Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heat shock 70 kDa protein 1-like

Gene

Hspa1l

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity 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. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei73ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 17ATPBy similarity4
Nucleotide bindingi204 – 206ATPBy similarity3
Nucleotide bindingi270 – 277ATPBy similarity8
Nucleotide bindingi341 – 344ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein
Biological processDifferentiation, Spermatogenesis, Stress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-3371453 Regulation of HSF1-mediated heat shock response
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-3371568 Attenuation phase
R-MMU-3371571 HSF1-dependent transactivation

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 1-like
Short name:
Heat shock 70 kDa protein 1L
Alternative name(s):
Heat shock 70 kDa-like protein 1
Spermatid-specific heat shock protein 70
Gene namesi
Name:Hspa1l
Synonyms:Hsc70t
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:96231 Hspa1l

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000782561 – 641Heat shock 70 kDa protein 1-likeAdd BLAST641

Proteomic databases

EPDiP16627
MaxQBiP16627
PaxDbiP16627
PRIDEiP16627

2D gel databases

REPRODUCTION-2DPAGEIPI00133208
P16627

PTM databases

CarbonylDBiP16627
iPTMnetiP16627
PhosphoSitePlusiP16627
SwissPalmiP16627

Expressioni

Tissue specificityi

Expressed in spermatids.

Developmental stagei

Specifically expressed in postmeiotic phases of spermatogenesis.

Gene expression databases

BgeeiENSMUSG00000007033
CleanExiMM_HSPA1L
ExpressionAtlasiP16627 baseline and differential
GenevisibleiP16627 MM

Interactioni

Subunit structurei

Interacts with PRKN.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200429, 4 interactors
IntActiP16627, 5 interactors
MINTiP16627
STRINGi10090.ENSMUSP00000007248

Structurei

3D structure databases

ProteinModelPortaliP16627
SMRiP16627
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni3 – 388Nucleotide-binding domain (NBD)By similarityAdd BLAST386
Regioni396 – 511Substrate-binding domain (SBD)By similarityAdd BLAST116

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.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00910000144045
HOGENOMiHOG000228135
HOVERGENiHBG051845
InParanoidiP16627
KOiK03283
OMAiGEKKAFY
OrthoDBiEOG091G03SF
PhylomeDBiP16627
TreeFamiTF105042

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit

Sequencei

Sequence statusi: Complete.

P16627-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAANKGMAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE
60 70 80 90 100
RLIGDAAKNQ VAMNPQNTVF DAKRLIGRKF NDPVVQSDMK LWPFQVINEA
110 120 130 140 150
GKPKVMVSYK GEKKAFYPEE ISSMVLTKMK ETAEAFLGHN VTNAVITVPA
160 170 180 190 200
YFNDSQRQAT KDAGVIAGLN VLRIINEPTA AAIAYGLDKG SHGERHVLIF
210 220 230 240 250
DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV SHFVEEFKRK
260 270 280 290 300
HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT
310 320 330 340 350
RARFEELCAD LFRGTLEPVE KSLRDAKMDK AKIHDIVLVG GSTRIPKVQK
360 370 380 390 400
LLQDYFNGRD LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP
410 420 430 440 450
LSLGLETAGG VMTVLIKRNS TIPTKQTQIF TTYSDNQPGV LIQVYEGERA
460 470 480 490 500
MTRDNNLLGR FDLTGIPPAP RGVPQIEVTF DIDANGILNV TAMDKSTGKA
510 520 530 540 550
NKITITNDKG RLSKEEIERM VQEAERYKAE DEGQREKIAA KNALESYAFN
560 570 580 590 600
MKSAVGDEGL KDKISESDKK KILDKCNEVL SWLEANQLAE KDEFDHKRKE
610 620 630 640
LENMCNPIIT KLYQSGCTGP TCTPGYTPGR AATGPTIEEV D
Length:641
Mass (Da):70,637
Last modified:December 21, 2004 - v4
Checksum:i94CA15217B03BC28
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti570K → N in BAA32522 (PubMed:9685725).Curated1
Sequence conflicti634G → D in AAA74906 (PubMed:2302214).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32218 mRNA Translation: AAA74906.1
L27086 Genomic DNA Translation: AAA59362.1
D85732 mRNA Translation: BAA32522.1
AF109906 Genomic DNA Translation: AAC84170.1
CCDSiCCDS28670.1
PIRiA34041
I49761
RefSeqiNP_038586.2, NM_013558.2
UniGeneiMm.14287

Genome annotation databases

EnsembliENSMUST00000007248; ENSMUSP00000007248; ENSMUSG00000007033
GeneIDi15482
KEGGimmu:15482
UCSCiuc008ceq.1 mouse

Similar proteinsi

Entry informationi

Entry nameiHS71L_MOUSE
AccessioniPrimary (citable) accession number: P16627
Secondary accession number(s): O88686, Q61693
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 21, 2004
Last modified: May 23, 2018
This is version 153 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health