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Protein

Heat shock 70 kDa protein 4L

Gene

Hspa4l

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 4L
Alternative name(s):
Heat shock 70-related protein APG-1
Osmotic stress protein 94
Gene namesi
Name:Hspa4l
Synonyms:Apg1, Hsp4l, Osp94
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:107422. Hspa4l.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: May translocate to the nucleus after heat shock.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 838838Heat shock 70 kDa protein 4LPRO_0000078281Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysineBy similarity
Modified residuei74 – 741PhosphoserineCombined sources
Modified residuei89 – 891PhosphotyrosineBy similarity
Modified residuei393 – 3931PhosphoserineBy similarity
Modified residuei430 – 4301N6-acetyllysineBy similarity
Modified residuei545 – 5451PhosphothreonineCombined sources
Modified residuei579 – 5791PhosphoserineCombined sources
Modified residuei663 – 6631PhosphotyrosineBy similarity
Modified residuei682 – 6821N6-acetyllysineBy similarity
Modified residuei759 – 7591PhosphoserineBy similarity
Modified residuei761 – 7611PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP48722.
MaxQBiP48722.
PaxDbiP48722.
PeptideAtlasiP48722.
PRIDEiP48722.

2D gel databases

REPRODUCTION-2DPAGEIPI00317710.
P48722.

PTM databases

iPTMnetiP48722.
PhosphoSiteiP48722.
SwissPalmiP48722.

Expressioni

Tissue specificityi

Highly expressed in testis. Also expressed in renal medulla of water-restricted animals.1 Publication

Inductioni

By hyperosmolar salt stress and heat shock.1 Publication

Gene expression databases

BgeeiP48722.
CleanExiMM_HSPA4L.
ExpressionAtlasiP48722. baseline and differential.
GenevisibleiP48722. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Rtn4Q99P724EBI-8314699,EBI-3869532
Rtn4Q9JK11-16EBI-8314699,EBI-919989From a different organism.

Protein-protein interaction databases

BioGridi201985. 1 interaction.
IntActiP48722. 3 interactions.
MINTiMINT-4098038.
STRINGi10090.ENSMUSP00000076336.

Structurei

3D structure databases

ProteinModelPortaliP48722.
SMRiP48722. Positions 5-700.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0103. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00390000016919.
HOVERGENiHBG047955.
InParanoidiP48722.
KOiK09485.
OMAiHMEHEER.
PhylomeDBiP48722.
TreeFamiTF105043.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 2 hits.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 2 hits.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P48722-1) [UniParc]FASTAAdd 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
MSVVGIDLGF LNCYIAVARS GGIETIANEY SDRCTPACIS LGSRTRAIGN
60 70 80 90 100
AAKSQIVTNV RNTIHGFKKL HGRSFDDPIV QTERIRLPYE LQKMPNGSTG
110 120 130 140 150
VKVRYLEEER PFAIEQVTGM LLAKLKETSE NALKKPVADC VISIPSFFTD
160 170 180 190 200
AERRSVMAAA QVAGLNCLRL MNETTAVALA YGIYKQDLPS LDEKPRNVVF
210 220 230 240 250
IDMGHSAYQV SVCAFNKGKL KVLATTFDPY LGGRNFDEAL VDYFCDEFKT
260 270 280 290 300
KYKINVKENS RALLRLYQEC EKLKKLMSAN ASDLPLNIEC FMNDLDVSSK
310 320 330 340 350
MNRAQFEQLC ASLLARVEPP LKSVMDQANL QREDINSIEI VGGATRIPAV
360 370 380 390 400
KEQVTRFFLK DISTTLNADE AVARGCALQC AILSPAFKVR EFSITDLVPY
410 420 430 440 450
SVTLRWKTSF EEGTGECEVF SKNHPAPFSK VITFHKKEPF ELEAFYTNLH
460 470 480 490 500
EVPYPDPRIG NFTIQNVFPQ SDGDSSKVKV KVRINIHGIF SVASASVIEK
510 520 530 540 550
QNLEGDHNDA AMETEAPKSE GKEDVDKMQV DQEEGGHQKC HAEHTPEEEI
560 570 580 590 600
DHTGAKAKAP PSDKQDRINQ TIKKGKIKSI DLPIQSSLYR QLTQDLLNSY
610 620 630 640 650
IENEGKMIMQ DKLEKERNDA KNAVEEYVYD FRDKLGTVYE KFITPEDMNK
660 670 680 690 700
LSAMLEDTEN WLYEEGEDQP KQVYVDRLQE LKKYGQPIQM KYVEHEERPK
710 720 730 740 750
ALNDLGKKIQ LVLKVIEAHR NKDERYDHLD PAEMERVEKY ISDSMNWLNS
760 770 780 790 800
KMNAQNKLSL TQDPVVKVSE IVTKSKELDN FCNPIVYKPK PKVEAPEDKA
810 820 830
KTGSEHNGPM DGQSGSETSP DPPKGSSQHT DSGEMEVD
Length:838
Mass (Da):94,382
Last modified:May 23, 2003 - v2
Checksum:iB2C5847DA7EAF6B7
GO
Isoform 2 (identifier: P48722-2) [UniParc]FASTAAdd to basket

Also known as: Apg-1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MSVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTP → MGGPPRHGVLDREER

Show »
Length:817
Mass (Da):92,252
Checksum:i38B0704DFEDE5DD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1762TA → HS in BAA08446 (PubMed:9006898).Curated
Sequence conflicti175 – 1762TA → HS in BAA19468 (Ref. 3) Curated
Sequence conflicti221 – 2211K → E in BAA08446 (PubMed:9006898).Curated
Sequence conflicti221 – 2211K → E in BAA19468 (Ref. 3) Curated
Sequence conflicti279 – 2791A → P in BAA08446 (PubMed:9006898).Curated
Sequence conflicti279 – 2791A → P in BAA19468 (Ref. 3) Curated
Sequence conflicti308 – 3081Q → R in BAA08446 (PubMed:9006898).Curated
Sequence conflicti308 – 3081Q → R in BAA19468 (Ref. 3) Curated
Sequence conflicti483 – 4831R → S in BAE37350 (PubMed:16141072).Curated
Sequence conflicti571 – 5711T → A in BAE37350 (PubMed:16141072).Curated
Sequence conflicti776 – 7761K → M in AAC52610 (PubMed:8647834).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MSVVG…DRCTP → MGGPPRHGVLDREER in isoform 2. 1 PublicationVSP_007500Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23921 mRNA. Translation: AAC52610.1.
D49482 mRNA. Translation: BAA08446.1.
AB001926 mRNA. Translation: BAA19468.1.
AK033950 mRNA. Translation: BAC28524.1.
AK050997 mRNA. Translation: BAC34491.1.
AK144225 mRNA. Translation: BAE25783.1.
AK163459 mRNA. Translation: BAE37350.1.
BC012712 mRNA. Translation: AAH12712.1.
BC057002 mRNA. Translation: AAH57002.1.
BC110662 mRNA. Translation: AAI10663.1.
CCDSiCCDS17327.1. [P48722-1]
RefSeqiNP_035150.3. NM_011020.3. [P48722-1]
XP_006500830.1. XM_006500767.2. [P48722-1]
UniGeneiMm.39330.

Genome annotation databases

EnsembliENSMUST00000108086; ENSMUSP00000103721; ENSMUSG00000025757. [P48722-2]
ENSMUST00000204702; ENSMUSP00000145468; ENSMUSG00000025757. [P48722-1]
GeneIDi18415.
KEGGimmu:18415.
UCSCiuc008pbk.1. mouse. [P48722-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23921 mRNA. Translation: AAC52610.1.
D49482 mRNA. Translation: BAA08446.1.
AB001926 mRNA. Translation: BAA19468.1.
AK033950 mRNA. Translation: BAC28524.1.
AK050997 mRNA. Translation: BAC34491.1.
AK144225 mRNA. Translation: BAE25783.1.
AK163459 mRNA. Translation: BAE37350.1.
BC012712 mRNA. Translation: AAH12712.1.
BC057002 mRNA. Translation: AAH57002.1.
BC110662 mRNA. Translation: AAI10663.1.
CCDSiCCDS17327.1. [P48722-1]
RefSeqiNP_035150.3. NM_011020.3. [P48722-1]
XP_006500830.1. XM_006500767.2. [P48722-1]
UniGeneiMm.39330.

3D structure databases

ProteinModelPortaliP48722.
SMRiP48722. Positions 5-700.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201985. 1 interaction.
IntActiP48722. 3 interactions.
MINTiMINT-4098038.
STRINGi10090.ENSMUSP00000076336.

PTM databases

iPTMnetiP48722.
PhosphoSiteiP48722.
SwissPalmiP48722.

2D gel databases

REPRODUCTION-2DPAGEIPI00317710.
P48722.

Proteomic databases

EPDiP48722.
MaxQBiP48722.
PaxDbiP48722.
PeptideAtlasiP48722.
PRIDEiP48722.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108086; ENSMUSP00000103721; ENSMUSG00000025757. [P48722-2]
ENSMUST00000204702; ENSMUSP00000145468; ENSMUSG00000025757. [P48722-1]
GeneIDi18415.
KEGGimmu:18415.
UCSCiuc008pbk.1. mouse. [P48722-1]

Organism-specific databases

CTDi22824.
MGIiMGI:107422. Hspa4l.

Phylogenomic databases

eggNOGiKOG0103. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00390000016919.
HOVERGENiHBG047955.
InParanoidiP48722.
KOiK09485.
OMAiHMEHEER.
PhylomeDBiP48722.
TreeFamiTF105043.

Miscellaneous databases

ChiTaRSiHspa4l. mouse.
PROiP48722.
SOURCEiSearch...

Gene expression databases

BgeeiP48722.
CleanExiMM_HSPA4L.
ExpressionAtlasiP48722. baseline and differential.
GenevisibleiP48722. MM.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 2 hits.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 2 hits.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Osmotic stress protein 94 (Osp94). A new member of the Hsp110/SSE gene subfamily."
    Kojima R., Randall J., Brenner B.M., Gullans S.R.
    J. Biol. Chem. 271:12327-12332(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "A novel hsp110-related gene, apg-1, that is abundantly expressed in the testis responds to a low temperature heat shock rather than the traditional elevated temperatures."
    Kaneko Y., Nishiyama H., Nonoguchi K., Higashitsuji H., Kishishita M., Fujita J.
    J. Biol. Chem. 272:2640-2645(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
    Strain: DDY/STD.
    Tissue: Testis.
  3. "Apg-1b, an alternative form of apg-1 transcript."
    Kaneko Y., Fujita J.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: ddY.
    Tissue: Testis.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Brain and Salivary gland.
  6. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 135-153; 484-500 AND 622-632, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  7. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; THR-545 AND SER-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiHS74L_MOUSE
AccessioniPrimary (citable) accession number: P48722
Secondary accession number(s): P97854
, Q3TQN2, Q3UNG4, Q8BQD0, Q8CC45, Q91X29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 23, 2003
Last modified: July 6, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.