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Q16627

- CCL14_HUMAN

UniProt

Q16627 - CCL14_HUMAN

Protein

C-C motif chemokine 14

Gene

CCL14

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

    Has weak activities on human monocytes and acts via receptors that also recognize MIP-1 alpha. It induced intracellular Ca2+ changes and enzyme release, but no chemotaxis, at concentrations of 100-1,000 nM, and was inactive on T-lymphocytes, neutrophils, and eosinophil leukocytes. Enhances the proliferation of CD34 myeloid progenitor cells. The processed form HCC-1(9-74) is a chemotactic factor that attracts monocytes eosinophils, and T-cells and is a ligand for CCR1, CCR3 and CCR5.1 Publication

    GO - Biological processi

    1. cell chemotaxis Source: GOC
    2. cellular calcium ion homeostasis Source: ProtInc
    3. immune response Source: InterPro
    4. positive regulation of cell proliferation Source: ProtInc

    Keywords - Molecular functioni

    Cytokine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-C motif chemokine 14
    Alternative name(s):
    Chemokine CC-1/CC-3
    Short name:
    HCC-1/HCC-3
    HCC-1(1-74)
    NCC-2
    Small-inducible cytokine A14
    Cleaved into the following 3 chains:
    Gene namesi
    Name:CCL14
    Synonyms:NCC2, SCYA14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:10612. CCL14.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35545.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19193 PublicationsAdd
    BLAST
    Chaini20 – 9374C-C motif chemokine 14PRO_0000005204Add
    BLAST
    Chaini22 – 9372HCC-1(3-74)PRO_0000005205Add
    BLAST
    Chaini23 – 9371HCC-1(4-74)PRO_0000005206Add
    BLAST
    Chaini28 – 9366HCC-1(9-74)PRO_0000005207Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi26 – 261O-linked (GalNAc...); partial1 Publication
    Disulfide bondi35 ↔ 59
    Disulfide bondi36 ↔ 75

    Post-translational modificationi

    The N-terminal processed forms HCC-1(3-74), HCC-1(4-74) and HCC-1(9-74) are produced in small amounts by proteolytic cleavage after secretion in blood.
    HCC-1(1-74), but not HCC-1(3-74) and HCC-1(4-74), is partially O-glycosylated; the O-linked glycan consists of one Gal-GalNAc disaccharide, further modified by two N-acetylneuraminic acids.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ16627.
    PRIDEiQ16627.

    PTM databases

    PhosphoSiteiQ16627.

    Expressioni

    Tissue specificityi

    Expressed constitutively in several normal tissues: spleen, liver, skeletal and heart muscle, gut, and bone marrow, present at high concentrations (1-80 nM) in plasma.1 Publication

    Gene expression databases

    BgeeiQ16627.
    CleanExiHS_CCL14.
    GenevestigatoriQ16627.

    Organism-specific databases

    HPAiCAB004423.
    HPA030268.

    Interactioni

    Protein-protein interaction databases

    BioGridi112261. 5 interactions.
    DIPiDIP-5861N.
    IntActiQ16627. 4 interactions.
    STRINGi9606.ENSP00000409197.

    Structurei

    Secondary structure

    1
    93
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 353
    Helixi46 – 483
    Beta strandi49 – 546
    Beta strandi59 – 613
    Beta strandi64 – 685
    Beta strandi73 – 764
    Helixi81 – 9010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q8RX-ray1.82E/F/G/H28-93[»]
    2Q8TX-ray2.23A/B/C/D20-93[»]
    ProteinModelPortaliQ16627.
    SMRiQ16627. Positions 28-93.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16627.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG84308.
    HOGENOMiHOG000036685.
    HOVERGENiHBG017871.
    InParanoidiQ16627.
    KOiK05514.
    OMAiVVKIQLK.
    PhylomeDBiQ16627.
    TreeFamiTF334888.

    Family and domain databases

    InterProiIPR000827. Chemokine_CC_CS.
    IPR001811. Chemokine_IL8-like_dom.
    [Graphical view]
    PfamiPF00048. IL8. 1 hit.
    [Graphical view]
    SMARTiSM00199. SCY. 1 hit.
    [Graphical view]
    SUPFAMiSSF54117. SSF54117. 1 hit.
    PROSITEiPS00472. SMALL_CYTOKINES_CC. 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 HCC-1 (identifier: Q16627-1) [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

    MKISVAAIPF FLLITIALGT KTESSSRGPY HPSECCFTYT TYKIPRQRIM   50
    DYYETNSQCS KPGIVFITKR GHSVCTNPSD KWVQDYIKDM KEN 93
    Length:93
    Mass (Da):10,678
    Last modified:November 1, 1997 - v1
    Checksum:iDDDB899DC9148836
    GO
    Isoform HCC-3 (identifier: Q16627-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         27-27: R → QTGGKPKVVKIQLKLVG

    Note: No experimental confirmation available.

    Show »
    Length:109
    Mass (Da):12,297
    Checksum:i73591D5CFF6D3C28
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti61 – 611K → E.
    Corresponds to variant rs16971802 [ dbSNP | Ensembl ].
    VAR_048707

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei27 – 271R → QTGGKPKVVKIQLKLVG in isoform HCC-3. 1 PublicationVSP_001060

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49270 mRNA. Translation: CAA89264.1.
    Z70292 mRNA. Translation: CAA94307.1.
    Z70293 mRNA. Translation: CAA94309.1.
    Z49269 Genomic DNA. Translation: CAA89263.1.
    AF088219 Genomic DNA. Translation: AAC63329.1.
    AF088219 Genomic DNA. Translation: AAF23982.1.
    CH471147 Genomic DNA. Translation: EAW80105.1.
    CH471147 Genomic DNA. Translation: EAW80106.1.
    CH471147 Genomic DNA. Translation: EAW80107.1.
    CH471147 Genomic DNA. Translation: EAW80108.1.
    BC038289 mRNA. Translation: AAH38289.1.
    BC045165 mRNA. Translation: AAH45165.1.
    CCDSiCCDS32624.1. [Q16627-1]
    CCDS45652.1. [Q16627-2]
    RefSeqiNP_116738.1. NM_032962.4. [Q16627-2]
    NP_116739.1. NM_032963.3. [Q16627-1]
    UniGeneiHs.272493.
    Hs.740501.

    Genome annotation databases

    GeneIDi6358.
    KEGGihsa:6358.
    UCSCiuc010wcq.1. human. [Q16627-2]
    uc010wcr.1. human. [Q16627-1]

    Polymorphism databases

    DMDMi2493670.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    CCL14 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49270 mRNA. Translation: CAA89264.1 .
    Z70292 mRNA. Translation: CAA94307.1 .
    Z70293 mRNA. Translation: CAA94309.1 .
    Z49269 Genomic DNA. Translation: CAA89263.1 .
    AF088219 Genomic DNA. Translation: AAC63329.1 .
    AF088219 Genomic DNA. Translation: AAF23982.1 .
    CH471147 Genomic DNA. Translation: EAW80105.1 .
    CH471147 Genomic DNA. Translation: EAW80106.1 .
    CH471147 Genomic DNA. Translation: EAW80107.1 .
    CH471147 Genomic DNA. Translation: EAW80108.1 .
    BC038289 mRNA. Translation: AAH38289.1 .
    BC045165 mRNA. Translation: AAH45165.1 .
    CCDSi CCDS32624.1. [Q16627-1 ]
    CCDS45652.1. [Q16627-2 ]
    RefSeqi NP_116738.1. NM_032962.4. [Q16627-2 ]
    NP_116739.1. NM_032963.3. [Q16627-1 ]
    UniGenei Hs.272493.
    Hs.740501.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q8R X-ray 1.82 E/F/G/H 28-93 [» ]
    2Q8T X-ray 2.23 A/B/C/D 20-93 [» ]
    ProteinModelPortali Q16627.
    SMRi Q16627. Positions 28-93.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112261. 5 interactions.
    DIPi DIP-5861N.
    IntActi Q16627. 4 interactions.
    STRINGi 9606.ENSP00000409197.

    PTM databases

    PhosphoSitei Q16627.

    Polymorphism databases

    DMDMi 2493670.

    Proteomic databases

    PaxDbi Q16627.
    PRIDEi Q16627.

    Protocols and materials databases

    DNASUi 6358.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6358.
    KEGGi hsa:6358.
    UCSCi uc010wcq.1. human. [Q16627-2 ]
    uc010wcr.1. human. [Q16627-1 ]

    Organism-specific databases

    CTDi 6358.
    GeneCardsi GC17M034343.
    H-InvDB HIX0039168.
    HGNCi HGNC:10612. CCL14.
    HPAi CAB004423.
    HPA030268.
    MIMi 601392. gene.
    neXtProti NX_Q16627.
    PharmGKBi PA35545.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG84308.
    HOGENOMi HOG000036685.
    HOVERGENi HBG017871.
    InParanoidi Q16627.
    KOi K05514.
    OMAi VVKIQLK.
    PhylomeDBi Q16627.
    TreeFami TF334888.

    Miscellaneous databases

    EvolutionaryTracei Q16627.
    GenomeRNAii 6358.
    NextBioi 24696.
    PROi Q16627.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16627.
    CleanExi HS_CCL14.
    Genevestigatori Q16627.

    Family and domain databases

    InterProi IPR000827. Chemokine_CC_CS.
    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.
    PROSITEi PS00472. SMALL_CYTOKINES_CC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HCC-1), PROTEIN SEQUENCE OF 20-93.
      Tissue: Bone marrow.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HCC-1 AND HCC-3), TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "Organization of the chemokine gene cluster on human chromosome 17q11.2 containing the genes for CC chemokine MPIF-1, HCC-2, LEC, and RANTES."
      Nomiyama H., Fukuda S., Iio M., Tanase S., Miura R., Yoshie O.
      J. Interferon Cytokine Res. 19:227-234(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 HCC-1).
      Tissue: Pancreas and Spleen.
    6. "Posttranslationally processed forms of the human chemokine HCC-1."
      Richter R., Schulz-Knappe P., John H., Forssmann W.-G.
      Biochemistry 39:10799-10805(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-32, IDENTIFICATION OF HCC-1(3-74) AND HCC-1(4-74), IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT SER-26.
    7. "Natural proteolytic processing of hemofiltrate CC chemokine 1 generates a potent CC chemokine receptor (CCR)1 and CCR5 agonist with anti-HIV properties."
      Detheux M., Staendker L., Vakili J., Muench J., Forssmann U., Adermann K., Poehlmann S., Vassart G., Kirchhoff F., Parmentier M., Forssmann W.-G.
      J. Exp. Med. 192:1501-1508(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-48, IDENTIFICATION OF HCC-1(9-74), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 28-93.

    Entry informationi

    Entry nameiCCL14_HUMAN
    AccessioniPrimary (citable) accession number: Q16627
    Secondary accession number(s): E1P649, E1P650, Q13954
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 130 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3