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Protein

Heat shock 70 kDa protein 4L

Gene

HSPA4L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 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

Enzyme and pathway databases

ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.

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, OSP94
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:17041. HSPA4L.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

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

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134905749.

Polymorphism and mutation databases

BioMutaiHSPA4L.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 839839Heat shock 70 kDa protein 4LPRO_0000078280Add
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 residuei508 – 5081PhosphoserineCombined sources
Modified residuei545 – 5451PhosphothreonineBy similarity
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

EPDiO95757.
MaxQBiO95757.
PaxDbiO95757.
PeptideAtlasiO95757.
PRIDEiO95757.

2D gel databases

REPRODUCTION-2DPAGEIPI00295485.

PTM databases

iPTMnetiO95757.
PhosphoSiteiO95757.

Expressioni

Inductioni

By heat shock and osmotic imbalance.1 Publication

Gene expression databases

BgeeiO95757.
CleanExiHS_HSPA4L.
ExpressionAtlasiO95757. baseline and differential.
GenevisibleiO95757. HS.

Organism-specific databases

HPAiCAB034450.
HPA039149.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi116500. 59 interactions.
IntActiO95757. 18 interactions.
MINTiMINT-1135179.
STRINGi9606.ENSP00000296464.

Structurei

3D structure databases

ProteinModelPortaliO95757.
SMRiO95757. Positions 3-568, 571-700.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0103. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00390000016919.
HOGENOMiHOG000228138.
HOVERGENiHBG047955.
InParanoidiO95757.
KOiK09485.
OMAiVEMENAN.
OrthoDBiEOG77M8N0.
PhylomeDBiO95757.
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. 2 hits.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 2 hits.
PROSITEiPS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95757-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVVGIDLGF LNCYIAVARS GGIETIANEY SDRCTPACIS LGSRTRAIGN
60 70 80 90 100
AAKSQIVTNV RNTIHGFKKL HGRSFDDPIV QTERIRLPYE LQKMPNGSAG
110 120 130 140 150
VKVRYLEEER PFAIEQVTGM LLAKLKETSE NALKKPVADC VISIPSFFTD
160 170 180 190 200
AERRSVMAAA QVAGLNCLRL MNETTAVALA YGIYKQDLPP LDEKPRNVVF
210 220 230 240 250
IDMGHSAYQV LVCAFNKGKL KVLATTFDPY LGGRNFDEAL VDYFCDEFKT
260 270 280 290 300
KYKINVKENS RALLRLYQEC EKLKKLMSAN ASDLPLNIEC FMNDLDVSSK
310 320 330 340 350
MNRAQFEQLC ASLLARVEPP LKAVMEQANL QREDISSIEI VGGATRIPAV
360 370 380 390 400
KEQITKFFLK DISTTLNADE AVARGCALQC AILSPAFKVR EFSITDLVPY
410 420 430 440 450
SITLRWKTSF EDGSGECEVF CKNHPAPFSK VITFHKKEPF ELEAFYTNLH
460 470 480 490 500
EVPYPDARIG SFTIQNVFPQ SDGDSSKVKV KVRVNIHGIF SVASASVIEK
510 520 530 540 550
QNLEGDHSDA PMETETSFKN ENKDNMDKMQ VDQEEGHQKC HAEHTPEEEI
560 570 580 590 600
DHTGAKTKSA VSDKQDRLNQ TLKKGKVKSI DLPIQSSLCR QLGQDLLNSY
610 620 630 640 650
IENEGKMIMQ DKLEKERNDA KNAVEEYVYD FRDRLGTVYE KFITPEDLSK
660 670 680 690 700
LSAVLEDTEN WLYEDGEDQP KQVYVDKLQE LKKYGQPIQM KYMEHEERPK
710 720 730 740 750
ALNDLGKKIQ LVMKVIEAYR NKDERYDHLD PTEMEKVEKC ISDAMSWLNS
760 770 780 790 800
KMNAQNKLSL TQDPVVKVSE IVAKSKELDN FCNPIIYKPK PKAEVPEDKP
810 820 830
KANSEHNGPM DGQSGTETKS DSTKDSSQHT KSSGEMEVD
Length:839
Mass (Da):94,512
Last modified:November 2, 2010 - v3
Checksum:i549933AECFF4369A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti806 – 8061H → R in BAA75063 (PubMed:10524232).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti211 – 2111L → S.1 Publication
Corresponds to variant rs1380154 [ dbSNP | Ensembl ].
VAR_025405
Natural varianti216 – 2161N → T.
Corresponds to variant rs12507229 [ dbSNP | Ensembl ].
VAR_031214
Natural varianti601 – 6011I → T.
Corresponds to variant rs35518193 [ dbSNP | Ensembl ].
VAR_055966

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023421 mRNA. Translation: BAA75063.1.
EF197155 mRNA. Translation: ABM69040.1.
AC093591 Genomic DNA. Translation: AAY40975.1.
CH471056 Genomic DNA. Translation: EAX05198.1.
BC040560 mRNA. Translation: AAH40560.1.
CCDSiCCDS3734.1.
RefSeqiNP_001304310.1. NM_001317381.1.
NP_001304311.1. NM_001317382.1.
NP_001304312.1. NM_001317383.1.
NP_055093.2. NM_014278.3.
UniGeneiHs.135554.

Genome annotation databases

EnsembliENST00000296464; ENSP00000296464; ENSG00000164070.
ENST00000508776; ENSP00000422482; ENSG00000164070.
GeneIDi22824.
KEGGihsa:22824.
UCSCiuc003ifm.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023421 mRNA. Translation: BAA75063.1.
EF197155 mRNA. Translation: ABM69040.1.
AC093591 Genomic DNA. Translation: AAY40975.1.
CH471056 Genomic DNA. Translation: EAX05198.1.
BC040560 mRNA. Translation: AAH40560.1.
CCDSiCCDS3734.1.
RefSeqiNP_001304310.1. NM_001317381.1.
NP_001304311.1. NM_001317382.1.
NP_001304312.1. NM_001317383.1.
NP_055093.2. NM_014278.3.
UniGeneiHs.135554.

3D structure databases

ProteinModelPortaliO95757.
SMRiO95757. Positions 3-568, 571-700.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116500. 59 interactions.
IntActiO95757. 18 interactions.
MINTiMINT-1135179.
STRINGi9606.ENSP00000296464.

PTM databases

iPTMnetiO95757.
PhosphoSiteiO95757.

Polymorphism and mutation databases

BioMutaiHSPA4L.

2D gel databases

REPRODUCTION-2DPAGEIPI00295485.

Proteomic databases

EPDiO95757.
MaxQBiO95757.
PaxDbiO95757.
PeptideAtlasiO95757.
PRIDEiO95757.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296464; ENSP00000296464; ENSG00000164070.
ENST00000508776; ENSP00000422482; ENSG00000164070.
GeneIDi22824.
KEGGihsa:22824.
UCSCiuc003ifm.4. human.

Organism-specific databases

CTDi22824.
GeneCardsiHSPA4L.
HGNCiHGNC:17041. HSPA4L.
HPAiCAB034450.
HPA039149.
neXtProtiNX_O95757.
PharmGKBiPA134905749.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0103. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00390000016919.
HOGENOMiHOG000228138.
HOVERGENiHBG047955.
InParanoidiO95757.
KOiK09485.
OMAiVEMENAN.
OrthoDBiEOG77M8N0.
PhylomeDBiO95757.
TreeFamiTF105043.

Enzyme and pathway databases

ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

ChiTaRSiHSPA4L. human.
GeneWikiiHSPA4L.
GenomeRNAii22824.
PROiO95757.

Gene expression databases

BgeeiO95757.
CleanExiHS_HSPA4L.
ExpressionAtlasiO95757. baseline and differential.
GenevisibleiO95757. HS.

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. 2 hits.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 2 hits.
PROSITEiPS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-211.
    Tissue: Testis.
  2. "Molecular cloning of OSP94: A significant biomarker protein of hypertensive human heart and a member of HSP110 family."
    Mala J.G., Takeuchi S.
    Mol. Biotechnol. 42:175-194(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Tissue: Heart.
  3. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-508 AND SER-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiHS74L_HUMAN
AccessioniPrimary (citable) accession number: O95757
Secondary accession number(s): A2ICT2, Q4W5M5, Q8IWA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 2, 2010
Last modified: July 6, 2016
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. 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.