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Gene Symbol |
SERPINH1 |
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Aliases |
AsTP3, CBP1, CBP2, HSP47, OI10, PIG14, PPROM, RA-A47, SERPINH2, gp46 |
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Entrez Gene ID |
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Gene Name |
Serpin family H member 1 |
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Chromosomal Location |
11q13.5 |
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HGNC ID |
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Summary |
This gene encodes a member of the serpin superfamily of serine proteinase inhibitors. The encoded protein is localized to the endoplasmic reticulum and plays a role in collagen biosynthesis as a collagen-specific molecular chaperone. Autoantibodies to the encoded protein have been found in patients with rheumatoid arthritis. Expression of this gene may be a marker for cancer, and nucleotide polymorphisms in this gene may be associated with preterm birth caused by preterm premature rupture of membranes. Alternatively spliced transcript variants have been observed for this gene, and a pseudogene of this gene is located on the short arm of chromosome 9. [provided by RefSeq, May 2011]
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RefSeq DNA |
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RefSeq mRNA |
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e!Ensembl
Gene |
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Transcript |
ENST00000533603, ENST00000358171, ENST00000526242, ENST00000649490, ENST00000526397, ENST00000529643, ENST00000525492, ENST00000530284, ENST00000532356, ENST00000524558, ENST00000528990, ENST00000533449, ENST00000525611, ENST00000528760, ENST00000525876, ENST00000526638 |
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Protein |
ENSP00000434657, ENSP00000350894, ENSP00000431384, ENSP00000497544, ENSP00000434964, ENSP00000435936, ENSP00000434482, ENSP00000436305, ENSP00000436040, ENSP00000434412, ENSP00000432007, ENSP00000431827, ENSP00000435452, ENSP00000437108, ENSP00000433532, ENSP00000436306
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Protein Information |
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Protein Name |
Serpin H1, 47 kDa heat shock protein, arsenic-transactivated protein 3, cell proliferation-inducing gene 14 protein, collagen binding protein 1, colligin-1, colligin-2, rheumatoid arthritis antigen A-47, rheumatoid arthritis-related antigen RA-A47, serine (or cysteine) proteinase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1), serine (or cysteine) proteinase inhibitor, clade H (heat shock protein 47), member 2, (collagen-binding protein 2), serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1) |
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Function |
Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen |
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UniProt |
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Pfam |
Pfam Accession |
Pfam ID |
PF00079 |
Serpin |
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Interactions |
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STRING |
MINT |
IntAct |
ENSP00000446007 |
P08670 |
P08670 |
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View interactions
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Associated Diseases
Disease group | Disease Name | References |
Cardiovascular Diseases |
Arteriosclerosis |
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Digestive System Diseases |
Liver Fibrosis |
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Liver Cirrhosis |
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Endocrine System Diseases |
PCOS |
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Musculoskeletal Diseases |
Osteogenesis Imperfecta |
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Nervous System Diseases |
Cerebral Artery Infarction |
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Cerebral Thrombosis |
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Middle Cerebral Artery Syndrome |
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Brain Infarction |
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Respiratory Tract Diseases |
Respiratory Distress Syndrome |
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References |
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Ma Xiang, Fan Lu, Meng Yan, Hou Zheng, Mao Yun-Dong, Wang Wei, Ding Wei, Liu Jia-Yin |
Laboratory of Reproductive Medicine, Nanjing Medical University, and The Center of Clinical Reproductive Medicine, The First Affiliated Hospital of Nanjing Medical University, People's Republic of China. |
Mol Hum Reprod. 2007 Aug;13(8):527-35. doi: 10.1093/molehr/gam036. Epub 2007 Jun |
Abstract
Polycystic ovary syndrome (PCOS) is the most common cause of anovulatory infertility, affecting 5-10% of females of reproductive age. Currently, little is known about the changes in whole proteins between PCOS and normal ovaries. In the present study, a proteomic approach comprised two-dimensional gel electrophoresis (2DE) analysis and mass spectroscopy was used to identify proteins and examine expression patterns in three PCOS and normal ovaries. One hundred and ten protein spots were separated and showed different intensities between PCOS and normal ovaries. Sixty-nine proteins associated with cellular metabolism and physiological process were identified from 72 spots. Fifty-four proteins were up-regulated in PCOS ovaries and 15 other proteins were up-regulated in normal ovaries. These data demonstrate, for the first time, the complexity in the regulation of ovarian protein expression in human PCOS, and will provide important insight for a better understanding of the pathogenetic mechanisms underlying this clinical disorder. |
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Gupta Sajal, Ghulmiyyah Jana, Sharma Rakesh, Halabi Jacques, Agarwal Ashok |
Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA. |
Biomed Res Int. 2014;2014:916212. doi: 10.1155/2014/916212. Epub 2014 May 12. |
Abstract
Endometriosis, PCOS, and unexplained infertility are currently the most common diseases rendering large numbers of women infertile worldwide. Oxidative stress, due to its deleterious effects on proteins and nucleic acids, is postulated to be the one of the important mechanistic pathways in differential expression of proteins and in these diseases. The emerging field of proteomics has allowed identification of proteins involved in cell cycle, as antioxidants, extracellular matrix (ECM), cytoskeleton, and their linkage to oxidative stress in female infertility related diseases. The aim of this paper is to assess the association of oxidative stress and protein expression in the reproductive microenvironments such as endometrial fluid, peritoneal fluid, and follicular fluid, as well as reproductive tissues and serum. The review also highlights the literature that proposes the use of the fertility related proteins as potential biomarkers for noninvasive and early diagnosis of the aforementioned diseases rather than utilizing the more invasive methods used currently. The review will highlight the power of proteomic profiles identified in infertility related disease conditions and their linkage with underlying oxidative stress. The power of proteomics will be reviewed with regard to eliciting molecular mechanisms for early detection and management of these infertility related conditions. |
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| © 2019, Biomedical Informatics Centre, NIRRH |
National Institute for Research in Reproductive Health, Jehangir Merwanji Street, Parel, Mumbai-400 012
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