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P48061

- SDF1_HUMAN

UniProt

P48061 - SDF1_HUMAN

Protein

Stromal cell-derived factor 1

Gene

CXCL12

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

    Chemoattractant active on T-lymphocytes, monocytes, but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei46 – 461Important for dimer formation
    Binding sitei62 – 621Heparin
    Binding sitei69 – 691Heparin
    Binding sitei85 – 851Heparin

    GO - Molecular functioni

    1. chemokine activity Source: UniProtKB
    2. chemokine receptor binding Source: UniProtKB
    3. CXCR chemokine receptor binding Source: BHF-UCL
    4. receptor binding Source: ProtInc

    GO - Biological processi

    1. adult locomotory behavior Source: Ensembl
    2. ameboidal cell migration Source: Ensembl
    3. blood circulation Source: ProtInc
    4. cell adhesion Source: ProtInc
    5. cell chemotaxis Source: GOC
    6. cellular calcium ion homeostasis Source: ProtInc
    7. chemokine-mediated signaling pathway Source: BHF-UCL
    8. chemotaxis Source: UniProtKB
    9. germ cell development Source: Ensembl
    10. germ cell migration Source: Ensembl
    11. G-protein coupled receptor signaling pathway Source: ProtInc
    12. immune response Source: ProtInc
    13. induction of positive chemotaxis Source: Ensembl
    14. motor neuron axon guidance Source: Ensembl
    15. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: BHF-UCL
    16. negative regulation of leukocyte apoptotic process Source: BHF-UCL
    17. neuron migration Source: Ensembl
    18. organ regeneration Source: Ensembl
    19. patterning of blood vessels Source: Ensembl
    20. positive regulation of axon extension involved in axon guidance Source: Ensembl
    21. positive regulation of calcium ion import Source: BHF-UCL
    22. positive regulation of cell adhesion Source: MGI
    23. positive regulation of dopamine secretion Source: Ensembl
    24. positive regulation of endothelial cell proliferation Source: Ensembl
    25. positive regulation of monocyte chemotaxis Source: UniProtKB
    26. positive regulation of neuron differentiation Source: Ensembl
    27. positive regulation of T cell migration Source: MGI
    28. regulation of actin polymerization or depolymerization Source: ProtInc
    29. response to heat Source: Ensembl
    30. response to hypoxia Source: Ensembl
    31. response to mechanical stimulus Source: Ensembl
    32. response to peptide hormone Source: Ensembl
    33. response to radiation Source: Ensembl
    34. response to virus Source: ProtInc
    35. signal transduction Source: ProtInc
    36. T cell proliferation Source: Ensembl
    37. telencephalon cell migration Source: Ensembl

    Keywords - Molecular functioni

    Cytokine, Growth factor

    Keywords - Biological processi

    Chemotaxis

    Enzyme and pathway databases

    ReactomeiREACT_116022. Nuclear signaling by ERBB4.
    REACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stromal cell-derived factor 1
    Short name:
    SDF-1
    Short name:
    hSDF-1
    Alternative name(s):
    C-X-C motif chemokine 12
    Intercrine reduced in hepatomas
    Short name:
    IRH
    Short name:
    hIRH
    Pre-B cell growth-stimulating factor
    Short name:
    PBSF
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CXCL12
    Synonyms:SDF1, SDF1A, SDF1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:10672. CXCL12.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProtKB-KW
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 232Missing: Abolished CXCR4 activation ability, but only slightly impaired binding to the receptor. 3 Publications
    Mutagenesisi22 – 221K → A: Loss of chemotactic activity. 3 Publications
    Mutagenesisi22 – 221K → R: Abolished CXCR4 activation ability, but only slightly impaired binding to the receptor. 3 Publications
    Mutagenesisi22 – 221Missing: Abolished CXCR4 activation ability, but only slightly impaired binding to the receptor. 3 Publications
    Mutagenesisi23 – 231P → G: Abolished CXCR4 activation ability, but only slightly impaired binding to the receptor. 2 Publications
    Mutagenesisi25 – 273SLS → AQA: Significantly impaired CXCR4 activation ability, but only slightly impaired binding to the receptor. 1 Publication
    Mutagenesisi28 – 281Y → A: Impaired CXCR4 activation ability, but only slightly impaired binding to the receptor. 2 Publications
    Mutagenesisi28 – 281Y → H: No significant effect on CXCR4 binding or activation. 2 Publications
    Mutagenesisi29 – 291R → K: Slightly impaired binding and activation of CXCR4. 3 Publications
    Mutagenesisi29 – 291R → Q: Greatly impaired chemotactic activity and enhanced inhibition by heparin. 3 Publications
    Mutagenesisi33 – 386RFFESH → AAAAAA: Significantly decreased chemotactic activity. 3 Publications
    Mutagenesisi33 – 331R → A: Significantly decreased anti-HIV-1 and chemotactic activities. 3 Publications
    Mutagenesisi33 – 331R → Q: Slightly impaired chemotactic activity and enhanced inhibition by heparin. Greatly impaired chemotactic activity; when associated with Q-29. 3 Publications
    Mutagenesisi34 – 341F → A: No effect on anti-HIV-1 and chemotactic activities. Slightly impaired chemotactic activity and no effect on inhibition by heparin; when associated with A-35. 2 Publications
    Mutagenesisi35 – 351F → A: No effect on anti-HIV-1 and chemotactic activities. Slightly impaired chemotactic activity and no effect on inhibition by heparin; when associated with A-34. 2 Publications
    Mutagenesisi36 – 383ESH → QSN: Slightly impaired chemotactic activity, no effect on inhibition by heparin. 2 Publications
    Mutagenesisi36 – 361E → A: No effect on anti-HIV-1 and chemotactic activities. 2 Publications
    Mutagenesisi37 – 371S → A: No effect on anti-HIV-1 and chemotactic activities. 2 Publications
    Mutagenesisi38 – 381H → A: No effect on anti-HIV-1 and chemotactic activities. 2 Publications
    Mutagenesisi41 – 411R → A: No effect on CXCR4 activation. 2 Publications
    Mutagenesisi45 – 484KHLK → SSLS: Loss of heparin-binding capacity. 1 Publication
    Mutagenesisi46 – 461H → A: Reduced dimerization in neutral pH. Eliminates the pH dependence of dimerization. 4 Publications
    Mutagenesisi46 – 461H → L: No significant effect on dimerization in neutral pH. Eliminates the pH dependence of dimerization. 4 Publications
    Mutagenesisi46 – 461H → N: Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with Q-48; Q-62; Q-68 and N-69. 4 Publications
    Mutagenesisi46 – 461H → R: No effect on CXCR4 activation. Impaired dimer formation, leading to increased chemotactic activity. Eliminates the pH dependence of dimerization. 4 Publications
    Mutagenesisi48 – 481K → A: Impaired CXCR4 activation. 3 Publications
    Mutagenesisi48 – 481K → E: Impaired CXCR4 activation. 3 Publications
    Mutagenesisi48 – 481K → Q: Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-62; Q-68 and N-69. 3 Publications
    Mutagenesisi52 – 565TPNCA → GPGCG: Slightly impaired chemotactic activity, no effect on inhibition by heparin. 1 Publication
    Mutagenesisi57 – 571L → C: Formation of an intermolecular disulfide bond, leading to a locked dimer; when associated with C-86. No effect on CXCR4 activation, but loss of chemotactic activity; when associated with C-86. 1 Publication
    Mutagenesisi60 – 601V → A: Impaired CXCR4 activation. 2 Publications
    Mutagenesisi62 – 621R → A: No effect on CXCR4 activation. 3 Publications
    Mutagenesisi62 – 621R → Q: Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-48; Q-68 and N-69. 3 Publications
    Mutagenesisi68 – 681R → A: Impaired CXCR4 activation. 3 Publications
    Mutagenesisi68 – 681R → E: Greatly impaired CXCR4 activation. 3 Publications
    Mutagenesisi68 – 681R → Q: Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-48; Q-62 and N-69. 3 Publications
    Mutagenesisi69 – 691Q → N: Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-48; Q-62 and Q-68. 2 Publications
    Mutagenesisi70 – 701V → A: Impaired CXCR4 activation. 2 Publications
    Mutagenesisi81 – 811E → A: No effect on CXCR4 activation. 2 Publications
    Mutagenesisi84 – 841E → A: No effect on CXCR4 activation. 2 Publications
    Mutagenesisi85 – 851K → A: No effect on CXCR4 activation. 2 Publications
    Mutagenesisi86 – 861A → C: Formation of an intermolecular disulfide bond, leading to a locked dimer; when associated with C-57. No effect on CXCR4 activation, but loss of chemotactic activity; when associated with C-57. 1 Publication

    Organism-specific databases

    PharmGKBiPA35602.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 9372Stromal cell-derived factor 1PRO_0000005109Add
    BLAST
    Chaini24 – 9370SDF-1-beta(3-72)PRO_0000005110Add
    BLAST
    Chaini24 – 8865SDF-1-alpha(3-67)PRO_0000005111Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 55
    Disulfide bondi32 ↔ 71

    Post-translational modificationi

    Processed forms SDF-1-beta(3-72) and SDF-1-alpha(3-67) are produced after secretion by proteolytic cleavage of isoforms Beta and Alpha, respectively. The N-terminal processing is probably achieved by DPP4. Isoform Alpha is first cleaved at the C-terminus to yield a SDF-1-alpha(1-67) intermediate before being processed at the N-terminus. The C-terminal processing of isoform Alpha is reduced by binding to heparin and, probably, cell surface proteoglycans.1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP48061.
    PRIDEiP48061.

    PTM databases

    PhosphoSiteiP48061.

    Miscellaneous databases

    PMAP-CutDBQ5IT36.

    Expressioni

    Tissue specificityi

    Isoform Alpha and isoform Beta are ubiquitously expressed, with highest levels detected in liver, pancreas and spleen. Isoform Gamma is mainly expressed in heart, with weak expression detected in several other tissues. Isoform Delta, isoform Epsilon and isoform Theta have highest expression levels in pancreas, with lower levels detected in heart, kidney, liver and spleen.1 Publication

    Developmental stagei

    Isoform Alpha is ubiquitously expressed in fetal tissues. Isoform Beta and isoform Delta have more limited expression patterns, with highest levels detected in fetal spleen and fetal liver, respectively. Isoform Gamma and isoform Theta are weakly detected in fetal kidney.1 Publication

    Gene expression databases

    ArrayExpressiP48061.
    BgeeiP48061.
    CleanExiHS_CXCL12.
    GenevestigatoriP48061.

    Organism-specific databases

    HPAiCAB017564.

    Interactioni

    Subunit structurei

    Monomer or homodimer; in equilibrium. Dimer formation is induced by non acidic pH and the presence of multivalent anions, and by binding to CXCR4 or heparin. Monomeric form is required for full chemotactic activity and resistance to ischemia/reperfusion injury, whereas the dimeric form acts as a partial agonist of CXCR4, stimulating Ca2+ mobilization but with no chemotactic activity and instead acts as a selective antagonist that blocks chemotaxis induced by the monomeric form. Interacts with the N-terminus of ACKR3.7 Publications

    Protein-protein interaction databases

    BioGridi112288. 6 interactions.
    DIPiDIP-391N.
    DIP-5894N.
    DIP-5895N.
    IntActiP48061. 3 interactions.
    MINTiMINT-6491347.
    STRINGi9606.ENSP00000363548.

    Structurei

    Secondary structure

    1
    93
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni24 – 263
    Beta strandi27 – 293
    Beta strandi31 – 344
    Beta strandi36 – 383
    Helixi41 – 433
    Beta strandi44 – 496
    Turni53 – 553
    Beta strandi59 – 635
    Turni64 – 663
    Beta strandi69 – 724
    Helixi79 – 868

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A15X-ray2.20A/B22-88[»]
    1QG7X-ray2.00A/B22-88[»]
    1SDFNMR-A22-88[»]
    1VMCNMR-A22-89[»]
    2J7ZX-ray1.95A/B22-89[»]
    2K01NMR-A/C22-89[»]
    2K03NMR-A/C22-89[»]
    2K04NMR-A/C22-89[»]
    2K05NMR-A/C22-89[»]
    2KECNMR-A22-89[»]
    2KEDNMR-A22-89[»]
    2KEENMR-A22-89[»]
    2KOLNMR-A22-89[»]
    2NWGX-ray2.07A/B22-88[»]
    2SDFNMR-A22-88[»]
    3GV3X-ray1.60A26-88[»]
    3HP3X-ray2.20A/B/C/D/E/F/G/H/I/J22-88[»]
    4LMQX-ray2.77D/F29-89[»]
    ProteinModelPortaliP48061.
    SMRiP48061. Positions 22-89.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48061.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni29 – 335Receptor and heparin bindingCurated
    Regioni39 – 413Receptor binding
    Regioni41 – 5111Heparin bindingAdd
    BLAST
    Regioni48 – 503Receptor binding
    Regioni60 – 7011Receptor bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi22 – 232Receptor activation motif

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG26489.
    HOGENOMiHOG000220915.
    HOVERGENiHBG107437.
    KOiK10031.
    OMAiWIQEYLD.
    OrthoDBiEOG7C5MBS.
    PhylomeDBiP48061.
    TreeFamiTF353159.

    Family and domain databases

    InterProiIPR001811. Chemokine_IL8-like_dom.
    [Graphical view]
    PfamiPF00048. IL8. 1 hit.
    [Graphical view]
    SMARTiSM00199. SCY. 1 hit.
    [Graphical view]
    SUPFAMiSSF54117. SSF54117. 1 hit.

    Sequences (7)i

    Sequence statusi: Complete.

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

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform Beta (identifier: P48061-1) [UniParc]FASTAAdd to Basket

    Also known as: SDF-1-beta(1-72), hSDF-1beta

    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

    MNAKVVVVLV LVLTALCLSD GKPVSLSYRC PCRFFESHVA RANVKHLKIL   50
    NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR FKM 93
    Length:93
    Mass (Da):10,666
    Last modified:February 1, 1996 - v1
    Checksum:i505B5A29C2B44E8D
    GO
    Isoform Alpha (identifier: P48061-2) [UniParc]FASTAAdd to Basket

    Also known as: SDF-1-alpha(1-68), hSDF-1alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         90-93: Missing.

    Show »
    Length:89
    Mass (Da):10,103
    Checksum:i62B44E8D209C3A14
    GO
    Isoform Gamma (identifier: P48061-3) [UniParc]FASTAAdd to Basket

    Also known as: hSDF-1gamma, SDF-1g

    The sequence of this isoform differs from the canonical sequence as follows:
         90-93: RFKM → GRREEKVGKKEKIGKKKRQKKRKAAQKRKN

    Show »
    Length:119
    Mass (Da):13,705
    Checksum:iC36297D68341B824
    GO
    Isoform Delta (identifier: P48061-4) [UniParc]FASTAAdd to Basket

    Also known as: hSDF-1delta

    The sequence of this isoform differs from the canonical sequence as follows:
         89-93: KRFKM → NLISAAPAGKRVIAGARALHPSPPRACPTARALCEIRLWPPPEWSWPSPGDV

    Show »
    Length:140
    Mass (Da):15,495
    Checksum:i602BFEB309014ED2
    GO
    Isoform Epsilon (identifier: P48061-5) [UniParc]FASTAAdd to Basket

    Also known as: hSDFepsilon

    The sequence of this isoform differs from the canonical sequence as follows:
         89-93: KRFKM → NC

    Show »
    Length:90
    Mass (Da):10,192
    Checksum:i7375C44E8D209C3A
    GO
    Isoform Theta (identifier: P48061-6) [UniParc]FASTAAdd to Basket

    Also known as: hSDFphi, hSDFtheta, Phi

    The sequence of this isoform differs from the canonical sequence as follows:
         90-93: RFKM → IWLYGNAETSR

    Show »
    Length:100
    Mass (Da):11,395
    Checksum:iBEF2739B8E70BAAD
    GO
    Isoform 7 (identifier: P48061-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         39-93: VARANVKHLK...EKALNKRFKM → YCTCLIRVSF...VPGPVNLGKA

    Note: Gene prediction based on EST data.

    Show »
    Length:103
    Mass (Da):11,004
    Checksum:i33B2517CA23D65D8
    GO

    Sequence cautioni

    The sequence CAC10202.1 differs from that shown. Reason: Erroneous gene model prediction.

    Mass spectrometryi

    Isoform Alpha : Molecular mass is 7959 Da from positions 22 - 89. Determined by ESI. 1 Publication
    Isoform Alpha : Molecular mass is 7606 Da from positions 24 - 88. Determined by ESI. 1 Publication
    Isoform Beta : Molecular mass is 8522 Da from positions 22 - 93. Determined by ESI. 1 Publication
    Isoform Beta : Molecular mass is 8297 Da from positions 24 - 93. Determined by ESI. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei39 – 9355VARAN…KRFKM → YCTCLIRVSFHGATPLTQGS WVLYSLSCAGGETGLREPGP MVSPRVESHQEGRLGVPGPV NLGKA in isoform 7. 1 PublicationVSP_054781Add
    BLAST
    Alternative sequencei89 – 935KRFKM → NLISAAPAGKRVIAGARALH PSPPRACPTARALCEIRLWP PPEWSWPSPGDV in isoform Delta. 1 PublicationVSP_042118
    Alternative sequencei89 – 935KRFKM → NC in isoform Epsilon. 1 PublicationVSP_042119
    Alternative sequencei90 – 934Missing in isoform Alpha. 6 PublicationsVSP_001056
    Alternative sequencei90 – 934RFKM → GRREEKVGKKEKIGKKKRQK KRKAAQKRKN in isoform Gamma. 2 PublicationsVSP_041209
    Alternative sequencei90 – 934RFKM → IWLYGNAETSR in isoform Theta. 1 PublicationVSP_042120

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36033 mRNA. Translation: AAB39332.1.
    L36034 mRNA. Translation: AAB39333.1.
    DQ345517 mRNA. Translation: ABC69270.1.
    DQ345518 mRNA. Translation: ABC69271.1.
    DQ345519 mRNA. Translation: ABC69272.1.
    DQ345520 mRNA. Translation: ABC69273.1.
    U16752 mRNA. Translation: AAA97434.1.
    U19495 mRNA. Translation: AAB40516.1.
    AY644456 mRNA. Translation: AAT76437.1.
    AY874118 mRNA. Translation: AAW82036.1.
    CR450283 mRNA. Translation: CAG29279.1.
    AK292628 mRNA. Translation: BAF85317.1.
    AK311814 mRNA. Translation: BAG34757.1.
    AU120056 mRNA. No translation available.
    AY802782 Genomic DNA. Translation: AAV49999.1.
    AL137026 Genomic DNA. Translation: CAC10202.1. Sequence problems.
    AL137026 Genomic DNA. Translation: CAC10203.1.
    CH471160 Genomic DNA. Translation: EAW86619.1.
    BC039893 mRNA. Translation: AAH39893.1.
    CCDSiCCDS31186.1. [P48061-3]
    CCDS44373.1. [P48061-1]
    CCDS53527.1. [P48061-4]
    CCDS60518.1. [P48061-7]
    CCDS7207.1. [P48061-2]
    PIRiG01540.
    RefSeqiNP_000600.1. NM_000609.6. [P48061-1]
    NP_001029058.1. NM_001033886.2. [P48061-3]
    NP_001171605.1. NM_001178134.1. [P48061-4]
    NP_001264919.1. NM_001277990.1. [P48061-7]
    NP_954637.1. NM_199168.3. [P48061-2]
    UniGeneiHs.522891.

    Genome annotation databases

    EnsembliENST00000343575; ENSP00000339913; ENSG00000107562. [P48061-2]
    ENST00000374426; ENSP00000363548; ENSG00000107562. [P48061-3]
    ENST00000374429; ENSP00000363551; ENSG00000107562. [P48061-1]
    ENST00000395793; ENSP00000379139; ENSG00000107562. [P48061-7]
    ENST00000395794; ENSP00000379140; ENSG00000107562. [P48061-4]
    ENST00000395795; ENSP00000379141; ENSG00000107562. [P48061-5]
    GeneIDi6387.
    KEGGihsa:6387.
    UCSCiuc001jbf.4. human. [P48061-1]
    uc001jbh.3. human. [P48061-3]
    uc021ppm.1. human. [P48061-4]

    Polymorphism databases

    DMDMi1352728.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    SDF-1 entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36033 mRNA. Translation: AAB39332.1 .
    L36034 mRNA. Translation: AAB39333.1 .
    DQ345517 mRNA. Translation: ABC69270.1 .
    DQ345518 mRNA. Translation: ABC69271.1 .
    DQ345519 mRNA. Translation: ABC69272.1 .
    DQ345520 mRNA. Translation: ABC69273.1 .
    U16752 mRNA. Translation: AAA97434.1 .
    U19495 mRNA. Translation: AAB40516.1 .
    AY644456 mRNA. Translation: AAT76437.1 .
    AY874118 mRNA. Translation: AAW82036.1 .
    CR450283 mRNA. Translation: CAG29279.1 .
    AK292628 mRNA. Translation: BAF85317.1 .
    AK311814 mRNA. Translation: BAG34757.1 .
    AU120056 mRNA. No translation available.
    AY802782 Genomic DNA. Translation: AAV49999.1 .
    AL137026 Genomic DNA. Translation: CAC10202.1 . Sequence problems.
    AL137026 Genomic DNA. Translation: CAC10203.1 .
    CH471160 Genomic DNA. Translation: EAW86619.1 .
    BC039893 mRNA. Translation: AAH39893.1 .
    CCDSi CCDS31186.1. [P48061-3 ]
    CCDS44373.1. [P48061-1 ]
    CCDS53527.1. [P48061-4 ]
    CCDS60518.1. [P48061-7 ]
    CCDS7207.1. [P48061-2 ]
    PIRi G01540.
    RefSeqi NP_000600.1. NM_000609.6. [P48061-1 ]
    NP_001029058.1. NM_001033886.2. [P48061-3 ]
    NP_001171605.1. NM_001178134.1. [P48061-4 ]
    NP_001264919.1. NM_001277990.1. [P48061-7 ]
    NP_954637.1. NM_199168.3. [P48061-2 ]
    UniGenei Hs.522891.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A15 X-ray 2.20 A/B 22-88 [» ]
    1QG7 X-ray 2.00 A/B 22-88 [» ]
    1SDF NMR - A 22-88 [» ]
    1VMC NMR - A 22-89 [» ]
    2J7Z X-ray 1.95 A/B 22-89 [» ]
    2K01 NMR - A/C 22-89 [» ]
    2K03 NMR - A/C 22-89 [» ]
    2K04 NMR - A/C 22-89 [» ]
    2K05 NMR - A/C 22-89 [» ]
    2KEC NMR - A 22-89 [» ]
    2KED NMR - A 22-89 [» ]
    2KEE NMR - A 22-89 [» ]
    2KOL NMR - A 22-89 [» ]
    2NWG X-ray 2.07 A/B 22-88 [» ]
    2SDF NMR - A 22-88 [» ]
    3GV3 X-ray 1.60 A 26-88 [» ]
    3HP3 X-ray 2.20 A/B/C/D/E/F/G/H/I/J 22-88 [» ]
    4LMQ X-ray 2.77 D/F 29-89 [» ]
    ProteinModelPortali P48061.
    SMRi P48061. Positions 22-89.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112288. 6 interactions.
    DIPi DIP-391N.
    DIP-5894N.
    DIP-5895N.
    IntActi P48061. 3 interactions.
    MINTi MINT-6491347.
    STRINGi 9606.ENSP00000363548.

    Chemistry

    DrugBanki DB01234. Dexamethasone.

    PTM databases

    PhosphoSitei P48061.

    Polymorphism databases

    DMDMi 1352728.

    Proteomic databases

    PaxDbi P48061.
    PRIDEi P48061.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343575 ; ENSP00000339913 ; ENSG00000107562 . [P48061-2 ]
    ENST00000374426 ; ENSP00000363548 ; ENSG00000107562 . [P48061-3 ]
    ENST00000374429 ; ENSP00000363551 ; ENSG00000107562 . [P48061-1 ]
    ENST00000395793 ; ENSP00000379139 ; ENSG00000107562 . [P48061-7 ]
    ENST00000395794 ; ENSP00000379140 ; ENSG00000107562 . [P48061-4 ]
    ENST00000395795 ; ENSP00000379141 ; ENSG00000107562 . [P48061-5 ]
    GeneIDi 6387.
    KEGGi hsa:6387.
    UCSCi uc001jbf.4. human. [P48061-1 ]
    uc001jbh.3. human. [P48061-3 ]
    uc021ppm.1. human. [P48061-4 ]

    Organism-specific databases

    CTDi 6387.
    GeneCardsi GC10M044865.
    H-InvDB HIX0008784.
    HGNCi HGNC:10672. CXCL12.
    HPAi CAB017564.
    MIMi 600835. gene.
    neXtProti NX_P48061.
    PharmGKBi PA35602.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG26489.
    HOGENOMi HOG000220915.
    HOVERGENi HBG107437.
    KOi K10031.
    OMAi WIQEYLD.
    OrthoDBi EOG7C5MBS.
    PhylomeDBi P48061.
    TreeFami TF353159.

    Enzyme and pathway databases

    Reactomei REACT_116022. Nuclear signaling by ERBB4.
    REACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    EvolutionaryTracei P48061.
    GeneWikii Stromal_cell-derived_factor-1.
    GenomeRNAii 6387.
    NextBioi 24808.
    PMAP-CutDB Q5IT36.
    PROi P48061.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48061.
    Bgeei P48061.
    CleanExi HS_CXCL12.
    Genevestigatori P48061.

    Family and domain databases

    InterProi IPR001811. Chemokine_IL8-like_dom.
    [Graphical view ]
    Pfami PF00048. IL8. 1 hit.
    [Graphical view ]
    SMARTi SM00199. SCY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54117. SSF54117. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Structure and chromosomal localization of the human stromal cell-derived factor 1 (SDF1) gene."
      Shirozu M., Nakano T., Inazawa J., Tashiro K., Tada H., Shinohara T., Honjo T.
      Genomics 28:495-500(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
    2. "Identification and expression of novel isoforms of human stromal cell-derived factor 1."
      Yu L., Cecil J., Peng S.B., Schrementi J., Kovacevic S., Paul D., Su E.W., Wang J.
      Gene 374:174-179(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA; DELTA; EPSILON AND THETA), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING.
      Tissue: Fetal brain, Fetal heart and Heart.
    3. Spotila L.D.
      Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
      Tissue: Fibroblast.
    4. "Nucleotide sequence of hIRH, human intercrine reduced in hepatomas."
      Begum N.A., Barnard G.F.
      Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
      Tissue: Liver.
    5. "Inhibition of X4 and R5 HIV-1 by human SDF-1g, a novel chemokine that interferes with HIV transcription."
      Callebaut C., Verdin E.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA).
    6. "Polymorphism study of cell-derived factor 1 (SDF1) gene and their correlation with HIV infection in a Chinese cohort."
      Zhao X., Zhang H., Lee S., Wong K., Zheng B.
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    8. "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] (ISOFORMS ALPHA AND BETA).
      Tissue: Thymus and Uterus.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
    10. SeattleSNPs variation discovery resource
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    11. "The DNA sequence and comparative analysis of human chromosome 10."
      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.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. "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 ALPHA).
      Tissue: Brain.
    14. "The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1."
      Oberlin E., Amara A., Bachelerie F., Bessia C., Virelizier J.-L., Arenzana-Seisdedos F., Schwartz O., Heard J.-M., Clark-Lewis I., Legler D.F., Loetscher M., Baggiolini M., Moser B.
      Nature 382:833-835(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. Cited for: INTERACTION WITH CXCR4.
    16. "Stromal cell-derived factor-1alpha associates with heparan sulfates through the first beta-strand of the chemokine."
      Amara A., Lorthioir O., Valenzuela A., Magerus A., Thelen M., Montes M., Virelizier J.L., Delepierre M., Baleux F., Lortat-Jacob H., Arenzana-Seisdedos F.
      J. Biol. Chem. 274:23916-23925(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HEPARAN SULFATE, MUTAGENESIS OF 45-LYS--LYS-48.
    17. "Characterization of a Xenopus laevis CXC chemokine receptor 4: implications for hematopoietic cell development in the vertebrate embryo."
      Moepps B., Braun M., Knoepfle K., Dillinger K., Knoechel W., Gierschik P.
      Eur. J. Immunol. 30:2924-2934(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Xenopus laevis stromal cell-derived factor 1: conservation of structure and function during vertebrate development."
      Braun M., Wunderlin M., Spieth K., Knoechel W., Gierschik P., Moepps B.
      J. Immunol. 168:2340-2347(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Differential processing of stromal-derived factor-1alpha and beta explains functional diversity."
      De La Luz Sierra M., Yang F., Narazaki M., Salvucci O., Davis D., Yarchoan R., Zhang H.H., Fales H., Tosato G.
      Blood 103:2452-2459(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF SDF-1ALPHA(3-67) AND SDF-1BETA(3-72) BY MASS SPECTROMETRY, PROTEOLYTIC PROCESSING OF N-TERMINUS AND C-TERMINUS.
    20. "The chemokine SDF-1/CXCL12 binds to and signals through the orphan receptor RDC1 in T lymphocytes."
      Balabanian K., Lagane B., Infantino S., Chow K.Y., Harriague J., Moepps B., Arenzana-Seisdedos F., Thelen M., Bachelerie F.
      J. Biol. Chem. 280:35760-35766(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ACKR3.
    21. "The monomer-dimer equilibrium of stromal cell-derived factor-1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin."
      Veldkamp C.T., Peterson F.C., Pelzek A.J., Volkman B.F.
      Protein Sci. 14:1071-1081(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DIMERIZATION, MUTAGENESIS OF HIS-46.
    22. "Recognition of a CXCR4 sulfotyrosine by the chemokine stromal cell-derived factor-1alpha (SDF-1alpha/CXCL12)."
      Veldkamp C.T., Seibert C., Peterson F.C., Sakmar T.P., Volkman B.F.
      J. Mol. Biol. 359:1400-1409(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DIMERIZATION, INTERACTION WITH CXCR4.
    23. "Monocyte migration and LFA-1-mediated attachment to brain microvascular endothelia is regulated by SDF-1 alpha through Lyn kinase."
      Malik M., Chen Y.-Y., Kienzle M.F., Tomkowicz B.E., Collman R.G., Ptasznik A.
      J. Immunol. 181:4632-4637(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. Cited for: FUNCTION, INTERACTION WITH ACKR3.
    25. Cited for: RECEPTOR INTERACTION.
    26. "Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1."
      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.
      EMBO J. 16:6996-7007(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 22-88, DISULFIDE BONDS, MUTAGENESIS OF LYS-22; PRO-23; 22-LYS-PRO-23; 25-SER--SER-27; TYR-28 AND ARG-29.
    27. "Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 'fusin' coreceptor."
      Dealwis C., Fernandez E.J., Thompson D.A., Simon R.J., Siani M.A., Lolis E.
      Proc. Natl. Acad. Sci. U.S.A. 95:6941-6946(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-88 OF MUTANT ALA-54, DISULFIDE BONDS.
    28. "Crystal structure of recombinant native SDF-1alpha with additional mutagenesis studies: an attempt at a more comprehensive interpretation of accumulated structure-activity relationship data."
      Ohnishi Y., Senda T., Nandhagopal N., Sugimoto K., Shioda T., Nagal Y., Mitsui Y.
      J. Interferon Cytokine Res. 20:691-700(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-88, DISULFIDE BONDS, MUTAGENESIS OF ARG-33; PHE-34; PHE-35; GLU-36; SER-37; HIS-38 AND 33-ARG--HIS-38.
    29. "Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1alpha."
      Gozansky E.K., Louis J.M., Caffrey M., Clore G.M.
      J. Mol. Biol. 345:651-658(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 22-89, DISULFIDE BONDS.
    30. "Structural and functional basis of CXCL12 (stromal cell-derived factor-1 alpha) binding to heparin."
      Murphy J.W., Cho Y., Sachpatzidis A., Fan C., Hodsdon M.E., Lolis E.
      J. Biol. Chem. 282:10018-10027(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 22-88 IN COMPLEX WITH HEPARIN DISACCHARIDE I-S, DISULFIDE BONDS, MUTAGENESIS OF ARG-29; ARG-33; 34-PHE-PHE-35; 36-GLU--HIS-38; HIS-46; LYS-48; 52-THR--ALA-56; ARG-62; ARG-68 AND GLN-69.
    31. "Crystal structure of recombinant human stromal cell-derived factor-1alpha."
      Ryu E.K., Kim T.G., Kwon T.H., Jung I.D., Ryu D., Park Y.M., Kim J., Ahn K.H., Ban C.
      Proteins 67:1193-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-89, DISULFIDE BONDS, MUTAGENESIS OF LYS-22.
    32. "Structural basis of CXCR4 sulfotyrosine recognition by the chemokine SDF-1/CXCL12."
      Veldkamp C.T., Seibert C., Peterson F.C., De la Cruz N.B., Haugner J.C. III, Basnet H., Sakmar T.P., Volkman B.F.
      Sci. Signal. 1:RA4-RA4(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 22-89 OF MUTANT CYS-57 AND CYS-86 IN COMPLEX WITH CXCR4 FRAGMENT, SUBUNIT, DIMERIZATION, DISULFIDE BONDS, MUTAGENESIS OF ARG-41; HIS-46; LYS-48; VAL-60; ARG-62; ARG-68; VAL-70; GLU-81; GLU-84 AND LYS-85.
    33. Cited for: STRUCTURE BY NMR OF 22-89, ASSAY ON RAT ISCHEMIA/REPERFUSION MODEL, DIMERIZATION, DISULFIDE BONDS.
    34. "Solution structure of human SDF1-alpha H25R."
      Ziarek J.J., Veldkamp C.T., Peterson F.C., Volkman B.F.
      Submitted (SEP-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 22-89, DISULFIDE BONDS.
    35. "Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family."
      Murphy J.W., Yuan H., Kong Y., Xiong Y., Lolis E.J.
      Proteins 78:1331-1337(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 22-88, DIMERIZATION.

    Entry informationi

    Entry nameiSDF1_HUMAN
    AccessioniPrimary (citable) accession number: P48061
    Secondary accession number(s): B2R4G0
    , E7EVL0, H7BYN8, Q2L985, Q2L986, Q2L988, Q5IT36, Q6ICW0, Q9H554
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 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, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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