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P01236

- PRL_HUMAN

UniProt

P01236 - PRL_HUMAN

Protein

Prolactin

Gene

PRL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Prolactin acts primarily on the mammary gland by promoting lactation.

    GO - Molecular functioni

    1. prolactin receptor binding Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. cell surface receptor signaling pathway Source: ProtInc
    3. female pregnancy Source: ProtInc
    4. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
    5. lactation Source: UniProtKB-KW
    6. positive regulation of JAK-STAT cascade Source: BHF-UCL
    7. regulation of multicellular organism growth Source: BHF-UCL

    Keywords - Molecular functioni

    Hormone

    Keywords - Biological processi

    Lactation

    Enzyme and pathway databases

    ReactomeiREACT_111133. Growth hormone receptor signaling.
    REACT_115697. Prolactin receptor signaling.
    REACT_75925. Amyloids.
    SignaLinkiP01236.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolactin
    Short name:
    PRL
    Gene namesi
    Name:PRL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9445. PRL.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi157 – 1571G → D, F, L, N, R, V or Y: Inhibits signaling via PRLR; mutant PRL acts as PRLR antagonist. 1 Publication

    Organism-specific databases

    PharmGKBiPA33790.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28282 PublicationsAdd
    BLAST
    Chaini29 – 227199ProlactinPRO_0000032916Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 391 Publication
    Modified residuei54 – 541PhosphoserineBy similarity
    Glycosylationi59 – 591N-linked (GlcNAc...); partial
    Modified residuei62 – 621PhosphoserineBy similarity
    Disulfide bondi86 ↔ 2021 Publication
    Modified residuei118 – 1181PhosphoserineBy similarity
    Modified residuei163 – 1631Phosphoserine1 Publication
    Modified residuei194 – 1941Phosphoserine1 Publication
    Disulfide bondi219 ↔ 2271 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP01236.
    PRIDEiP01236.

    PTM databases

    PhosphoSiteiP01236.

    Miscellaneous databases

    PMAP-CutDBP01236.

    Expressioni

    Gene expression databases

    ArrayExpressiP01236.
    BgeeiP01236.
    CleanExiHS_PRL.
    GenevestigatoriP01236.

    Organism-specific databases

    HPAiCAB023353.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRLRP16471-74EBI-6903064,EBI-6903057

    Protein-protein interaction databases

    BioGridi111602. 2 interactions.
    DIPiDIP-59635N.
    IntActiP01236. 1 interaction.
    STRINGi9606.ENSP00000302150.

    Structurei

    Secondary structure

    1
    227
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 344
    Helixi43 – 7230
    Turni73 – 753
    Helixi78 – 825
    Turni87 – 904
    Helixi97 – 1026
    Helixi105 – 11814
    Helixi120 – 13112
    Beta strandi133 – 1353
    Helixi138 – 16528
    Beta strandi166 – 1683
    Helixi181 – 1855
    Helixi189 – 22335

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RW5NMR-A29-227[»]
    2Q98X-ray2.70A38-227[»]
    3D48X-ray2.50P40-227[»]
    3EW3X-ray3.80A39-227[»]
    3MZGX-ray2.10A43-227[»]
    3N06X-ray2.00A43-227[»]
    3N0PX-ray2.10A43-227[»]
    3NCBX-ray2.10A43-227[»]
    3NCCX-ray2.50A43-227[»]
    3NCEX-ray2.00A43-227[»]
    3NCFX-ray2.80A43-227[»]
    3NPZX-ray3.35A29-227[»]
    ProteinModelPortaliP01236.
    SMRiP01236. Positions 29-227.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01236.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the somatotropin/prolactin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG47376.
    HOGENOMiHOG000264241.
    HOVERGENiHBG104895.
    KOiK05439.
    OMAiYSVWSGL.
    OrthoDBiEOG74FF24.
    PhylomeDBiP01236.
    TreeFamiTF332592.

    Family and domain databases

    Gene3Di1.20.1250.10. 1 hit.
    InterProiIPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR001400. Somatotropin.
    IPR018116. Somatotropin_CS.
    [Graphical view]
    PANTHERiPTHR11417. PTHR11417. 1 hit.
    PfamiPF00103. Hormone_1. 1 hit.
    [Graphical view]
    PRINTSiPR00836. SOMATOTROPIN.
    SUPFAMiSSF47266. SSF47266. 1 hit.
    PROSITEiPS00266. SOMATOTROPIN_1. 1 hit.
    PS00338. SOMATOTROPIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01236-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIKGSPWKG SLLLLLVSNL LLCQSVAPLP ICPGGAARCQ VTLRDLFDRA    50
    VVLSHYIHNL SSEMFSEFDK RYTHGRGFIT KAINSCHTSS LATPEDKEQA 100
    QQMNQKDFLS LIVSILRSWN EPLYHLVTEV RGMQEAPEAI LSKAVEIEEQ 150
    TKRLLEGMEL IVSQVHPETK ENEIYPVWSG LPSLQMADEE SRLSAYYNLL 200
    HCLRRDSHKI DNYLKLLKCR IIHNNNC 227
    Length:227
    Mass (Da):25,876
    Last modified:July 21, 1986 - v1
    Checksum:i952BBA1B6A955527
    GO

    Sequence cautioni

    The sequence CAA38264.1 differs from that shown. Reason: Frameshift at position 8.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421T → A in AAB70858. (PubMed:9266104)Curated
    Sequence conflicti110 – 1112SL → VS AA sequence (PubMed:925136)Curated
    Sequence conflicti113 – 1142VS → L AA sequence (PubMed:925136)Curated
    Sequence conflicti118 – 1181S → P in AAB70858. (PubMed:9266104)Curated
    Sequence conflicti148 – 1481E → Q in BAA00312. (PubMed:6146607)Curated
    Sequence conflicti172 – 1721N → D AA sequence (PubMed:925136)Curated
    Sequence conflicti190 – 1912ES → SE AA sequence (PubMed:925136)Curated
    Sequence conflicti206 – 2061D → H in AAA60173. (PubMed:6146607)Curated
    Sequence conflicti206 – 2061D → H in BAA00312. (PubMed:6146607)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00566 mRNA. Translation: CAA23829.1.
    X00540
    , X00541, X00543, X00544 Genomic DNA. Translation: CAA25214.1.
    X54393 mRNA. Translation: CAA38263.1. Frameshift.
    X54393 mRNA. Translation: CAA38264.1. Frameshift.
    BC015850 mRNA. Translation: AAH15850.1.
    M29386 mRNA. Translation: AAA60173.1.
    D00411 mRNA. Translation: BAA00312.1.
    U75583 mRNA. Translation: AAB70858.1.
    CCDSiCCDS4548.1.
    PIRiA61402.
    A90998. LCHU.
    RefSeqiNP_000939.1. NM_000948.5.
    NP_001157030.1. NM_001163558.2.
    UniGeneiHs.1905.
    Hs.735971.

    Genome annotation databases

    EnsembliENST00000306482; ENSP00000302150; ENSG00000172179.
    GeneIDi5617.
    KEGGihsa:5617.
    UCSCiuc003ndp.3. human.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Prolactin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00566 mRNA. Translation: CAA23829.1 .
    X00540
    , X00541 , X00543 , X00544 Genomic DNA. Translation: CAA25214.1 .
    X54393 mRNA. Translation: CAA38263.1 . Frameshift.
    X54393 mRNA. Translation: CAA38264.1 . Frameshift.
    BC015850 mRNA. Translation: AAH15850.1 .
    M29386 mRNA. Translation: AAA60173.1 .
    D00411 mRNA. Translation: BAA00312.1 .
    U75583 mRNA. Translation: AAB70858.1 .
    CCDSi CCDS4548.1.
    PIRi A61402.
    A90998. LCHU.
    RefSeqi NP_000939.1. NM_000948.5.
    NP_001157030.1. NM_001163558.2.
    UniGenei Hs.1905.
    Hs.735971.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RW5 NMR - A 29-227 [» ]
    2Q98 X-ray 2.70 A 38-227 [» ]
    3D48 X-ray 2.50 P 40-227 [» ]
    3EW3 X-ray 3.80 A 39-227 [» ]
    3MZG X-ray 2.10 A 43-227 [» ]
    3N06 X-ray 2.00 A 43-227 [» ]
    3N0P X-ray 2.10 A 43-227 [» ]
    3NCB X-ray 2.10 A 43-227 [» ]
    3NCC X-ray 2.50 A 43-227 [» ]
    3NCE X-ray 2.00 A 43-227 [» ]
    3NCF X-ray 2.80 A 43-227 [» ]
    3NPZ X-ray 3.35 A 29-227 [» ]
    ProteinModelPortali P01236.
    SMRi P01236. Positions 29-227.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111602. 2 interactions.
    DIPi DIP-59635N.
    IntActi P01236. 1 interaction.
    STRINGi 9606.ENSP00000302150.

    PTM databases

    PhosphoSitei P01236.

    Proteomic databases

    PaxDbi P01236.
    PRIDEi P01236.

    Protocols and materials databases

    DNASUi 5617.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306482 ; ENSP00000302150 ; ENSG00000172179 .
    GeneIDi 5617.
    KEGGi hsa:5617.
    UCSCi uc003ndp.3. human.

    Organism-specific databases

    CTDi 5617.
    GeneCardsi GC06M022230.
    HGNCi HGNC:9445. PRL.
    HPAi CAB023353.
    MIMi 176760. gene.
    neXtProti NX_P01236.
    PharmGKBi PA33790.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47376.
    HOGENOMi HOG000264241.
    HOVERGENi HBG104895.
    KOi K05439.
    OMAi YSVWSGL.
    OrthoDBi EOG74FF24.
    PhylomeDBi P01236.
    TreeFami TF332592.

    Enzyme and pathway databases

    Reactomei REACT_111133. Growth hormone receptor signaling.
    REACT_115697. Prolactin receptor signaling.
    REACT_75925. Amyloids.
    SignaLinki P01236.

    Miscellaneous databases

    ChiTaRSi PRL. human.
    EvolutionaryTracei P01236.
    GeneWikii Prolactin.
    GenomeRNAii 5617.
    NextBioi 21828.
    PMAP-CutDB P01236.
    PROi P01236.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01236.
    Bgeei P01236.
    CleanExi HS_PRL.
    Genevestigatori P01236.

    Family and domain databases

    Gene3Di 1.20.1250.10. 1 hit.
    InterProi IPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR001400. Somatotropin.
    IPR018116. Somatotropin_CS.
    [Graphical view ]
    PANTHERi PTHR11417. PTHR11417. 1 hit.
    Pfami PF00103. Hormone_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00836. SOMATOTROPIN.
    SUPFAMi SSF47266. SSF47266. 1 hit.
    PROSITEi PS00266. SOMATOTROPIN_1. 1 hit.
    PS00338. SOMATOTROPIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human prolactin. cDNA structural analysis and evolutionary comparisons."
      Cooke N.E., Coit D., Shine J., Baxter J.D., Martial J.A.
      J. Biol. Chem. 256:4007-4016(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Isolation and characterization of the human prolactin gene."
      Truong A.T., Duez C., Belayew A., Renard A., Pictet R.L., Bell G.I., Martial J.A.
      EMBO J. 3:429-437(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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].
      Tissue: Testis.
    5. "Molecular cloning and nucleotide sequence of DNA complementary to human decidual prolactin mRNA."
      Takahashi H., Nabeshima Y., Nabeshima Y., Ogata K., Takeuchi S.
      J. Biochem. 95:1491-1499(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-227.
    6. "Expression of the prolactin gene in normal and neoplastic human breast tissues and human mammary cell lines: promoter usage and alternative mRNA splicing."
      Shaw-Bruha C.M., Pirrucello S.J., Shull J.D.
      Breast Cancer Res. Treat. 44:243-253(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-201.
      Tissue: Mammary gland.
    7. "Human pituitary prolactin (hPRL): the entire linear amino acid sequence."
      Shome B., Parlow A.F.
      J. Clin. Endocrinol. Metab. 45:1112-1115(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-227.
    8. "High sensitivity automated sequence determination of polypeptides."
      Jacobs J.W., Niall H.D.
      J. Biol. Chem. 250:3629-3636(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-53.
    9. "Immunoglobulin G subclasses and prolactin (PRL) isoforms in macroprolactinemia due to anti-PRL autoantibodies."
      Hattori N., Ikekubo K., Nakaya Y., Kitagawa K., Inagaki C.
      J. Clin. Endocrinol. Metab. 90:3036-3044(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-163 AND SER-194.
    10. "The tertiary structure and backbone dynamics of human prolactin."
      Keeler C., Dannies P.S., Hodsdon M.E.
      J. Mol. Biol. 328:1105-1121(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 29-227.
    11. Cited for: STRUCTURE BY NMR OF 29-227, INTERACTION WITH PRLR.
    12. "Structural and thermodynamic bases for the design of pure prolactin receptor antagonists: X-ray structure of Del1-9-G129R-hPRL."
      Jomain J.-B., Tallet E., Broutin I., Hoos S., van Agthoven J., Ducruix A., Kelly P.A., Kragelund B.B., England P., Goffin V.
      J. Biol. Chem. 282:33118-33131(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 38-227, MUTAGENESIS OF GLY-157.
    13. "Crystal structure of a prolactin receptor antagonist bound to the extracellular domain of the prolactin receptor."
      Svensson L.A., Bondensgaard K., Noerskov-Lauritsen L., Christensen L., Becker P., Andersen M.D., Maltesen M.J., Rand K.D., Breinholt J.
      J. Biol. Chem. 283:19085-19094(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 41-227 IN COMPLEX WITH PRLR, IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BONDS.

    Entry informationi

    Entry nameiPRL_HUMAN
    AccessioniPrimary (citable) accession number: P01236
    Secondary accession number(s): Q15199, Q92996
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 153 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 6
      Human chromosome 6: 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