HSPA8

Functionⁱ

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462).2 Publications10 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	71	ATP		1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	12 – 15	ATP	4
Nucleotide bindingⁱ	202 – 204	ATP	3
Nucleotide bindingⁱ	268 – 275	ATP	8
Nucleotide bindingⁱ	339 – 342	ATP	4

GO - Molecular functionⁱ

ATPase activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 23921388
ATPase activity, coupled
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
ATP binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 23921388
C3HC4-type RING finger domain binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 25281747
cadherin binding
Source: BHF-UCL
Inferred from high throughput direct assayⁱ
- 25468996
chaperone binding
Source: ARUK-UCL
Inferred from physical interactionⁱ
- 16207813
clathrin-uncoating ATPase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
enzyme binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 23921388
G protein-coupled receptor binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 12150907
heat shock protein binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17182002
MHC class II protein complex binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 20458337
misfolded protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
phosphatidylserine binding Source: Ensembl
protein binding, bridging
Source: ARUK-UCL
Inferred from physical interactionⁱ
- 16207813
protein binding involved in protein folding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22658674
- 22681889
ubiquitin protein ligase binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 12150907
unfolded protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 21231916

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

ATP metabolic process
Source: BHF-UCL
Inferred from direct assayⁱ
- 23921388
axo-dendritic transport
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular response to heat
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular response to starvation
Source: ParkinsonsUK-UCL
Traceable author statementⁱ
- 20176123
cellular response to unfolded protein
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
chaperone cofactor-dependent protein refolding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
chaperone-mediated autophagy Source: ParkinsonsUK-UCL
chaperone-mediated autophagy translocation complex disassembly Source: ParkinsonsUK-UCL
chaperone-mediated protein transport involved in chaperone-mediated autophagy
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cytokine-mediated signaling pathway Source: Reactome
late endosomal microautophagy
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
membrane organization Source: Reactome
mRNA splicing, via spliceosome Source: Reactome
negative regulation of supramolecular fiber organization
Source: BHF-UCL
Inferred from direct assayⁱ
- 23921388
negative regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 10722728
neutrophil degranulation Source: Reactome
positive regulation by host of viral genome replication Source: Ensembl
positive regulation of mRNA splicing, via spliceosome Source: Ensembl
protein folding
Source: UniProtKB
Non-traceable author statementⁱ
- 8530083
protein refolding
Source: UniProtKB
Inferred from direct assayⁱ
- 21231916
protein targeting to lysosome involved in chaperone-mediated autophagy
Source: ParkinsonsUK-UCL
Inferred from mutant phenotypeⁱ
- 26212789
regulation of cell cycle Source: Ensembl
regulation of cellular response to heat Source: Reactome
regulation of mRNA stability Source: Reactome
regulation of postsynapse organization Source: Ensembl
regulation of protein complex assembly
Source: ParkinsonsUK-UCL
Traceable author statementⁱ
- 20176123
regulation of protein complex stability Source: ParkinsonsUK-UCL
regulation of protein import
Source: ParkinsonsUK-UCL
Traceable author statementⁱ
- 20176123
regulation of protein stability
Source: ParkinsonsUK-UCL
Inferred from mutant phenotypeⁱ
- 26212789
response to unfolded protein
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
slow axonal transport
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
vesicle-mediated transport
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
viral process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chaperone, Repressor
Biological process	Host-virus interaction, mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	3.6.3.51 2681
Reactomeⁱ	R-HSA-3371453 Regulation of HSF1-mediated heat shock response R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR) R-HSA-3371568 Attenuation phase R-HSA-3371571 HSF1-dependent transactivation R-HSA-432720 Lysosome Vesicle Biogenesis R-HSA-432722 Golgi Associated Vesicle Biogenesis R-HSA-447041 CHL1 interactions R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling R-HSA-6798695 Neutrophil degranulation R-HSA-72163 mRNA Splicing - Major Pathway R-HSA-8856828 Clathrin-mediated endocytosis R-HSA-8876725 Protein methylation R-HSA-888590 GABA synthesis, release, reuptake and degradation
SIGNORⁱ	P11142

Protein family/group databases

MoonDBⁱ	P11142 Predicted

MoonDBⁱ

P11142 Predicted

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Heat shock cognate 71 kDa protein Alternative name(s): Heat shock 70 kDa protein 8 Lipopolysaccharide-associated protein 1 Short name: LAP-1 Short name: LPS-associated protein 1
Gene namesⁱ	Name:HSPA8 Synonyms:HSC70, HSP73, HSPA10
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 11

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000109971.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:5241 HSPA8
MIMⁱ	600816 gene
neXtProtⁱ	NX_P11142

Keywords - Cellular componentⁱ

Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	561	K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3312
Open Targets More...OpenTargetsⁱ	ENSG00000109971
PharmGKBⁱ	PA29507

Chemistry databases

ChEMBLⁱ	CHEMBL1275223

ChEMBLⁱ

CHEMBL1275223

Polymorphism and mutation databases

DMDMⁱ	123648

DMDMⁱ

123648

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources2 Publications
ChainⁱPRO_0000078270	2 – 646	Heat shock cognate 71 kDa proteinAdd BLAST		645

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserineCombined sources2 Publications	1
Modified residueⁱ	108	N6-acetyllysineBy similarity	1
Modified residueⁱ	153	PhosphoserineCombined sources	1
Modified residueⁱ	246	N6-acetyllysineCombined sources	1
Modified residueⁱ	319	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	319	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	328	N6-acetyllysineBy similarity	1
Modified residueⁱ	329	PhosphoserineCombined sources	1
Modified residueⁱ	362	PhosphoserineCombined sources	1
Modified residueⁱ	469	Omega-N-methylarginineCombined sources	1
Modified residueⁱ	512	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	512	N6-succinyllysine; alternateBy similarity	1
Cross-linkⁱ	512	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linkⁱ	512	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residueⁱ	524	N6-acetyllysineBy similarity	1
Modified residueⁱ	541	PhosphoserineCombined sources	1
Modified residueⁱ	561	N6,N6,N6-trimethyllysine; by METTL21A; alternate2 Publications	1
Modified residueⁱ	561	N6,N6-dimethyllysine; alternateCombined sources	1
Modified residueⁱ	589	N6-acetyllysineCombined sources	1
Modified residueⁱ	597	N6-acetyllysineCombined sources	1
Modified residueⁱ	601	N6-acetyllysineCombined sources	1

Post-translational modificationⁱ

Trimethylation at Lys-561 reduces fibrillar SNCA binding.

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P11142
PaxDbⁱ	P11142
PeptideAtlas More...PeptideAtlasⁱ	P11142
PRIDEⁱ	P11142
ProteomicsDBⁱ	52698 52699 [P11142-2]
TopDownProteomicsⁱ	P11142-1 [P11142-1] P11142-2 [P11142-2]

2D gel databases

DOSAC-COBS 2D-PAGE database More...DOSAC-COBS-2DPAGEⁱ	P11142
USC-OGP 2-DE database More...OGPⁱ	P11142
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00003865
SWISS-2DPAGEⁱ	P11142
UCD-2DPAGEⁱ	P11142

PTM databases

GlyConnectⁱ	1299
iPTMnetⁱ	P11142
PhosphoSitePlusⁱ	P11142
SwissPalmⁱ	P11142

Miscellaneous databases

PMAP-CutDBⁱ	P11142

PMAP-CutDBⁱ

P11142

Expressionⁱ

Tissue specificityⁱ

Ubiquitous.1 Publication

Inductionⁱ

Constitutively synthesized.

Gene expression databases

Bgeeⁱ	ENSG00000109971 Expressed in 91 organ(s), highest expression level in frontal cortex
CleanExⁱ	HS_HSPA8
ExpressionAtlasⁱ	P11142 baseline and differential
Genevisibleⁱ	P11142 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB002056 HPA052504

HPAⁱ

CAB002056
HPA052504

Interactionⁱ

Subunit structureⁱ

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7. Interacts with DNAJB12 (via J domain) (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). Interacts with DNAJB14 (via J domain) (PubMed:23018488, PubMed:24732912, PubMed:27916661). Interacts (via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex of one CHIP and two HSPA8 molecules. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with TRIM5. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with METTL21A. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PRKN. Interacts with FOXP3. Interacts with DNAJC9 (via J domain) (PubMed:17182002). Interacts with MLLT11 (PubMed:24880125). Interacts with RNF207 (PubMed:25281747). Interacts with DNAJC21 (PubMed:27346687). Interacts with DNAJB2 (PubMed:15936278). Interacts with TTC1 (via TPR repeats) (PubMed:15708368). Interacts with SGTA (via TPR repeats) (By similarity). Interacts with HSF1 (via transactivation domain) (PubMed:9499401). Interacts with HOPX, HSP40 and HSP90 (PubMed:27708256). Interacts with STUB1 (PubMed:27708256). Interacts with BAG2 (PubMed:24318877). Interacts with BAG3 (PubMed:27474739, PubMed:24318877). Interacts with DNAJC12 (PubMed:24122553). Interacts with ZMYND10 (PubMed:29601588). Interacts with HSPC138 (PubMed:25760597).By similarity33 Publications

(Microbial infection) Interacts with SV40 VP1.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	Q99IB8	3	EBI-351896,EBI-6927928	From Hepatitis C virus genotype 2a (isolate JFH-1).
ACTB	P60709	2	EBI-351896,EBI-353944
AICDA	Q9GZX7	2	EBI-351896,EBI-3834328
ARRB1	P49407	4	EBI-351896,EBI-743313
ARRB2	P32121	4	EBI-351896,EBI-714559
ATP13A2	Q9NQ11	2	EBI-351896,EBI-6308763
BAG1	Q99933	13	EBI-351896,EBI-1030678
BAG2	O95816	7	EBI-351896,EBI-355275
BAG4	O95429	3	EBI-351896,EBI-2949658
EBNA-LP	Q8AZK7	3	EBI-351896,EBI-1185167	From Epstein-Barr virus (strain B95-8).
EGFR	P00533	5	EBI-351896,EBI-297353
GAK	O14976	6	EBI-351896,EBI-714707
HSPA4	P34932	5	EBI-351896,EBI-356933
HSPBP1	Q9NZL4	11	EBI-351896,EBI-356763
JUN	P05412	3	EBI-351896,EBI-852823
LDHA	P00338	4	EBI-351896,EBI-372327
LRRK2	Q5S007	5	EBI-351896,EBI-5323863
M	P03485	4	EBI-351896,EBI-2547543	From Influenza A virus (strain A/Puerto Rico/8/1934 H1N1).
NCF1	P14598	2	EBI-351896,EBI-395044
STUB1	Q9UNE7	8	EBI-351896,EBI-357085
STUB1	Q9UNE7-1	4	EBI-351908,EBI-15687717
STXBP1	P61764	2	EBI-351896,EBI-960169
TRIM38	O00635	5	EBI-351896,EBI-2130415

GO - Molecular functionⁱ

C3HC4-type RING finger domain binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 25281747
cadherin binding
Source: BHF-UCL
Inferred from high throughput direct assayⁱ
- 25468996
chaperone binding
Source: ARUK-UCL
Inferred from physical interactionⁱ
- 16207813
enzyme binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 23921388
G protein-coupled receptor binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 12150907
heat shock protein binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17182002
misfolded protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein binding, bridging
Source: ARUK-UCL
Inferred from physical interactionⁱ
- 16207813
protein binding involved in protein folding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
ubiquitin protein ligase binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 12150907
unfolded protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 21231916

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109544, 578 interactors
CORUMⁱ	P11142
Database of interacting proteins More...DIPⁱ	DIP-32874N
IntActⁱ	P11142, 219 interactors
Molecular INTeraction database More...MINTⁱ	P11142
STRINGⁱ	9606.ENSP00000227378

Chemistry databases

BindingDBⁱ

P11142

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	7 – 10	Combined sources	4
Beta strandⁱ	13 – 22	Combined sources	10
Beta strandⁱ	25 – 28	Combined sources	4
Beta strandⁱ	36 – 39	Combined sources	4
Beta strandⁱ	42 – 44	Combined sources	3
Beta strandⁱ	49 – 51	Combined sources	3
Helixⁱ	53 – 57	Combined sources	5
Turnⁱ	58 – 61	Combined sources	4
Helixⁱ	63 – 65	Combined sources	3
Helixⁱ	70 – 72	Combined sources	3
Turnⁱ	73 – 75	Combined sources	3
Helixⁱ	81 – 87	Combined sources	7
Beta strandⁱ	91 – 97	Combined sources	7
Beta strandⁱ	100 – 107	Combined sources	8
Beta strandⁱ	110 – 114	Combined sources	5
Helixⁱ	116 – 135	Combined sources	20
Beta strandⁱ	136 – 138	Combined sources	3
Beta strandⁱ	141 – 146	Combined sources	6
Helixⁱ	152 – 164	Combined sources	13
Beta strandⁱ	168 – 174	Combined sources	7
Helixⁱ	175 – 182	Combined sources	8
Helixⁱ	185 – 187	Combined sources	3
Beta strandⁱ	188 – 191	Combined sources	4
Beta strandⁱ	193 – 201	Combined sources	9
Beta strandⁱ	204 – 213	Combined sources	10
Beta strandⁱ	216 – 225	Combined sources	10
Helixⁱ	230 – 249	Combined sources	20
Helixⁱ	253 – 255	Combined sources	3
Helixⁱ	257 – 276	Combined sources	20
Beta strandⁱ	278 – 288	Combined sources	11
Beta strandⁱ	291 – 298	Combined sources	8
Helixⁱ	299 – 305	Combined sources	7
Helixⁱ	307 – 312	Combined sources	6
Helixⁱ	314 – 324	Combined sources	11
Helixⁱ	328 – 330	Combined sources	3
Beta strandⁱ	333 – 338	Combined sources	6
Helixⁱ	339 – 342	Combined sources	4
Helixⁱ	344 – 353	Combined sources	10
Turnⁱ	354 – 356	Combined sources	3
Beta strandⁱ	357 – 360	Combined sources	4
Turnⁱ	365 – 367	Combined sources	3
Helixⁱ	368 – 380	Combined sources	13
Helixⁱ	541 – 556	Combined sources	16
Helixⁱ	564 – 582	Combined sources	19
Helixⁱ	594 – 612	Combined sources	19
Helixⁱ	613 – 616	Combined sources	4
Beta strandⁱ	641 – 644	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	P11142
SMRⁱ	P11142
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P11142

EvolutionaryTraceⁱ

P11142

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	2 – 386	Nucleotide-binding domain (NBD)1 PublicationAdd BLAST	385
Regionⁱ	186 – 377	Interaction with BAG1Add BLAST	192
Regionⁱ	394 – 509	Substrate-binding domain (SBD)1 PublicationAdd BLAST	116

Domainⁱ

The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.1 Publication

Sequence similaritiesⁱ

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGⁱ	KOG0101 Eukaryota COG0443 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00930000150862
HOGENOMⁱ	HOG000228135
HOVERGENⁱ	HBG051845
InParanoidⁱ	P11142
KEGG Orthology (KO) More...KOⁱ	K03283
OMAⁱ	AYTKNQD
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G03SF
PhylomeDBⁱ	P11142
TreeFamⁱ	TF105042

Family and domain databases

Gene3Dⁱ	1.20.1270.10, 1 hit 2.60.34.10, 1 hit
InterProⁱ	View protein in InterPro IPR018181 Heat_shock_70_CS IPR029048 HSP70_C_sf IPR029047 HSP70_peptide-bd_sf IPR013126 Hsp_70_fam
PANTHERⁱ	PTHR19375 PTHR19375, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00012 HSP70, 1 hit
PRINTSⁱ	PR00301 HEATSHOCK70
SUPFAMⁱ	SSF100920 SSF100920, 1 hit SSF100934 SSF100934, 1 hit
PROSITEⁱ	View protein in PROSITE PS00297 HSP70_1, 1 hit PS00329 HSP70_2, 1 hit PS01036 HSP70_3, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 13 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P11142-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL 
        60         70         80         90        100
IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR 
       110        120        130        140        150
PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF 
       160        170        180        190        200
NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL 
       210        220        230        240        250
GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK 
       260        270        280        290        300
KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 
       310        320        330        340        350
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL 
       360        370        380        390        400
QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS 
       410        420        430        440        450
LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT 
       460        470        480        490        500
KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK 
       510        520        530        540        550
ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK 
       560        570        580        590        600
ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE 
       610        620        630        640 
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD

Length:646

Mass (Da):70,898

Last modified:July 1, 1989 - v1

Checksum:ⁱ9AA27B210730670C

GO

Isoform 2 (identifier: P11142-2) [UniParc]FASTA Add to basket

Also known as: HSC54

The sequence of this isoform differs from the canonical sequence as follows:
464-616: Missing.

« Hide

        10         20         30         40         50
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL 
        60         70         80         90        100
IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR 
       110        120        130        140        150
PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF 
       160        170        180        190        200
NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL 
       210        220        230        240        250
GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK 
       260        270        280        290        300
KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 
       310        320        330        340        350
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL 
       360        370        380        390        400
QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS 
       410        420        430        440        450
LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT 
       460        470        480        490 
KDNNLLGKFE LTGMPGGMPG GFPGGGAPPS GGASSGPTIE EVD

Show »

Length:493

Mass (Da):53,518

Checksum:ⁱBA2CFBD68F17784E

GO

Computationally mapped potential isoform sequencesⁱ

There are 13 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name	Protein names	Gene names	Length	Annotation

	A8K7Q2	A8K7Q2_HUMAN	Heat shock cognate 71 kDa protein Heat shock cognate 71 kDa protein (cDNA FLJ77848)	HSPA8	410	Annotation score:
	E9PNE6	E9PNE6_HUMAN	Heat shock cognate 71 kDa protein Heat shock cognate 71 kDa protein	HSPA8	500	Annotation score:
	E9PKE3	E9PKE3_HUMAN	Heat shock cognate 71 kDa protein Heat shock cognate 71 kDa protein	HSPA8	627	Annotation score:
	E9PN89	E9PN89_HUMAN	Heat shock cognate 71 kDa protein Heat shock cognate 71 kDa protein	HSPA8	312	Annotation score:
	E9PLF4	E9PLF4_HUMAN	Heat shock cognate 71 kDa protein Heat shock cognate 71 kDa protein	HSPA8	187	Annotation score:
	E9PPY6	E9PPY6_HUMAN	Heat shock cognate 71 kDa protein Heat shock cognate 71 kDa protein	HSPA8	137	Annotation score:
	E9PN25	E9PN25_HUMAN	Heat shock cognate 71 kDa protein Heat shock cognate 71 kDa protein	HSPA8	132	Annotation score:
	E9PK54	E9PK54_HUMAN	Heat shock cognate 71 kDa protein Heat shock cognate 71 kDa protein	HSPA8	183	Annotation score:
	E9PQK7	E9PQK7_HUMAN	Heat shock cognate 71 kDa protein Heat shock cognate 71 kDa protein	HSPA8	178	Annotation score:
	E9PI65	E9PI65_HUMAN	Heat shock cognate 71 kDa protein Heat shock cognate 71 kDa protein	HSPA8	168	Annotation score:
There are more potential isoformsShow all

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_049619	32	D → Y. Corresponds to variant dbSNP:rs11551602Ensembl.		1
Natural variantⁱVAR_049620	459	F → L. Corresponds to variant dbSNP:rs11551598Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_002427	464 – 616	Missing in isoform 2. 1 PublicationAdd BLAST		153

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Y00371 Genomic DNA Translation: CAA68445.1 AB034951 mRNA Translation: BAB18615.1 AF352832 mRNA Translation: AAK17898.1 BC016179 mRNA Translation: AAH16179.1 BC016660 mRNA Translation: AAH16660.1 BC019816 mRNA Translation: AAH19816.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS44754.1 [P11142-2] CCDS8440.1 [P11142-1]
PIRⁱ	A27077
NCBI Reference Sequences More...RefSeqⁱ	NP_006588.1, NM_006597.5 [P11142-1] NP_694881.1, NM_153201.3 [P11142-2] XP_011541100.1, XM_011542798.1 [P11142-1]
UniGeneⁱ	Hs.180414

Genome annotation databases

Ensemblⁱ	ENST00000227378; ENSP00000227378; ENSG00000109971 [P11142-1] ENST00000453788; ENSP00000404372; ENSG00000109971 [P11142-2] ENST00000532636; ENSP00000437125; ENSG00000109971 [P11142-1] ENST00000534624; ENSP00000432083; ENSG00000109971 [P11142-1]
GeneIDⁱ	3312
KEGGⁱ	hsa:3312
UCSC genome browser More...UCSCⁱ	uc001pyp.5 human [P11142-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P11142	Heat shock cognate 71 kDa protein		HORSE		646	UniRef100_P11142
Heat shock cognate 71 kDa protein		SAGOE		646
Uncharacterized bone marrow protein BM034		HUMAN		129
Heat shock cognate 71 kDa protein		FUKDA		1041
Heat shock cognate 71 kDa protein (Fragment)		MUSPF		96
+77
P11142-2	HSPA8 isoform 5		PANTR		493	UniRef100_A0A2I3T323
Uncharacterized protein		SAIBB		493
Uncharacterized protein		MACMU		493
Uncharacterized protein		COLAP		493
HSPA8 isoform 5		PONAB		493
+8

Protein	Similar proteins		Species	Score	Length	Source
P11142	Heat shock cognate 71 kDa protein		HORSE		646	UniRef90_P11142
Heat shock cognate 71 kDa protein		SAGOE		646
Uncharacterized bone marrow protein BM034		HUMAN		129
Heat shock cognate 71 kDa protein		FUKDA		1041
Heat shock cognate 71 kDa protein (Fragment)		MUSPF		96
+77
P11142-2	Heat shock 70kDa protein 8 isoform 2 variant (Fragment)		HUMAN		493	UniRef90_Q53HF2
heat shock cognate 71 kDa protein		Florida manatee		550
Heat shock 70 kDa protein cognate		Daphnia magna		506
Heat shock protein 70		MACRS		499
Uncharacterized protein		PROCO		497
+44

Protein	Similar proteins		Species	Score	Length	Source
P11142	Heat shock cognate 71 kDa protein		HORSE		646	UniRef50_P11142
Heat shock cognate 71 kDa protein		SAGOE		646
Uncharacterized bone marrow protein BM034		HUMAN		129
Heat shock cognate 71 kDa protein		FUKDA		1041
Heat shock cognate 71 kDa protein (Fragment)		MUSPF		96
+125
P11142-2	Uncharacterized protein		CALJA		613	UniRef50_F6R5D6
78 kDa glucose-regulated protein		OPHHA		609
Luminal-binding protein		AEGTA		643
Heat shock protein 70e		Pyropia seriata		720
Uncharacterized protein		PORUM		674
+100

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Y00371 Genomic DNA Translation: CAA68445.1 AB034951 mRNA Translation: BAB18615.1 AF352832 mRNA Translation: AAK17898.1 BC016179 mRNA Translation: AAH16179.1 BC016660 mRNA Translation: AAH16660.1 BC019816 mRNA Translation: AAH19816.1
CCDSⁱ	CCDS44754.1 [P11142-2] CCDS8440.1 [P11142-1]
PIRⁱ	A27077
RefSeqⁱ	NP_006588.1, NM_006597.5 [P11142-1] NP_694881.1, NM_153201.3 [P11142-2] XP_011541100.1, XM_011542798.1 [P11142-1]
UniGeneⁱ	Hs.180414

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3AGY	X-ray	1.85	C/D/F	639-646	[»]
	3AGZ	X-ray	2.51	C/D/E/F	639-646	[»]
	3ESK	X-ray	2.05	B	635-646	[»]
	3FZF	X-ray	2.20	A	4-381	[»]
	3FZH	X-ray	2.00	A	4-381	[»]
	3FZK	X-ray	2.10	A	4-381	[»]
	3FZL	X-ray	2.20	A	4-381	[»]
	3FZM	X-ray	2.30	A	4-381	[»]
	3LDQ	X-ray	1.90	A	4-381	[»]
	3M3Z	X-ray	2.10	A	4-381	[»]
	4H5N	X-ray	1.86	A/B	2-384	[»]
	4H5R	X-ray	1.64	A/B	2-384	[»]
	4H5T	X-ray	1.90	A	2-384	[»]
	4H5V	X-ray	1.75	A	2-384	[»]
	4H5W	X-ray	1.94	A/B	2-384	[»]
	4HWI	X-ray	2.27	A	5-381	[»]
	4KBQ	X-ray	2.91	C/D	541-646	[»]
	5AQF	X-ray	1.88	A/C	1-381	[»]
	5AQG	X-ray	2.24	A/C/E	1-381	[»]
	5AQH	X-ray	2.00	A	1-381	[»]
	5AQI	X-ray	1.98	A/C	1-381	[»]
	5AQJ	X-ray	1.96	A/C/E	1-381	[»]
	5AQK	X-ray	2.09	A	1-381	[»]
	5AQL	X-ray	1.69	A/C	1-381	[»]
	5AQM	X-ray	1.63	A/C	1-381	[»]
	5AQN	X-ray	2.45	A/C/E	1-381	[»]
	5AQO	X-ray	2.12	A/C/E	1-381	[»]
	5AQP	X-ray	2.08	A/C/E	1-381	[»]
	5AQQ	X-ray	2.72	A/C/E	1-381	[»]
	5AQR	X-ray	1.91	A/C/E	1-381	[»]
	5AQS	X-ray	2.00	A/C	1-381	[»]
	5AQT	X-ray	1.90	A	1-381	[»]
	5AQU	X-ray	1.92	A	1-381	[»]
	5AQV	X-ray	1.75	A	1-381	[»]
	6B1I	X-ray	2.30	A/B	5-381	[»]
	6B1M	X-ray	1.90	A/B	5-381	[»]
	6B1N	X-ray	1.80	A/B	5-381	[»]
ProteinModelPortalⁱ	P11142
SMRⁱ	P11142
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	109544, 578 interactors
CORUMⁱ	P11142
DIPⁱ	DIP-32874N
IntActⁱ	P11142, 219 interactors
MINTⁱ	P11142
STRINGⁱ	9606.ENSP00000227378

Chemistry databases

BindingDBⁱ	P11142
ChEMBLⁱ	CHEMBL1275223

Protein family/group databases

MoonDBⁱ	P11142 Predicted

MoonDBⁱ

P11142 Predicted

PTM databases

GlyConnectⁱ	1299
iPTMnetⁱ	P11142
PhosphoSitePlusⁱ	P11142
SwissPalmⁱ	P11142

Polymorphism and mutation databases

DMDMⁱ	123648

DMDMⁱ

123648

2D gel databases

DOSAC-COBS-2DPAGEⁱ	P11142
OGPⁱ	P11142
REPRODUCTION-2DPAGEⁱ	IPI00003865
SWISS-2DPAGEⁱ	P11142
UCD-2DPAGEⁱ	P11142

Proteomic databases

EPDⁱ	P11142
PaxDbⁱ	P11142
PeptideAtlasⁱ	P11142
PRIDEⁱ	P11142
ProteomicsDBⁱ	52698 52699 [P11142-2]
TopDownProteomicsⁱ	P11142-1 [P11142-1] P11142-2 [P11142-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	3312
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000227378; ENSP00000227378; ENSG00000109971 [P11142-1] ENST00000453788; ENSP00000404372; ENSG00000109971 [P11142-2] ENST00000532636; ENSP00000437125; ENSG00000109971 [P11142-1] ENST00000534624; ENSP00000432083; ENSG00000109971 [P11142-1]
GeneIDⁱ	3312
KEGGⁱ	hsa:3312
UCSCⁱ	uc001pyp.5 human [P11142-1]

Organism-specific databases

CTDⁱ	3312
DisGeNETⁱ	3312
EuPathDBⁱ	HostDB:ENSG00000109971.13
GeneCardsⁱ	HSPA8
H-InvDBⁱ	HIX0033867
HGNCⁱ	HGNC:5241 HSPA8
HPAⁱ	CAB002056 HPA052504
MIMⁱ	600816 gene
neXtProtⁱ	NX_P11142
OpenTargetsⁱ	ENSG00000109971
PharmGKBⁱ	PA29507
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0101 Eukaryota COG0443 LUCA
GeneTreeⁱ	ENSGT00930000150862
HOGENOMⁱ	HOG000228135
HOVERGENⁱ	HBG051845
InParanoidⁱ	P11142
KOⁱ	K03283
OMAⁱ	AYTKNQD
OrthoDBⁱ	EOG091G03SF
PhylomeDBⁱ	P11142
TreeFamⁱ	TF105042

Enzyme and pathway databases

BRENDAⁱ	3.6.3.51 2681
Reactomeⁱ	R-HSA-3371453 Regulation of HSF1-mediated heat shock response R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR) R-HSA-3371568 Attenuation phase R-HSA-3371571 HSF1-dependent transactivation R-HSA-432720 Lysosome Vesicle Biogenesis R-HSA-432722 Golgi Associated Vesicle Biogenesis R-HSA-447041 CHL1 interactions R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling R-HSA-6798695 Neutrophil degranulation R-HSA-72163 mRNA Splicing - Major Pathway R-HSA-8856828 Clathrin-mediated endocytosis R-HSA-8876725 Protein methylation R-HSA-888590 GABA synthesis, release, reuptake and degradation
SIGNORⁱ	P11142

Miscellaneous databases

ChiTaRSⁱ	HSPA8 human
EvolutionaryTraceⁱ	P11142
GeneWikiⁱ	HSPA8
GenomeRNAiⁱ	3312
PMAP-CutDBⁱ	P11142
Protein Ontology More...PROⁱ	PR:P11142
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000109971 Expressed in 91 organ(s), highest expression level in frontal cortex
CleanExⁱ	HS_HSPA8
ExpressionAtlasⁱ	P11142 baseline and differential
Genevisibleⁱ	P11142 HS

Family and domain databases

Gene3Dⁱ	1.20.1270.10, 1 hit 2.60.34.10, 1 hit
InterProⁱ	View protein in InterPro IPR018181 Heat_shock_70_CS IPR029048 HSP70_C_sf IPR029047 HSP70_peptide-bd_sf IPR013126 Hsp_70_fam
PANTHERⁱ	PTHR19375 PTHR19375, 1 hit
Pfamⁱ	View protein in Pfam PF00012 HSP70, 1 hit
PRINTSⁱ	PR00301 HEATSHOCK70
SUPFAMⁱ	SSF100920 SSF100920, 1 hit SSF100934 SSF100934, 1 hit
PROSITEⁱ	View protein in PROSITE PS00297 HSP70_1, 1 hit PS00329 HSP70_2, 1 hit PS01036 HSP70_3, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HSP7C_HUMAN
Accessionⁱ	P11142Primary (citable) accession number: P11142 Secondary accession number(s): Q9H3R6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	July 1, 1989
	Last modified:	November 7, 2018
	This is version 227 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM

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UniProtKB - P11142 (HSP7C_HUMAN)

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Heat shock cognate 71 kDa protein

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Plasma membrane

Other locations

Cytosol

Endosome

Extracellular region or secreted

Lysosome

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ