SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00007692 
UniProt Accession
Theoretical PI
5.35  
Molecular Weight
60955 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Hspd1 
Gene Synonyms/Alias
Hsp60 
Protein Name
60 kDa heat shock protein, mitochondrial 
Protein Synonyms/Alias
60 kDa chaperonin; Chaperonin 60;CPN60 HSP-65; Heat shock protein 60;HSP-60Hsp60 Mitochondrial matrix protein P1;Flags: Precursor 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:1;55134679-55145087;-1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.16392534 
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
2. Ras proteins play a crucial role in the development of neoplasia and in signal transduction in normal cells. In a search for proteins interacting with p21ras, we previously identified a protein of 60 kDa (p60) through use of a chemical cross-linker. Using information from partial amino acid sequencing of the purified protein, we isolated full-length cDNA clones encoding this 60-kDa protein. Nucleotide sequence analysis revealed that p60 is the murine heat shock protein hsp60, a chaperonin. Association of hsp60 with p21ras appears physiological, as the amount of hsp60 complexed to p21ras was similar even in cells over-expressing p21ras, and reversing the order of cross-linking and lysis of the cells, which releases large amounts of hsp60 from mitochondria, did not alter the amount of hsp60 cross-linked to p21ras. PMID: [1347942] 

3. 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] 

4. 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] 

5. The cDNA sequence of the 60 kDa heat-shock protein from mouse 3T3 cells has been determined. The deduced amino acid sequence of mouse hsp60 protein differs from the corresponding proteins from Chinese hamster and human cells in 7 and 13 residues, respectively, most of which are conservative replacements. PMID: [1979012] 

6. Strategies are needed for rapid protein isolation in order to identify disease-related proteins and facilitate the design of oligonucleotides for further molecular inquiry. In our laboratory, C3H10T1/2 murine fibroblasts have been found to express a variety of proteins in various subcellular fractions which are relevant to experimental transformation and carcinogenesis. Preparative two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) procedures were developed to identify major cytoplasmic proteins by electroblotting and microsequencing. Isoelectric focusing tube gels were enlarged to 6 mm ID to accommodate larger protein loads at 0.5 to 2 mg protein. Separated proteins were electrotransferred from 6 mm thick slab gels onto 0.22 mu polyvinylidene difluoride membranes. Nearly 100 prominent blotted proteins were stained with Coomassie Brilliant Blue between pI 4.5-7.0 and 18-106 kDa and, of these, 27 prominent and well-resolved proteins were selected for sequencing. Sequences of 14 to 24 amino acid residues in length were obtained from 11 proteins which were identified from computerized databases. Some of these identified proteins had structural or enzymatic functions while others had only recently been discovered, including a newly reported Hsp 70 class member and a novel calcium-binding protein, reticulocalbin. The new heat shock protein has a molecular mass of 75 kDa and has been designated as Grp75, PBP74, CSA or p66mot-1 in mice and humans with purported roles in transformation and antigen processing. Reticulocalbin is an endoplasmic reticular protein which contains six domains of the EF-hand motif associated with high-affinity calcium-binding proteins. It may be involved in protein transport and luminal protein processing. In addition, sequences of 5 to 11 residues in length were also obtained from six other unidentified proteins. Thus, we have found that preparative 2-D PAGE serves as a powerful one-step purification method for protein isolation and characterization from an important in vitro murine model for the study of carcinogenesis. PMID: [7523108] 

7. A system which consisted of multidimensional liquid chromatography (Yin-yang MDLC) coupled with mass spectrometry was used for the identification of peptides and phosphopeptides. The multidimensional liquid chromatography combines the strong-cation exchange (SCX), strong-anion exchange (SAX), and reverse-phase methods for the separation. Protein digests were first loaded on an SCX column. The flow-through peptides from SCX were collected and further loaded on an SAX column. Both columns were eluted by offline pH steps, and the collected fractions were identified by reverse-phase liquid chromatography tandem mass spectrometry. Comprehensive peptide identification was achieved by the Yin-yang MDLC-MS/MS for a 1 mg mouse liver. In total, 14 105 unique peptides were identified with high confidence, including 13 256 unmodified peptides and 849 phosphopeptides with 809 phosphorylated sites. The SCX and SAX in the Yin-Yang system displayed complementary features of binding and separation for peptides. When coupled with reverse-phase liquid chromatography mass spectrometry, the SAX-based method can detect more extremely acidic (pI < 4.0) and phosphorylated peptides, while the SCX-based method detects more relatively basic peptides (pI > 4.0). In total, 134 groups of phosphorylated peptide isoforms were obtained, with common peptide sequences but different phosphorylated states. This unbiased profiling of protein expression and phosphorylation provides a powerful approach to probe protein dynamics, without using any prefractionation and chemical derivation. PMID: [17203969] 

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Function
Implicated in mitochondrial protein import andmacromolecular assembly. May facilitate the correct folding ofimported proteins. May also prevent misfolding and promote therefolding and proper assembly of unfolded polypeptides generatedunder stress conditions in the mitochondrial matrix. 
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Subcellular Location
Mitochondrion matrix (By similarity). 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0009986 C:cell surface IEA:Compara.
GO:0005905 C:coated pit IEA:Compara.
GO:0030135 C:coated vesicle IEA:Compara.
GO:0019907 C:cyclin-dependent protein kinase activating kinase holoenzyme complex IEA:Compara.
GO:0005829 C:cytosol IEA:Compara.
GO:0005769 C:early endosome IEA:Compara.
GO:0005615 C:extracellular space IEA:Compara.
GO:0046696 C:lipopolysaccharide receptor complex IEA:Compara.
GO:0005743 C:mitochondrial inner membrane IDA:MGI.
GO:0005759 C:mitochondrial matrix IEA:UniProtKB-SubCell.
GO:0044459 C:plasma membrane part IDA:MGI.
GO:0030141 C:secretory granule IDA:MGI.
GO:0005524 F:ATP binding IEA:UniProtKB-KW.
GO:0043498 F:cell surface binding IEA:Compara.
GO:0001530 F:lipopolysaccharide binding IDA:BHF-UCL.
GO:0006919 P:activation of cysteine-type endopeptidase activity involved in apoptotic process IEA:Compara.
GO:0002368 P:B cell cytokine production IEA:Compara.
GO:0042100 P:B cell proliferation IEA:Compara.
GO:0048291 P:isotype switching to IgG isotypes IEA:Compara.
GO:0002755 P:MyD88-dependent toll-like receptor signaling pathway IEA:Compara.
GO:0043066 P:negative regulation of apoptotic process IEA:Compara.
GO:0043065 P:positive regulation of apoptotic process IEA:Compara.
GO:0032727 P:positive regulation of interferon-alpha production IDA:MGI.
GO:0032729 P:positive regulation of interferon-gamma production IDA:BHF-UCL.
GO:0032733 P:positive regulation of interleukin-10 production IEA:Compara.
GO:0032735 P:positive regulation of interleukin-12 production IEA:Compara.
GO:0032755 P:positive regulation of interleukin-6 production IEA:Compara.
GO:0043032 P:positive regulation of macrophage activation IEA:Compara.
GO:0050870 P:positive regulation of T cell activation IDA:BHF-UCL.
GO:0002842 P:positive regulation of T cell mediated immune response to tumor cell IEA:Compara.
GO:0042026 P:protein refolding IEA:Compara.
GO:0006986 P:response to unfolded protein IEA:Compara.
GO:0042110 P:T cell activation IDA:MGI.
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Interpro
IPR018370;    Chaperonin_Cpn60_CS.
IPR001844;    Chaprnin_Cpn60.
IPR002423;    Cpn60/TCP-1.
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Pfam
PF00118;    Cpn60_TCP1;    1.
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SMART
PROSITE
PS00296;    CHAPERONINS_CPN60;    1.
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PRINTS
PR00298;    CHAPERONIN60.;   
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Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
TRANSIT       1     26       Mitochondrion.
CHAIN        27    573       60 kDa heat shock protein, mitochondrial.
                             /FTId=PRO_0000005027.
MOD_RES      31     31       N6-acetyllysine (By similarity).
MOD_RES      70     70       Phosphoserine (By similarity).
MOD_RES      82     82       N6-acetyllysine (By similarity).
MOD_RES     125    125       N6-acetyllysine (By similarity).
MOD_RES     130    130       N6-acetyllysine (By similarity).
MOD_RES     133    133       N6-malonyllysine (By similarity).
MOD_RES     202    202       N6-acetyllysine (By similarity).
MOD_RES     218    218       N6-acetyllysine (By similarity).
MOD_RES     223    223       Phosphotyrosine.
MOD_RES     227    227       Phosphotyrosine (By similarity).
MOD_RES     269    269       N6-acetyllysine (By similarity).
MOD_RES     352    352       N6-acetyllysine (By similarity).
MOD_RES     359    359       N6-acetyllysine (By similarity).
MOD_RES     396    396       N6-acetyllysine (By similarity).
MOD_RES     469    469       N6-acetyllysine (By similarity).
MOD_RES     473    473       N6-acetyllysine (By similarity).
MOD_RES     523    523       N6-acetyllysine (By similarity).
VAR_SEQ       1    315       Missing (in isoform 2).
                             /FTId=VSP_025020.
CONFLICT      4      4       L -> H (in Ref. 2; AA sequence).
CONFLICT    139    139       E -> K (in Ref. 2; AA sequence).
CONFLICT    251    251       I -> F (in Ref. 5; CAA37653).
CONFLICT    364    364       K -> E (in Ref. 3; BAC40607).
CONFLICT    518    518       I -> V (in Ref. 1; CAA38762).
CONFLICT    527    527       T -> Q (in Ref. 2; AA sequence).
CONFLICT    547    547       T -> V (in Ref. 2; AA sequence).
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Nucleotide Sequence
Length: 1746 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 573 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
YwhabIntAct 
OGG1MINT 
CrklIntAct 
Dlg4IntAct 
Kcnma1IntAct 
PrkceIntAct 
Mcl1MINT 
Other Protein-Protein interaction resources
String database  
View Microarray data
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