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UniProtKB/Swiss-Prot entry P48061


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SDF1_HUMAN
Primary accession number P48061
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on February 1, 1996 (Sequence version 1)
Annotations were last modified on    June 10, 2008 (Entry version 90)
Name and origin of the protein
Protein name Stromal cell-derived factor 1 [Precursor]
Synonyms SDF-1
C-X-C motif chemokine 12
Pre-B cell growth-stimulating factor
PBSF
hIRH
Contains SDF-1-beta(3-72)
SDF-1-alpha(3-67)
Gene name
Name: CXCL12
Synonyms: SDF1, SDF1A, SDF1B
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Spotila L.D.;
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1006/geno.1995.1180; PubMed=7490086 [NCBI, ExPASy, EBI, Israel, Japan]
Shirozu M., Nakano T., Inazawa J., Tashiro K., Tada H., Shinohara T., Honjo T.;
"Structure and chromosomal localization of the human stromal cell-derived factor 1 (SDF1) gene.";
Genomics 28:495-500(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Liver;
Begum N.A., Barnard G.F.;
"Nucleotide sequence of hIRH, human intercrine reduced in hepatomas.";
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs program for genomic applications;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION OF SDF-1ALPHA(3-67) AND SDF-1BETA(3-72) BY MASS SPECTROMETRY, AND PROTEOLYTIC PROCESSING OF N-TERMINAL AND C-TERMINAL.
DOI=10.1182/blood-2003-08-2857; PubMed=14525775 [NCBI, ExPASy, EBI, Israel, Japan]
De La Luz Sierra M., Yang F., Narazaki M., Salvucci O., Davis D., Yarchoan R., Zhang H.H., Fales H., Tosato G.;
"Differential processing of stromal-derived factor-1alpha and beta explains functional diversity.";
Blood 103:2452-2459(2004).
[8]
STRUCTURE BY NMR OF 22-88.
DOI=10.1093/emboj/16.23.6996; PubMed=9384579 [NCBI, ExPASy, EBI, Israel, Japan]
Crump M.P., Gong J.H., Loetscher P., Rajarathnam K., Amara A., Arenzana-Seisdedos F., Virelizier J.-L., Baggiolini M., Sykes B.D., Clark-Lewis I.;
"Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1.";
EMBO J. 16:6996-7007(1997).
[9]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-88.
DOI=10.1073/pnas.95.12.6941; PubMed=9618518 [NCBI, ExPASy, EBI, Israel, Japan]
Dealwis C., Fernandez E.J., Thompson D.A., Simon R.J., Siani M.A., Lolis E.;
"Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 'fusin' coreceptor.";
Proc. Natl. Acad. Sci. U.S.A. 95:6941-6946(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U16752; AAA97434.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L36033; AAB39332.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L36034; AAB39333.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U19495; AAB40516.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY802782; AAV49999.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL137026; CAC10203.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039893; AAH39893.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G01540; G01540.
RefSeq NP_000600.1; -.
NP_954637.1; -.
UniGene Hs.522891
3D structure databases
PDB
1A15; X-ray; 2.20 A; A/B=22-88.[ExPASy / RCSB / EBI]
1QG7; X-ray; 2.00 A; A/B=22-88.[ExPASy / RCSB / EBI]
1SDF; NMR; -; A=22-88.[ExPASy / RCSB / EBI]
1VMC; NMR; -; A=19-89.[ExPASy / RCSB / EBI]
2J7Z; X-ray; 1.95 A; A/B=22-89.[ExPASy / RCSB / EBI]
2NWG; X-ray; 2.07 A; A/B=22-88.[ExPASy / RCSB / EBI]
2SDF; NMR; -; A=22-88.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A15; -.
1QG7; -.
1SDF; -.
1VMC; -.
2J7Z; -.
2NWG; -.
2SDF; -.
ModBase P48061.
Protein-protein interaction databases
DIP DIP:391N; -.
DIP:5895N; -.
Organism-specific databases
H-InvDB HIX0008784; -.
HGNC HGNC:10672; CXCL12.
GeneLynx CXCL12; Homo sapiens.
GenAtlas CXCL12.
MIM 600835; gene. [NCBI / EBI]
PharmGKB PA35602; -.
GeneCards P48061.
Gene expression databases
ArrayExpress P48061; -.
CleanEx HS_CXCL12; -.
GermOnline ENSG00000107562; Homo sapiens.
Ontologies
GO
GO:0008009; Molecular function: chemokine activity (traceable author statement from ProtInc).
GO:0004871; Molecular function: signal transducer activity (traceable author statement from ProtInc).
GO:0008015; Biological process: blood circulation (traceable author statement from ProtInc).
GO:0007155; Biological process: cell adhesion (traceable author statement from ProtInc).
GO:0006874; Biological process: cellular calcium ion homeostasis (traceable author statement from ProtInc).
GO:0006935; Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from ProtInc).
GO:0006955; Biological process: immune response (traceable author statement from ProtInc).
GO:0008064; Biological process: regulation of actin polymerization and/or depolymerization (traceable author statement from ProtInc).
GO:0009615; Biological process: response to virus (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002473; C-X-C/Interlkn_8.
IPR001811; Chemokine_IL8.
IPR001089; CXC_chmkine_smll.
Graphical view of domain structure.
Pfam PF00048; IL8; 1.
Pfam graphical view of domain structure.
PRINTS PR00436; INTERLEUKIN8.
SMART SM00199; SCY; 1.
SMART graphical view of domain structure.
PROSITE PS00471; SMALL_CYTOKINES_CXC; FALSE_NEG.
BLOCKS P48061.
Genome annotation databases
Ensembl ENSG00000107562; Homo sapiens. [Contig view]
GeneID 6387; -.
KEGG hsa:6387; -.
Phylogenomic databases
HOVERGEN P48061; -.
Other
DrugBank DB01234; Dexamethasone.
LinkHub P48061; -.
SOURCE CXCL12; Homo sapiens.
ProtoNet P48061.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Chemotaxis; Cytokine; Growth factor; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
SIGNAL   1   21  21     Potential. 
CHAIN   22   93  72     Stromal cell-derived factor 1. PRO_0000005109
CHAIN   24   93  70     SDF-1-beta(3-72). PRO_0000005110
CHAIN   24   88  65     SDF-1-alpha(3-67). PRO_0000005111
DISULFID   30   55         
DISULFID   32   71         
VAR_SEQ   90   93        Missing (in isoform Alpha). VSP_001056
STRAND   25   28  4      
HELIX   41   43  3      
STRAND   44   52  9      
TURN   53   55  3      
STRAND   56   63  8      
TURN   64   66  3      
STRAND   69   72  4      
HELIX   77   85  9      
Sequence information
Length: 93 AA [This is the length of the unprocessed precursor] Molecular weight: 10666 Da [This is the MW of the unprocessed precursor] CRC64: 505B5A29C2B44E8D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNAKVVVVLV LVLTALCLSD GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV 

        70         80         90 
ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR FKM 

P48061 in FASTA format

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View entry in raw text format (no links)
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