SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00003848 
UniProt Accession
Theoretical PI
5.37  
Molecular Weight
70871 Da  
Genbank Nucleotide ID
Genbank Protein ID
AAA37869.1; AAC52836.1; AAB18391.1; BAC29016.1; BAC36065.1; BAE26523.1; BAE27374.1; BAE27588.1; BAE28187.1; BAE29591.1; BAE29612.1; BAE29780.1; BAE29990.1; BAE30081.1; BAE30135.1; BAE30272.1; BAE30398.1; BAE30465.1; BAE30484.1; BAE30681.1; BAE30707.1; BAE30753.1; BAE30776.1; BAE30822.1; BAE30861.1; BAE31346.1; BAE31427.1; BAE31432.1; BAE31508.1; BAE31664.1; BAE32204.1; BAE35116.1; BAE37581.1; BAE38912.1; BAE38970.1; BAE39005.1; BAE39012.1; BAE39036.1; BAE39053.1; BAE39065.1; BAE39076.1; BAE39084.1; BAE39109.1; BAE39111.1; BAE39113.1; BAE39127.1; BAE39211.1; BAE39269.1; BAE39270.1; BAE39280.1; BAE39304.1; BAE39344.1; BAE39353.1; BAE39865.1; BAE39917.1; BAE40379.1; BAE40398.1; BAE40419.1; BAE40553.1; BAE40590.1; BAE40612.1; BAE40704.1; BAE40745.1; BAE40876.1; BAE40957.1; BAE41004.1; BAE41049.1; AAH06722.1; AAH66191.1; AAH85486.1; AAH89322.1; AAH89457.1; AAI06194.1; CAA38267.1; CAA38268.1; CAA38269.1; 
Gene Name
Hspa8 
Gene Synonyms/Alias
Hsc70, Hsc73 
Protein Name
Heat shock cognate 71 kDa protein 
Protein Synonyms/Alias
Heat shock 70 kDa protein 8; 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:9;40609067-40613283;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.148706096 
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Description
Temporarily unavailable 
Abstract of related literatures
1. Multiple heat shock cognate (hsc70) cDNA clones were isolated from the mouse embryonal carcinoma cell line F9. They all encode a single 72-kDa protein, which is constitutively expressed in all mouse cell lines and tissues tested, and which is only slightly induced by hyperthermia. hsc70 RNA is very abundant in F9 stem cells and brain, but very little is found in 14-day-old embryos. Upon differentiation of F9 stem cells induced by retinoic acid and cyclic AMP, expression of the hsc70 gene decreases only slightly, suggesting that hsc70 is highly expressed in early mouse development and is then down-regulated towards the end of embryogenesis. In adult tissues only the brain retains the high level of hsc70 gene expression found in F9 stem cells. We also show that expression of hsc70 protein and clathrin is uncoupled in F9 cells, indicating that the uncoating activity of coated vesicles may not be the only function of hsc70 protein. PMID: [3334718] 

2. A partial integrin beta 1 subunit-encoding cDNA (Itg beta 1) and a new heat-shock protein 70-like-encoding cDNA (Hsc73) homologous to rat Hsc73 were cloned by differential display and RT-PCR from mouse mammary gland. Their developmental regulation during pregnancy, lactation and involution is reported. The Itg beta 1 mRNA content was stable in the first half of gestation, decreased to a minimum during lactation and increased markedly in early involution. Hsc73 gene expression was high in the first half of gestation and decreased to a minimum during lactation. The possible significance of the two observed patterns of expression is discussed. PMID: [8682318] 

3. A genomic clone encoding the mouse Hsc70 gene has been isolated and characterized by DNA sequence analysis. The gene is approximately 3. 9 kb in length and contains eight introns, the fifth, sixth and eighth of which encode the three U14 snoRNAs. The gene has been located on Chr 9 in the order Fli1-Itm1-Olfr7-Hsc70(Rnu14)-Cbl by genetic analysis. Expression of Hsc70 is universal in all tissues of the mouse, but is slightly elevated in liver, skeletal muscle and kidney tissue, while being depressed in testes. In cultured mouse NIH 3T3 cells or human HeLa cells, Hsc70 mRNA levels are low under normal conditions, but can be induced 8-fold higher in both lines by treatment with the amino acid analog azetidine. A similar induction is seen in cells treated with the proteosome inhibitor MG132 suggesting that elevated Hsc70 expression may be coupled to protein degradation. Surprisingly, expression of the human Hsc70 gene is also regulated by cell-cycle position being 8-10-fold higher in late G1/S-phase cells as opposed to the levels in early G1-phase cells. PMID: [10095055] 

4. This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development. PMID: [16141072] 

5. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

6. Mouse U14 snRNA (previously designated mouse 4.5S hybRNA) is an evolutionarily conserved eukaryotic low molecular weight RNA capable of intermolecular hybridization with both homologous and heterologous 18S rRNA (1). A single genomic fragment of mouse DNA containing the U14 snRNA gene(s) has been isolated from a Charon 4A lambda phage mouse genomic library and sequenced. Results have surprisingly revealed the presence of three U14 snRNA-homologous regions positioned within introns 5, 6, and 8 of the mouse cognate hsc70 heat shock gene. Comparative analysis with the previously reported rat and human cognate hsc70 genes revealed a similar positioning of U14 snRNA-homologous sequences within introns 5, 6 and 8 of the respective rat and human genes. The U14 sequences contained in all three introns of all three organisms are highly homologous to each other and well conserved with respect to the diverging intron sequences flanking each U14-homologous sequence. Comparison of the mouse U14 snRNA sequence with the U14 DNA sequences contained in the three mouse hsc70 introns indicates that intron 5 is utilized for U14 snRNA synthesis in normally growing mouse ascites cells. Analysis of the determined mouse, rat, and human U14-homologous sequences and the upstream and downstream flanking regions did not reveal the presence of any previously defined RNA polymerase I, II, or III binding sites. This suggests that either higher eukaryotic U14 snRNA is transcribed from a unique transcriptional promoter sequence, or alternatively, is generated by intron processing of the hsc70 pre-mRNA transcript. PMID: [2251119] 

7. The 105-kDa stress proteins HSP105alpha and HSP105beta belong to a high molecular mass heat shock protein family which has been found in organisms from yeast to mammals. Here we demonstrated the interaction of HSP105 with HSP70 family proteins in mouse FM3A cells. The association of HSP105 with HSC70 was shown by immunoprecipitation using anti-HSP105 antibody. Furthermore, when cell extracts or partially purified HSP105 fractions from nonstressed or heat-shocked cells were analyzed by size exclusion chromatography, density gradient centrifugation or cross-linking, HSP105 was detected as HSP105/HSC70 complexes with molecular masses of approximately 300-500-kDa, 160-kDa or 200-kDa, respectively. Since the 160-200-kDa complexes must be HSP105/HSC70 heterodimers, the 300-500-kDa complexes seemed to consist of HSP105/HSC70 heterotetramers possibly with other proteins. Our finding that HSP105 is complexed with HSC70 suggests that HSP105 may function cooperatively with HSC70, that HSP105 regulates the function of HSC70 or that HSC70 reversibly regulates the function of HSP105 in cells under both nonstressed and stressed conditions. PMID: [9675148] 

8. Hsp105alpha is a mammalian member of the HSP105/110 family, a diverged subgroup of the HSP70 family. Hsp105alpha associates with Hsp70/Hsc70 as complexes in vivo and regulates the chaperone activity of Hsp70/Hsc70 negatively in vitro and in vivo. In this study, we examined the mechanisms by which Hsp105alpha regulates Hsc70 chaperone activity. Using a series of deletion mutants of Hsp105alpha and Hsc70, we found that the interaction between Hsp105alpha and Hsc70 was necessary for the suppression of Hsc70 chaperone activity by Hsp105alpha. Furthermore, Hsp105alpha and deletion mutants of Hsp105alpha that interacted with Hsc70 suppressed the ATPase activity of Hsc70, with the concomitant appearance of ATPase activity of Hsp105alpha. As the ATPase activity of Hsp70/Hsc70 is essential for the efficient folding of nonnative protein substrates, Hsp105alpha is suggested to regulate the substrate binding cycle of Hsp70/Hsc70 by inhibiting the ATPase activity of Hsp70/Hsc70, thereby functioning as a negative regulator of the Hsp70/Hsc70 chaperone system. PMID: [15292236] 

9. Though the interferon-inducible protein ISG15 was one of the first ubiquitin-like modifiers to be discovered, much remains unknown about the identity of proteins conjugated to ISG15 or the biologic consequences of modification. To gain a better understanding of the cellular pathways affected by ISG15, we identified proteins targeted for ISGylation using a proteomic approach. Mass spectrometric analysis identified 76 candidate ISGylation targets in anti-ISG15 immunoprecipitates from interferon-treated mouse or human cells. Twenty-one proteins were found in both mouse and human samples, including STAT1, a known target of ISGylation. Candidates identified in both species were tested for ISGylation in a transfection system: 18 of 19 proteins tested were ISGylated in this system. Two candidates, EF-2 and VCP, were also shown to be ISGylated in an interferon-dependent manner in the absence of exogenous over-expression. Seven proteins identified from a single species, but functionally related to candidates found in both species, were also ISGylated in the over-expression system. Proteins that can be ISGylated play important roles in translation, glycolysis, stress responses, and cell motility. These data indicate that ISGylation targets proteins found in several fundamentally important cellular pathways and will contribute to understanding the physiologic role of interferon-induced ISG15 and ISG15 conjugation. PMID: [16139798] 

10. The p65 coactivator SIMPL is a small protein that lacks any conserved domains of known function. To better understand regulation of SIMPL activity, we sought to identify novel SIMPL interacting proteins using mass spectrometry analysis of SIMPL containing complexes. Two members of the 70-kDa heat-shock protein family, Hsp70 and Hsc70, were identified as SIMPL binding proteins. Subsequent immunocomplexing assays confirmed this interaction and demonstrated that the amino-terminus of SIMPL is required for this interaction. Using a combination of amino acid composition analysis, PONDR VL-XT prediction, charge-hydropathy plots, and cumulative distribution functions, the amino-terminal region of both mouse and human SIMPL proteins was predicted to be intrinsically disordered. These data, taken together, suggest that Hsp70/Hsc70 bind the intrinsically disordered amino-terminal region of SIMPL to stabilize the protein and thereby regulate its activity. Understanding the regulation of SIMPL through its interaction with Hsp70/Hsc70 may serve as a novel means of modulating tumor necrosis factor alpha signaling. PMID: [17233114] 

11. Metazoans employ reversible tyrosine phosphorylation to regulate innumerable biological processes. Thus, the large-scale identification of tyrosine phosphorylation sites from primary tissues is an essential step toward a molecular systems understanding of dynamic regulation in vivo. The relative paucity of phosphotyrosine has greatly limited its identification in large-scale phosphoproteomic experiments. However, using antiphosphotyrosine peptide immunoprecipitations, we report the largest study to date of tyrosine phosphorylation sites from primary tissue, identifying 414 unique tyrosine phosphorylation sites from murine brain. To measure the conservation of phosphorylated tyrosines and their surrounding residues, we constructed a computational pipeline and identified patterns of conservation within the signature of phosphotyrosine. PMID: [18034455] 

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Function
Acts as a repressor of transcriptional activation.Inhibits the transcriptional coactivator activity of CITED1 onSmad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome andis required for activating pre-mRNA splicing. May have ascaffolding role in the spliceosome assembly as it contacts allother components of the core complex (By similarity). 
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Subcellular Location
Cytoplasm (By similarity). Melanosome (Bysimilarity). Nucleus, nucleolus (By similarity). Note=Localized incytoplasmic mRNP granules containing untranslated mRNAs.Translocates rapidly from the cytoplasm to the nuclei, andespecially to the nucleoli, upon heat shock (By similarity). 
Tissue Specificity
Ubiquitous. 
Gene Ontology
GO IDGO termEvidence
GO:0009986 C:cell surface IEA:Compara.
GO:0005829 C:cytosol IDA:MGI.
GO:0070062 C:extracellular vesicular exosome IDA:MGI.
GO:0042470 C:melanosome IEA:UniProtKB-SubCell.
GO:0043005 C:neuron projection IEA:Compara.
GO:0043025 C:neuronal cell body IEA:Compara.
GO:0005730 C:nucleolus ISS:UniProtKB.
GO:0000974 C:Prp19 complex ISS:UniProtKB.
GO:0030529 C:ribonucleoprotein complex ISS:UniProtKB.
GO:0005625 C:soluble fraction IEA:Compara.
GO:0008021 C:synaptic vesicle IEA:Compara.
GO:0043531 F:ADP binding IEA:Compara.
GO:0005524 F:ATP binding IEA:UniProtKB-KW.
GO:0042623 F:ATPase activity, coupled IDA:MGI.
GO:0051085 P:chaperone mediated protein folding requiring cofactor IGI:MGI.
GO:0045892 P:negative regulation of transcription, DNA-dependent ISS:UniProtKB.
GO:0051726 P:regulation of cell cycle IDA:MGI.
GO:0006950 P:response to stress IEA:UniProtKB-KW.
GO:0006351 P:transcription, DNA-dependent IEA:UniProtKB-KW.
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Interpro
IPR018181;    Heat_shock_70_CS.
IPR013126;    Hsp_70_fam.
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Pfam
PF00012;    HSP70;    1.
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SMART
PROSITE
PS00297;    HSP70_1;    1.
PS00329;    HSP70_2;    1.
PS01036;    HSP70_3;    1.
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PRINTS
PR00301;    HEATSHOCK70.;   
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Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
INIT_MET      1      1       Removed (By similarity).
CHAIN         2    646       Heat shock cognate 71 kDa protein.
                             /FTId=PRO_0000078271.
REGION      186    377       Interaction with BAG1 (By similarity).
MOD_RES       2      2       N-acetylserine (By similarity).
MOD_RES      15     15       Phosphotyrosine.
MOD_RES      41     41       Phosphotyrosine.
MOD_RES      88     88       N6-acetyllysine (By similarity).
MOD_RES     107    107       Phosphotyrosine (By similarity).
MOD_RES     108    108       N6-acetyllysine (By similarity).
MOD_RES     113    113       Phosphoserine (By similarity).
MOD_RES     115    115       Phosphotyrosine (By similarity).
MOD_RES     120    120       Phosphoserine (By similarity).
MOD_RES     121    121       Phosphoserine (By similarity).
MOD_RES     153    153       Phosphoserine (By similarity).
MOD_RES     246    246       N6-acetyllysine (By similarity).
MOD_RES     319    319       N6-acetyllysine (By similarity).
MOD_RES     348    348       N6-acetyllysine (By similarity).
MOD_RES     477    477       Phosphothreonine (By similarity).
MOD_RES     512    512       N6-acetyllysine (By similarity).
MOD_RES     524    524       N6-acetyllysine (By similarity).
MOD_RES     541    541       Phosphoserine (By similarity).
MOD_RES     589    589       N6-acetyllysine (By similarity).
MOD_RES     597    597       N6-acetyllysine (By similarity).
MOD_RES     601    601       N6-acetyllysine (By similarity).
MOD_RES     637    637       Phosphoserine (By similarity).
MOD_RES     638    638       Phosphoserine (By similarity).
CONFLICT      9      9       I -> V (in Ref. 4; BAE28187).
CONFLICT     35     35       N -> K (in Ref. 4; BAE30081/BAE30861/
                             BAE30753).
CONFLICT    268    268       E -> G (in Ref. 4; BAE31432/BAE31346).
CONFLICT    269    269       R -> G (in Ref. 4; BAE31508).
CONFLICT    353    353       F -> C (in Ref. 4; BAE31664).
CONFLICT    428    428       F -> L (in Ref. 1; AAA37869 and 3;
                             AAB18391).
CONFLICT    432    432       S -> Y (in Ref. 4; BAE30707).
CONFLICT    589    589       K -> E (in Ref. 5; AAH66191).
CONFLICT    645    645       V -> M (in Ref. 4; BAE30272/BAE31427).
STRAND        7     11
STRAND       13     22
STRAND       25     28
STRAND       36     39
STRAND       42     44
STRAND       49     51
HELIX        53     57
TURN         58     61
HELIX        63     65
HELIX        70     72
TURN         73     75
HELIX        81     86
TURN         87     89
STRAND       91     97
STRAND      100    107
STRAND      110    114
HELIX       116    135
STRAND      141    146
HELIX       152    164
STRAND      168    174
HELIX       175    182
TURN        183    186
STRAND      187    200
STRAND      205    213
STRAND      216    225
HELIX       230    249
HELIX       257    273
TURN        274    276
STRAND      278    288
STRAND      291    298
HELIX       299    312
HELIX       314    324
HELIX       328    330
STRAND      333    338
HELIX       339    342
HELIX       344    353
TURN        354    356
TURN        365    367
HELIX       368    380
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Nucleotide Sequence
Length: 2089 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 646 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Other Protein-Protein interaction resources
String database  
View Microarray data
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