SpermatogenesisOnline 1.0
 

Tag Content
SG ID
SG00000443 
UniProt Accession
Theoretical PI
4.95  
Molecular Weight
33670 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
HNRNPC 
Gene Synonyms/Alias
HNRPC 
Protein Name
Heterogeneous nuclear ribonucleoproteins C1/C2 
Protein Synonyms/Alias
hnRNP C1/C2 
Organism
Homo sapiens (Human) 
NCBI Taxonomy ID
9606 
Chromosome Location
chr:14;21677295-21737653;-1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Some men mutations in the HNRNP G-T gene can cause impaired spermatogenesis. Exploitation of the hnRNP G-T marker, enhances sensitivity and accuracy of diagnosis in the histologic evaluation of testicular biopsies. 
The information of related literatures
1. G. H. Westerveld, J. Gianotten, N. J. Leschot, F. van der Veen, S. Repping and M. P. Lombardi (2004) Heterogeneous nuclear ribonucleoprotein G-T (HNRNP G-T) mutations in men with impaired spermatogenesis. Mol Hum Reprod 10(4): 265-9. 

Abstract
The genetic cause of male subfertility due to impaired spermatogenesis is unknown in the majority of cases, but the general assumption is that it is a complex disorder. The aim of this study was to determine whether mutations occur in the HNRNP G-T gene in men with idiopathic impaired spermatogenesis. The heterogeneous nuclear ribonucleoprotein G-T (HNRNP G-T) gene is located in chromosomal region 11p15 that has been shown to be associated with impaired spermatogenesis. It is a member of the hnRNP gene family and is predominantly expressed in pachytene spermatocytes and round spermatids, where it is thought to affect splicing and signal transduction. We identified eight single nucleotide variants in our patient group of 153 subfertile men by sequencing the HNRNP G-T gene. Two of the mutations, R100H and G388del, did not occur in a control group of 143 normozoospermic men. The R100H mutation causes loss of a conserved arginine, thereby affecting a putative site of methylation possibly required for RNA-binding. Interestingly, this mutation was inherited from the mother. The G388del mutation causes loss of one non-conserved glycine located in a glycine stretch at the end of the protein that is not a known functional motif or domain. Our data show that HNRNP G -T mutations are not a frequent cause of impaired spermatogenesis. Nevertheless, the R100H mutation detected suggests that in some men mutations in the HNRNP G-T gene can cause impaired spermatogenesis. PMID: [14996998] 

2. B. B. Maymon, G. Paz, D. J. Elliott, B. Lifschitz-Mercer, L. Yogev, S. E. Kleiman, A. Botchan, R. Hauser, L. Schreiber and H. Yavetz (2002) Localization of the germ cell-specific protein, hnRNP G-T, in testicular biopsies of azoospermic men. Acta Histochem 104(3): 255-61. 

Abstract
The increasing interest in the application of in vitro fertilization techniques in human reproduction has led to a wide use of testicular biopsies to identify the presence of spermatogenic foci in testes of azoospermic men. Histopathologic evaluation of these testicular biopsies is required to determine the spermatogenic state with respect to fertility potential and to rule out preinvasive testicular lesions. Heterogeneous nuclear ribonucleoprotein G-T (hnRNP G-T) is a germ cell-specific protein expressed most prominently during meiosis. We studied the usefulness of hnRNP G-T antibody in the evaluation of these biopsies and reasoned that its germ cell-restricted expression pattern might provide a marker to improve accuracy of diagnosis. Testicular biopsies with various spermatogenic impairments were evaluated immunohistochemically for hnRNP G-T expression. In biopsies exhibiting normal spermatogenesis (obstructive azoospermia), hnRNP G-T was localized in meiotic pachytene spermatocytes and round spermatids. Immunostaining was barely detected when maturation was arrested at the spermatocyte level and not at all in cases of Sertoli cell-only syndrome. Biopsies with a mixed histologic phenotype and minute concentrations of spermatogenesis demonstrated strong immunostaining only in tubules with full spermatogenesis. This distribution pattern of hnRNP G-T enabled instant identification of spermatogenic foci. Thus, exploitation of the hnRNP G-T marker, which is expressed preferentially as meiosis proceeds, enhances sensitivity and accuracy of diagnosis in the histologic evaluation of testicular biopsies. PMID: [12389739] 

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Figures for illustrating the function of this protein/gene
Function
Binds pre-mRNA and nucleates the assembly of 40S hnRNPparticles. Single HNRNPC tetramers bind 230-240 nucleotides.Trimers of HNRNPC tetramers bind 700 nucleotides. May play a rolein the early steps of spliceosome assembly and pre-mRNA splicing.Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA andmodulates the stability and the level of translation of bound mRNAmolecules. 
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Subcellular Location
Nucleus. Note=Component of ribonucleosomes. 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0071013 C:catalytic step 2 spliceosome IDA:UniProtKB.
GO:0005654 C:nucleoplasm TAS:Reactome.
GO:0000166 F:nucleotide binding IEA:InterPro.
GO:0003723 F:RNA binding NAS:HGNC.
GO:0000398 P:nuclear mRNA splicing, via spliceosome IC:UniProtKB.
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Interpro
IPR017347;    hnRNP_C_Raly.
IPR012677;    Nucleotide-bd_a/b_plait.
IPR000504;    RRM_dom.
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Pfam
PF00076;    RRM_1;    1.
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SMART
SM00360;    RRM;    1.
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PROSITE
PS50102;    RRM;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
INIT_MET      1      1       Removed.
CHAIN         2    306       Heterogeneous nuclear ribonucleoproteins
                             C1/C2.
                             /FTId=PRO_0000081844.
DOMAIN       16     87       RRM.
MOTIF       155    161       Nuclear localization signal (Potential).
COMPBIAS    181    303       Asp/Glu-rich (acidic).
MOD_RES       2      2       N-acetylalanine.
MOD_RES      39     39       N6-acetyllysine.
MOD_RES     107    107       Phosphoserine.
MOD_RES     109    109       Phosphothreonine.
MOD_RES     113    113       Phosphoserine.
MOD_RES     115    115       Phosphoserine.
MOD_RES     120    120       Phosphoserine.
MOD_RES     121    121       Phosphoserine.
MOD_RES     138    138       Phosphoserine.
MOD_RES     162    162       Phosphoserine.
MOD_RES     170    170       N6-acetyllysine.
MOD_RES     216    216       N6-acetyllysine.
MOD_RES     233    233       Phosphoserine.
MOD_RES     238    238       Phosphoserine.
MOD_RES     239    239       Phosphoserine.
MOD_RES     240    240       Phosphoserine.
MOD_RES     241    241       Phosphoserine.
MOD_RES     253    253       Phosphoserine.
MOD_RES     260    260       Phosphoserine.
MOD_RES     299    299       Phosphoserine.
MOD_RES     306    306       Phosphoserine.
CROSSLNK    250    250       Glycyl lysine isopeptide (Lys-Gly)
                             (interchain with G-Cter in SUMO).
VAR_SEQ      39    119       KYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQV
                             LDINLAAEPKVNRGKAGVKRSAAEMYGSVTEHPSPSPLLS
                             -> N (in isoform 3).
                             /FTId=VSP_019225.
VAR_SEQ     108    120       Missing (in isoform C1 and isoform 4).
                             /FTId=VSP_005831.
VAR_SEQ     153    195       Missing (in isoform 4).
                             /FTId=VSP_019226.
VARIANT     167    167       R -> Q (in dbSNP:rs3272).
                             /FTId=VAR_052224.
MUTAGEN     197    197       K->R: No effect on sumoylation.
MUTAGEN     250    250       K->R: Loss of sumoylation.
CONFLICT    110    110       E -> G (in Ref. 6; AAH08423).
CONFLICT    217    217       I -> M (in Ref. 1 and 2).
CONFLICT    224    224       Q -> R (in Ref. 6; AAH08364).
CONFLICT    244    244       K -> R (in Ref. 6; AAH08364).
CONFLICT    254    254       E -> G (in Ref. 6; AAH07052).
CONFLICT    303    306       EDDS -> G (in Ref. 1 and 2).
STRAND       18     23
TURN         25     27
HELIX        30     35
STRAND       43     49
STRAND       51     59
HELIX        60     68
TURN         69     72
STRAND       81     84
HELIX       194    216
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Nucleotide Sequence
Length: 1398 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 306 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
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YWHAZMINT 
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SMARCA4BioGRID 
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EIF2C4IntAct 
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GRB2BioGRID 
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SMARCA4BioGRID 
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AP1M1BioGRID 
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SMARCA4BioGRID 
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CCDC85BBioGRID 
CHD4BioGRID 
CNBPIntAct 
DHX9BioGRID 
FXR2BioGRID 
HNRNPCBioGRID 
HNRNPCBioGRID 
KPNA3BioGRID 
KHDRBS3IntAct 
PHKBBioGRID 
LMO3BioGRID 
MYCIntAct 
NFKB2IntAct 
PIN1BioGRID 
PUF60IntAct 
CHD4BioGRID 
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UBE2IMINT 
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SMARCA4BioGRID 
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RALYLBioGRID 
KRASBioGRID 
RBM41BioGRID 
RBM8AIntAct 
UPF3AIntAct 
HNRNPA1IntAct 
SMARCA4BioGRID 
SMARCC1BioGRID 
GH1IntAct 
THOC4IntAct 
TNFRSF1BIntAct 
TRAF6IntAct 
UBE2IBioGRID 
ZNF581BioGRID 
EIF4A3IntAct 
IFIT1IntAct 
IKBKEIntAct 
ILF3DIP 
KHDRBS2BioGRID 
PHKBIntAct 
lcrRIntAct 
LMO3IntAct 
MEPCEBioGRID 
MAP1LC3AIntAct 
MAP1LC3BIntAct 
MYCBioGRID 
NFKB2MINT 
PIN1IntAct 
PUF60BioGRID 
CHD4BioGRID 
ZNF9BioGRID 
ZNF9BioGRID 
CNBPBioGRID 
GABARAPL2IntAct 
KPNA3IntAct 
SMARCA4BioGRID 
RALYLIntAct 
KRASIntAct 
RBM41IntAct 
RBM8AIntAct 
HNRNPA1BioGRID 
SMARCA4BioGRID 
GH1DIP 
SRRM2BioGRID 
TNFRSF1BMINT 
TOP1IntAct 
UBE2IIntAct 
ZNF581IntAct 
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