Human Gene SERPIND1 (ENST00000215727.10_4) from GENCODE V47lift37
  Description: serpin family D member 1 (from RefSeq NM_000185.4)
Gencode Transcript: ENST00000215727.10_4
Gencode Gene: ENSG00000099937.11_7
Transcript (Including UTRs)
   Position: hg19 chr22:21,128,401-21,142,008 Size: 13,608 Total Exon Count: 5 Strand: +
Coding Region
   Position: hg19 chr22:21,133,601-21,141,354 Size: 7,754 Coding Exon Count: 4 

Page IndexSequence and LinksUniProtKB CommentsPrimersMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr22:21,128,401-21,142,008)mRNA (may differ from genome)Protein (499 aa)
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HGNCMalacardsMGIOMIMPubMedReactome
UniProtKBWikipediaBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: HEP2_HUMAN
DESCRIPTION: RecName: Full=Heparin cofactor 2; AltName: Full=Heparin cofactor II; Short=HC-II; AltName: Full=Protease inhibitor leuserpin-2; Short=HLS2; AltName: Full=Serpin D1; Flags: Precursor;
FUNCTION: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner.
FUNCTION: Peptides at the N-terminal of HC-II have chemotactic activity for both monocytes and neutrophils.
TISSUE SPECIFICITY: Expressed predominantly in liver. Also present in plasma.
DOMAIN: The N-terminal acidic repeat region mediates, in part, the glycosaminoglycan-accelerated thrombin inhibition.
PTM: Phosphorylation sites are present in the extracellular medium.
DISEASE: Defects in SERPIND1 are the cause of thrombophilia due to heparin cofactor 2 deficiency (THPH10) [MIM:612356]. A hemostatic disorder characterized by a tendency to recurrent thrombosis.
SIMILARITY: Belongs to the serpin family.
SEQUENCE CAUTION: Sequence=CAG30459.1; Type=Erroneous initiation;

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  MalaCards Disease Associations
  MalaCards Gene Search: SERPIND1
Diseases sorted by gene-association score: thrombophilia due to heparin cofactor ii deficiency* (1200), cervix uteri carcinoma in situ (17), thrombophilia (17), acute cervicitis (15), cervix disease (12), chronic cervicitis (11), dysfibrinogenemia (9), cervicitis (7), thrombophilia due to antithrombin iii deficiency (7), pre-malignant neoplasm (5), in situ carcinoma (4), stroke, ischemic (2)
* = Manually curated disease association

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 122.41 RPKM in Liver
Total median expression: 132.25 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -8.7049-0.178 Picture PostScript Text
3' UTR -187.00654-0.286 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR000295 - Prot_inh_Lserp2
IPR023795 - Protease_inhib_I4_serpin_CS
IPR023796 - Serpin_dom
IPR000215 - Serpin_fam

Pfam Domains:
PF00079 - Serpin (serine protease inhibitor)

SCOP Domains:
56574 - Serpins

Protein Data Bank (PDB) 3-D Structure
MuPIT help
1JMJ - X-ray 1JMO - X-ray MuPIT


ModBase Predicted Comparative 3D Structure on P05546
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologNo orthologNo orthologNo orthologNo ortholog
Gene DetailsGene Details    
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-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0004866 endopeptidase inhibitor activity
GO:0004867 serine-type endopeptidase inhibitor activity
GO:0008201 heparin binding
GO:0030414 peptidase inhibitor activity

Biological Process:
GO:0006935 chemotaxis
GO:0007596 blood coagulation
GO:0007599 hemostasis
GO:0010466 negative regulation of peptidase activity
GO:0010951 negative regulation of endopeptidase activity
GO:0043687 post-translational protein modification
GO:0044267 cellular protein metabolic process

Cellular Component:
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005788 endoplasmic reticulum lumen
GO:0070062 extracellular exosome


-  Descriptions from all associated GenBank mRNAs
  JD543773 - Sequence 524797 from Patent EP1572962.
AK314200 - Homo sapiens cDNA, FLJ94926, highly similar to Homo sapiens serine (or cysteine) proteinase inhibitor, clade D(heparin cofactor), member 1 (SERPIND1), mRNA.
AK225292 - Homo sapiens mRNA for heparin cofactor II precursor variant, clone: HEP03383.
BC035028 - Homo sapiens serpin peptidase inhibitor, clade D (heparin cofactor), member 1, mRNA (cDNA clone MGC:33758 IMAGE:5262187), complete cds.
CR456573 - Homo sapiens SERPIND1 full length open reading frame (ORF) cDNA clone (cDNA clone C22ORF:pGEM.SERPIND1.V2).
AB463254 - Synthetic construct DNA, clone: pF1KB8724, Homo sapiens SERPIND1 gene for serpin peptidase inhibitor, clade D (heparin cofactor), member 1, without stop codon, in Flexi system.
CU013460 - Homo sapiens SERPIND1, mRNA (cDNA clone IMAGE:100000430), complete cds, without stop codon, in Gateway system.
CU013172 - Homo sapiens SERPIND1, mRNA (cDNA clone IMAGE:100000526), complete cds, with stop codon, in Gateway system.
M12849 - Human heparin cofactor II (HC-II) mRNA, complete cds.
CU690034 - Synthetic construct Homo sapiens gateway clone IMAGE:100019690 5' read SERPIND1 mRNA.
DQ894386 - Synthetic construct Homo sapiens clone IMAGE:100008846; FLH170124.01L; RZPDo839C0197D serpin peptidase inhibitor, clade D (heparin cofactor), member 1 (SERPIND1) gene, encodes complete protein.
DQ891203 - Synthetic construct clone IMAGE:100003833; FLH170128.01X; RZPDo839C0198D serpin peptidase inhibitor, clade D (heparin cofactor), member 1 (SERPIND1) gene, encodes complete protein.
KJ896960 - Synthetic construct Homo sapiens clone ccsbBroadEn_06354 SERPIND1 gene, encodes complete protein.
KR709540 - Synthetic construct Homo sapiens clone CCSBHm_00003304 SERPIND1 (SERPIND1) mRNA, encodes complete protein.
KR709541 - Synthetic construct Homo sapiens clone CCSBHm_00003305 SERPIND1 (SERPIND1) mRNA, encodes complete protein.
KR709542 - Synthetic construct Homo sapiens clone CCSBHm_00003306 SERPIND1 (SERPIND1) mRNA, encodes complete protein.
E00997 - cDNA encoding protease inhibitor.
X03498 - Human mRNA for protease inhibitor leuserpin 2 (hLS2).
JD223594 - Sequence 204618 from Patent EP1572962.
JD411436 - Sequence 392460 from Patent EP1572962.
JD065999 - Sequence 47023 from Patent EP1572962.
JD416393 - Sequence 397417 from Patent EP1572962.
JD051192 - Sequence 32216 from Patent EP1572962.
JD412418 - Sequence 393442 from Patent EP1572962.
JD071500 - Sequence 52524 from Patent EP1572962.
JD195658 - Sequence 176682 from Patent EP1572962.
JD232870 - Sequence 213894 from Patent EP1572962.
JD121018 - Sequence 102042 from Patent EP1572962.
JD507971 - Sequence 488995 from Patent EP1572962.
JD310374 - Sequence 291398 from Patent EP1572962.
JD495481 - Sequence 476505 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein P05546 (Reactome details) participates in the following event(s):

R-HSA-5578883 Heparin cofactor 2 (SERPIND1) binds activated thrombin (factor IIa)
R-HSA-8952289 FAM20C phosphorylates FAM20C substrates
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-140877 Formation of Fibrin Clot (Clotting Cascade)
R-HSA-109582 Hemostasis
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-8957275 Post-translational protein phosphorylation
R-HSA-392499 Metabolism of proteins
R-HSA-597592 Post-translational protein modification

-  Other Names for This Gene
  Alternate Gene Symbols: B2RAI1, D3DX34, ENST00000215727.1, ENST00000215727.2, ENST00000215727.3, ENST00000215727.4, ENST00000215727.5, ENST00000215727.6, ENST00000215727.7, ENST00000215727.8, ENST00000215727.9, HCF2, HEP2_HUMAN, NM_000185, P05546, Q6IBZ5, uc317cml.1, uc317cml.2
UCSC ID: ENST00000215727.10_4
RefSeq Accession: NM_000185.4
Protein: P05546 (aka HEP2_HUMAN)

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.