Protein:PRLR |
Protein Summary |
 Gene summary |
| Gene name: PRLR | ASpdb.0 ID: 5618 | Gene | Gene symbol | PRLR | Gene ID | 5618 |
| Gene name | prolactin receptor |
| Synonyms | HPRL|MFAB|RI-PRLR|hPRLrI |
| Cytomap | 5p13.2 |
| Type of gene | protein-coding |
| Description | prolactin receptorhPRL receptorsecreted prolactin binding protein |
| Modification date | 20240411 |
| UniProtAcc | P16471 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | PRLR | GO:0004925 | prolactin receptor activity | 10585417 |
| Gene | PRLR | GO:0007171 | activation of transmembrane receptor protein tyrosine kinase activity | 10585417 |
| Gene | PRLR | GO:0009986 | cell surface | 10585417 |
| Gene | PRLR | GO:0042976 | activation of Janus kinase activity | 10585417 |
| Gene | PRLR | GO:0043066 | negative regulation of apoptotic process | 10585417 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P16471-1 | P16471-1_3n06_B.pdb | 3N06 | X-ray | 2.0 | B | 26 | 230 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P16471 | PRLR | P16471-1 | P16471-2 | 622 | 521 | 24 | 124 | Deletion | none | none | 23 | 23 |
| P16471 | PRLR | P16471-1 | P16471-3 | 622 | 230 | 229 | 230 | Substitution | DF | AW | 229 | 230 |
| P16471 | PRLR | P16471-1 | P16471-3 | 622 | 230 | 231 | 622 | Deletion | none | none | 230 | 230 |
| P16471 | PRLR | P16471-1 | P16471-4 | 622 | 376 | 338 | 376 | Substitution | MKPTYLDPDTDSGRGSCDSPSLLSEKCEEPQANPSTFYD | DPLMLGASHYKNLKSYRPRKISSQGRLAVFTKATLTTVQ | 338 | 376 |
| P16471 | PRLR | P16471-1 | P16471-4 | 622 | 376 | 377 | 622 | Deletion | none | none | 376 | 376 |
| P16471 | PRLR | P16471-1 | P16471-5 | 622 | 349 | 337 | 349 | Substitution | GMKPTYLDPDTDS | EREQRQAQEARDS | 337 | 349 |
| P16471 | PRLR | P16471-1 | P16471-5 | 622 | 349 | 350 | 622 | Deletion | none | none | 349 | 349 |
| P16471 | PRLR | P16471-1 | P16471-6 | 622 | 288 | 286 | 288 | Substitution | KGK | VTP | 286 | 288 |
| P16471 | PRLR | P16471-1 | P16471-6 | 622 | 288 | 289 | 622 | Deletion | none | none | 288 | 288 |
| P16471 | PRLR | P16471-1 | P16471-7 | 622 | 268 | 229 | 268 | Substitution | DFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIF | GDPLMLGASHYKNLKSYRPRKISSQGRLAVFTKATLTTVQ | 229 | 268 |
| P16471 | PRLR | P16471-1 | P16471-7 | 622 | 268 | 269 | 622 | Deletion | none | none | 268 | 268 |
| P16471 | PRLR | P16471-1 | P16471-8 | 622 | 217 | 1 | 71 | Deletion | none | none | 0 | 0 |
| P16471 | PRLR | P16471-1 | P16471-8 | 622 | 217 | 286 | 288 | Substitution | KGK | VTP | 215 | 217 |
| P16471 | PRLR | P16471-1 | P16471-8 | 622 | 217 | 289 | 622 | Deletion | none | none | 217 | 217 |
| P16471 | PRLR | P16471-1 | P16471-9 | 622 | 309 | 286 | 309 | Substitution | KGKSEELLSALGCQDFPPTSDYED | DRLCTPGRCCVSTGLTDLDYSCST | 286 | 309 |
| P16471 | PRLR | P16471-1 | P16471-9 | 622 | 309 | 310 | 622 | Deletion | none | none | 309 | 309 |
| Multiple sequence alignment of our canonical and alternatively spliced PRLR |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of PRLR |
| UniProt-id | ENSG | ENST | ENSP |
| P16471-1 | ENSG00000113494.17 | ENST00000618457.5 | ENSP00000482954.1 |
| P16471-2 | ENSG00000113494.17 | ENST00000511486.5 | ENSP00000422556.1 |
| P16471-2 | ENSG00000113494.17 | ENST00000620785.4 | ENSP00000482689.1 |
| P16471-4 | ENSG00000113494.17 | ENST00000231423.7 | ENSP00000231423.3 |
| P16471-4 | ENSG00000113494.17 | ENST00000542609.5 | ENSP00000441813.2 |
| P16471-5 | ENSG00000113494.17 | ENST00000310101.9 | ENSP00000309008.5 |
| P16471-5 | ENSG00000113494.17 | ENST00000619676.4 | ENSP00000484768.1 |
| P16471-6 | ENSG00000113494.17 | ENST00000509140.5 | ENSP00000425300.2 |
| P16471-6 | ENSG00000113494.17 | ENST00000513753.5 | ENSP00000424841.1 |
| P16471-7 | ENSG00000113494.17 | ENST00000348262.7 | ENSP00000311613.3 |
| P16471-7 | ENSG00000113494.17 | ENST00000514088.5 | ENSP00000422935.2 |
| UniProt-id | NM ID | NP ID |
| P16471-1 | NM_000949.6 | NP_000940.1 |
| P16471-1 | XM_006714484.2 | XP_006714547.1 |
| P16471-1 | XM_011514068.2 | XP_011512370.1 |
| P16471-2 | NM_001204314.2 | NP_001191243.1 |
| P16471-4 | NM_001204316.1 | NP_001191245.1 |
| P16471-5 | NM_001204315.1 | NP_001191244.1 |
| P16471-6 | NM_001204317.1 | NP_001191246.1 |
| P16471-7 | NM_001204318.1 | NP_001191247.1 |
| Amino acid sequences of our canonical and alternatively spliced PRLR |
| accession_id | Protein sequence |
| P16471-1 | MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGK QYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEW EIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIFPP VPGPKIKGFDAHLLEKGKSEELLSALGCQDFPPTSDYEDLLVEYLEVDDSEDQHLMSVHSKEHPSQGMKPTYLDPDTDSGRGSCDSPSLL SEKCEEPQANPSTFYDPEVIEKPENPETTHTWDPQCISMEGKIPYFHAGGSKCSTWPLPQPSQHNPRSSYHNITDVCELAVGPAGAPATL LNEAGKDALKSSQTIKSREEGKATQQREVESFHSETDQDTPWLLPQEKTPFGSAKPLDYVEIHKVNKDGALSLLPKQRENSGKPKKPGTP |
| P16471-2 | MKENVASATVFTLLLFLNTCLLNVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEWEIHFAGQQTEF KILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIFPPVPGPKIKGFDA HLLEKGKSEELLSALGCQDFPPTSDYEDLLVEYLEVDDSEDQHLMSVHSKEHPSQGMKPTYLDPDTDSGRGSCDSPSLLSEKCEEPQANP STFYDPEVIEKPENPETTHTWDPQCISMEGKIPYFHAGGSKCSTWPLPQPSQHNPRSSYHNITDVCELAVGPAGAPATLLNEAGKDALKS SQTIKSREEGKATQQREVESFHSETDQDTPWLLPQEKTPFGSAKPLDYVEIHKVNKDGALSLLPKQRENSGKPKKPGTPENNKEYAKVSG |
| P16471-3 | MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGK QYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEW |
| P16471-4 | MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGK QYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEW EIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIFPP VPGPKIKGFDAHLLEKGKSEELLSALGCQDFPPTSDYEDLLVEYLEVDDSEDQHLMSVHSKEHPSQGDPLMLGASHYKNLKSYRPRKISS |
| P16471-5 | MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGK QYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEW EIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIFPP |
| P16471-6 | MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGK QYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEW EIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIFPP |
| P16471-7 | MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGK QYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEW |
| P16471-8 | MHECPDYITGGPNSCHFGKQYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKT GWFTLLYEIRLKPEKAAEWEIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLI |
| P16471-9 | MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGK QYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEW EIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIFPP |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| PRLR (go to UniProt):P16471 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P16471 | Topological domain | 25 | 234 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=24;End=124 |
| P16471 | Topological domain | 25 | 234 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=229;End=230 |
| P16471 | Topological domain | 25 | 234 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=231;End=622 |
| P16471 | Topological domain | 25 | 234 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=229;End=268 |
| P16471 | Topological domain | 25 | 234 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=1;End=71 |
| P16471 | Transmembrane | 235 | 258 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=231;End=622 |
| P16471 | Transmembrane | 235 | 258 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=229;End=268 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=231;End=622 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=338;End=376 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=377;End=622 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=337;End=349 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=350;End=622 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=286;End=288 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=289;End=622 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=229;End=268 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=269;End=622 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=286;End=288 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=289;End=622 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=286;End=309 |
| P16471 | Topological domain | 259 | 622 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=310;End=622 |
| P16471 | Domain | 27 | 128 | Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Deletion;Start=24;End=124 |
| P16471 | Domain | 27 | 128 | Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Deletion;Start=1;End=71 |
| P16471 | Domain | 129 | 229 | Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Substitution;Start=229;End=230 |
| P16471 | Domain | 129 | 229 | Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Substitution;Start=229;End=268 |
| P16471 | Region | 326 | 378 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=231;End=622 |
| P16471 | Region | 326 | 378 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=338;End=376 |
| P16471 | Region | 326 | 378 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=377;End=622 |
| P16471 | Region | 326 | 378 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=337;End=349 |
| P16471 | Region | 326 | 378 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=350;End=622 |
| P16471 | Region | 326 | 378 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=289;End=622 |
| P16471 | Region | 326 | 378 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=269;End=622 |
| P16471 | Region | 326 | 378 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=289;End=622 |
| P16471 | Region | 326 | 378 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=310;End=622 |
| P16471 | Region | 461 | 505 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=231;End=622 |
| P16471 | Region | 461 | 505 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=377;End=622 |
| P16471 | Region | 461 | 505 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=350;End=622 |
| P16471 | Region | 461 | 505 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=289;End=622 |
| P16471 | Region | 461 | 505 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=269;End=622 |
| P16471 | Region | 461 | 505 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=289;End=622 |
| P16471 | Region | 461 | 505 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=310;End=622 |
| P16471 | Region | 520 | 545 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=231;End=622 |
| P16471 | Region | 520 | 545 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=377;End=622 |
| P16471 | Region | 520 | 545 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=350;End=622 |
| P16471 | Region | 520 | 545 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=289;End=622 |
| P16471 | Region | 520 | 545 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=269;End=622 |
| P16471 | Region | 520 | 545 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=289;End=622 |
| P16471 | Region | 520 | 545 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=310;End=622 |
| P16471 | Motif | 267 | 275 | Note=Box 1 motif | Type=Deletion;Start=231;End=622 |
| P16471 | Motif | 267 | 275 | Note=Box 1 motif | Type=Substitution;Start=229;End=268 |
| P16471 | Motif | 267 | 275 | Note=Box 1 motif | Type=Deletion;Start=269;End=622 |
| P16471 | Compositional bias | 462 | 485 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=231;End=622 |
| P16471 | Compositional bias | 462 | 485 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=377;End=622 |
| P16471 | Compositional bias | 462 | 485 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=350;End=622 |
| P16471 | Compositional bias | 462 | 485 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=289;End=622 |
| P16471 | Compositional bias | 462 | 485 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=269;End=622 |
| P16471 | Compositional bias | 462 | 485 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=289;End=622 |
| P16471 | Compositional bias | 462 | 485 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=310;End=622 |
Gene Isoform Structures and Expression Levels for PRLR |
| Gene structures of our canonical and alternative spliced genes of PRLR * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of P16471-1 |
| 3D view using mol* of P16471-2 |
| 3D view using mol* of P16471-3 |
| 3D view using mol* of P16471-4 |
| 3D view using mol* of P16471-5 |
| 3D view using mol* of P16471-6 |
| 3D view using mol* of P16471-7 |
| 3D view using mol* of P16471-8 |
| 3D view using mol* of P16471-9 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of P16471-1 |
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| pLDDT distribution across the protein length of P16471-2 |
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| pLDDT distribution across the protein length of P16471-3 |
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| pLDDT distribution across the protein length of P16471-4 |
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| pLDDT distribution across the protein length of P16471-5 |
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| pLDDT distribution across the protein length of P16471-6 |
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| pLDDT distribution across the protein length of P16471-7 |
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| pLDDT distribution across the protein length of P16471-8 |
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| pLDDT distribution across the protein length of P16471-9 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of P16471-1 |
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| Ramachandran plot of P16471-2 |
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| Ramachandran plot of P16471-3 |
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| Ramachandran plot of P16471-5 |
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| Ramachandran plot of P16471-7 |
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| Ramachandran plot of P16471-8 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P16471-1 | 1.026 | 161 | 1.093 | 439.383 | 0.566 | 0.642 | 0.856 | 0.802 | 0.714 | 1.123 | 0.985 | 30,31,32,33,34,35,36,37,114,115,116,117,118,119,12 0,123,124,126,214,400,401,402,403,404,405,406 |
| P16471-2 | 0.994 | 159 | 1.052 | 466.137 | 0.607 | 0.617 | 0.806 | 0.75 | 0.792 | 0.946 | 0.984 | 406,407,408,409,411,412,413,415,419,420,421,422,42 3,424,439,440,441,442,443,444,445,446,455,456,457, 459,461,462,465,466 |
| P16471-3 | 0.477 | 17 | 0.432 | 36.015 | 0.809 | 0.472 | 0.553 | 0.048 | 0.734 | 0.065 | 1.94 | 159,165,166,168,187
|
| P16471-4 | 0.766 | 44 | 0.765 | 100.499 | 0.532 | 0.622 | 0.91 | 1.142 | 0.709 | 1.611 | 0.806 | 278,279,280,283,284,286,287,288,289,291,292
|
| P16471-5 | 0.822 | 44 | 0.849 | 91.581 | 0.551 | 0.643 | 0.893 | 1.486 | 0.493 | 3.017 | 1.593 | 279,280,283,284,286,288,291,292
|
| P16471-6 | 0.605 | 27 | 0.581 | 100.156 | 0.853 | 0.537 | 0.685 | 0.383 | 0.705 | 0.543 | 0.412 | 30,31,32,33,35,36,114,115,117,118,119,120,123,124, 126,214 |
| P16471-7 | 0.912 | 67 | 0.956 | 114.905 | 0.528 | 0.64 | 0.885 | 1.492 | 0.606 | 2.463 | 0.514 | 137,139,144,145,146,147,194,195,196,198,226,227,22 8,229,230 |
| P16471-8 | 1.03 | 117 | 1.106 | 288.463 | 0.565 | 0.633 | 0.879 | 1.139 | 0.656 | 1.735 | 0.884 | 1,2,3,4,5,7,15,17,21,22,26,28,29,30,31,32,33,43,46 |
| P16471-9 | 0.453 | 16 | 0.379 | 22.638 | 0.742 | 0.501 | 0.806 | 0.15 | 0.913 | 0.165 | 0.205 | 174,175,176,200,201
|
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
 |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P16471-1_P16471-1_3n06_B.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P16471-1_3n06_B_P16471-2.pdb |
| 3D view using mol* of P16471-1_3n06_B_P16471-3.pdb |
| 3D view using mol* of P16471-1_3n06_B_P16471-4.pdb |
| 3D view using mol* of P16471-1_3n06_B_P16471-5.pdb |
| 3D view using mol* of P16471-1_3n06_B_P16471-6.pdb |
| 3D view using mol* of P16471-1_3n06_B_P16471-7.pdb |
| 3D view using mol* of P16471-1_3n06_B_P16471-8.pdb |
| 3D view using mol* of P16471-1_3n06_B_P16471-9.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P16471-1_P16471-2.pdb |
| 3D view using mol* of P16471-1_P16471-3.pdb |
| 3D view using mol* of P16471-1_P16471-4.pdb |
| 3D view using mol* of P16471-1_P16471-5.pdb |
| 3D view using mol* of P16471-1_P16471-6.pdb |
| 3D view using mol* of P16471-1_P16471-7.pdb |
| 3D view using mol* of P16471-1_P16471-8.pdb |
| 3D view using mol* of P16471-1_P16471-9.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P16471-1_vs_P16471-2.png |
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| ./stats/secondary_structure/figure/P16471-1_vs_P16471-3.png |
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| ./stats/secondary_structure/figure/P16471-1_vs_P16471-4.png |
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| ./stats/secondary_structure/figure/P16471-1_vs_P16471-5.png |
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| ./stats/secondary_structure/figure/P16471-1_vs_P16471-6.png |
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| ./stats/secondary_structure/figure/P16471-1_vs_P16471-7.png |
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| ./stats/secondary_structure/figure/P16471-1_vs_P16471-8.png |
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| ./stats/secondary_structure/figure/P16471-1_vs_P16471-9.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P16471-1_vs_P16471-2.png |
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| ./stats/relative_asa/P16471-1_vs_P16471-3.png |
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| ./stats/relative_asa/P16471-1_vs_P16471-4.png |
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| ./stats/relative_asa/P16471-1_vs_P16471-5.png |
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| ./stats/relative_asa/P16471-1_vs_P16471-6.png |
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| ./stats/relative_asa/P16471-1_vs_P16471-7.png |
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| ./stats/relative_asa/P16471-1_vs_P16471-8.png |
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| ./stats/relative_asa/P16471-1_vs_P16471-9.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to PRLR |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| P16471 | PRLR | DB16220 | Lonapegsomatropin | approved, investigational | ligand |
| P16471 | PRLR | DB00052 | Somatotropin | approved, investigational | ligand |
Related Diseases to PRLR |
| Previous studies relating to the alternative splicing of PRLR and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| PRLR | 24032713 | Histone trimethylation of the p53 gene by expression of a constitutively active prolactin receptor in prostate cancer cells. | Prolactin (PRL) is a pituitary polypeptide hormone characterized by multiple biological actions including stimulation of growth in the prostate, breast and ovarian epithelial cells. A sizable body of reports has presented evidences to indicate the involvement of PRL in the pathogenic process of cancers of the reproductive system, such as prostate and breast cancers. PRL exerts its effects by dimerizing its receptor (PRLR) on the plasma membrane, and initiating cellular Jak-Stat signal pathway. We have previously cloned from prostate cancer cells a natural variant of PRLR in which the S2 subdomain of the extracellular domain is missing (ΔS2). Our preliminary data showed that ΔS2 PRLR was able to dimerize and to constitutively activate the β-casein promoter (in the absence of its ligand, PRL) in breast and prostate epithelial cells. Enhancer of zeste homologue 2 (EZH2), an important histone-modifying enzyme, is able to trimethylate histone 3 on lysine 27 (H3K27Me3), consequently leading to gene silencing, especially silencing of tumor suppressor genes such as p53. We hypothesized that ΔS2 PRLR played an important pathogenic role in prostate cancer through, at least partly, alterations in the expression of EZH2 and the trimethylation of histone 3 on lysine 27. In the present study, overexpression of ΔS2 PRLR in prostate epithelial cells was achieved by infection with an adenoviral vector carrying the cDNA. The viable cell number overexpressing ΔS2 PRLR was assessed using MTS reagent. Western blot, chromatin immunoprecipitation (ChIP) assay and acid histone extraction were applied to detect expression of EZH2 as well as trimethylation of histone 3, respectively. In prostate epithelial cells, overexpression of ΔS2 PRLR increased the levels of EZH2 methyltransferase mRNA and protein, induced EZH2 methyltransferase recruitment to chromatin, increased the trimethylation of histone 3 on lysine 27, and decreased expression of the p53 gene. We concluded that ΔS2 PRLR plays an important pathogenic role in prostate cancer through epigenetic covalent modification leading to chromatin remodeling. Hypertrimethylation on H3K27 of the p53 gene promoter region due to elevated expression of ΔS2 PRLR by alternative splicing of the pre-mRNA in its full-length form might serve as a new mechanism underlying human prostate cancer. | D011471 | Prostatic Neoplasms |
Clinically important variants in PRLR |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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