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

Deletion assay, Mutagenesis experiment

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

39 structures for P11142

Entry ID Method Resolution Chain Position Source
3AGY X-ray 185 A C/D/F 639-646 PDB
3AGZ X-ray 251 A C/D/E/F 639-646 PDB
3ESK X-ray 205 A B 635-646 PDB
3FZF X-ray 220 A A 4-381 PDB
3FZH X-ray 200 A A 4-381 PDB
3FZK X-ray 210 A A 4-381 PDB
3FZL X-ray 220 A A 4-381 PDB
3FZM X-ray 230 A A 4-381 PDB
3LDQ X-ray 190 A A 4-381 PDB
3M3Z X-ray 210 A A 4-381 PDB
4H5N X-ray 186 A A/B 2-384 PDB
4H5R X-ray 164 A A/B 2-384 PDB
4H5T X-ray 190 A A 2-384 PDB
4H5V X-ray 175 A A 2-384 PDB
4H5W X-ray 194 A A/B 2-384 PDB
4HWI X-ray 227 A A 5-381 PDB
4KBQ X-ray 291 A C/D 541-646 PDB
5AQF X-ray 188 A A/C 1-381 PDB
5AQG X-ray 224 A A/C/E 1-381 PDB
5AQH X-ray 200 A A 1-381 PDB
5AQI X-ray 198 A A/C 1-381 PDB
5AQJ X-ray 196 A A/C/E 1-381 PDB
5AQK X-ray 209 A A 1-381 PDB
5AQL X-ray 169 A A/C 1-381 PDB
5AQM X-ray 163 A A/C 1-381 PDB
5AQN X-ray 245 A A/C/E 1-381 PDB
5AQO X-ray 212 A A/C/E 1-381 PDB
5AQP X-ray 208 A A/C/E 1-381 PDB
5AQQ X-ray 272 A A/C/E 1-381 PDB
5AQR X-ray 191 A A/C/E 1-381 PDB
5AQS X-ray 200 A A/C 1-381 PDB
5AQT X-ray 190 A A 1-381 PDB
5AQU X-ray 192 A A 1-381 PDB
5AQV X-ray 175 A A 1-381 PDB
6B1I X-ray 230 A A/B 5-381 PDB
6B1M X-ray 190 A A/B 5-381 PDB
6B1N X-ray 180 A A/B 5-381 PDB
6ZYJ X-ray 185 A A/B 5-384 PDB
AF-P11142-F1 Predicted AlphaFoldDB

211 variants for P11142

Variant ID(s) Position Change Description Diseaes Association Provenance
rs1470313419
CA383061178
3 K>R No ClinGen
TOPMed
CA6332870
rs749485084
5 P>L No ClinGen
ExAC
gnomAD
CA383061165
rs1449602133
5 P>S No ClinGen
TOPMed
gnomAD
CA6332869
rs778022948
6 A>S No ClinGen
ExAC
TOPMed
gnomAD
CA383061058
rs1427745924
22 Q>* No ClinGen
gnomAD
rs1565369691
CA383061008
28 I>M No ClinGen
Ensembl
rs11551602
CA229970012
VAR_049619
32 D>Y No ClinGen
UniProt
Ensembl
dbSNP
rs950960741
CA229969991
41 Y>* No ClinGen
Ensembl
rs765012279
CA6332860
41 Y>C No ClinGen
ExAC
gnomAD
CA229970001
rs75739900
41 Y>H No ClinGen
Ensembl
rs201477863
CA229969960
45 T>M No ClinGen
1000Genomes
gnomAD
CA229969963
rs201477863
45 T>R No ClinGen
1000Genomes
gnomAD
CA383060890
rs1166201725
46 D>E No ClinGen
gnomAD
rs770980780
CA6332854
47 T>A No ClinGen
ExAC
gnomAD
CA383060858
rs376156706
51 I>M No ClinGen
ESP
ExAC
TOPMed
gnomAD
rs1252070613
CA383060792
COSM202734
61 M>T large_intestine [Cosmic] No ClinGen
cosmic curated
TOPMed
rs764381465
CA6332812
73 L>V No ClinGen
ExAC
TOPMed
gnomAD
CA383060600
rs1328280148
87 M>R No ClinGen
gnomAD
CA383060559
rs775043697
92 F>L No ClinGen
ExAC
TOPMed
gnomAD
rs1366901063
CA383060550
93 M>I No ClinGen
gnomAD
CA383060553
rs1445257474
93 M>T No ClinGen
gnomAD
CA383060556
rs1283020583
COSM924154
93 M>V endometrium [Cosmic] No ClinGen
cosmic curated
gnomAD
CA383060539
rs1591439268
95 V>G No ClinGen
Ensembl
rs777228127
CA6332804
96 N>S No ClinGen
ExAC
TOPMed
gnomAD
rs1388306788
CA383060520
98 A>S No ClinGen
gnomAD
rs1591439236
CA383060483
103 V>G No ClinGen
Ensembl
CA6332798
rs766369333
104 Q>R No ClinGen
ExAC
TOPMed
gnomAD
rs200601870
CA6332797
106 E>Q No ClinGen
1000Genomes
ExAC
TOPMed
gnomAD
CA229969389
rs748008431
107 Y>C No ClinGen
Ensembl
CA383060448
rs1464641326
108 K>N No ClinGen
gnomAD
CA229969372
rs781044959
109 G>E No ClinGen
Ensembl
CA383060434
rs760971468
110 E>D No ClinGen
ExAC
TOPMed
gnomAD
rs1289131268
CA383060415
113 S>N No ClinGen
gnomAD
rs11551608
CA229969354
116 P>T No ClinGen
gnomAD
CA229969348
rs879004891
123 V>L No ClinGen
Ensembl
rs1286131382
CA383060309
128 K>R No ClinGen
TOPMed
CA383060296
rs1591439159
130 I>V No ClinGen
Ensembl
CA6332784
rs780873363
132 E>G No ClinGen
ExAC
gnomAD
CA6332785
rs747769427
132 E>Q No ClinGen
ExAC
gnomAD
rs1281904116
CA383060254
136 G>A No ClinGen
TOPMed
CA383060233
rs1591438530
138 T>P No ClinGen
Ensembl
rs774366889
CA6332737
138 T>S No ClinGen
ExAC
gnomAD
rs141156763
CA229968728
140 T>N No ClinGen
1000Genomes
ExAC
TOPMed
rs141156763
CA6332735
140 T>S No ClinGen
1000Genomes
ExAC
TOPMed
rs569651128
CA6332733
141 N>S No ClinGen
ExAC
gnomAD
CA6332732
rs755052827
142 A>V No ClinGen
ExAC
gnomAD
CA229968693
rs11551603
157 A>V No ClinGen
Ensembl
rs11551606
CA229968692
158 T>I No ClinGen
Ensembl
CA383060057
rs1565368756
165 A>P No ClinGen
Ensembl
CA229968654
rs866713011
182 A>S No ClinGen
Ensembl
rs199619043
CA6332698
189 V>G No ClinGen
ExAC
gnomAD
rs775427523
CA6332694
191 A>G No ClinGen
ExAC
gnomAD
rs769624839
CA6332695
191 A>T No ClinGen
ExAC
gnomAD
rs775427523
CA6332693
191 A>V No ClinGen
ExAC
gnomAD
CA6332690
rs779126635
194 N>K No ClinGen
ExAC
TOPMed
gnomAD
rs778283472
CA6332687
209 I>V No ClinGen
ExAC
TOPMed
gnomAD
CA383059678
rs1431250178
220 K>Q No ClinGen
gnomAD
rs11551599
CA6332684
222 T>A No ClinGen
ExAC
gnomAD
CA383059659
rs1402476075
223 A>S No ClinGen
gnomAD
rs1427790009
CA383059567
236 R>* No ClinGen
gnomAD
rs1184917258
CA383059566
236 R>Q No ClinGen
gnomAD
rs536669943
CA6332681
239 N>S No ClinGen
1000Genomes
ExAC
TOPMed
gnomAD
rs765204439
CA229968387
243 A>S No ClinGen
Ensembl
rs1228883118
CA383059458
251 K>E No ClinGen
gnomAD
CA6332674
rs759639896
253 I>V No ClinGen
ExAC
gnomAD
rs1591438086
CA383059421
255 E>D No ClinGen
Ensembl
CA383059380
rs777998627
261 R>S No ClinGen
ExAC
gnomAD
CA383059379
rs777998627
261 R>S No ClinGen
ExAC
gnomAD
COSM42681
CA229968335
rs1003257093
262 R>C central_nervous_system [Cosmic] No ClinGen
cosmic curated
TOPMed
rs770238029
CA6332669
263 L>F No ClinGen
ExAC
TOPMed
gnomAD
rs748585744
CA6332668
264 R>C No ClinGen
ExAC
gnomAD
CA383059357
rs1277369023
266 A>T No ClinGen
TOPMed
CA229968288
rs11551604
269 R>C No ClinGen
Ensembl
CA383059333
rs1440328569
COSM1559337
269 R>H liver central_nervous_system [Cosmic] No ClinGen
cosmic curated
TOPMed
CA229968274
rs11551605
272 R>C No ClinGen
Ensembl
rs1239556225
CA383059314
272 R>H No ClinGen
TOPMed
rs751121248
CA6332665
274 L>V No ClinGen
ExAC
gnomAD
rs750129947
CA6332662
282 I>T No ClinGen
ExAC
gnomAD
CA383059232
rs148846437
284 I>M No ClinGen
ESP
ExAC
TOPMed
gnomAD
rs1446357941
CA383059208
288 Y>C No ClinGen
gnomAD
CA383059210
rs1216243283
288 Y>H No ClinGen
gnomAD
CA6332657
rs532778326
291 I>V No ClinGen
ExAC
TOPMed
gnomAD
CA383059183
rs1313762341
292 D>N No ClinGen
gnomAD
CA383059169
rs1366918784
293 F>L No ClinGen
gnomAD
CA6332654
rs763133730
295 T>I No ClinGen
ExAC
TOPMed
gnomAD
CA6332653
rs773536032
296 S>F No ClinGen
ExAC
gnomAD
rs778115074
CA6332650
305 L>V No ClinGen
ExAC
gnomAD
CA6332648
rs747578888
307 A>V No ClinGen
ExAC
gnomAD
rs1565368268
CA383059053
311 R>H No ClinGen
Ensembl
COSM1195742
CA229968107
rs1000333769
317 V>I lung [Cosmic] No ClinGen
cosmic curated
TOPMed
CA383059001
rs1223624505
319 K>R No ClinGen
gnomAD
CA383058932
rs1215490797
329 S>L No ClinGen
gnomAD
CA6332640
rs373235233
330 Q>L No ClinGen
ESP
ExAC
gnomAD
CA6332638
rs766425028
331 I>M No ClinGen
ExAC
TOPMed
gnomAD
rs752672546
CA6332639
331 I>V No ClinGen
ExAC
TOPMed
gnomAD
rs1302623127
CA383058918
332 H>D No ClinGen
gnomAD
rs763116637
CA6332637
COSM1704727
334 I>T skin [Cosmic] No ClinGen
cosmic curated
ExAC
gnomAD
CA383058902
rs1422888266
334 I>V No ClinGen
TOPMed
gnomAD
rs1591437770
CA383058854
342 R>S No ClinGen
Ensembl
CA6332634
rs762028517
349 L>F No ClinGen
ExAC
gnomAD
rs1410331792
CA383058799
350 L>F No ClinGen
TOPMed
CA6332631
rs747492962
353 F>Y No ClinGen
ExAC
TOPMed
gnomAD
rs771663386
CA383058766
354 F>L No ClinGen
ExAC
TOPMed
gnomAD
rs1251414344
CA383058760
355 N>S No ClinGen
gnomAD
CA6332626
rs756920138
360 N>S No ClinGen
ExAC
gnomAD
CA6332540
rs746781077
374 A>V No ClinGen
ExAC
gnomAD
CA383058543
rs1250487224
385 S>Y No ClinGen
gnomAD
rs745866854
CA383058533
386 E>D No ClinGen
ExAC
TOPMed
gnomAD
CA383058517
rs1565367621
389 Q>E No ClinGen
Ensembl
rs1395408526
CA383058435
398 P>S No ClinGen
gnomAD
CA6332532
rs755304850
399 L>F No ClinGen
ExAC
gnomAD
CA383058371
rs1245759796
COSM123666
403 I>V upper_aerodigestive_tract [Cosmic] No ClinGen
cosmic curated
TOPMed
rs372928718
CA6332530
409 V>I No ClinGen
ESP
ExAC
TOPMed
gnomAD
CA383058257
rs1480411360
411 T>S No ClinGen
gnomAD
CA383058250
rs1397356715
412 V>I No ClinGen
TOPMed
CA383058202
rs1184086544
415 K>N No ClinGen
gnomAD
CA383058171
rs1591437035
418 T>P No ClinGen
Ensembl
rs1591437024
CA383058155
419 T>P No ClinGen
Ensembl
rs1263548986
CA383058091
424 Q>K No ClinGen
gnomAD
rs763663403
CA6332524
427 T>I No ClinGen
ExAC
gnomAD
rs1555074367
CA383058012
429 T>S No ClinGen
Ensembl
CA6332521
rs772031159
434 N>S No ClinGen
ExAC
gnomAD
CA383057864
rs1226429373
440 I>V No ClinGen
TOPMed
CA229967216
rs1029079461
441 Q>* No ClinGen
TOPMed
CA383057491
rs1426678244
442 V>A No ClinGen
gnomAD
rs1163128822
CA383057417
453 N>D No ClinGen
gnomAD
rs11551598
VAR_049620
CA229966880
459 F>L No ClinGen
UniProt
Ensembl
dbSNP
rs746441724
COSM924146
CA6332478
462 T>A endometrium [Cosmic] No ClinGen
cosmic curated
ExAC
TOPMed
gnomAD
CA229966875
rs925044940
464 I>L No ClinGen
TOPMed
gnomAD
rs1290423049
CA383057330
465 P>L No ClinGen
gnomAD
rs1042085144
CA229966870
466 P>A No ClinGen
TOPMed
rs773253340
CA6332477
466 P>L No ClinGen
ExAC
gnomAD
CA383057286
rs1555074255
473 Q>R No ClinGen
Ensembl
rs1302645687
CA383057195
486 L>F No ClinGen
gnomAD
CA6332469
rs749707173
487 N>S No ClinGen
ExAC
TOPMed
gnomAD
rs1451018519
CA383057103
499 N>S No ClinGen
TOPMed
CA6332465
rs780908558
500 K>R No ClinGen
ExAC
gnomAD
CA6332462
rs766069802
504 T>S No ClinGen
ExAC
gnomAD
rs1219667932
CA383056965
509 R>C No ClinGen
gnomAD
CA383056947
rs1255945488
511 S>N No ClinGen
gnomAD
rs1355011382
CA383056919
515 I>V No ClinGen
gnomAD
CA383056903
rs1180559000
517 R>C No ClinGen
TOPMed
gnomAD
rs771746646
CA6332423
517 R>H No ClinGen
ExAC
TOPMed
gnomAD
CA6332424
rs771746646
517 R>L No ClinGen
ExAC
TOPMed
gnomAD
CA229966466
rs909420393
518 M>V No ClinGen
TOPMed
CA6332421
rs778743630
519 V>I No ClinGen
ExAC
gnomAD
rs753733140
CA6332419
524 K>E No ClinGen
ExAC
gnomAD
CA383056843
rs1314984351
526 K>Q No ClinGen
gnomAD
CA383056831
rs1355626720
527 A>G No ClinGen
TOPMed
rs1324030336
CA383056811
530 E>K No ClinGen
TOPMed
rs766437819
CA6332415
533 R>K No ClinGen
ExAC
gnomAD
rs763204793
CA6332414
534 D>A No ClinGen
ExAC
gnomAD
rs1417379667
CA383056783
534 D>N No ClinGen
gnomAD
rs1359549189
CA383056711
544 S>T No ClinGen
TOPMed
CA6332408
rs769269163
545 Y>C No ClinGen
ExAC
rs761149194
CA6332406
546 A>S No ClinGen
ExAC
gnomAD
rs775032110
CA6332404
547 F>L No ClinGen
ExAC
gnomAD
CA6332402
rs568778183
549 M>V No ClinGen
1000Genomes
ExAC
TOPMed
gnomAD
rs745475251
CA6332401
550 K>R No ClinGen
ExAC
TOPMed
gnomAD
rs745475251
CA383056668
550 K>T No ClinGen
ExAC
TOPMed
gnomAD
rs1334087304
CA383056660
551 A>G No ClinGen
TOPMed
rs778459169
CA6332398
552 T>A No ClinGen
ExAC
gnomAD
CA383056651
rs1307984893
553 V>A No ClinGen
TOPMed
gnomAD
CA383056652
rs770645829
553 V>F No ClinGen
ExAC
gnomAD
CA383056649
rs1307984893
553 V>G No ClinGen
TOPMed
gnomAD
CA6332397
rs770645829
553 V>I No ClinGen
ExAC
gnomAD
rs749093478
CA6332395
559 Q>E No ClinGen
ExAC
TOPMed
gnomAD
rs749093478
CA383056610
559 Q>K No ClinGen
ExAC
TOPMed
gnomAD
rs1468625294
CA383056607
559 Q>R No ClinGen
TOPMed
rs777603150
CA6332394
562 I>V No ClinGen
ExAC
gnomAD
CA6332392
rs199882006
563 N>K No ClinGen
1000Genomes
ESP
ExAC
TOPMed
gnomAD
rs756041393
CA6332393
563 N>S No ClinGen
ExAC
TOPMed
gnomAD
CA229966371
rs765561454
564 D>N No ClinGen
TOPMed
gnomAD
CA383056567
rs1463886962
565 E>G No ClinGen
gnomAD
CA383056554
rs1420825439
567 K>Q No ClinGen
TOPMed
rs754246861
CA6332386
574 C>S No ClinGen
ExAC
gnomAD
CA6332385
rs764589322
578 I>V No ClinGen
ExAC
gnomAD
rs1317857757
CA383056463
579 N>S No ClinGen
TOPMed
rs1480815795
CA383056421
584 N>K No ClinGen
gnomAD
CA383056419
rs1591435739
585 Q>K No ClinGen
Ensembl
rs963847272
CA229965801
586 T>S No ClinGen
TOPMed
rs1385383759
CA383056392
587 A>T No ClinGen
gnomAD
CA383056352
rs1339299808
592 F>S No ClinGen
gnomAD
CA383056344
rs1320337416
593 E>G No ClinGen
gnomAD
rs41487746
CA383056333
594 H>Q No ClinGen
TOPMed
rs776255814
CA6332306
595 Q>K No ClinGen
ExAC
TOPMed
gnomAD
CA229965729
rs775363477
596 Q>K No ClinGen
Ensembl
CA383056322
rs1591434728
596 Q>R No ClinGen
Ensembl
rs1322018211
CA383056317
597 K>E No ClinGen
TOPMed
rs760638348
CA6332304
598 E>K No ClinGen
ExAC
gnomAD
CA383056291
rs1162494106
600 E>D No ClinGen
gnomAD
CA6332301
rs377681653
605 P>L No ClinGen
ESP
ExAC
TOPMed
gnomAD
rs1056656311
CA229965705
607 I>V No ClinGen
TOPMed
CA383056238
rs1487646632
608 T>S No ClinGen
TOPMed
gnomAD
rs781388678
CA6332297
610 L>R No ClinGen
ExAC
gnomAD
CA383056200
rs1228155115
614 A>T No ClinGen
gnomAD
CA6332295
rs752022565
614 A>V No ClinGen
ExAC
TOPMed
gnomAD
rs1401181468
CA383056195
615 G>R No ClinGen
gnomAD
rs780546314
CA6332294
616 G>S No ClinGen
ExAC
gnomAD
CA383056182
rs1296437764
616 G>V No ClinGen
gnomAD
rs1401650031
CA383056175
617 M>I No ClinGen
TOPMed
CA6332293
rs757849635
620 G>E No ClinGen
ExAC
TOPMed
gnomAD
rs1261030266
CA383056151
621 M>T No ClinGen
gnomAD
CA383056145
rs1199609003
622 P>A No ClinGen
TOPMed
gnomAD
rs1199609003
CA383056146
622 P>T No ClinGen
TOPMed
gnomAD
CA383056129
rs1403445047
624 G>V No ClinGen
gnomAD
CA6332290
rs764872570
628 G>S No ClinGen
ExAC
gnomAD
CA383056103
rs1477455686
629 G>R No ClinGen
gnomAD
CA6332288
rs753546825
630 A>V No ClinGen
ExAC
gnomAD
CA229965662
rs946722582
633 S>C No ClinGen
TOPMed
rs1219260728
CA383056052
637 S>F No ClinGen
TOPMed

No associated diseases with P11142

2 regional properties for P11142

Type Name Position InterPro Accession
domain Kinesin motor domain 3 - 343 IPR001752
conserved_site Kinesin motor domain, conserved site 234 - 245 IPR019821

Functions

Description
EC Number 3.6.4.10 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Cytoplasm
  • Melanosome
  • Nucleus, nucleolus
  • Cell membrane
  • Lysosome membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661)
  • Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock (PubMed:1586970)
PANTHER Family PTHR19375 HEAT SHOCK PROTEIN 70KDA
PANTHER Subfamily PTHR19375:SF379 HEAT SHOCK COGNATE 71 KDA PROTEIN
PANTHER Protein Class Hsp70 family chaperone
PANTHER Pathway Category Parkinson disease
Hsp70
Apoptosis signaling pathway
HSP70

35 GO annotations of cellular component

Name Definition
autophagosome A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the lytic vacuole/lysosome for degradation as part of macroautophagy.
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.
chaperone complex A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins.
clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane The lipid bilayer surrounding a clathrin-sculpted gamma-aminobutyric acid transport vesicle.
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.
dendrite A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
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).
glutamatergic synapse A synapse that uses glutamate as a neurotransmitter.
glycinergic synapse A synapse that uses glycine as a neurotransmitter.
late endosome A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center.
lumenal side of lysosomal membrane The side (leaflet) of the lysosomal membrane that faces the lumen.
lysosomal lumen The volume enclosed within the lysosomal membrane.
lysosomal membrane The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
lysosome A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions.
melanosome A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
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.
photoreceptor ribbon synapse A ribbon synapse between a retinal photoreceptor cell (rod or cone) and a retinal bipolar cell. These contain a plate-like synaptic ribbon.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
postsynaptic cytosol The region of the cytosol consisting of all cytosol that is part of the postsynapse.
postsynaptic specialization membrane The membrane component of the postsynaptic specialization. This is the region of the postsynaptic membrane in which the population of neurotransmitter receptors involved in synaptic transmission are concentrated.
presynaptic cytosol The region of the cytosol consisting of all cytosol that is part of the presynapse.
Prp19 complex A protein complex consisting of Prp19 and associated proteins that is involved in the transition from the precatalytic spliceosome to the activated form that catalyzes step 1 of splicing, and which remains associated with the spliceosome through the second catalytic step. It is widely conserved, found in both yeast and mammals, though the exact composition varies. In S. cerevisiae, it contains Prp19p, Ntc20p, Snt309p, Isy1p, Syf2p, Cwc2p, Prp46p, Clf1p, Cef1p, and Syf1p.
ribonucleoprotein complex A macromolecular complex that contains both RNA and protein molecules.
secretory granule lumen The volume enclosed by the membrane of a secretory granule.
spliceosomal complex Any of a series of ribonucleoprotein complexes that contain snRNA(s) and small nuclear ribonucleoproteins (snRNPs), and are formed sequentially during the spliceosomal splicing of one or more substrate RNAs, and which also contain the RNA substrate(s) from the initial target RNAs of splicing, the splicing intermediate RNA(s), to the final RNA products. During cis-splicing, the initial target RNA is a single, contiguous RNA transcript, whether mRNA, snoRNA, etc., and the released products are a spliced RNA and an excised intron, generally as a lariat structure. During trans-splicing, there are two initial substrate RNAs, the spliced leader RNA and a pre-mRNA.
terminal bouton Terminal inflated portion of the axon, containing the specialized apparatus necessary to release neurotransmitters. The axon terminus is considered to be the whole region of thickening and the terminal bouton is a specialized region of it.

19 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 + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
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: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C, where X is any amino acid. Many proteins containing a C3HC4-type RING finger play a key role in the ubiquitination pathway.
cadherin binding Binding to cadherin, a type I membrane protein involved in cell adhesion.
chaperone binding Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
clathrin-uncoating ATPase activity Catalysis of the reaction: ATP + H2O = ADP + phosphate. Catalysis of the removal of clathrin from vesicle membranes, coupled to the hydrolysis of ATP.
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.
MHC class II protein complex binding Binding to a class II major histocompatibility complex.
misfolded protein binding Binding to a misfolded protein.
phosphatidylserine binding Binding to phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine.
protein carrier chaperone Binding to and carrying a protein between two different cellular components by moving along with the target protein.
protein disaggregase activity An ATP-dependent molecular chaperone activity that mediates the solubilization of ordered protein aggregates.
protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process.
protein-macromolecule adaptor activity The binding activity of a protein that brings together two or more macromolecules in contact, permitting those molecules to function in a coordinated way. The adaptor can bring together two proteins, or a protein and another macromolecule such as a lipid or a nucleic acid.
RNA binding Binding to an RNA molecule or a portion thereof.
ubiquitin protein ligase binding Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.
unfolded protein binding Binding to an unfolded protein.

27 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 response to starvation 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 deprivation of nourishment.
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 autophagy The autophagy process which begins when chaperones and co-chaperones recognize a target motif and unfold the substrate protein. The proteins are then transported to the lysosome where they are degraded.
chaperone-mediated autophagy translocation complex disassembly The disaggregation of a chaperone-mediated autophagy translocation complex into its constituent components.
late endosomal microautophagy The autophagy process by which cytosolic proteins targeted for degradation are tagged with a chaperone and are directly transferred into and degraded in a late endosomal compartment.
membrane organization A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins.
mRNA processing Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
negative regulation of supramolecular fiber organization Any process that stops, prevents or reduces the frequency, rate or extent of fibril organization.
negative regulation of transcription, DNA-templated Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
positive regulation by host of viral genome replication A process in which a host organism activates or increases the frequency, rate or extent of viral genome replication.
positive regulation of mRNA splicing, via spliceosome Any process that activates or increases the rate or extent of mRNA splicing via a spliceosomal mechanism.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
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 targeting to lysosome involved in chaperone-mediated autophagy The targeting of a protein to the lysosome process in which an input protein binds to a chaperone and subsequently to a lysosomal receptor.
regulation of cell cycle Any process that modulates the rate or extent of progression through the cell cycle.
regulation of postsynapse organization Any process that modulates the physical form of a postsynapse.
regulation of protein complex stability Any process that affects the structure and integrity of a protein complex by altering the likelihood of its assembly or disassembly.
regulation of protein import Any process that modulates the frequency, rate or extent of protein import.
regulation of protein stability Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
regulation of protein-containing complex assembly Any process that modulates the frequency, rate or extent of protein complex assembly.
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.
RNA splicing The process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA.
slow axonal transport The directed slow movement of non-membranous molecules in nerve cell axons. It is comprised of a Slow Component a (SCa) and a Slow Component b (SCb) which differ in transport rates and protein composition.
vesicle-mediated transport A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane.

64 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P11484 SSB1 Ribosome-associated molecular chaperone SSB1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P40150 SSB2 Ribosome-associated molecular chaperone SSB2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P22202 SSA4 Heat shock protein SSA4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P09435 SSA3 Heat shock protein SSA3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P10592 SSA2 Heat shock protein SSA2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P10591 SSA1 Heat shock protein SSA1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
Q27975 HSPA1A Heat shock 70 kDa protein 1A 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
P19120 HSPA8 Heat shock cognate 71 kDa protein Bos taurus (Bovine) SS
E1C2P3 HSPA14 Heat shock 70 kDa protein 14 Gallus gallus (Chicken) SS
P08106 Heat shock 70 kDa protein Gallus gallus (Chicken) SS
O73885 HSPA8 Heat shock cognate 71 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
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
Q9VG58 Hsp70Bbb Major heat shock 70 kDa protein Bbb Drosophila melanogaster (Fruit fly) SS
Q9BIR7 Hsp70Bc Major heat shock 70 kDa protein Bc Drosophila melanogaster (Fruit fly) SS
Q8INI8 Hsp70Ba Major heat shock 70 kDa protein Ba Drosophila melanogaster (Fruit fly) SS
Q9BIS2 Hsp70Bb Major heat shock 70 kDa protein Bb Drosophila melanogaster (Fruit fly) SS
P11146 Hsc70-2 Heat shock 70 kDa protein cognate 2 Drosophila melanogaster (Fruit fly) SS
O97125 Hsp68 Heat shock protein 68 Drosophila melanogaster (Fruit fly) SS
P29843 Hsc70-1 Heat shock 70 kDa protein cognate 1 Drosophila melanogaster (Fruit fly) SS
P11147 Hsc70-4 Heat shock 70 kDa protein cognate 4 Drosophila melanogaster (Fruit fly) SS
A2Q0Z1 HSPA8 Heat shock cognate 71 kDa protein Equus caballus (Horse) 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
Q0VDF9 HSPA14 Heat shock 70 kDa protein 14 Homo sapiens (Human) SS
P54652 HSPA2 Heat shock-related 70 kDa protein 2 Homo sapiens (Human) SS
P38646 HSPA9 Stress-70 protein, mitochondrial Homo sapiens (Human) SS
P11021 HSPA5 Endoplasmic reticulum chaperone BiP Homo sapiens (Human) SS
P34931 HSPA1L Heat shock 70 kDa protein 1-like Homo sapiens (Human) SS
P17066 HSPA6 Heat shock 70 kDa protein 6 Homo sapiens (Human) SS
P0DMV8 HSPA1A Heat shock 70 kDa protein 1A Homo sapiens (Human) SS
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
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
Q61696 Hspa1a Heat shock 70 kDa protein 1A 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
P63017 Hspa8 Heat shock cognate 71 kDa protein 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
P0DMW1 Hspa1b Heat shock 70 kDa protein 1B Rattus norvegicus (Rat) SS
P0DMW0 Hspa1a Heat shock 70 kDa protein 1A Rattus norvegicus (Rat) SS
P55063 Hspa1l Heat shock 70 kDa protein 1-like Rattus norvegicus (Rat) SS
P63018 Hspa8 Heat shock cognate 71 kDa protein 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
Q9S9N1 HSP70-5 Heat shock 70 kDa protein 5 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
O65719 HSP70-3 Heat shock 70 kDa protein 3 Arabidopsis thaliana (Mouse-ear cress) SS
Q9LHA8 HSP70-4 Heat shock 70 kDa protein 4 Arabidopsis thaliana (Mouse-ear cress) SS
P22953 HSP70-1 Heat shock 70 kDa protein 1 Arabidopsis thaliana (Mouse-ear cress) SS
P27322 HSC-2 Heat shock cognate 70 kDa protein 2 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
P24629 HSC-I Heat shock cognate 70 kDa protein 1 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
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
70 80 90 100 110 120
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS
130 140 150 160 170 180
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
190 200 210 220 230 240
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
250 260 270 280 290 300
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
310 320 330 340 350 360
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
370 380 390 400 410 420
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
430 440 450 460 470 480
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
490 500 510 520 530 540
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN
550 560 570 580 590 600
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE
610 620 630 640
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD