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P34932

- HSP74_HUMAN

UniProt

P34932 - HSP74_HUMAN

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Protein

Heat shock 70 kDa protein 4

Gene
HSPA4, APG2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. ATP binding Source: UniProtKB

GO - Biological processi

  1. chaperone-mediated protein complex assembly Source: BHF-UCL
  2. protein import into mitochondrial outer membrane Source: BHF-UCL
  3. response to unfolded protein Source: UniProtKB
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):
HSP70RY
Heat shock 70-related protein APG-2
Gene namesi
Name:HSPA4
Synonyms:APG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:5237. HSPA4.

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29503.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 840840Heat shock 70 kDa protein 4PRO_0000078262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysine By similarity
Modified residuei76 – 761Phosphoserine2 Publications
Modified residuei89 – 891Phosphotyrosine1 Publication
Modified residuei336 – 3361Phosphotyrosine2 Publications
Modified residuei430 – 4301N6-acetyllysine1 Publication
Modified residuei538 – 5381Phosphothreonine1 Publication
Modified residuei546 – 5461Phosphoserine1 Publication
Modified residuei660 – 6601Phosphotyrosine By similarity
Modified residuei679 – 6791N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP34932.
PaxDbiP34932.
PRIDEiP34932.

2D gel databases

DOSAC-COBS-2DPAGEP34932.
REPRODUCTION-2DPAGEIPI00002966.
P34932.

PTM databases

PhosphoSiteiP34932.

Expressioni

Gene expression databases

ArrayExpressiP34932.
BgeeiP34932.
CleanExiHS_HSPA4.
GenevestigatoriP34932.

Organism-specific databases

HPAiCAB025529.
HPA010023.

Interactioni

Subunit structurei

Interacts with TJP1/ZO-1 By similarity.

Protein-protein interaction databases

BioGridi109540. 277 interactions.
DIPiDIP-460N.
IntActiP34932. 23 interactions.
MINTiMINT-1159519.
STRINGi9606.ENSP00000302961.

Structurei

3D structure databases

ProteinModelPortaliP34932.
SMRiP34932. Positions 5-697.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0443.
HOGENOMiHOG000228138.
HOVERGENiHBG047955.
InParanoidiP34932.
KOiK09489.
OMAiKVKYMEE.
OrthoDBiEOG77M8N0.
PhylomeDBiP34932.
TreeFamiTF105043.

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. 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]

Sequencei

Sequence statusi: Complete.

P34932-1 [UniParc]FASTAAdd to Basket

« Hide

MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACIS FGPKNRSIGA    50
AAKSQVISNA KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG 100
IKVTYMEEER NFTTEQVTAM LLSKLKETAE SVLKKPVVDC VVSVPCFYTD 150
AERRSVMDAT QIAGLNCLRL MNETTAVALA YGIYKQDLPA LEEKPRNVVF 200
VDMGHSAYQV SVCAFNRGKL KVLATAFDTT LGGRKFDEVL VNHFCEEFGK 250
KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDVDVSGT 300
MNRGKFLEMC NDLLARVEPP LRSVLEQTKL KKEDIYAVEI VGGATRIPAV 350
KEKISKFFGK ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY 400
PISLRWNSPA EEGSSDCEVF SKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ 450
DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV KVRVNVHGIF SVSSASLVEV 500
HKSEENEEPM ETDQNAKEEE KMQVDQEEPH VEEQQQQTPA ENKAESEEME 550
TSQAGSKDKK MDQPPQAKKA KVKTSTVDLP IENQLLWQID REMLNLYIEN 600
EGKMIMQDKL EKERNDAKNA VEEYVYEMRD KLSGEYEKFV SEDDRNSFTL 650
KLEDTENWLY EDGEDQPKQV YVDKLAELKN LGQPIKIRFQ ESEERPKLFE 700
ELGKQIQQYM KIISSFKNKE DQYDHLDAAD MTKVEKSTNE AMEWMNNKLN 750
LQNKQSLTMD PVVKSKEIEA KIKELTSTCS PIISKPKPKV EPPKEEQKNA 800
EQNGPVDGQG DNPGPQAAEQ GTDTAVPSDS DKKLPEMDID 840
Length:840
Mass (Da):94,331
Last modified:September 23, 2008 - v4
Checksum:i8B690A52A0729C2A
GO

Sequence cautioni

The sequence AAA02807.1 differs from that shown. Reason: Frameshift at positions 567, 586, 697, 715 and 722.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941L → W in AAA02807. 1 Publication
Sequence conflicti190 – 1901A → R in AAA02807. 1 Publication
Sequence conflicti583 – 5864NQLL → ESAI in AAA02807. 1 Publication
Sequence conflicti622 – 6221E → R in BAA75062. 1 Publication
Sequence conflicti644 – 6441D → G in BAA75062. 1 Publication
Sequence conflicti746 – 7494NNKL → EVTP in AAA02807. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB023420 mRNA. Translation: BAA75062.1.
AC113410 Genomic DNA. No translation available.
BC110861 mRNA. Translation: AAI10862.1.
BC126122 mRNA. Translation: AAI26123.1.
BC126124 mRNA. Translation: AAI26125.1.
L12723 mRNA. Translation: AAA02807.1. Frameshift.
CCDSiCCDS4166.1.
PIRiI56208.
RefSeqiNP_002145.3. NM_002154.3.
UniGeneiHs.90093.

Genome annotation databases

EnsembliENST00000304858; ENSP00000302961; ENSG00000170606.
GeneIDi3308.
KEGGihsa:3308.
UCSCiuc003kyj.3. human.

Polymorphism databases

DMDMi206729934.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB023420 mRNA. Translation: BAA75062.1 .
AC113410 Genomic DNA. No translation available.
BC110861 mRNA. Translation: AAI10862.1 .
BC126122 mRNA. Translation: AAI26123.1 .
BC126124 mRNA. Translation: AAI26125.1 .
L12723 mRNA. Translation: AAA02807.1 . Frameshift.
CCDSi CCDS4166.1.
PIRi I56208.
RefSeqi NP_002145.3. NM_002154.3.
UniGenei Hs.90093.

3D structure databases

ProteinModelPortali P34932.
SMRi P34932. Positions 5-697.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109540. 277 interactions.
DIPi DIP-460N.
IntActi P34932. 23 interactions.
MINTi MINT-1159519.
STRINGi 9606.ENSP00000302961.

PTM databases

PhosphoSitei P34932.

Polymorphism databases

DMDMi 206729934.

2D gel databases

DOSAC-COBS-2DPAGE P34932.
REPRODUCTION-2DPAGE IPI00002966.
P34932.

Proteomic databases

MaxQBi P34932.
PaxDbi P34932.
PRIDEi P34932.

Protocols and materials databases

DNASUi 3308.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304858 ; ENSP00000302961 ; ENSG00000170606 .
GeneIDi 3308.
KEGGi hsa:3308.
UCSCi uc003kyj.3. human.

Organism-specific databases

CTDi 3308.
GeneCardsi GC05P132415.
HGNCi HGNC:5237. HSPA4.
HPAi CAB025529.
HPA010023.
MIMi 601113. gene.
neXtProti NX_P34932.
PharmGKBi PA29503.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0443.
HOGENOMi HOG000228138.
HOVERGENi HBG047955.
InParanoidi P34932.
KOi K09489.
OMAi KVKYMEE.
OrthoDBi EOG77M8N0.
PhylomeDBi P34932.
TreeFami TF105043.

Miscellaneous databases

ChiTaRSi HSPA4. human.
GeneWikii HSPA4.
GenomeRNAii 3308.
NextBioi 13119.
PROi P34932.
SOURCEi Search...

Gene expression databases

ArrayExpressi P34932.
Bgeei P34932.
CleanExi HS_HSPA4.
Genevestigatori P34932.

Family and domain databases

Gene3Di 1.20.1270.10. 2 hits.
2.60.34.10. 2 hits.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 2 hits.
PROSITEi PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of human apg-1 and apg-2, members of the hsp110 family, cDNAs and chromosomal assignment of the genes."
    Nonoguchi K., Fujita J.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Skin.
  4. "Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5."
    Fathallah D.M., Cherif D., Dellagi K., Arnaout M.A.
    J. Immunol. 151:810-813(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-749.
    Tissue: Lymphocyte.
  5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 20-33; 111-124; 170-185; 222-234; 333-346; 361-374 AND 391-422, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89 AND TYR-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND TYR-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430 AND LYS-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHSP74_HUMAN
AccessioniPrimary (citable) accession number: P34932
Secondary accession number(s): O95756, Q2TAL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: September 23, 2008
Last modified: September 3, 2014
This is version 142 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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