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P15018 (LIF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leukemia inhibitory factor

Short name=LIF
Alternative name(s):
Differentiation-stimulating factor
Short name=D factor
Melanoma-derived LPL inhibitor
Short name=MLPLI
INN=Emfilermin
Gene names
Name:LIF
Synonyms:HILDA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.

Subcellular location

Secreted.

Pharmaceutical use

In phase II clinical trial. The drug is being developed by Amrad to assist embryo implantation in women who have failed to become pregnant despite assisted reproductive technologies (ART).

Sequence similarities

Belongs to the LIF/OSM family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionCytokine
Growth factor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

decidualization

Inferred from electronic annotation. Source: Ensembl

embryo implantation

Inferred from electronic annotation. Source: Ensembl

immune response

Inferred from electronic annotation. Source: InterPro

leukemia inhibitory factor signaling pathway

Inferred from direct assay PubMed 12643274PubMed 8999038. Source: BHF-UCL

lung alveolus development

Inferred from electronic annotation. Source: Ensembl

lung lobe morphogenesis

Inferred from electronic annotation. Source: Ensembl

lung vasculature development

Inferred from electronic annotation. Source: Ensembl

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

muscle organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of hormone secretion

Inferred from direct assay PubMed 7867561. Source: MGI

negative regulation of meiosis

Inferred from electronic annotation. Source: Ensembl

neuron development

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from direct assay PubMed 7508917. Source: MGI

positive regulation of astrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay PubMed 8999038. Source: BHF-UCL

positive regulation of histone H3-K27 acetylation

Inferred from direct assay PubMed 22783022. Source: BHF-UCL

positive regulation of macrophage differentiation

Inferred from direct assay PubMed 7957045. Source: MGI

positive regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis

Inferred from direct assay PubMed 20624457. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 7508917. Source: MGI

positive regulation of peptidyl-serine phosphorylation of STAT protein

Inferred from direct assay PubMed 20624457. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 7508917. Source: MGI

positive regulation of protein localization to nucleus

Inferred from direct assay PubMed 22783022. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20624457PubMed 22783022. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of Stat1 protein

Inferred from direct assay PubMed 20624457. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of Stat3 protein

Inferred from direct assay PubMed 12643274PubMed 20624457PubMed 22783022. Source: BHF-UCL

regulation of metanephric nephron tubule epithelial cell differentiation

Inferred from direct assay PubMed 20624457. Source: BHF-UCL

spongiotrophoblast differentiation

Inferred from electronic annotation. Source: Ensembl

stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 22783022. Source: GOC

trophoblast giant cell differentiation

Inferred from electronic annotation. Source: Ensembl

tyrosine phosphorylation of Stat3 protein

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

extracellular space

Inferred by curator PubMed 12643274. Source: BHF-UCL

   Molecular_functionRNA polymerase II transcription factor recruiting transcription factor activity

Inferred from direct assay PubMed 22783022. Source: BHF-UCL

cytokine activity

Inferred from direct assay PubMed 7957045. Source: MGI

growth factor activity

Inferred from direct assay PubMed 12643274PubMed 8999038. Source: BHF-UCL

leukemia inhibitory factor receptor binding

Inferred from physical interaction PubMed 8999038. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 8999038. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15018-1)

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.
Isoform 2 (identifier: P15018-2)

The sequence of this isoform differs from the canonical sequence as follows:
     7-88: GVVPLLLVLH...DKLCGPNVTD → VHSPGGAVPQ...RHRRHPARPP
     89-202: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.10
Chain23 – 202180Leukemia inhibitory factor
PRO_0000017715

Amino acid modifications

Glycosylation311N-linked (GlcNAc...) Ref.11
Glycosylation561N-linked (GlcNAc...) Ref.11
Glycosylation851N-linked (GlcNAc...) Ref.11
Glycosylation951N-linked (GlcNAc...) Ref.11
Glycosylation1181N-linked (GlcNAc...) Ref.11
Glycosylation1381N-linked (GlcNAc...) Ref.11
Disulfide bond34 ↔ 156 Ref.11
Disulfide bond40 ↔ 153 Ref.11
Disulfide bond82 ↔ 185 Ref.11

Natural variations

Alternative sequence7 – 8882GVVPL…PNVTD → VHSPGGAVPQQPGQAMWPQR DGLPALPRQRHGEGQAGGAV PHSRVPWHLPGQHHPGPEDP QPQCPQPPQQAQRHRRHPAR PP in isoform 2.
VSP_045551
Alternative sequence89 – 202114Missing in isoform 2.
VSP_045552

Secondary structure

............... 202
Helix Strand Turn

Details...

Sequences

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

Last modified April 1, 1990. Version 1.
Checksum: 634CD10BFF67A217

FASTA20222,008
        10         20         30         40         50         60 
MKVLAAGVVP LLLVLHWKHG AGSPLPITPV NATCAIRHPC HNNLMNQIRS QLAQLNGSAN 

        70         80         90        100        110        120 
ALFILYYTAQ GEPFPNNLDK LCGPNVTDFP PFHANGTEKA KLVELYRIVV YLGTSLGNIT 

       130        140        150        160        170        180 
RDQKILNPSA LSLHSKLNAT ADILRGLLSN VLCRLCSKYH VGHVDVTYGP DTSGKDVFQK 

       190        200 
KKLGCQLLGK YKQIIAVLAQ AF 

« Hide

Isoform 2 [UniParc].

Checksum: C27010E1B89B18E5
Show »

FASTA889,563

References

« Hide 'large scale' references
[1]"Leukaemia inhibitory factor is identical to the myeloid growth factor human interleukin for DA cells."
Moreau J.-F., Donaldson D.D., Bennett F., Witek-Giannotti J., Clark S.C., Wong G.G.
Nature 336:690-692(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Genomic cloning and heterologous expression of human differentiation-stimulating factor."
Lowe D.G., Nunes W., Bombara M., McCabe S., Ranges G.E., Henzel W., Tomida M., Yamamoto-Yamaguchi Y., Hozumi M., Goeddel D.V.
DNA 8:351-359(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation."
Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y., Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J., Stanton L.W.
Nat. Biotechnol. 22:707-716(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Embryonic stem cell.
[4]"Structural organization of the genes for murine and human leukemia inhibitory factor. Evolutionary conservation of coding and non-coding regions."
Stahl J., Gearing D.P., Willson T.A., Brown M.A., King J.A., Gough N.M.
J. Biol. Chem. 265:8833-8841(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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 1).
[6]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1).
Tissue: Colon.
[9]"Molecular cloning and expression of the human homologue of the murine gene encoding myeloid leukemia-inhibitory factor."
Gough N.M., Gearing D.P., King J.A., Willson T.A., Hilton D.J., Nicola N.A., Metcalf D.
Proc. Natl. Acad. Sci. U.S.A. 85:2623-2627(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-202.
[10]"Purification of a lipoprotein lipase-inhibiting protein produced by a melanoma cell line associated with cancer cachexia."
Mori M., Yamaguchi K., Abe K.
Biochem. Biophys. Res. Commun. 160:1085-1092(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-39.
[11]"Glycosylation pattern and disulfide assignments of recombinant human differentiation-stimulating factor."
Schmelzer C.H., Harris R.J., Butler D., Yedinak C.M., Wagner K.L., Burton L.E.
Arch. Biochem. Biophys. 302:484-489(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, GLYCOSYLATION AT ASN-31; ASN-56; ASN-85; ASN-95; ASN-118 AND ASN-138.
[12]"Convergent mechanisms for recognition of divergent cytokines by the shared signaling receptor gp130."
Boulanger M.J., Bankovich A.J., Kortemme T., Baker D., Garcia K.C.
Mol. Cell 12:577-589(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-202 IN COMPLEX WITH IL6ST.
[13]"An unusual cytokine:Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor."
Huyton T., Zhang J.G., Luo C.S., Lou M.Z., Hilton D.J., Nicola N.A., Garrett T.P.
Proc. Natl. Acad. Sci. U.S.A. 104:12737-12742(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 23-202 IN COMPLEX WITH MOUSE LIFR.
+Additional computationally mapped references.

Web resources

Wikipedia

Leukemia inhibitory factor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13967 mRNA. Translation: CAA32147.1.
M27053, M27052 Genomic DNA. Translation: AAA53188.1.
AC004264 Genomic DNA. Translation: AAC05174.1.
M63420 Genomic DNA. Translation: AAA51699.1.
CN409468 mRNA. No translation available.
AK315310 mRNA. Translation: BAG37714.1.
CH471095 Genomic DNA. Translation: EAW59863.1.
BC069540 mRNA. Translation: AAH69540.1.
BC093733 mRNA. Translation: AAH93733.1.
BC093735 mRNA. Translation: AAH93735.1.
J03261 Genomic DNA. Translation: AAA59517.1.
CCDSCCDS13872.1. [P15018-1]
CCDS58799.1. [P15018-2]
PIRB36282.
RefSeqNP_001244064.1. NM_001257135.1. [P15018-2]
NP_002300.1. NM_002309.4. [P15018-1]
XP_006724303.1. XM_006724240.1. [P15018-1]
UniGeneHs.2250.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EMRX-ray3.50A44-202[»]
1PVHX-ray2.50B/D34-202[»]
2Q7NX-ray4.00B/D23-202[»]
ProteinModelPortalP15018.
SMRP15018. Positions 23-202.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110164. 1 interaction.
DIPDIP-5769N.
IntActP15018. 1 interaction.
MINTMINT-1352030.
STRING9606.ENSP00000249075.

Polymorphism databases

DMDM126279.

Proteomic databases

PaxDbP15018.
PRIDEP15018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000249075; ENSP00000249075; ENSG00000128342. [P15018-1]
ENST00000403987; ENSP00000384450; ENSG00000128342. [P15018-2]
GeneID3976.
KEGGhsa:3976.
UCSCuc003agz.3. human. [P15018-1]

Organism-specific databases

CTD3976.
GeneCardsGC22M030636.
HGNCHGNC:6596. LIF.
HPACAB025985.
HPA018844.
MIM159540. gene.
neXtProtNX_P15018.
PharmGKBPA30370.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45686.
HOGENOMHOG000059647.
HOVERGENHBG006267.
InParanoidP15018.
KOK05419.
OMASNLMNQI.
OrthoDBEOG7JX359.
PhylomeDBP15018.
TreeFamTF336245.

Enzyme and pathway databases

SignaLinkP15018.

Gene expression databases

BgeeP15018.
CleanExHS_LIF.
GenevestigatorP15018.

Family and domain databases

Gene3D1.20.1250.10. 1 hit.
InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR003624. Leukemia_IF.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view]
PANTHERPTHR10633. PTHR10633. 1 hit.
PfamPF01291. LIF_OSM. 1 hit.
[Graphical view]
PRINTSPR01883. LEUKAEMIAIF.
SMARTSM00080. LIF_OSM. 1 hit.
[Graphical view]
SUPFAMSSF47266. SSF47266. 1 hit.
PROSITEPS00590. LIF_OSM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15018.
GeneWikiLeukemia_inhibitory_factor.
GenomeRNAi3976.
NextBio15584.
PMAP-CutDBP15018.
PROP15018.
SOURCESearch...

Entry information

Entry nameLIF_HUMAN
AccessionPrimary (citable) accession number: P15018
Secondary accession number(s): B2RCW7, B5MC23, Q52LZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 154 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 chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM