SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00016544 
UniProt Accession
Theoretical PI
8.39  
Molecular Weight
65606 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Krt1 
Gene Synonyms/Alias
Krt2-1 
Protein Name
Keratin, type II cytoskeletal 1 
Protein Synonyms/Alias
67 kDa cytokeratin; Cytokeratin-1;CK-1 Keratin-1;K1 Type-II keratin Kb1; 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:15;101675859-101681217;-1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.069934331 
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. From the nucleotide sequences of specific cDNA clones, we present partial amino acid sequences (75-90% of the total) of 67-kDa type II keratin subunits expressed in terminally differentiating mouse and human epidermis. Analysis of the sequence information reveals that their secondary structures conform to the pattern common for all intermediate filament (IF) subunits. Together with the previously published sequence of the mouse 59-kDa type I keratin (Steinert, P. M., Rice, R. H., Roop, D. R., Trus, B. L., and Steven, A. C. (1983) Nature 302, 794-800) these data allow us to make comparisons between two keratins which are coexpressed in an epithelial cell type and which coassemble into the same IF. Moreover, these comparisons suggest a systematic plan for the general organization of the end domains of other keratin subunits. We postulate that each end domain consists of a set of subdomains which are distributed with bilateral symmetry with respect to the central alpha-helical domain. Type II (but not type I) keratins contain short globular sequences, H1 and H2, immediately adjacent to the central domain, that have been conserved in size and sequence and which account for most of the difference in mass between coexpressed type II and type I keratins. These are flanked by subdomains V1 and V2 that are highly variable in both length and sequence, often contain tandem peptide repeats, and are conspicuously rich in glycines and/or serines. At the termini are strongly basic subdomains (N and C, respectively) that are variable in sequence. Among keratins of a given type, their variability in mass appears to reside in the size of their V1 and V2 subdomains. However, coexpressed type I and type II keratins have generally similar V1 and/or V2 sequences. By virtue of the ease with which large portions of these subdomain sequences can be removed from intact keratin IF by limited proteolysis, we hypothesize that they lie on the periphery of the IF where they participate in interactions with other constituents of epithelial cells. PMID: [2581964] 

2. 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] 

3. 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] 

4. The final step of keratinocyte differentiation, transition from the granular cells to the cornified cells, involves various post-translational modifications that include deimination of arginine residues. Major deiminated epidermal proteins are derived from K1. Two preferred deimination sites were identified in mouse K1, one in the V1 and the other in the V2 subdomains. An antibody against the deiminated peptide sequence in the V2 subdomain recognized not only deiminated mouse K1 but also deiminated human K1. In this study we analyzed distribution of deiminated K1 in normal human skin and in bullous congenital ichthyosiform erythroderma at light and electron microscopic levels. In normal skin the first few (1-3) cornified cell layers were positive for filaggrin and negative for the antibody against deiminated mouse K1 peptide, whereas the more superficial cells were negative for filaggrin and strongly positive for the antibody against deiminated mouse K1 peptide, indicating slightly delayed onset of K1 deimination at the initial stage of cornification. The clumped keratin in bullous congenital ichthyosiform erythroderma that was not properly compacted with filaggrin was poorly positive to the antibody against deiminated mouse K1 peptide. In addition, K1 derivatives in bullous congenital ichthyosiform erythroderma reacted poorly with the antibody against deiminated mouse K1 peptide compared with the normal control in immunoblot analyses. Our results suggest sequential reorganization of cornified cell keratin filaments involving filaggrin-mediated compaction and K1 deimination. Abnormal keratin aggregation in bullous congenital ichthyosiform erythroderma is likely to disturb the normal deimination of K1. PMID: [11841545] 

5. Kinases play a prominent role in tumor development, pointing to the presence of specific phosphorylation patterns in tumor tissues. Here, we investigate whether recently developed high resolution mass spectrometric (MS) methods for proteome and phosphoproteome analysis can also be applied to solid tumors. As tumor model, we used TG3 mutant mice carrying skin melanomas. At total of 100 microg of solid tumor lysate yielded a melanoma proteome of 4443 identified proteins, including at least 88 putative melanoma markers previously found by cDNA microarray technology. Analysis of 2 mg of lysate from dissected melanoma with titansphere chromatography and 8 mg with strong cation exchange together resulted in the identification of more than 5600 phosphorylation sites on 2250 proteins. The phosphoproteome included many hits from pathways important in melanoma. One-month storage at -80 degrees C did not significantly decrease the number of identified phosphorylation sites. Thus, solid tumor can be analyzed by MS-based proteomics with similar efficiency as cell culture models and in amounts compatible with biopsies. PMID: [19367708] 

6. Chemical mutagenesis in the mouse has increased the utility of phenotype-driven genetics as a means for studying different organ systems, developmental pathways, and pathologic processes. From a large-scale screen for dominant phenotypes in mice, a novel class of pigmentation mutants was identified by dark skin (Dsk). We describe a Dsk mutant, Dsk12, which models the human disease, epidermolytic hyperkeratosis (EHK). At 2 days of age, mutant animals exhibit intraepidermal blisters and erosions at sites of trauma, and by 2 weeks of age develop significant hyperkeratosis. We identified a missense mutation in mutant animals that predicts an S194P amino acid substitution in the 1A domain of Keratin 1, a known target for human mutations that cause EHK. Dsk12 recapitulates the gross pathologic, histologic, and genetic aspects of the human disorder, EHK. PMID: [16528356] 

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Function
May regulate the activity of kinases such as PKC and SRCvia binding to integrin beta-1 (ITB1) and the receptor ofactivated protein kinase C (RACK1/GNB2L1) (By similarity). 
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Subcellular Location
Cell membrane (By similarity). 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0045095 C:keratin filament IDA:MGI.
GO:0005886 C:plasma membrane IEA:UniProtKB-SubCell.
GO:0030246 F:carbohydrate binding IEA:Compara.
GO:0005198 F:structural molecule activity IEA:InterPro.
GO:0001867 P:complement activation, lectin pathway IEA:Compara.
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Interpro
IPR016044;    F.
IPR001664;    IF.
IPR018039;    Intermediate_filament_CS.
IPR003054;    Keratin_II.
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Pfam
PF00038;    Filament;    1.
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SMART
PROSITE
PS00226;    IF;    1.
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PRINTS
PR01276;    TYPE2KERATIN.;   
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Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
INIT_MET      1      1       Removed (By similarity).
CHAIN         2    637       Keratin, type II cytoskeletal 1.
                             /FTId=PRO_0000063710.
REGION        2    187       Head.
REGION      188    497       Rod.
REGION      188    223       Coil 1A.
REGION      224    243       Linker 1.
REGION      244    334       Coil 1B.
REGION      335    358       Linker 12.
REGION      359    497       Coil 2.
REGION      498    637       Tail.
COILED      180    328       Potential.
COILED      397    483       Potential.
COMPBIAS     13    159       Gly-rich.
COMPBIAS    522    621       Gly-rich.
SITE        452    452       Stutter.
MOD_RES      24     24       Phosphoserine.
MOD_RES      67     67       Phosphoserine (By similarity).
MOD_RES     284    284       N6,N6-dimethyllysine (By similarity).
MOD_RES     303    303       Phosphotyrosine (By similarity).
MOD_RES     305    305       Phosphothreonine (By similarity).
MOD_RES     352    352       Phosphoserine.
VARIANT     194    194       S -> P (in EHK).
CONFLICT     99     99       G -> R (in Ref. 1; AAD05191).
CONFLICT    131    131       L -> S (in Ref. 1; AAD05191).
CONFLICT    147    147       R -> T (in Ref. 3; BAB31776).
CONFLICT    150    151       SM -> GY (in Ref. 1; AAD05191).
CONFLICT    156    158       PPG -> SPS (in Ref. 1; AAD05191).
CONFLICT    165    165       I -> L (in Ref. 1; AAD05191).
CONFLICT    176    176       E -> K (in Ref. 1; AAD05191).
CONFLICT    214    214       Q -> K (in Ref. 1; AAD05191).
CONFLICT    261    261       D -> E (in Ref. 1; AAD05191).
CONFLICT    313    313       A -> R (in Ref. 1; AAD05191).
CONFLICT    321    321       D -> N (in Ref. 1; AAD05191).
CONFLICT    325    325       A -> T (in Ref. 1; AAD05191).
CONFLICT    352    353       SL -> QF (in Ref. 1; AAD05191).
CONFLICT    428    428       S -> Y (in Ref. 3; BAB31776).
CONFLICT    572    580       Missing (in Ref. 1; AAD05191).
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Nucleotide Sequence
Length: 2341 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 637 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
Stat3IntAct 
Other Protein-Protein interaction resources
String database  
View Microarray data
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