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Reviewed, UniProtKB/Swiss-Prot O95757 (HS74L_HUMAN)

Last modified June 16, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Heat shock 70 kDa protein 4L
Alternative name(s):
    Osmotic stress protein 94
    Heat shock 70-related protein APG-1
Gene names
Name: HSPA4L
Synonyms: APG1, OSP94
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length839 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Induction

By heat shock.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.4 Ref.5

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processprotein folding

Inferred from sequence or structural similarity. Source: UniProtKB

response to unfolded protein Ref.1

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

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 839839Heat shock 70 kDa protein 4L
PRO_0000078280

Amino acid modifications

Modified residue741Phosphoserine By similarity
Modified residue5711Phosphothreonine Ref.5
Modified residue7611Phosphothreonine Ref.4

Natural variations

Natural variant2111S → L: dbSNP rs1380154. Ref.2 Ref.3
VAR_025405
Natural variant2161N → T: dbSNP rs12507229.
VAR_031214
Natural variant6011I → T: dbSNP rs35518193.
VAR_055966

Experimental info

Sequence conflict8061H → R in BAA75063. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O95757-1 [UniParc].

Last modified May 23, 2003. Version 2.
Checksum: AB9936A3F32AAE8E

FASTA83994,486
        10         20         30         40         50         60 
MSVVGIDLGF LNCYIAVARS GGIETIANEY SDRCTPACIS LGSRTRAIGN AAKSQIVTNV 

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

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

       190        200        210        220        230        240 
YGIYKQDLPP 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 LKAVMEQANL QREDISSIEI VGGATRIPAV KEQITKFFLK 

       370        380        390        400        410        420 
DISTTLNADE AVARGCALQC AILSPAFKVR EFSITDLVPY SITLRWKTSF EDGSGECEVF 

       430        440        450        460        470        480 
CKNHPAPFSK VITFHKKEPF ELEAFYTNLH EVPYPDARIG SFTIQNVFPQ SDGDSSKVKV 

       490        500        510        520        530        540 
KVRVNIHGIF SVASASVIEK QNLEGDHSDA PMETETSFKN ENKDNMDKMQ VDQEEGHQKC 

       550        560        570        580        590        600 
HAEHTPEEEI DHTGAKTKSA VSDKQDRLNQ TLKKGKVKSI DLPIQSSLCR QLGQDLLNSY 

       610        620        630        640        650        660 
IENEGKMIMQ DKLEKERNDA KNAVEEYVYD FRDRLGTVYE KFITPEDLSK LSAVLEDTEN 

       670        680        690        700        710        720 
WLYEDGEDQP KQVYVDKLQE LKKYGQPIQM KYMEHEERPK ALNDLGKKIQ LVMKVIEAYR 

       730        740        750        760        770        780 
NKDERYDHLD PTEMEKVEKC ISDAMSWLNS KMNAQNKLSL TQDPVVKVSE IVAKSKELDN 

       790        800        810        820        830 
FCNPIIYKPK PKAEVPEDKP KANSEHNGPM DGQSGTETKS DSTKDSSQHT KSSGEMEVD 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of human cDNAs for Apg-1 and Apg-2, members of the Hsp110 family, and chromosomal assignment of their genes."
Nonoguchi K., Itoh K., Xue J.H., Tokuchi H., Nishiyama H., Kaneko Y., Tatsumi K., Okuno H., Tomiwa K., Fujita J.
Gene 237:21-28(1999) [PubMed: 10524232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-211.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-211.
[4]"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: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-761, MASS SPECTROMETRY.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571, MASS SPECTROMETRY.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

AB023421 mRNA. Translation: BAA75063.1.
AC093591 Genomic DNA. Translation: AAY40975.1.
BC040560 mRNA. Translation: AAH40560.1.
IPIIPI00295485.
RefSeqNP_055093.2.
UniGeneHs.135554

3D structure databases

HSSPHSSP built from PDB template 1HJO based on UniProtKB P08107.
ModBaseSearch...

Protein-protein interaction databases

IntActO95757. 13 interactions.

PTM databases

PhosphoSiteO95757.

2-D gel databases

REPRODUCTION-2DPAGEIPI00295485.

Proteomic databases

PRIDEO95757.

Genome annotation databases

EnsemblENSG00000164070. Homo sapiens. [Contig view]
GeneID22824.
KEGGhsa:22824.

Organism-specific databases

GeneCardsGC04P128922.
HGNCHGNC:17041. HSPA4L.
PharmGKBPA134905749.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO95757.
HOVERGENO95757.

Gene expression databases

ArrayExpressO95757.
BgeeO95757.
CleanExHS_HSPA4L.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]
PANTHERPTHR19375. Hsp70. 1 hit.
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
ProDomPD000089. Hsp70. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00297. HSP70_1. False negative.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio43228.

Entry information

Entry nameHS74L_HUMAN
AccessionPrimary (citable) accession number: O95757
Secondary accession number(s): Q4W5M5, Q8IWA2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 23, 2003
Last modified: June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents