Kong X., Deng M., Xia Y., Xu H., Le W., Hu L., Kong X.
Am. J. Hum. Genet. 84:672-677(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FPH SER-36, CHARACTERIZATION OF VARIANT FPH SER-36.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59964 mRNA. Translation: AAA85450.1.
AF119835 mRNA. Translation: AAD22048.1.
AF400436 mRNA. Translation: AAK92485.1.
AF400437 mRNA. Translation: AAK92486.1.
AK290319 mRNA. Translation: BAF83008.1.
AK293002 mRNA. Translation: BAF85691.1.
CR749222 mRNA. Translation: CAH18078.1.
CH471054 Genomic DNA. Translation: EAW97417.1.
BC069733 mRNA. Translation: AAH69733.1.
BC069783 mRNA. Translation: AAH69783.1.
BC069797 mRNA. Translation: AAH69797.1.
BC074725 mRNA. Translation: AAH74725.1.
BC126166 mRNA. Translation: AAI26167.1.
BC143899 mRNA. Translation: AAI43900.1.
S42571 mRNA. Translation: AAB22846.2.
CCDSCCDS31867.1. [P21583-2]
CCDS31868.1. [P21583-1]
PIRA35974.
B61190.
S29052.
RefSeqNP_000890.1. NM_000899.4. [P21583-1]
NP_003985.2. NM_003994.5. [P21583-2]
UniGeneHs.1048.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EXZX-ray2.30A/B/C/D26-166[»]
1SCFX-ray2.20A/B/C/D1-273[»]
2E9WX-ray3.50C/D26-166[»]
ProteinModelPortalP21583.
SMRP21583. Positions 36-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110410. 4 interactions.
IntActP21583. 1 interaction.
STRING9606.ENSP00000228280.

Chemistry

BindingDBP21583.
ChEMBLCHEMBL2346489.

PTM databases

PhosphoSiteP21583.

Polymorphism databases

DMDM134289.

Proteomic databases

MaxQBP21583.
PaxDbP21583.
PRIDEP21583.

Protocols and materials databases

DNASU4254.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228280; ENSP00000228280; ENSG00000049130. [P21583-1]
ENST00000347404; ENSP00000054216; ENSG00000049130. [P21583-2]
GeneID4254.
KEGGhsa:4254.
UCSCuc001tav.3. human. [P21583-1]
uc001taw.3. human. [P21583-2]

Organism-specific databases

CTD4254.
GeneCardsGC12M088823.
HGNCHGNC:6343. KITLG.
HPACAB004569.
MIM145250. phenotype.
184745. gene.
611664. phenotype.
neXtProtNX_P21583.
Orphanet280628. Familial progressive hyper- and hypopigmentation.
79146. Familial progressive hyperpigmentation.
363494. Testicular non seminomatous germ cell tumor.
842. Testicular seminomatous germ cell tumor.
PharmGKBPA30129.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39386.
HOVERGENHBG036146.
KOK05461.
OMAVKTKGIC.
OrthoDBEOG70ZZP2.
PhylomeDBP21583.
TreeFamTF330811.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

BgeeP21583.
CleanExHS_KITLG.
GenevestigatorP21583.

Family and domain databases

Gene3D1.20.1250.10. 1 hit.
InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR003452. SCF.
[Graphical view]
PANTHERPTHR11574. PTHR11574. 1 hit.
PfamPF02404. SCF. 1 hit.
[Graphical view]
PIRSFPIRSF015599. SCF. 1 hit.
SUPFAMSSF47266. SSF47266. 1 hit.
ProtoNetSearch...

Other

ChiTaRSKITLG. human.
EvolutionaryTraceP21583.
GeneWikiStem_cell_factor.
GenomeRNAi4254.
NextBio16773.
PMAP-CutDBP21583.
PROP21583.
SOURCESearch...

Entry information

Entry nameSCF_HUMAN
AccessionPrimary (citable) accession number: P21583
Secondary accession number(s): A0AV09 expand/collapse secondary AC list , A8K2Q4, B7ZLM4, Q16487, Q68DZ2, Q7M4N8, Q9UQK7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM