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P15018

- LIF_HUMAN

UniProt

P15018 - LIF_HUMAN

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Protein

Leukemia inhibitory factor

Gene

LIF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. cytokine activity Source: MGI
  2. growth factor activity Source: BHF-UCL
  3. leukemia inhibitory factor receptor binding Source: BHF-UCL
  4. receptor binding Source: BHF-UCL
  5. RNA polymerase II transcription factor recruiting transcription factor activity Source: BHF-UCL

GO - Biological processi

  1. blood vessel remodeling Source: Ensembl
  2. decidualization Source: Ensembl
  3. embryo implantation Source: Ensembl
  4. immune response Source: InterPro
  5. leukemia inhibitory factor signaling pathway Source: BHF-UCL
  6. lung alveolus development Source: Ensembl
  7. lung lobe morphogenesis Source: Ensembl
  8. lung vasculature development Source: Ensembl
  9. multicellular organismal development Source: ProtInc
  10. muscle organ morphogenesis Source: Ensembl
  11. negative regulation of cell proliferation Source: Ensembl
  12. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
  13. negative regulation of hormone secretion Source: MGI
  14. negative regulation of meiosis Source: Ensembl
  15. neuron development Source: Ensembl
  16. positive regulation of astrocyte differentiation Source: Ensembl
  17. positive regulation of cell proliferation Source: BHF-UCL
  18. positive regulation of histone H3-K27 acetylation Source: BHF-UCL
  19. positive regulation of macrophage differentiation Source: MGI
  20. positive regulation of MAPK cascade Source: MGI
  21. positive regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis Source: BHF-UCL
  22. positive regulation of peptidyl-serine phosphorylation Source: MGI
  23. positive regulation of peptidyl-serine phosphorylation of STAT protein Source: BHF-UCL
  24. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  25. positive regulation of protein localization to nucleus Source: BHF-UCL
  26. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  27. positive regulation of tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
  28. positive regulation of tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
  29. regulation of metanephric nephron tubule epithelial cell differentiation Source: BHF-UCL
  30. spongiotrophoblast differentiation Source: Ensembl
  31. stem cell maintenance Source: Ensembl
  32. transcription from RNA polymerase II promoter Source: GOC
  33. trophoblast giant cell differentiation Source: Ensembl
  34. tyrosine phosphorylation of Stat3 protein Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor

Enzyme and pathway databases

SignaLinkiP15018.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:LIF
Synonyms:HILDA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:6596. LIF.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular space Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

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).

Organism-specific databases

PharmGKBiPA30370.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 202180Leukemia inhibitory factorPRO_0000017715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi31 – 311N-linked (GlcNAc...)1 Publication
Disulfide bondi34 ↔ 1561 Publication
Disulfide bondi40 ↔ 1531 Publication
Glycosylationi56 – 561N-linked (GlcNAc...)1 Publication
Disulfide bondi82 ↔ 1851 Publication
Glycosylationi85 – 851N-linked (GlcNAc...)1 Publication
Glycosylationi95 – 951N-linked (GlcNAc...)1 Publication
Glycosylationi118 – 1181N-linked (GlcNAc...)1 Publication
Glycosylationi138 – 1381N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP15018.
PRIDEiP15018.

Miscellaneous databases

PMAP-CutDBP15018.

Expressioni

Gene expression databases

BgeeiP15018.
CleanExiHS_LIF.
GenevestigatoriP15018.

Organism-specific databases

HPAiCAB025985.
HPA018844.

Interactioni

Protein-protein interaction databases

BioGridi110164. 1 interaction.
DIPiDIP-5769N.
IntActiP15018. 1 interaction.
MINTiMINT-1352030.
STRINGi9606.ENSP00000249075.

Structurei

Secondary structure

1
202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 7027
Turni72 – 776
Helixi78 – 814
Beta strandi82 – 843
Beta strandi94 – 963
Helixi98 – 12629
Helixi131 – 15727
Helixi177 – 19923

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EMRX-ray3.50A44-202[»]
1PVHX-ray2.50B/D34-202[»]
2Q7NX-ray4.00B/D23-202[»]
ProteinModelPortaliP15018.
SMRiP15018. Positions 23-202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15018.

Family & Domainsi

Sequence similaritiesi

Belongs to the LIF/OSM family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG45686.
GeneTreeiENSGT00390000000059.
HOGENOMiHOG000059647.
HOVERGENiHBG006267.
InParanoidiP15018.
KOiK05419.
OMAiSNLMNQI.
OrthoDBiEOG7JX359.
PhylomeDBiP15018.
TreeFamiTF336245.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR003624. Leukemia_IF.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view]
PANTHERiPTHR10633. PTHR10633. 1 hit.
PfamiPF01291. LIF_OSM. 1 hit.
[Graphical view]
PRINTSiPR01883. LEUKAEMIAIF.
SMARTiSM00080. LIF_OSM. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00590. LIF_OSM. 1 hit.
[Graphical view]

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. Align

Isoform 1 (identifier: P15018-1) [UniParc]FASTAAdd to Basket

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
MKVLAAGVVP LLLVLHWKHG AGSPLPITPV NATCAIRHPC HNNLMNQIRS
60 70 80 90 100
QLAQLNGSAN ALFILYYTAQ GEPFPNNLDK LCGPNVTDFP PFHANGTEKA
110 120 130 140 150
KLVELYRIVV YLGTSLGNIT RDQKILNPSA LSLHSKLNAT ADILRGLLSN
160 170 180 190 200
VLCRLCSKYH VGHVDVTYGP DTSGKDVFQK KKLGCQLLGK YKQIIAVLAQ

AF
Length:202
Mass (Da):22,008
Last modified:April 1, 1990 - v1
Checksum:i634CD10BFF67A217
GO
Isoform 2 (identifier: P15018-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:88
Mass (Da):9,563
Checksum:iC27010E1B89B18E5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei7 – 8882GVVPL…PNVTD → VHSPGGAVPQQPGQAMWPQR DGLPALPRQRHGEGQAGGAV PHSRVPWHLPGQHHPGPEDP QPQCPQPPQQAQRHRRHPAR PP in isoform 2. 1 PublicationVSP_045551Add
BLAST
Alternative sequencei89 – 202114Missing in isoform 2. 1 PublicationVSP_045552Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13872.1. [P15018-1]
CCDS58799.1. [P15018-2]
PIRiB36282.
RefSeqiNP_001244064.1. NM_001257135.1. [P15018-2]
NP_002300.1. NM_002309.4. [P15018-1]
XP_006724303.1. XM_006724240.1. [P15018-1]
UniGeneiHs.2250.

Genome annotation databases

EnsembliENST00000249075; ENSP00000249075; ENSG00000128342. [P15018-1]
ENST00000403987; ENSP00000384450; ENSG00000128342. [P15018-2]
GeneIDi3976.
KEGGihsa:3976.
UCSCiuc003agz.3. human. [P15018-1]

Polymorphism databases

DMDMi126279.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Leukemia inhibitory factor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13872.1. [P15018-1 ]
CCDS58799.1. [P15018-2 ]
PIRi B36282.
RefSeqi NP_001244064.1. NM_001257135.1. [P15018-2 ]
NP_002300.1. NM_002309.4. [P15018-1 ]
XP_006724303.1. XM_006724240.1. [P15018-1 ]
UniGenei Hs.2250.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EMR X-ray 3.50 A 44-202 [» ]
1PVH X-ray 2.50 B/D 34-202 [» ]
2Q7N X-ray 4.00 B/D 23-202 [» ]
ProteinModelPortali P15018.
SMRi P15018. Positions 23-202.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110164. 1 interaction.
DIPi DIP-5769N.
IntActi P15018. 1 interaction.
MINTi MINT-1352030.
STRINGi 9606.ENSP00000249075.

Polymorphism databases

DMDMi 126279.

Proteomic databases

PaxDbi P15018.
PRIDEi P15018.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000249075 ; ENSP00000249075 ; ENSG00000128342 . [P15018-1 ]
ENST00000403987 ; ENSP00000384450 ; ENSG00000128342 . [P15018-2 ]
GeneIDi 3976.
KEGGi hsa:3976.
UCSCi uc003agz.3. human. [P15018-1 ]

Organism-specific databases

CTDi 3976.
GeneCardsi GC22M030636.
HGNCi HGNC:6596. LIF.
HPAi CAB025985.
HPA018844.
MIMi 159540. gene.
neXtProti NX_P15018.
PharmGKBi PA30370.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG45686.
GeneTreei ENSGT00390000000059.
HOGENOMi HOG000059647.
HOVERGENi HBG006267.
InParanoidi P15018.
KOi K05419.
OMAi SNLMNQI.
OrthoDBi EOG7JX359.
PhylomeDBi P15018.
TreeFami TF336245.

Enzyme and pathway databases

SignaLinki P15018.

Miscellaneous databases

EvolutionaryTracei P15018.
GeneWikii Leukemia_inhibitory_factor.
GenomeRNAii 3976.
NextBioi 15584.
PMAP-CutDB P15018.
PROi P15018.
SOURCEi Search...

Gene expression databases

Bgeei P15018.
CleanExi HS_LIF.
Genevestigatori P15018.

Family and domain databases

Gene3Di 1.20.1250.10. 1 hit.
InterProi IPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR003624. Leukemia_IF.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view ]
PANTHERi PTHR10633. PTHR10633. 1 hit.
Pfami PF01291. LIF_OSM. 1 hit.
[Graphical view ]
PRINTSi PR01883. LEUKAEMIAIF.
SMARTi SM00080. LIF_OSM. 1 hit.
[Graphical view ]
SUPFAMi SSF47266. SSF47266. 1 hit.
PROSITEi PS00590. LIF_OSM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiLIF_HUMAN
AccessioniPrimary (citable) accession number: P15018
Secondary accession number(s): B2RCW7, B5MC23, Q52LZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3