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 4

Gene

Hspa4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. chaperone-mediated protein complex assembly Source: MGI
  2. protein import into mitochondrial outer membrane Source: MGI
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 4
Alternative name(s):
Heat shock 70-related protein APG-2
Gene namesi
Name:Hspa4
Synonyms:Apg2, Hsp110
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1342292. Hspa4.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytosol Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 841841Heat shock 70 kDa protein 4PRO_0000078263Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysine1 Publication
Modified residuei76 – 761PhosphoserineBy similarity
Modified residuei89 – 891PhosphotyrosineBy similarity
Modified residuei336 – 3361Phosphotyrosine2 Publications
Modified residuei430 – 4301N6-acetyllysineBy similarity
Modified residuei540 – 5401PhosphothreonineBy similarity
Modified residuei548 – 5481PhosphoserineBy similarity
Modified residuei661 – 6611Phosphotyrosine1 Publication
Modified residuei680 – 6801N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61316.
PaxDbiQ61316.
PRIDEiQ61316.

2D gel databases

REPRODUCTION-2DPAGEQ61316.

PTM databases

PhosphoSiteiQ61316.

Expressioni

Gene expression databases

CleanExiMM_HSPA4.
GenevestigatoriQ61316.

Interactioni

Subunit structurei

Interacts with TJP1/ZO-1.By similarity

Protein-protein interaction databases

DIPiDIP-46965N.
IntActiQ61316. 3 interactions.
MINTiMINT-1869188.
STRINGi10090.ENSMUSP00000020630.

Structurei

3D structure databases

ProteinModelPortaliQ61316.
SMRiQ61316. Positions 5-698.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiCOG0443.
HOVERGENiHBG047955.
InParanoidiQ61316.

Family and domain databases

Gene3Di1.20.1270.10. 2 hits.
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. 1 hit.
SSF100934. SSF100934. 2 hits.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61316-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACVS FGPKNRSIGA
60 70 80 90 100
AAKSQVISNA KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG
110 120 130 140 150
IKVTYMEEER NFTTEQVTAM LLSKLKETAE SVLKKPVVDC VVSVPSFYTD
160 170 180 190 200
AERRSVMDAT QIAGLNCLRL MNETTAVALA YGIYKQDLPA LEEKPRNVVF
210 220 230 240 250
VDMGHSAYQV SVCAFNKGKL KVLATAFDTT LGGRKFDEVL VNHFCEEFGK
260 270 280 290 300
KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDIDVSGT
310 320 330 340 350
MNRGKFLEMC DDLLARVEPP LRSVLEQSKL KKEDIYAVEI VGGATRIPAV
360 370 380 390 400
KEKISKFFGK ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY
410 420 430 440 450
PISLRWNSPA EEGLSDCEVF PKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ
460 470 480 490 500
DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV KVRVNVHGIF SVSSAALVEV
510 520 530 540 550
HKSEESEEPM ETDQNAKEEE KMQVDQEEPH TEEQQQQPQT PAENKAESEE
560 570 580 590 600
METSQAGSKD KKTDQPPQAK KAKVKTSTVD LPIEHTLWQL DREMLALYTE
610 620 630 640 650
NEGKMIMQDK LEKERNDAKN AVEEYVYEMR DKLSGEYEKF VSEDDRNTFT
660 670 680 690 700
LKLEDTENWL YEDGEDQPKQ VYVDKLAELK SLGQPIKTRF QESEERPKLF
710 720 730 740 750
EELGKQIQQY MKVISSFKNK EDQYEHLDAA DVTKVEKSTN EAMEWMNSKL
760 770 780 790 800
NLQNKQSLTV DPVVKTKEIE AKIKELTSIC SPIISKPKPK VEPPKEEPKH
810 820 830 840
AEQNGPVDGQ GDNPGSQAAE HGADTAVPSD GDKKLPEMDI D
Length:841
Mass (Da):94,133
Last modified:November 1, 1996 - v1
Checksum:iE7FF19F555C115ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85904 mRNA. Translation: BAA12914.1.
UniGeneiMm.239865.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85904 mRNA. Translation: BAA12914.1.
UniGeneiMm.239865.

3D structure databases

ProteinModelPortaliQ61316.
SMRiQ61316. Positions 5-698.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46965N.
IntActiQ61316. 3 interactions.
MINTiMINT-1869188.
STRINGi10090.ENSMUSP00000020630.

PTM databases

PhosphoSiteiQ61316.

2D gel databases

REPRODUCTION-2DPAGEQ61316.

Proteomic databases

MaxQBiQ61316.
PaxDbiQ61316.
PRIDEiQ61316.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1342292. Hspa4.

Phylogenomic databases

eggNOGiCOG0443.
HOVERGENiHBG047955.
InParanoidiQ61316.

Miscellaneous databases

ChiTaRSiHspa4. mouse.
PROiQ61316.
SOURCEiSearch...

Gene expression databases

CleanExiMM_HSPA4.
GenevestigatoriQ61316.

Family and domain databases

Gene3Di1.20.1270.10. 2 hits.
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. 1 hit.
SSF100934. SSF100934. 2 hits.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of apg-2 encoding a novel member of heat shock protein 110 family."
    Kaneko Y., Kimura T., Kishishita M., Noda Y., Fujita J.
    Gene 189:19-24(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: DDY/STD.
    Tissue: Testis.
  2. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 74-124; 155-169; 186-196; 220-234; 330-346; 361-374; 391-405; 699-705 AND 719-734, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  3. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336 AND TYR-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHSP74_MOUSE
AccessioniPrimary (citable) accession number: Q61316
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 4, 2015
This is version 109 of the entry and version 1 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

External Data

Dasty 3

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 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.