Skip Header

Contribute Send feedback
Read comments (?) or add your own

P48722 (HS74L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock 70 kDa protein 4L
Alternative name(s):
Heat shock 70-related protein APG-1
Osmotic stress protein 94
Gene names
Name:Hspa4l
Synonyms:Apg1, Hsp4l, Osp94
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length838 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Homodimer By similarity.

Subcellular location

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

Tissue specificity

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

Induction

By hyperosmolar salt stress and heat shock. Ref.2

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from sequence or structural similarity. Source: UniProtKB

response to unfolded protein

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48722-1)

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.
Isoform 2 (identifier: P48722-2)

Also known as: Apg-1b;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 838838Heat shock 70 kDa protein 4L
PRO_0000078281

Amino acid modifications

Modified residue741Phosphoserine Ref.7
Modified residue7611Phosphothreonine Ref.8

Natural variations

Alternative sequence1 – 3636MSVVG…DRCTP → MGGPPRHGVLDREER in isoform 2.
VSP_007500

Experimental info

Sequence conflict175 – 1762TA → HS in BAA08446. Ref.2
Sequence conflict175 – 1762TA → HS in BAA19468. Ref.3
Sequence conflict2211K → E in BAA08446. Ref.2
Sequence conflict2211K → E in BAA19468. Ref.3
Sequence conflict2791A → P in BAA08446. Ref.2
Sequence conflict2791A → P in BAA19468. Ref.3
Sequence conflict3081Q → R in BAA08446. Ref.2
Sequence conflict3081Q → R in BAA19468. Ref.3
Sequence conflict4831R → S in BAE37350. Ref.4
Sequence conflict5711T → A in BAE37350. Ref.4
Sequence conflict7761K → M in AAC52610. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 23, 2003. Version 2.
Checksum: B2C5847DA7EAF6B7

FASTA83894,382
        10         20         30         40         50         60 
MSVVGIDLGF LNCYIAVARS GGIETIANEY SDRCTPACIS LGSRTRAIGN AAKSQIVTNV 

        70         80         90        100        110        120 
RNTIHGFKKL HGRSFDDPIV QTERIRLPYE LQKMPNGSTG VKVRYLEEER PFAIEQVTGM 

       130        140        150        160        170        180 
LLAKLKETSE NALKKPVADC VISIPSFFTD AERRSVMAAA QVAGLNCLRL MNETTAVALA 

       190        200        210        220        230        240 
YGIYKQDLPS LDEKPRNVVF IDMGHSAYQV SVCAFNKGKL KVLATTFDPY LGGRNFDEAL 

       250        260        270        280        290        300 
VDYFCDEFKT KYKINVKENS RALLRLYQEC EKLKKLMSAN ASDLPLNIEC FMNDLDVSSK 

       310        320        330        340        350        360 
MNRAQFEQLC ASLLARVEPP LKSVMDQANL QREDINSIEI VGGATRIPAV KEQVTRFFLK 

       370        380        390        400        410        420 
DISTTLNADE AVARGCALQC AILSPAFKVR EFSITDLVPY SVTLRWKTSF EEGTGECEVF 

       430        440        450        460        470        480 
SKNHPAPFSK VITFHKKEPF ELEAFYTNLH EVPYPDPRIG NFTIQNVFPQ SDGDSSKVKV 

       490        500        510        520        530        540 
KVRINIHGIF SVASASVIEK QNLEGDHNDA AMETEAPKSE GKEDVDKMQV DQEEGGHQKC 

       550        560        570        580        590        600 
HAEHTPEEEI DHTGAKAKAP PSDKQDRINQ TIKKGKIKSI DLPIQSSLYR QLTQDLLNSY 

       610        620        630        640        650        660 
IENEGKMIMQ DKLEKERNDA KNAVEEYVYD FRDKLGTVYE KFITPEDMNK LSAMLEDTEN 

       670        680        690        700        710        720 
WLYEEGEDQP KQVYVDRLQE LKKYGQPIQM KYVEHEERPK ALNDLGKKIQ LVLKVIEAHR 

       730        740        750        760        770        780 
NKDERYDHLD PAEMERVEKY ISDSMNWLNS KMNAQNKLSL TQDPVVKVSE IVTKSKELDN 

       790        800        810        820        830 
FCNPIVYKPK PKVEAPEDKA KTGSEHNGPM DGQSGSETSP DPPKGSSQHT DSGEMEVD 

« Hide

Isoform 2 (Apg-1b) [UniParc].

Checksum: 38B0704DFEDE5DD4
Show »

FASTA81792,252

References

« Hide 'large scale' references
[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. expand/collapse author list , 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, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, MASS SPECTROMETRY.
Tissue: Brain cortex.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-761, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00317710.
IPI00317711.
RefSeqNP_035150.3. NM_011020.3.
UniGeneMm.39330.

3D structure databases

ProteinModelPortalP48722.
SMRP48722. Positions 5-700.
ModBaseSearch...

PTM databases

PhosphoSiteP48722.

2D gel databases

REPRODUCTION-2DPAGEIPI00317710.
P48722.

Proteomic databases

PaxDbP48722.
PRIDEP48722.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077083; ENSMUSP00000076336; ENSMUSG00000025757.
ENSMUST00000108086; ENSMUSP00000103721; ENSMUSG00000025757.
GeneID18415.
KEGGmmu:18415.
UCSCuc008pbk.1. mouse.
uc008pbl.1. mouse.

Organism-specific databases

CTD22824.
MGIMGI:107422. Hspa4l.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00390000016919.
HOVERGENHBG047955.
InParanoidP48722.
KOK09485.
OMAFITPEDM.
OrthoDBEOG40K7Z4.

Gene expression databases

ArrayExpressP48722.
BgeeP48722.
CleanExMM_HSPA4L.
GenevestigatorP48722.
GermOnlineENSMUSG00000025757. Mus musculus.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
PROSITEPS00297. HSP70_1. False negative.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSPA4L. mouse.
NextBio294048.
SOURCESearch...

Entry information

Entry nameHS74L_MOUSE
AccessionPrimary (citable) accession number: P48722
Secondary accession number(s): P97854 expand/collapse secondary AC list , Q3TQN2, Q3UNG4, Q8BQD0, Q8CC45, Q91X29
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 23, 2003
Last modified: May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families