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Protein

Kit ligand

Gene

Kitlg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • cytokine activity Source: MGI
  • stem cell factor receptor binding Source: MGI

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • ectopic germ cell programmed cell death Source: MGI
  • embryonic hemopoiesis Source: MGI
  • extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • germ cell development Source: MGI
  • male gonad development Source: Ensembl
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of mast cell apoptotic process Source: MGI
  • neural crest cell migration Source: MGI
  • ovarian follicle development Source: Ensembl
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of DNA replication Source: MGI
  • positive regulation of hematopoietic stem cell proliferation Source: MGI
  • positive regulation of leukocyte migration Source: MGI
  • positive regulation of MAP kinase activity Source: MGI
  • positive regulation of mast cell proliferation Source: MGI
  • positive regulation of melanocyte differentiation Source: MGI
  • positive regulation of myeloid leukocyte differentiation Source: MGI
  • positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of Ras protein signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1433559. Regulation of KIT signaling.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Kit ligand
Alternative name(s):
Hematopoietic growth factor KL
Mast cell growth factor
Short name:
MGF
Steel factor
Stem cell factor
Short name:
SCF
c-Kit ligand
Cleaved into the following chain:
Soluble KIT ligand
Short name:
sKITLG
Gene namesi
Name:Kitlg
Synonyms:Kitl, Mgf, Sl, Slf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:96974. Kitl.

Subcellular locationi

Isoform 2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 214189ExtracellularSequence analysisAdd
BLAST
Transmembranei215 – 23723HelicalSequence analysisAdd
BLAST
Topological domaini238 – 27336CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • extracellular region Source: Reactome
  • extracellular space Source: MGI
  • integral component of membrane Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25253 PublicationsAdd
BLAST
Chaini26 – 273248Kit ligandPRO_0000031914Add
BLAST
Chaini26 – 190165Soluble KIT ligandBy similarityPRO_0000403392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 1141 Publication
Disulfide bondi68 ↔ 1631 Publication
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence analysis
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP20826.
PaxDbiP20826.
PRIDEiP20826.

PTM databases

PhosphoSiteiP20826.

Miscellaneous databases

PMAP-CutDBP20826.

Expressioni

Developmental stagei

Acts in the early stages of hematopoiesis.

Gene expression databases

BgeeiP20826.
CleanExiMM_KITL.
ExpressionAtlasiP20826. baseline and differential.
GenevisibleiP20826. MM.

Interactioni

Subunit structurei

Homodimer, non-covalently linked (Probable). Heterotetramer with KIT, binding two KIT molecules; thereby mediates KIT dimerization and subsequent activation by autophosphorylation.Curated1 Publication

GO - Molecular functioni

  • cytokine activity Source: MGI
  • stem cell factor receptor binding Source: MGI

Protein-protein interaction databases

BioGridi201412. 1 interaction.
STRINGi10090.ENSMUSP00000100920.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 395Combined sources
Helixi40 – 456Combined sources
Beta strandi53 – 575Combined sources
Turni59 – 635Combined sources
Helixi66 – 683Combined sources
Helixi70 – 8516Combined sources
Helixi97 – 11822Combined sources
Beta strandi131 – 1355Combined sources
Helixi137 – 15115Combined sources
Turni153 – 1564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O26X-ray2.50A/B/E/F28-166[»]
2O27X-ray2.20A/B28-166[»]
ProteinModelPortaliP20826.
SMRiP20826. Positions 28-166.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20826.

Family & Domainsi

Sequence similaritiesi

Belongs to the SCF family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IF3Y. Eukaryota.
ENOG410XYQR. LUCA.
GeneTreeiENSGT00390000018272.
HOGENOMiHOG000082493.
HOVERGENiHBG036146.
InParanoidiP20826.
KOiK05461.
OMAiVKTKGIC.
OrthoDBiEOG70ZZP2.
PhylomeDBiP20826.
TreeFamiTF330811.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR003452. SCF.
[Graphical view]
PANTHERiPTHR11574. PTHR11574. 1 hit.
PfamiPF02404. SCF. 1 hit.
[Graphical view]
PIRSFiPIRSF015599. SCF. 1 hit.
SUPFAMiSSF47266. SSF47266. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P20826-1) [UniParc]FASTAAdd to basket

Also known as: KL-1

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.

« Hide

        10         20         30         40         50
MKKTQTWIIT CIYLQLLLFN PLVKTKEICG NPVTDNVKDI TKLVANLPND
60 70 80 90 100
YMITLNYVAG MDVLPSHCWL RDMVIQLSLS LTTLLDKFSN ISEGLSNYSI
110 120 130 140 150
IDKLGKIVDD LVLCMEENAP KNIKESPKRP ETRSFTPEEF FSIFNRSIDA
160 170 180 190 200
FKDFMVASDT SDCVLSSTLG PEKDSRVSVT KPFMLPPVAA SSLRNDSSSS
210 220 230 240 250
NRKAAKAPED SGLQWTAMAL PALISLVIGF AFGALYWKKK QSSLTRAVEN
260 270
IQINEEDNEI SMLQQKEREF QEV
Length:273
Mass (Da):30,645
Last modified:February 1, 1991 - v1
Checksum:iA7FC899B592A7967
GO
Isoform 2 (identifier: P20826-2) [UniParc]FASTAAdd to basket

Also known as: KL-2

The sequence of this isoform differs from the canonical sequence as follows:
     174-202: DSRVSVTKPFMLPPVAASSLRNDSSSSNR → G

Show »
Length:245
Mass (Da):27,614
Checksum:i78160A204FABF93B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2151W → L in AAB22555 (PubMed:1378327).Curated
Sequence conflicti215 – 2151W → L in AAB22554 (PubMed:1378327).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti122 – 1221N → S in MGFSL-3NEU. 1 Publication
Natural varianti193 – 1931L → P.2 Publications
Natural varianti207 – 2071A → S.3 Publications

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei174 – 20229DSRVS…SSSNR → G in isoform 2. CuratedVSP_006023Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59915 mRNA. Translation: AAA40095.1.
M57647 mRNA. Translation: AAA39538.1.
S40534 mRNA. Translation: AAB22555.2.
X68989 mRNA. Translation: CAA48778.1.
U44724 Genomic DNA. No translation available.
U44725 mRNA. Translation: AAC52447.1.
X95381 mRNA. Translation: CAA64667.1.
X99322 mRNA. Translation: CAA67698.1.
Y10287 mRNA. Translation: CAA71329.1.
AK018777 mRNA. Translation: BAB31402.1.
AK134301 mRNA. Translation: BAE22091.1.
AK165233 mRNA. Translation: BAE38091.1.
BC011322 mRNA. Translation: AAH11322.1.
S40364 mRNA. Translation: AAB22554.2.
M59912 mRNA. Translation: AAA39539.1.
CCDSiCCDS36046.1. [P20826-1]
PIRiA35971.
A37934.
B35971.
S65801.
RefSeqiNP_038626.1. NM_013598.2. [P20826-1]
UniGeneiMm.45124.

Genome annotation databases

EnsembliENSMUST00000020129; ENSMUSP00000020129; ENSMUSG00000019966. [P20826-2]
ENSMUST00000105283; ENSMUSP00000100920; ENSMUSG00000019966. [P20826-1]
GeneIDi17311.
KEGGimmu:17311.
UCSCiuc007gxp.1. mouse. [P20826-1]
uc007gxq.1. mouse. [P20826-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59915 mRNA. Translation: AAA40095.1.
M57647 mRNA. Translation: AAA39538.1.
S40534 mRNA. Translation: AAB22555.2.
X68989 mRNA. Translation: CAA48778.1.
U44724 Genomic DNA. No translation available.
U44725 mRNA. Translation: AAC52447.1.
X95381 mRNA. Translation: CAA64667.1.
X99322 mRNA. Translation: CAA67698.1.
Y10287 mRNA. Translation: CAA71329.1.
AK018777 mRNA. Translation: BAB31402.1.
AK134301 mRNA. Translation: BAE22091.1.
AK165233 mRNA. Translation: BAE38091.1.
BC011322 mRNA. Translation: AAH11322.1.
S40364 mRNA. Translation: AAB22554.2.
M59912 mRNA. Translation: AAA39539.1.
CCDSiCCDS36046.1. [P20826-1]
PIRiA35971.
A37934.
B35971.
S65801.
RefSeqiNP_038626.1. NM_013598.2. [P20826-1]
UniGeneiMm.45124.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O26X-ray2.50A/B/E/F28-166[»]
2O27X-ray2.20A/B28-166[»]
ProteinModelPortaliP20826.
SMRiP20826. Positions 28-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201412. 1 interaction.
STRINGi10090.ENSMUSP00000100920.

PTM databases

PhosphoSiteiP20826.

Proteomic databases

MaxQBiP20826.
PaxDbiP20826.
PRIDEiP20826.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020129; ENSMUSP00000020129; ENSMUSG00000019966. [P20826-2]
ENSMUST00000105283; ENSMUSP00000100920; ENSMUSG00000019966. [P20826-1]
GeneIDi17311.
KEGGimmu:17311.
UCSCiuc007gxp.1. mouse. [P20826-1]
uc007gxq.1. mouse. [P20826-2]

Organism-specific databases

CTDi17311.
MGIiMGI:96974. Kitl.

Phylogenomic databases

eggNOGiENOG410IF3Y. Eukaryota.
ENOG410XYQR. LUCA.
GeneTreeiENSGT00390000018272.
HOGENOMiHOG000082493.
HOVERGENiHBG036146.
InParanoidiP20826.
KOiK05461.
OMAiVKTKGIC.
OrthoDBiEOG70ZZP2.
PhylomeDBiP20826.
TreeFamiTF330811.

Enzyme and pathway databases

ReactomeiR-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1433559. Regulation of KIT signaling.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Miscellaneous databases

EvolutionaryTraceiP20826.
PMAP-CutDBP20826.
PROiP20826.
SOURCEiSearch...

Gene expression databases

BgeeiP20826.
CleanExiMM_KITL.
ExpressionAtlasiP20826. baseline and differential.
GenevisibleiP20826. MM.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR003452. SCF.
[Graphical view]
PANTHERiPTHR11574. PTHR11574. 1 hit.
PfamiPF02404. SCF. 1 hit.
[Graphical view]
PIRSFiPIRSF015599. SCF. 1 hit.
SUPFAMiSSF47266. SSF47266. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of mast cell growth factor, a hematopoietin that is active in both membrane bound and soluble forms."
    Anderson D.M., Lyman S.D., Baird A., Wignall J.M., Eisenman J., Rauch C., March C.J., Boswell H.S., Gimpel S.D., Cosman D., Williams D.E.
    Cell 63:235-243(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: WCB6F1.
  2. "Differential expression and processing of two cell associated forms of the kit-ligand: KL-1 and KL-2."
    Huang E.J., Nocka K.H., Buck J., Besmer P.
    Mol. Biol. Cell 3:349-362(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
  3. "Transmembrane form of the kit ligand growth factor is determined by alternative splicing and is missing in the Sld mutant."
    Flanagan J.G., Chan D.C., Leder P.
    Cell 64:1025-1035(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
    Strain: WCB6F1.
  4. "Developmental abnormalities in Steel17H mice result from a splicing defect in the steel factor cytoplasmic tail."
    Brannan C.I., Bedell M.A., Resnick J.L., Eppig J.J., Handel M.A., Williams D.E., Lyman S.D., Donovan P.J., Jenkins N.A., Copeland N.G.
    Genes Dev. 6:1832-1842(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
  5. "Multiple pathways for Steel regulation suggested by genomic and sequence analysis of the murine Steel gene."
    Bedell M.A., Copeland N.G., Jenkins N.A.
    Genetics 142:927-934(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  6. "Molecular analysis of two new Steel mutations in mice shows a transversion or an insertion."
    Graw J., Loester J., Neuhaeuser-Klaus A., Pretsch W., Schmitt-John T.
    Mamm. Genome 7:843-846(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PRO-193 AND SER-207.
    Strain: C3H/E1.
    Tissue: Brain.
  7. "Detection of a point mutation (A to G) in exon 5 of the murine Mgf gene defines a novel allele at the Steel locus with a weak phenotype."
    Graw J., Neuhauser-Klaus A., Pretsch W.
    Mutat. Res. 382:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-122; PRO-193 AND SER-207.
    Strain: 102/E1 X C3H/E1.
  8. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Cerebellum and Testis.
  9. "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] (ISOFORM 1), VARIANT SER-207.
  10. "The hematopoietic growth factor KL is encoded by the Sl locus and is the ligand of the c-kit receptor, the gene product of the W locus."
    Huang E., Nocka K., Beier D.R., Chu T.Y., Buck J., Lahm H.W., Wellner D., Leder P., Besmer P.
    Cell 63:225-233(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-270 (ISOFORM 1), PROTEIN SEQUENCE OF 26-65.
  11. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-201.
  12. "Mast cell growth factor maps near the steel locus on mouse chromosome 10 and is deleted in a number of steel alleles."
    Copeland N.G., Gilbert D.J., Cho B.C., Donovan P.J., Jenkins N.A., Cosman D., Anderson D., Lyman S.D., Williams D.E.
    Cell 63:175-183(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-53.
  13. Cited for: PROTEIN SEQUENCE OF 26-78.
  14. "Structural basis for stem cell factor-KIT signaling and activation of class III receptor tyrosine kinases."
    Liu H., Chen X., Focia P.J., He X.
    EMBO J. 26:891-901(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 28-166 ALONE AND IN COMPLEX WITH KIT, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiSCF_MOUSE
AccessioniPrimary (citable) accession number: P20826
Secondary accession number(s): P97332
, Q3TNJ7, Q62524, Q64222, Q921N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 8, 2016
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.