Reviewed,
UniProtKB/Swiss-Prot P34932 (HSP74_HUMAN)
Last modified
November 3, 2009.
Version 97.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Heat shock 70 kDa protein 4 Alternative name(s): Heat shock 70-related protein APG-2 HSP70RY | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 840 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Subunit structure | Interacts with TJP1/ZO-1 By similarity. |
| Subcellular location | Cytoplasm Probable. |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 Ref.8 |
| Sequence similarities | Belongs to the heat shock protein 70 family. |
| Sequence caution | The sequence AAA02807.1 differs from that shown. Reason: Frameshift at positions 567, 586, 697, 715 and 722. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Stress response |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cellular chaperone-mediated protein complex assembly Inferred from direct assay. Source: UniProtKB mitochondrial outer membrane translocase complex assemblyInferred from direct assay. Source: UniProtKB response to unfolded protein Ref.4Non-traceable author statement. Source: UniProtKB |
| Cellular component | cytoplasm Non-traceable author statement. Source: UniProtKB nucleusInferred from direct assay. Source: HPA |
| Molecular function | ATP binding Ref.4 Non-traceable author statement. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 840 | 840 | Heat shock 70 kDa protein 4 | PRO_0000078262 | |||||
Amino acid modifications | |||||||||
| Modified residue | 76 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 89 | 1 | Phosphotyrosine Ref.6 | ||||||
| Modified residue | 336 | 1 | Phosphotyrosine Ref.6 | ||||||
| Modified residue | 430 | 1 | N6-acetyllysine Ref.10 | ||||||
| Modified residue | 538 | 1 | Phosphothreonine Ref.8 | ||||||
| Modified residue | 552 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 660 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 679 | 1 | N6-acetyllysine Ref.10 | ||||||
Experimental info | |||||||||
| Sequence conflict | 94 | 1 | L → W in AAA02807. Ref.4 | ||||||
| Sequence conflict | 190 | 1 | A → R in AAA02807. Ref.4 | ||||||
| Sequence conflict | 583 – 586 | 4 | NQLL → ESAI in AAA02807. Ref.4 | ||||||
| Sequence conflict | 622 | 1 | E → R in BAA75062. Ref.1 | ||||||
| Sequence conflict | 644 | 1 | D → G in BAA75062. Ref.1 | ||||||
| Sequence conflict | 746 – 749 | 4 | NNKL → EVTP in AAA02807. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. Rubin E.M.Nature 431:268-274(2004) [PubMed: 15372022] [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: 15489334] [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: 8335910] [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, 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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89 AND TYR-336, MASS SPECTROMETRY. |
| [7] | "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 SER-552, MASS SPECTROMETRY. |
| [8] | "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 SER-76 AND THR-538, MASS SPECTROMETRY. |
| [9] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430 AND LYS-679, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| 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. | |
| IPI | IPI00002966. |
| PIR | I56208. |
| RefSeq | NP_002145.3. |
| UniGene | Hs.90093 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BA1 based on UniProtKB P19120. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P34932. 7 interactions. |
| STRING | P34932. |
PTM databases | |
| PhosphoSite | P34932. |
2-D gel databases | |
| DOSAC-COBS-2DPAGE | P34932. |
| REPRODUCTION-2DPAGE | IPI00002966. P34932. |
Proteomic databases | |
| PRIDE | P34932. |
Genome annotation databases | |
| Ensembl | ENST00000304858; ENSP00000302961; ENSG00000170606; Homo sapiens. [Genome view] ENST00000321956; ENSP00000320397; ENSG00000170606; Homo sapiens. [Genome view] |
| GeneID | 3308. |
| KEGG | hsa:3308. |
| UCSC | uc003kyj.1. human. |
Organism-specific databases | |
| CTD | 3308. |
| GeneCards | GC05P132415. |
| H-InvDB | HIX0005166. |
| HGNC | HGNC:5237. HSPA4. |
| HPA | HPA010023. |
| MIM | 601113. gene. |
| PharmGKB | PA29503. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | P34932. |
| HOVERGEN | P34932. |
| OMA | QGDNPGP. |
Gene expression databases | |
| ArrayExpress | P34932. |
| Bgee | P34932. |
| CleanEx | HS_HSPA4. |
| Genevestigator | P34932. |
| GermOnline | ENSG00000170606. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR018181. Heat_shock_70_CS. IPR001023. Hsp70. IPR013126. Hsp_70. [Graphical view] |
| PANTHER | PTHR19375. Hsp70. 1 hit. |
| Pfam | PF00012. HSP70. 2 hits. [Graphical view] |
| PRINTS | PR00301. HEATSHOCK70. |
| ProDom | PD000089. Hsp70. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00297. HSP70_1. False negative. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 13119. |
| SOURCE | Search... |
Entry information
| Entry name | HSP74_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P34932 Secondary accession number(s): O95756, Q2TAL4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 5 Human chromosome 5: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


