Descriptions

HSPA8 (or hsc70) is a heat shock cognate protein involved in many cellular processes. During recovery from stress, HSPA8, initially accumulating in the nucleoplasm for folding/refolding of proteins, transiently concentrates in nucleoli for nucleolar morphology and function restoration. The inhibitory region is positioned at one of the three domains of HSPA8 protein, which is the N-terminal ATPase domain, specifically in residues 263-287 of domain IIB. Under normal growth conditions, the constitutive nucleolar targeting function that is provided by residues 225-262 is diminished by the autoinhibitory element located in residues 263-287. When cells recover from stress, the autoinhibitory element is inactivated, and the constitutive nucleolar targeting function restores.

Autoinhibitory domains (AIDs)

Target domain

225-262 (Nucleolar targeting region)

Relief mechanism

Others

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

45 structures for P0DMV8

Entry ID Method Resolution Chain Position Source
1HJO X-ray 230 A A 3-382 PDB
1S3X X-ray 184 A A 1-382 PDB
1XQS X-ray 290 A C/D 184-371 PDB
2E88 X-ray 180 A A 1-388 PDB
2E8A X-ray 177 A A 1-388 PDB
2LMG NMR - A 537-610 PDB
3A8Y X-ray 230 A A/B 1-388 PDB
3ATU X-ray 165 A A 1-388 PDB
3ATV X-ray 158 A A 1-388 PDB
3AY9 X-ray 175 A A 1-388 PDB
3D2E X-ray 235 A B/D 1-382 PDB
3D2F X-ray 230 A B/D 1-382 PDB
3JXU X-ray 214 A A 1-387 PDB
3LOF X-ray 240 A A/B/C/D/E/F 534-641 PDB
3Q49 X-ray 154 A C 634-641 PDB
4IO8 X-ray 258 A A 1-382 PDB
4J8F X-ray 270 A A 1-382 PDB
4PO2 X-ray 200 A A/B 386-613 PDB
4WV5 X-ray 204 A A/B 395-543 PDB
4WV7 X-ray 242 A A/B 395-543 PDB
5AQW X-ray 153 A A 1-380 PDB
5AQX X-ray 212 A A 1-380 PDB
5AQY X-ray 156 A A 1-380 PDB
5AQZ X-ray 165 A A 1-380 PDB
5AR0 X-ray 190 A A 1-380 PDB
5BN8 X-ray 134 A A 1-388 PDB
5BN9 X-ray 169 A A 1-388 PDB
5BPL X-ray 193 A A 1-388 PDB
5BPM X-ray 183 A A 1-388 PDB
5BPN X-ray 210 A A 1-388 PDB
5GJJ NMR - A 385-641 PDB
5MKR X-ray 187 A A 1-380 PDB
5MKS X-ray 199 A A 1-380 PDB
5XI9 NMR - A 381-564 PDB
5XIR NMR - A 381-564 PDB
6FHK X-ray 166 A A/B 1-381 PDB
6G3R X-ray 140 A A 3-382 PDB
6G3S X-ray 230 A A 3-382 PDB
6JPV X-ray 215 A A/B 395-537 PDB
6K39 X-ray 140 A A/B 395-537 PDB
6ZYI X-ray 152 A A 4-381 PDB
7FGM X-ray 220 A A 1-382 PDB
7KW7 EM 357 A C/D 1-641 PDB
7Q4R X-ray 179 A A 1-380 PDB
AF-P0DMV8-F1 Predicted AlphaFoldDB

347 variants for P0DMV8

Variant ID(s) Position Change Description Diseaes Association Provenance
VAR_029053
RCV000856574
rs562047
110 E>D Chronic obstructive pulmonary disease [ClinVar] Yes ClinVar
UniProt
1000Genomes
ExAC
dbSNP
gnomAD
rs748557276 2 A>V No ExAC
TOPMed
gnomAD
rs1336701870 3 K>T No gnomAD
COSM3861840 4 A>S Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA Cosmic
rs987547251 4 A>T No TOPMed
gnomAD
rs1381532215 5 A>E No TOPMed
gnomAD
rs1381532215 5 A>G No TOPMed
gnomAD
TCGA novel 5 A>V Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
rs912379394 6 A>V No TOPMed
gnomAD
rs778220828 7 I>M No ExAC
TOPMed
gnomAD
rs747251905 8 G>R No ExAC
TOPMed
gnomAD
rs771342261 9 I>M No ExAC
gnomAD
COSM1312020 10 D>N Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA Cosmic
TCGA novel 11 L>P Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
rs769712470 12 G>D No ExAC
TOPMed
gnomAD
rs1815912754 13 T>P No TOPMed
rs1815913009 14 T>P No TOPMed
gnomAD
rs1815913262 15 Y>C No TOPMed
rs367576856 16 S>C No ESP
ExAC
TOPMed
gnomAD
rs367576856 16 S>F No ESP
ExAC
TOPMed
gnomAD
rs200520712 16 S>P No Ensembl
rs367576856 16 S>Y No ESP
ExAC
TOPMed
gnomAD
rs1815914575 17 C>S No gnomAD
rs202172229 18 V>M No ESP
ExAC
TOPMed
gnomAD
rs753411347 20 V>A No ExAC
TOPMed
gnomAD
rs753411347 20 V>G No ExAC
TOPMed
gnomAD
rs766060629 20 V>L No ExAC
gnomAD
rs368507842 21 F>I No ESP
ExAC
gnomAD
rs764614987 22 Q>R No ExAC
gnomAD
rs758776902 28 I>S No ExAC
TOPMed
gnomAD
rs758776902 28 I>T No ExAC
TOPMed
gnomAD
rs199499427 30 A>T No TOPMed
rs1409537221 31 N>K No TOPMed
gnomAD
rs1815920158 32 D>N No Ensembl
rs1344138338 34 G>R No gnomAD
rs1344138338 34 G>S Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
gnomAD
rs757670500 36 R>C No ExAC
TOPMed
rs1472074191 36 R>H No Ensembl
rs781585045 37 T>A No ExAC
TOPMed
gnomAD
rs1815921080 37 T>I No Ensembl
rs746034999 38 T>S No ExAC
gnomAD
rs1815922210 39 P>S No TOPMed
gnomAD
rs1815922210 39 P>T No TOPMed
gnomAD
rs779938408 40 S>N Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No ExAC
NCI-TCGA
gnomAD
rs1249226560 40 S>R No gnomAD
rs1581710998 40 S>R No Ensembl
rs1489709990 42 V>M No TOPMed
rs1266531928 43 A>D No Ensembl
rs1221488262 44 F>L No TOPMed
rs749373372 45 T>M No ExAC
gnomAD
rs749373372 45 T>R No ExAC
gnomAD
rs201204185 48 E>K No 1000Genomes
TOPMed
gnomAD
rs1171408004 52 G>R No TOPMed
gnomAD
rs1328718689 55 A>S No gnomAD
rs1815926718 55 A>V No Ensembl
rs759046329 56 K>N No ExAC
gnomAD
rs2151471288 56 K>R No Ensembl
rs764821183 57 N>H No ExAC
gnomAD
rs752211354 58 Q>* No 1000Genomes
ExAC
gnomAD
rs2151471308 60 A>S No Ensembl
rs762517250 60 A>V Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No ExAC
NCI-TCGA
gnomAD
rs1319000912 62 N>D No TOPMed
gnomAD
rs1292804428 63 P>S No Ensembl
rs752061501 64 Q>H No ExAC
gnomAD
rs757725542 69 D>E No ExAC
TOPMed
gnomAD
rs1239107980 69 D>H No gnomAD
rs1456284629 70 A>G No TOPMed
gnomAD
rs1489033064 70 A>T No gnomAD
rs750670211 71 K>N No ExAC
gnomAD
rs780318868 72 R>L No ExAC
TOPMed
gnomAD
rs780318868 72 R>Q No ExAC
TOPMed
gnomAD
rs756347651 72 R>W Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No ExAC
NCI-TCGA
gnomAD
rs1043620 74 I>M No 1000Genomes
ExAC
TOPMed
gnomAD
rs1378872651 75 G>V No gnomAD
rs777711495 76 R>C No 1000Genomes
ExAC
gnomAD
rs777711495 76 R>S No 1000Genomes
ExAC
gnomAD
rs1815937213 79 G>S No Ensembl
rs1581711620 80 D>* No Ensembl
rs1815938244 81 P>L No TOPMed
rs1325643642 81 P>S No gnomAD
rs1445970278 84 Q>L No gnomAD
rs1306780874 85 S>L No gnomAD
rs1306780874 85 S>W No gnomAD
rs1365914703 86 D>A No gnomAD
rs2151471537 87 M>I No Ensembl
rs1355637110 87 M>K No gnomAD
rs1235703632 87 M>L No gnomAD
rs1355637110 87 M>T No gnomAD
rs1312515387 89 H>R No Ensembl
rs1581711753 90 W>R No Ensembl
rs1408858916 91 P>A No TOPMed
gnomAD
rs1815943230 93 Q>E No Ensembl
rs1217315817 95 I>M No TOPMed
rs759366790 96 N>S No ExAC
gnomAD
rs2151471592 97 D>G No 1000Genomes
rs1815944033 97 D>N No Ensembl
rs1562350759 98 G>R No Ensembl
rs1385821034 103 V>L No TOPMed
gnomAD
rs1385821034 103 V>M No TOPMed
gnomAD
rs775181598 104 Q>E No ExAC
gnomAD
rs1815946301 106 S>R No Ensembl
rs1253114194 109 G>R No gnomAD
rs1236730785 111 T>S No gnomAD
rs1441999499 112 K>N No gnomAD
rs1581711912 112 K>R No Ensembl
rs1815948387 113 A>V No Ensembl
rs1815948651 114 F>L No TOPMed
rs1183006115 114 F>Y No gnomAD
rs1378520531 115 Y>C No Ensembl
rs1378520531 115 Y>S No Ensembl
rs1175766859 116 P>R No TOPMed
rs1456613441 117 E>* No gnomAD
rs1392557673 117 E>D No Ensembl
rs1456613441 117 E>K No gnomAD
TCGA novel 118 E>G Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
rs1165027921 122 M>V No gnomAD
rs1581712034 125 T>S No Ensembl
rs1815951295 126 K>Q No Ensembl
rs1815951880 132 E>Q No Ensembl
rs1464449378 144 I>T No Ensembl
rs1581712121 145 T>P No Ensembl
rs1338293191 153 S>T No gnomAD
rs1246559171 158 T>I No gnomAD
rs1815956218 163 V>M No Ensembl
rs1316794009 169 V>M No gnomAD
rs1198560256 174 N>S No gnomAD
rs1196709808 183 Y>H No gnomAD
rs916283384 184 G>S No gnomAD
rs1422262645 186 D>G No gnomAD
rs1189928425 188 T>R No gnomAD
rs1402284965 194 N>Y No gnomAD
rs2151471869 195 V>G No Ensembl
rs1339464388 225 D>N No gnomAD
rs1216182922 237 L>V No gnomAD
rs2151471916 242 V>G No Ensembl
rs1309731120 245 F>L No gnomAD
rs1279580121 245 F>V No gnomAD
rs1255739575 258 R>* No gnomAD
rs1213273451 322 R>C No gnomAD
rs1258418503 324 A>T No gnomAD
rs1421764976 342 R>C No gnomAD
rs1429024081 346 V>M No gnomAD
rs1375714124 357 R>C No gnomAD
rs1313269531 360 N>K No gnomAD
rs1359459553 365 P>S No gnomAD
rs1562351234 367 E>D No Ensembl
rs1397777494 368 A>D No gnomAD
rs1215663509 372 G>R No gnomAD
rs1310970727 374 A>V No gnomAD
rs1486270856 381 M>I No gnomAD
rs1265100476 383 D>N No gnomAD
rs1265100476 383 D>Y No gnomAD
rs1417449856 401 L>V No gnomAD
rs1160157291 405 T>M No gnomAD
rs1366059433 426 Q>* No gnomAD
rs1443779332 433 D>N No gnomAD
rs1304595645 434 N>S No 1000Genomes
gnomAD
rs1815972723 435 Q>* No Ensembl
rs1376676573 436 P>A No gnomAD
rs1815973235 437 G>E No Ensembl
rs1238236912 441 Q>* No gnomAD
rs1815975176 448 A>T No gnomAD
rs1396152164 450 T>R No Ensembl
rs1401010615 453 N>D No Ensembl
rs1300779102 455 L>M No Ensembl
rs1469749122 458 R>H No gnomAD
TCGA novel 463 G>D Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
rs1815977372 463 G>R No TOPMed
rs1815977610 464 I>M No TOPMed
rs1437656390 466 P>L No gnomAD
rs578191843 466 P>S No 1000Genomes
ExAC
gnomAD
rs1292976696 467 A>V No gnomAD
rs1178742095 468 P>S No gnomAD
rs1408175188 469 R>K No gnomAD
rs1815979750 475 E>K No TOPMed
rs1404429075 478 F>L No TOPMed
gnomAD
rs1482895124 479 D>N No gnomAD
rs1815981568 481 D>V No gnomAD
rs1815982010 484 G>D No Ensembl
TCGA novel 484 G>V Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
rs1327237373 487 N>S No gnomAD
rs1815983089 489 T>A No Ensembl
rs1483873641 489 T>K No Ensembl
rs1483873641 489 T>M No Ensembl
rs1203357768 490 A>T No gnomAD
rs1815984199 490 A>V No Ensembl
rs1376607623 491 T>K No gnomAD
rs1376607623 491 T>M No gnomAD
rs1204291632 492 D>V No Ensembl
rs1339946518 493 K>E No TOPMed
gnomAD
rs1228015319 494 S>R No gnomAD
rs1310627419 495 T>I No gnomAD
rs1310627419 495 T>N No gnomAD
rs1815986853 496 G>S No Ensembl
TCGA novel 498 A>T Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
rs1214232421 498 A>V No gnomAD
rs1339381396 499 N>D No TOPMed
gnomAD
rs768054024 499 N>K No ExAC
TOPMed
gnomAD
rs762351513 499 N>S No 1000Genomes
ExAC
gnomAD
rs1472247171 505 N>K No gnomAD
rs1352667739 506 D>E No TOPMed
rs1815989301 506 D>N No gnomAD
rs1419380472 509 R>C No TOPMed
gnomAD
rs1475279596 509 R>H No gnomAD
rs1169353073 510 L>P No gnomAD
rs1165566788 512 K>E No TOPMed
gnomAD
rs750819847 515 I>M No 1000Genomes
ExAC
gnomAD
rs1366756759 516 E>K No gnomAD
rs1366756759 516 E>Q No gnomAD
rs1471784258 516 E>V No gnomAD
rs1331268437 517 R>C No gnomAD
rs1331268437 517 R>G No gnomAD
rs1815993032 517 R>H No TOPMed
gnomAD
rs1428864215 518 M>I No gnomAD
rs1269307670 518 M>T No 1000Genomes
gnomAD
rs754012082 518 M>V No ExAC
gnomAD
rs1354992180 519 V>M No TOPMed
rs1311355981 522 A>V No gnomAD
rs1233905003 524 K>* No gnomAD
rs755082889 527 A>G No ExAC
gnomAD
rs755082889 527 A>V No ExAC
gnomAD
rs1398159966 528 E>K No gnomAD
rs778899955 529 D>N No ExAC
gnomAD
rs1259104378 530 E>Q No gnomAD
rs1192248244 531 V>A No gnomAD
rs1485814751 531 V>M No gnomAD
TCGA novel
rs1815998208
533 R>C Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
TOPMed
rs1815998208 533 R>G No TOPMed
rs1420904860 533 R>H No gnomAD
rs1170216525 534 E>K No gnomAD
rs1170216525 534 E>Q No gnomAD
rs1815999244 535 R>G No Ensembl
rs1334364454 535 R>K No gnomAD
rs746965839 536 V>A No 1000Genomes
ExAC
gnomAD
rs1420655259 536 V>L No gnomAD
rs757246842 537 S>* No ExAC
gnomAD
rs757246842 537 S>L No ExAC
gnomAD
rs1816001057 538 A>S No gnomAD
rs1816001470 541 A>V No Ensembl
TCGA novel 542 L>P Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
rs781188477 545 Y>* No ExAC
gnomAD
rs1391567883 546 A>G No TOPMed
gnomAD
rs1816002137 546 A>P No Ensembl
rs1387888207 547 F>L No gnomAD
rs1816002927 549 M>R No gnomAD
rs2151472605 551 S>N No Ensembl
rs769578848 552 A>P No ExAC
gnomAD
rs769578848 552 A>T No ExAC
gnomAD
rs1816004460 553 V>G No gnomAD
rs768292679 553 V>L No ExAC
TOPMed
gnomAD
rs768292679 553 V>M No ExAC
TOPMed
gnomAD
rs774061665 554 E>K No ExAC
TOPMed
gnomAD
rs2151472645 555 D>G No 1000Genomes
rs1448287629 555 D>N No gnomAD
rs761403622 557 G>R No ExAC
TOPMed
gnomAD
rs144685460 559 K>E No ESP
ExAC
TOPMed
gnomAD
rs144685460 559 K>Q No ESP
ExAC
TOPMed
gnomAD
rs1816006775 560 G>D No Ensembl
rs1816007180 562 I>V No Ensembl
rs374175801 563 S>R No 1000Genomes
ESP
ExAC
TOPMed
gnomAD
rs1435535907 564 E>A No gnomAD
rs1054002904 564 E>K Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No Ensembl
NCI-TCGA
rs147878843 565 A>S No ESP
ExAC
TOPMed
gnomAD
TCGA novel 565 A>V Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
rs1402458557 566 D>N No TOPMed
gnomAD
rs1319690589 567 K>N No Ensembl
rs752811220 567 K>R No ExAC
rs1330403100 568 K>R No gnomAD
rs758495885 569 K>E No ExAC
TOPMed
gnomAD
rs781009367 569 K>M No ExAC
TOPMed
gnomAD
rs779947748 572 D>H No ExAC
gnomAD
rs779947748 572 D>N No ExAC
gnomAD
rs1288553034 576 E>D No gnomAD
rs768464421 577 V>I No ExAC
gnomAD
rs1192350091 578 I>V No gnomAD
rs774143469 579 S>L No ExAC
TOPMed
gnomAD
rs1816013353
COSM1443377
579 S>P large_intestine [Cosmic] No cosmic curated
Ensembl
rs1816014126 581 L>M No TOPMed
rs747719061 581 L>P No ExAC
gnomAD
rs771552351 582 D>E No ExAC
TOPMed
gnomAD
rs1389477837 584 N>K No TOPMed
rs1362206200 585 T>I No TOPMed
gnomAD
rs1362206200 585 T>S No TOPMed
gnomAD
rs1816015866 586 L>S No TOPMed
rs777027010 588 E>K Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No ExAC
NCI-TCGA
TOPMed
gnomAD
rs199729109 590 D>E No ExAC
gnomAD
rs540214133 592 F>S No 1000Genomes
ExAC
TOPMed
gnomAD
rs1816017235 593 E>D No TOPMed
rs750353273 597 K>N No ExAC
TOPMed
gnomAD
rs764197379 597 K>T No ExAC
gnomAD
rs1562352410 598 E>D No gnomAD
rs756128298 599 L>V No ExAC
gnomAD
rs1185418612 601 Q>E No TOPMed
gnomAD
rs754807027 602 V>M No ExAC
rs778721578 603 C>G No ExAC
gnomAD
rs747768908 604 N>K No ExAC
gnomAD
rs777286374 605 P>R No ExAC
rs771512819 605 P>S No 1000Genomes
ExAC
gnomAD
rs746476471 606 I>L No ExAC
gnomAD
rs777114966 606 I>M No ExAC
gnomAD
rs771505399 606 I>T No ExAC
gnomAD
rs759946698 609 G>* No ExAC
TOPMed
gnomAD
rs759946698 609 G>R No ExAC
TOPMed
gnomAD
rs1301796206 612 Q>H No TOPMed
TCGA novel 614 A>V Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
rs763188460 615 G>D No ExAC
gnomAD
rs775724932 615 G>S No ExAC
TOPMed
gnomAD
rs1448701811 616 G>V No TOPMed
gnomAD
rs764202242 617 P>A No ExAC
TOPMed
gnomAD
TCGA novel 617 P>S Variant assessed as Somatic; HIGH impact. [NCI-TCGA] No NCI-TCGA
rs764202242 617 P>T No ExAC
TOPMed
gnomAD
rs761795494 618 G>E No ExAC
gnomAD
rs751703293 618 G>R No ExAC
TOPMed
gnomAD
rs1293405502 619 P>L No TOPMed
gnomAD
rs753771041 619 P>S No ExAC
gnomAD
rs754825210 620 G>R No ExAC
gnomAD
rs1227397377 620 G>V No gnomAD
rs752313605 621 G>S No ExAC
TOPMed
gnomAD
rs758117058 621 G>V No ExAC
gnomAD
rs777256711 622 F>I No ExAC
TOPMed
gnomAD
rs746592204 622 F>L No ExAC
TOPMed
gnomAD
rs1418727739 623 G>E No gnomAD
rs770410665 623 G>R No ExAC
TOPMed
gnomAD
COSM3861843 623 G>W Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA Cosmic
rs1816029389 624 A>T No Ensembl
COSM1077722 626 G>C Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA Cosmic
rs1816030246 627 P>H No TOPMed
gnomAD
rs781669728 629 G>V No ExAC
gnomAD
rs2151473110 631 S>P No Ensembl
rs2151473115 631 S>Y No Ensembl
rs1462251279 632 G>V Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA
gnomAD
rs529162552 633 S>* No 1000Genomes
ExAC
gnomAD
rs2151473130 633 S>A No Ensembl
rs529162552 633 S>L No 1000Genomes
ExAC
gnomAD
rs1473531749 634 G>D No TOPMed
rs1816031274 634 G>S No TOPMed
rs1816031724 635 P>S No TOPMed
rs775974928 636 T>A No ExAC
gnomAD
rs1312926887 636 T>I No gnomAD
rs1816033265 637 I>M No TOPMed
rs1816033046 637 I>T No Ensembl
rs1562352786 638 E>D No Ensembl
COSM1312022 638 E>K Variant assessed as Somatic; MODERATE impact. [NCI-TCGA] No NCI-TCGA Cosmic
rs1293990368 639 E>V No gnomAD
rs1309787748 640 V>I No gnomAD
rs768990311 641 D>Y No ExAC
TOPMed
gnomAD
rs1937393256 642 D>L No TOPMed

1 associated diseases with P0DMV8

Without disease ID

3 regional properties for P0DMV8

Type Name Position InterPro Accession
conserved_site Heat shock protein 70, conserved site 9 - 16 IPR018181-1
conserved_site Heat shock protein 70, conserved site 197 - 210 IPR018181-2
conserved_site Heat shock protein 70, conserved site 334 - 348 IPR018181-3

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
  • Secreted
  • Localized in cytoplasmic mRNP granules containing untranslated mRNAs
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

22 GO annotations of cellular component

Name Definition
aggresome An inclusion body formed by dynein-dependent retrograde transport of an aggregated protein on microtubules.
blood microparticle A phospholipid microvesicle that is derived from any of several cell types, such as platelets, blood cells, endothelial cells, or others, and contains membrane receptors as well as other proteins characteristic of the parental cell. Microparticles are heterogeneous in size, and are characterized as microvesicles free of nucleic acids.
centriole A cellular organelle, found close to the nucleus in many eukaryotic cells, consisting of a small cylinder with microtubular walls, 300-500 nm long and 150-250 nm in diameter. It contains nine short, parallel, peripheral microtubular fibrils, each fibril consisting of one complete microtubule fused to two incomplete microtubules. Cells usually have two centrioles, lying at right angles to each other. At division, each pair of centrioles generates another pair and the twin pairs form the pole of the mitotic spindle.
centrosome A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
extracellular exosome A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
ficolin-1-rich granule lumen Any membrane-enclosed lumen that is part of a ficolin-1-rich granule.
focal adhesion A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).
inclusion body A discrete intracellular part formed of aggregated molecules such as proteins or other biopolymers.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
nuclear speck A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
ribonucleoprotein complex A macromolecular complex that contains both RNA and protein molecules.
vesicle Any small, fluid-filled, spherical organelle enclosed by membrane.

23 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction
ATP-dependent protein disaggregase activity An ATP-dependent molecular chaperone activity that mediates the solubilization of ordered protein aggregates.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
C3HC4-type RING finger domain binding Binding to a C3HC4-type zinc finger domain of a protein. The C3HC4-type zinc finger is a variant of RING finger, is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence
cadherin binding Binding to cadherin, a type I membrane protein involved in cell adhesion.
death receptor agonist activity Interacting with a death receptor such that the proportion of death receptors in an active form is increased. Ligand binding to a death receptor often induces a conformational change to activate the receptor.
denatured protein binding Binding to a denatured protein.
disordered domain specific binding Binding to a disordered domain of a protein.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
G protein-coupled receptor binding Binding to a G protein-coupled receptor.
heat shock protein binding Binding to a heat shock protein, a protein synthesized or activated in response to heat shock.
histone deacetylase binding Binding to histone deacetylase.
misfolded protein binding Binding to a misfolded protein.
protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process.
receptor ligand activity The activity of a gene product that interacts with a receptor to effect a change in the activity of the receptor. Ligands may be produced by the same, or different, cell that expresses the receptor. Ligands may diffuse extracellularly from their point of origin to the receiving cell, or remain attached to an adjacent cell surface (e.g. Notch ligands).
RNA binding Binding to an RNA molecule or a portion thereof.
signaling receptor binding Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
transcription corepressor activity A transcription coregulator activity that represses or decreases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription corepressors modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators.
transcription regulator inhibitor activity A molecular function regulator that inhibits the activity of a transcription regulator via direct binding and/or post-translational modification.
ubiquitin protein ligase binding Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.
unfolded protein binding Binding to an unfolded protein.
virus receptor activity Combining with a virus component and mediating entry of the virus into the cell.

35 GO annotations of biological process

Name Definition
ATP metabolic process The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator.
cellular heat acclimation Any process that increases heat tolerance of a cell in response to high temperatures.
cellular response to heat Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
cellular response to oxidative stress Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
cellular response to steroid hormone stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a steroid hormone stimulus.
cellular response to unfolded protein Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.
chaperone cofactor-dependent protein refolding The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.
chaperone-mediated protein complex assembly The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
lysosomal transport The directed movement of substances into, out of or within a lysosome.
mRNA catabolic process The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes.
negative regulation of apoptotic process Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
negative regulation of cell growth Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
negative regulation of cell population proliferation Any process that stops, prevents or reduces the rate or extent of cell proliferation.
negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Any process that stops, prevents or reduces the frequency, rate or extent of an endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway.
negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Any process that stops, prevents or reduces the frequency, rate or extent of extrinsic apoptotic signaling pathway in absence of ligand.
negative regulation of inclusion body assembly Any process that decreases the rate, frequency, or extent of inclusion body assembly. Inclusion body assembly is the aggregation, arrangement and bonding together of a set of components to form an inclusion body.
negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Any process that stops, prevents or reduces the frequency, rate or extent of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway.
negative regulation of protein ubiquitination Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein.
negative regulation of transcription by RNA polymerase II Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II.
negative regulation of transforming growth factor beta receptor signaling pathway Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
positive regulation of endoribonuclease activity Any process that activates or increases the frequency, rate or extent of endoribonuclease activity.
positive regulation of erythrocyte differentiation Any process that activates or increases the frequency, rate or extent of erythrocyte differentiation.
positive regulation of gene expression Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).
positive regulation of interleukin-8 production Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
positive regulation of microtubule nucleation Any process that increases the rate, frequency or extent of microtubule nucleation. Microtubule nucleation is the 'de novo' formation of a microtubule, in which tubulin heterodimers form metastable oligomeric aggregates, some of which go on to support formation of a complete microtubule. Microtubule nucleation usually occurs from a specific site within a cell.
positive regulation of NF-kappaB transcription factor activity Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.
positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway Any process that activates or increases the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing 2 (NOD2) pathway.
positive regulation of proteasomal ubiquitin-dependent protein catabolic process Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
positive regulation of RNA splicing Any process that activates or increases the frequency, rate or extent of RNA splicing.
positive regulation of tumor necrosis factor-mediated signaling pathway Any process that activates or increases the frequency, rate or extent of tumor necrosis factor-mediated signaling pathway.
protein refolding The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
protein stabilization Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
regulation of mitotic spindle assembly Any process that modulates the frequency, rate or extent of mitotic spindle assembly.
regulation of protein ubiquitination Any process that modulates the frequency, rate or extent of the addition of ubiquitin groups to a protein.
response to unfolded protein Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.

57 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P19120 HSPA8 Heat shock cognate 71 kDa protein Bos taurus (Bovine) SS
Q2YDD0 HSPA14 Heat shock 70 kDa protein 14 Bos taurus (Bovine) SS
P0CB32 HSPA1L Heat shock 70 kDa protein 1-like Bos taurus (Bovine) SS
Q27975 HSPA1A Heat shock 70 kDa protein 1A Bos taurus (Bovine) SS
O73885 HSPA8 Heat shock cognate 71 kDa protein Gallus gallus (Chicken) SS
E1C2P3 HSPA14 Heat shock 70 kDa protein 14 Gallus gallus (Chicken) SS
P08106 Heat shock 70 kDa protein Gallus gallus (Chicken) SS
P77319 hscC Chaperone protein HscC Escherichia coli (strain K12) PR
P0A6Y8 dnaK Chaperone protein DnaK Escherichia coli (strain K12) SS
P29843 Hsc70-1 Heat shock 70 kDa protein cognate 1 Drosophila melanogaster (Fruit fly) SS
P02825 Hsp70Ab Major heat shock 70 kDa protein Ab Drosophila melanogaster (Fruit fly) SS
P82910 Hsp70Aa Major heat shock 70 kDa protein Aa Drosophila melanogaster (Fruit fly) SS
Q8INI8 Hsp70Ba Major heat shock 70 kDa protein Ba Drosophila melanogaster (Fruit fly) SS
Q9BIR7 Hsp70Bc Major heat shock 70 kDa protein Bc Drosophila melanogaster (Fruit fly) SS
Q9BIS2 Hsp70Bb Major heat shock 70 kDa protein Bb Drosophila melanogaster (Fruit fly) SS
O97125 Hsp68 Heat shock protein 68 Drosophila melanogaster (Fruit fly) SS
P11146 Hsc70-2 Heat shock 70 kDa protein cognate 2 Drosophila melanogaster (Fruit fly) SS
P11147 Hsc70-4 Heat shock 70 kDa protein cognate 4 Drosophila melanogaster (Fruit fly) SS
Q9VG58 Hsp70Bbb Major heat shock 70 kDa protein Bbb Drosophila melanogaster (Fruit fly) SS
Q96MM6 HSPA12B Heat shock 70 kDa protein 12B Homo sapiens (Human) PR
O43301 HSPA12A Heat shock 70 kDa protein 12A Homo sapiens (Human) PR
P0DMV9 HSPA1B Heat shock 70 kDa protein 1B Homo sapiens (Human) SS
P17066 HSPA6 Heat shock 70 kDa protein 6 Homo sapiens (Human) SS
P34931 HSPA1L Heat shock 70 kDa protein 1-like Homo sapiens (Human) SS
P54652 HSPA2 Heat shock-related 70 kDa protein 2 Homo sapiens (Human) SS
Q0VDF9 HSPA14 Heat shock 70 kDa protein 14 Homo sapiens (Human) SS
P38646 HSPA9 Stress-70 protein, mitochondrial Homo sapiens (Human) SS
P11021 HSPA5 Endoplasmic reticulum chaperone BiP Homo sapiens (Human) SS
P11142 HSPA8 Heat shock cognate 71 kDa protein Homo sapiens (Human) EV
P48741 HSPA7 Putative heat shock 70 kDa protein 7 Homo sapiens (Human) SS
P11143 HSP70 Heat shock 70 kDa protein Zea mays (Maize) SS
P16627 Hspa1l Heat shock 70 kDa protein 1-like Mus musculus (Mouse) SS
P63017 Hspa8 Heat shock cognate 71 kDa protein Mus musculus (Mouse) SS
Q99M31 Hspa14 Heat shock 70 kDa protein 14 Mus musculus (Mouse) SS
Q8K0U4 Hspa12a Heat shock 70 kDa protein 12A Mus musculus (Mouse) PR
P17156 Hspa2 Heat shock-related 70 kDa protein 2 Mus musculus (Mouse) SS
Q9CZJ2 Hspa12b Heat shock 70 kDa protein 12B Mus musculus (Mouse) PR
P17879 Hspa1b Heat shock 70 kDa protein 1B Mus musculus (Mouse) SS
Q61696 Hspa1a Heat shock 70 kDa protein 1A Mus musculus (Mouse) SS
Q6S4N2 HSPA1B Heat shock 70 kDa protein 1B Sus scrofa (Pig) SS
P14659 Hspa2 Heat shock-related 70 kDa protein 2 Rattus norvegicus (Rat) SS
P63018 Hspa8 Heat shock cognate 71 kDa protein Rattus norvegicus (Rat) SS
P55063 Hspa1l Heat shock 70 kDa protein 1-like Rattus norvegicus (Rat) SS
P0DMW0 Hspa1a Heat shock 70 kDa protein 1A Rattus norvegicus (Rat) SS
P0DMW1 Hspa1b Heat shock 70 kDa protein 1B Rattus norvegicus (Rat) SS
P09446 hsp-1 Heat shock protein hsp-1 Caenorhabditis elegans SS
P26413 HSP70 Heat shock 70 kDa protein Glycine max (Soybean) (Glycine hispida) SS
O65719 HSP70-3 Heat shock 70 kDa protein 3 Arabidopsis thaliana (Mouse-ear cress) SS
P22954 HSP70-2 Heat shock 70 kDa protein 2 Arabidopsis thaliana (Mouse-ear cress) SS
Q9C7X7 HSP70-18 Heat shock 70 kDa protein 18 Arabidopsis thaliana (Mouse-ear cress) SS
Q9LHA8 HSP70-4 Heat shock 70 kDa protein 4 Arabidopsis thaliana (Mouse-ear cress) SS
Q9S9N1 HSP70-5 Heat shock 70 kDa protein 5 Arabidopsis thaliana (Mouse-ear cress) SS
P22953 HSP70-1 Heat shock 70 kDa protein 1 Arabidopsis thaliana (Mouse-ear cress) SS
P24629 HSC-I Heat shock cognate 70 kDa protein 1 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
P27322 HSC-2 Heat shock cognate 70 kDa protein 2 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
Q5RGE6 hspa14 Heat shock 70 kDa protein 14 Danio rerio (Zebrafish) (Brachydanio rerio) SS
Q90473 hspa8 Heat shock cognate 71 kDa protein Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
70 80 90 100 110 120
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS
130 140 150 160 170 180
SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
190 200 210 220 230 240
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH
250 260 270 280 290 300
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
310 320 330 340 350 360
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
370 380 390 400 410 420
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
430 440 450 460 470 480
PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
490 500 510 520 530 540
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN
550 560 570 580 590 600
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
610 620 630 640
QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D