Tag Content
SG ID
SG00012168 
UniProt Accession
Theoretical PI
5.86  
Molecular Weight
82791 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Trim36 
Gene Synonyms/Alias
 
Protein Name
E3 ubiquitin-protein ligase Trim36 
Protein Synonyms/Alias
EC=6.3.2.- Acrosome RBCC protein; Haprin; Tripartite motif-containing protein 36; 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:18;46324956-46372261;-1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.615969613 
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. The acrosome reaction (i.e. the exocytosis of the sperm vesicle) is a prerequisite for fertilization, but its molecular mechanism is largely unknown. We have identified a cDNA clone for a gene named haprin, which encodes a haploid germ cell-specific RING finger protein. This protein is a novel member of the RBCC (RING finger, B-box type zinc finger, and coiled-coil domain) motif family that has roles in several cellular processes, such as exocytosis. It is transcribed exclusively in testicular germ cells after meiotic division. Western blot and immunohistochemical analyses showed the molecular weight of Haprin protein to be Mr approximately 82,000. It was localized in the acrosomal region of elongated spermatids and mature sperm and was not present in acrosome-reacted sperm. The specific antibody against the RING finger domain of Haprin inhibited the acrosome reaction in permeabilized sperm. These results indicated that the novel RBCC protein Haprin plays a key role in the acrosome reaction and fertilization. PMID: [12917430] 

2. The biological significance of RBCC (N-terminal RING finger/B-box/coiled coil) proteins is increasingly being appreciated following demonstrated roles in disease pathogenesis, tumorigenesis, and retroviral protective activity. Found in all multicellular eukaryotes, RBCC proteins are involved in a vast array of intracellular functions; but as a general rule, they appear to function as part of large protein complexes and possess ubiquitin-protein isopeptide ligase activity. Those members characterized to date have diverse C-terminal domain compositions and equally diverse subcellular localizations and functions. Using a bioinformatics approach, we have identified some new RBCC proteins that help define a subfamily that shares an identical domain arrangement (MID1, MID2, TRIM9, TNL, TRIM36, and TRIFIC). Significantly, we show that all analyzed members of this subfamily associate with the microtubule cytoskeleton, suggesting that subcellular compartmentalization is determined by the unique domain architecture, which may in turn reflect basic functional similarities. We also report a new motif called the COS box, which is found within these proteins, the MURF family, and a distantly related non-RBCC microtubule-binding protein. Notably, we demonstrate that mutations in the COS box abolish microtubule binding ability, whereas its incorporation into a nonmicrotubule-binding RBCC protein redirects it to microtubule structures. Further bioinformatics investigation permitted subclassification of the entire human RBCC complement into nine subfamilies based on their varied C-terminal domain compositions. This classification schema may aid the understanding of the molecular function of members of each subgroup and their potential involvement in both basic cellular processes and human disease. PMID: [16434393] 

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 tripartite motif-containing protein (TRIM) family is defined by the presence of a common domain structure composed of a RING finger, a B-box, and a coiled-coil motif. TRIM family proteins are involved in a broad range of biological processes and, consistently, their alterations result in diverse pathological conditions such as genetic diseases, viral infection, and cancer development. In this study, we found by using yeast two-hybrid screening that TRIM36 has a ubiquitin ligase activity and interacts with centromere protein-H, one of the kinetochore proteins. We also found by immunofluorescence analysis that TRIM36 colocalizes with alpha-tubulin, one of the microtubule proteins. Moreover, we found that overexpression of TRIM36 decelerates the cell cycle and attenuates cell growth. These results indicate that TRIM36 is potentially associated with chromosome segregation and that an excess of TRIM36 may cause chromosomal instability. PMID: [19232519] 

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Function
E3 ubiquitin-protein ligase which mediatesubiquitination and subsequent proteasomal degradation of targetproteins. Involved in chromosome segregation and cell cycleregulation. May play a role in the acrosome reaction andfertilization. 
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Subcellular Location
Cytoplasm. Cytoplasmic vesicle, secretoryvesicle, acrosome. Cytoplasm, cytoskeleton. Note=Found in theacrosomal region of elongated spermatids and mature sperm. 
Tissue Specificity
Expressed only in testis. 
Gene Ontology
GO IDGO termEvidence
GO:0001669 C:acrosomal vesicle IDA:MGI.
GO:0005856 C:cytoskeleton IEA:UniProtKB-SubCell.
GO:0016874 F:ligase activity IEA:UniProtKB-KW.
GO:0008270 F:zinc ion binding IEA:InterPro.
GO:0007340 P:acrosome reaction IMP:MGI.
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Interpro
IPR001870;    B30.2/SPRY.
IPR008985;    ConA-like_lec_gl.
IPR017903;    COS_domain.
IPR003961;    Fibronectin_type3.
IPR013783;    Ig-like_fold.
IPR003877;    SPRY_rcpt.
IPR000315;    Znf_B-box.
IPR001841;    Znf_RING.
IPR013083;    Znf_RING/FYVE/PHD.
IPR017907;    Znf_RING_CS.
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Pfam
PF00041;    fn3;    1.
PF00622;    SPRY;    1.
PF00643;    zf-B_box;    1.
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SMART
SM00336;    BBOX;    1.
SM00060;    FN3;    1.
SM00184;    RING;    1.
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PROSITE
PS50188;    B302_SPRY;    1.
PS51262;    COS;    1.
PS50853;    FN3;    1.
PS50119;    ZF_BBOX;    1.
PS00518;    ZF_RING_1;    1.
PS50089;    ZF_RING_2;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    729       E3 ubiquitin-protein ligase Trim36.
                             /FTId=PRO_0000056253.
DOMAIN      356    413       COS.
DOMAIN      414    508       Fibronectin type-III.
DOMAIN      509    723       B30.2/SPRY.
ZN_FING      33     84       RING-type; degenerate.
ZN_FING     154    192       B box-type 1.
ZN_FING     207    249       B box-type 2.
COILED      271    302       Potential.
CONFLICT    292    292       G -> V (in Ref. 1; BAC76066).
CONFLICT    532    532       N -> D (in Ref. 1; BAC76066).
CONFLICT    601    602       WL -> CV (in Ref. 1; BAC76066).
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Nucleotide Sequence
Length: 2324 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 729 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
Gene Symbol Ref Databases
Other Protein-Protein interaction resources
String database  
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