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P13232 (IL7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-7

Short name=IL-7
Gene names
Name:IL7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hematopoietic growth factor capable of stimulating the proliferation of lymphoid progenitors. It is important for proliferation during certain stages of B-cell maturation.

Subcellular location

Secreted.

Sequence similarities

Belongs to the IL-7/IL-9 family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionCytokine
Growth factor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell lineage commitment

Inferred from electronic annotation. Source: Ensembl

bone resorption

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

homeostasis of number of cells within a tissue

Inferred from electronic annotation. Source: Ensembl

humoral immune response

Traceable author statement Ref.1. Source: ProtInc

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of catalytic activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

organ morphogenesis

Traceable author statement Ref.1. Source: ProtInc

positive regulation of B cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of T cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Traceable author statement Ref.1. Source: ProtInc

positive regulation of organ growth

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiongrowth factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

interleukin-7 receptor binding

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 8266077. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IL2RGP317852EBI-80516,EBI-80475
IL7RP168713EBI-80516,EBI-80490

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P13232-1)

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: P13232-2)

The sequence of this isoform differs from the canonical sequence as follows:
     77-120: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P13232-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.
     77-138: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 177152Interleukin-7
PRO_0000015623

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1411N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 166 Ref.8 Ref.11
Disulfide bond59 ↔ 154 Ref.8 Ref.11
Disulfide bond72 ↔ 117 Ref.8 Ref.11

Natural variations

Alternative sequence1 – 5151Missing in isoform 3.
VSP_047579
Alternative sequence77 – 13862Missing in isoform 3.
VSP_047580
Alternative sequence77 – 12044Missing in isoform 2.
VSP_042926

Secondary structure

.................. 177
Helix Strand Turn

Details...

Sequences

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

Last modified January 1, 1990. Version 1.
Checksum: 8FC5243F9169617F

FASTA17720,187
        10         20         30         40         50         60 
MFHVSFRYIF GLPPLILVLL PVASSDCDIE GKDGKQYESV LMVSIDQLLD SMKEIGSNCL 

        70         80         90        100        110        120 
NNEFNFFKRH ICDANKEGMF LFRAARKLRQ FLKMNSTGDF DLHLLKVSEG TTILLNCTGQ 

       130        140        150        160        170 
VKGRKPAALG EAQPTKSLEE NKSLKEQKKL NDLCFLKRLL QEIKTCWNKI LMGTKEH 

« Hide

Isoform 2 [UniParc].

Checksum: B2DD9AB838924186
Show »

FASTA13315,203
Isoform 3 [UniParc].

Checksum: D03218F01F5AA3EA
Show »

FASTA647,687

References

« Hide 'large scale' references
[1]"Human interleukin 7: molecular cloning and growth factor activity on human and murine B-lineage cells."
Goodwin R.G., Lupton S., Schmierer A., Hjerrild K.J., Jerzy R., Clevenger W., Gillis S., Cosman D., Namen A.E.
Proc. Natl. Acad. Sci. U.S.A. 86:302-306(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Characterization of the human and murine IL-7 genes."
Lupton S.D., Gimpel S., Jerzy R., Brunton L.L., Hjerrild K.A., Cosman D., Goodwin R.G.
J. Immunol. 144:3592-3601(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"interleukin7 mRNA,nirs splice variant2."
Sameshima E., Tabata Y., Hayashi A., Iida K., Mitsuyama M., Kanai S., Furuya T.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
[4]Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., Nickerson D.A.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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: Pancreas.
[8]"Disulfide bond assignment in human interleukin-7 by matrix-assisted laser desorption/ionization mass spectroscopy and site-directed cysteine to serine mutational analysis."
Cosenza L., Sweeney E., Murphy J.R.
J. Biol. Chem. 272:32995-33000(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Prediction of the three-dimensional structure of human interleukin-7 by homology modeling."
Kroemer R.T., Doughty S.W., Robinson A.J., Richards W.G.
Protein Eng. 9:493-498(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[10]"Comparative model building of interleukin-7 using interleukin-4 as a template: a structural hypothesis that displays atypical surface chemistry in helix D important for receptor activation."
Cosenza L., Rosenbach A., White J.V., Murphy J.R., Smith T.F.
Protein Sci. 9:916-926(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[11]"Structural and biophysical studies of the human IL-7/IL-7Ralpha complex."
McElroy C.A., Dohm J.A., Walsh S.T.
Structure 17:54-65(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 26-177 IN COMPLEX WITH IL7R, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Wikipedia

Interleukin-7 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04156 mRNA. Translation: AAA59156.1.
M29053 expand/collapse EMBL AC list , M29048, M29049, M29050, M29051, M29052 Genomic DNA. Translation: AAC63047.1.
AB102879 mRNA. Translation: BAD89408.1.
AB102883 mRNA. Translation: BAD89412.1.
EF064721 Genomic DNA. Translation: ABK41904.1.
AC083837 Genomic DNA. No translation available.
AC100854 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW87060.1.
CH471068 Genomic DNA. Translation: EAW87062.1.
BC047698 mRNA. Translation: AAH47698.1.
CCDSCCDS56541.1. [P13232-2]
CCDS6224.1. [P13232-1]
PIRA32223. A43527.
B32223.
C32223.
RefSeqNP_000871.1. NM_000880.3. [P13232-1]
NP_001186815.1. NM_001199886.1. [P13232-2]
NP_001186816.1. NM_001199887.1.
NP_001186817.1. NM_001199888.1.
UniGeneHs.591873.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IL7model-A26-177[»]
3DI2X-ray2.70A/C26-177[»]
3DI3X-ray2.90A26-177[»]
ProteinModelPortalP13232.
SMRP13232. Positions 32-172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109788. 2 interactions.
DIPDIP-3044N.
IntActP13232. 2 interactions.
STRING9606.ENSP00000263851.

Polymorphism databases

DMDM124354.

Proteomic databases

PaxDbP13232.
PRIDEP13232.

Protocols and materials databases

DNASU3574.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263851; ENSP00000263851; ENSG00000104432. [P13232-1]
ENST00000520269; ENSP00000427750; ENSG00000104432. [P13232-2]
ENST00000541183; ENSP00000438922; ENSG00000104432. [P13232-3]
GeneID3574.
KEGGhsa:3574.
UCSCuc003ybg.3. human. [P13232-1]
uc022awi.1. human. [P13232-2]

Organism-specific databases

CTD3574.
GeneCardsGC08M079587.
HGNCHGNC:6023. IL7.
HPAHPA019590.
MIM146660. gene.
neXtProtNX_P13232.
PharmGKBPA29839.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41411.
HOGENOMHOG000036891.
HOVERGENHBG004609.
InParanoidP13232.
KOK05431.
OMANNEPNFF.
OrthoDBEOG7S220M.
PhylomeDBP13232.
TreeFamTF338065.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP13232.

Gene expression databases

ArrayExpressP13232.
BgeeP13232.
CleanExHS_IL7.
GenevestigatorP13232.

Family and domain databases

InterProIPR001181. IL-7.
IPR018049. IL-7/IL-9_CS.
IPR000226. IL-7/IL-9_fam.
[Graphical view]
PANTHERPTHR10526. PTHR10526. 1 hit.
PfamPF01415. IL7. 1 hit.
[Graphical view]
PIRSFPIRSF001942. IL-7. 1 hit.
PRINTSPR00435. INTERLEUKIN7.
SMARTSM00127. IL7. 1 hit.
[Graphical view]
PROSITEPS00255. INTERLEUKIN_7_9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIL7. human.
EvolutionaryTraceP13232.
GeneWikiInterleukin_7.
GenomeRNAi3574.
NextBio13968.
PROP13232.
SOURCESearch...

Entry information

Entry nameIL7_HUMAN
AccessionPrimary (citable) accession number: P13232
Secondary accession number(s): A0N0L3, Q5FBY5, Q5FBY9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 142 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 8

Human chromosome 8: entries, gene names and cross-references to MIM