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P05121 (PAI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plasminogen activator inhibitor 1

Short name=PAI
Short name=PAI-1
Alternative name(s):
Endothelial plasminogen activator inhibitor
Serpin E1
Gene names
Name:SERPINE1
Synonyms:PAI1, PLANH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis. Ref.18

Subunit structure

Forms protease inhibiting heterodimer with TMPRSS7. Interacts with VTN. Binds LRP1B; binding is followed by internalization and degradation. Ref.15 Ref.17

Subcellular location

Secreted.

Tissue specificity

Found in plasma and platelets and in endothelial, hepatoma and fibrosarcoma cells.

Post-translational modification

Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-|-Met-370 bond.

Involvement in disease

Plasminogen activator inhibitor-1 deficiency (PAI-1D) [MIM:613329]: A hematologic disorder characterized by increased bleeding after trauma, injury, or surgery. Affected females have menorrhagia. The bleeding defect is due to increased fibrinolysis of fibrin blood clots due to deficiency of plasminogen activator inhibitor-1, which inhibits tissue and urinary activators of plasminogen.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions.

Sequence similarities

Belongs to the serpin family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from expression pattern PubMed 11866539. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cellular response to lipopolysaccharide

Inferred from mutant phenotype PubMed 19916862. Source: BHF-UCL

chronological cell aging

Inferred from expression pattern PubMed 18974388. Source: BHF-UCL

defense response to Gram-negative bacterium

Inferred from genetic interaction PubMed 17032919. Source: BHF-UCL

extracellular matrix organization

Traceable author statement. Source: Reactome

fibrinolysis

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

negative regulation of blood coagulation

Inferred by curator PubMed 1695900. Source: BHF-UCL

negative regulation of cell adhesion mediated by integrin

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

negative regulation of cell migration

Inferred from direct assay PubMed 10902815. Source: BHF-UCL

negative regulation of endopeptidase activity

Inferred from direct assay PubMed 1695900. Source: BHF-UCL

negative regulation of endothelial cell apoptotic process

Inferred from mutant phenotype PubMed 18835034. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from mutant phenotype PubMed 18835034. Source: BHF-UCL

negative regulation of fibrinolysis

Inferred from direct assay PubMed 2503541. Source: BHF-UCL

negative regulation of plasminogen activation

Inferred from direct assay PubMed 8508955. Source: BHF-UCL

negative regulation of smooth muscle cell migration

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

negative regulation of smooth muscle cell-matrix adhesion

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

negative regulation of vascular wound healing

Inferred from genetic interaction PubMed 9386191. Source: BHF-UCL

negative regulation of wound healing

Inferred by curator PubMed 8837777. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of angiogenesis

Inferred from mutant phenotype PubMed 18835034. Source: BHF-UCL

positive regulation of blood coagulation

Inferred from mutant phenotype Ref.16. Source: BHF-UCL

positive regulation of inflammatory response

Inferred from genetic interaction PubMed 17032919. Source: BHF-UCL

positive regulation of interleukin-8 production

Inferred from mutant phenotype PubMed 19916862. Source: BHF-UCL

positive regulation of leukotriene production involved in inflammatory response

Inferred from mutant phenotype PubMed 19916862. Source: BHF-UCL

positive regulation of monocyte chemotaxis

Inferred from mutant phenotype PubMed 19916862. Source: BHF-UCL

positive regulation of receptor-mediated endocytosis

Inferred from direct assay PubMed 8626514. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of receptor activity

Inferred from direct assay PubMed 8837777. Source: BHF-UCL

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentextracellular matrix

Inferred from direct assay PubMed 1632457. Source: BHF-UCL

extracellular region

Inferred from direct assay PubMed 9386191. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 1695900PubMed 18835034. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionprotease binding

Inferred from physical interaction PubMed 12114510Ref.18. Source: UniProtKB

serine-type endopeptidase inhibitor activity

Inferred from direct assay PubMed 1695900PubMed 8508955. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ORM1P027634EBI-953978,EBI-976767

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05121-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P05121-2)

The sequence of this isoform differs from the canonical sequence as follows:
     31-45: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 402379Plasminogen activator inhibitor 1
PRO_0000032499

Sites

Site369 – 3702Reactive bond

Amino acid modifications

Glycosylation2321N-linked (GlcNAc...)
Glycosylation2881N-linked (GlcNAc...)
Glycosylation3521N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence31 – 4515Missing in isoform 2.
VSP_045493
Natural variant151A → T. Ref.8 Ref.24 Ref.25
Corresponds to variant rs6092 [ dbSNP | Ensembl ].
VAR_007099
Natural variant171V → I. Ref.8 Ref.25
Corresponds to variant rs6090 [ dbSNP | Ensembl ].
VAR_011750
Natural variant251H → P. Ref.8
Corresponds to variant rs2227647 [ dbSNP | Ensembl ].
VAR_013086
Natural variant2091R → H. Ref.8
Corresponds to variant rs2227669 [ dbSNP | Ensembl ].
VAR_013087
Natural variant2551T → N. Ref.8
Corresponds to variant rs2227685 [ dbSNP | Ensembl ].
VAR_013088

Experimental info

Sequence conflict531R → A in CAA31208. Ref.7
Sequence conflict551V → L in AAA60009. Ref.2
Sequence conflict751G → V in CAA31208. Ref.7
Sequence conflict1381R → K in CAA31208. Ref.7
Sequence conflict2261A → V in BAH12656. Ref.9
Sequence conflict280 – 2823QLI → HVM in CAA31208. Ref.7

Secondary structure

...................................................................... 402
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: A2E181ED28DD6082

FASTA40245,060
        10         20         30         40         50         60 
MQMSPALTCL VLGLALVFGE GSAVHHPPSY VAHLASDFGV RVFQQVAQAS KDRNVVFSPY 

        70         80         90        100        110        120 
GVASVLAMLQ LTTGGETQQQ IQAAMGFKID DKGMAPALRH LYKELMGPWN KDEISTTDAI 

       130        140        150        160        170        180 
FVQRDLKLVQ GFMPHFFRLF RSTVKQVDFS EVERARFIIN DWVKTHTKGM ISNLLGKGAV 

       190        200        210        220        230        240 
DQLTRLVLVN ALYFNGQWKT PFPDSSTHRR LFHKSDGSTV SVPMMAQTNK FNYTEFTTPD 

       250        260        270        280        290        300 
GHYYDILELP YHGDTLSMFI AAPYEKEVPL SALTNILSAQ LISHWKGNMT RLPRLLVLPK 

       310        320        330        340        350        360 
FSLETEVDLR KPLENLGMTD MFRQFQADFT SLSDQEPLHV AQALQKVKIE VNESGTVASS 

       370        380        390        400 
STAVIVSARM APEEIIMDRP FLFVVRHNPT GTVLFMGQVM EP 

« Hide

Isoform 2 [UniParc].

Checksum: 9BFE4D37D0F81361
Show »

FASTA38743,404

References

« Hide 'large scale' references
[1]"Endothelial plasminogen activator inhibitor (PAI): a new member of the Serpin gene family."
Pannekoek H., Veerman H., Lambers H., Diergaarde P., Verweij C.L., van Zonneveld A.-J., van Mourik J.A.
EMBO J. 5:2539-2544(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Structure of the human plasminogen activator inhibitor 1 gene: nonrandom distribution of introns."
Loskutoff D.J., Linders M., Keijer J., Veerman H., van Heerikhuizen H., Pannekoek H.
Biochemistry 26:3763-3768(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"cDNA cloning of human plasminogen activator-inhibitor from endothelial cells."
Ginsburg D., Zeheb R., Yang A.Y., Rafferty U.M., Andreasen P.A., Nielsen L., Dano K., Lebo R.V., Gelehrter T.D.
J. Clin. Invest. 78:1673-1680(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Structure and expression of the human gene encoding plasminogen activator inhibitor, PAI-1."
Follo M., Ginsburg D.
Gene 84:447-453(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family."
Strandberg L., Lawrence D., Ny T.
Eur. J. Biochem. 176:609-616(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Human plasminogen activator inhibitor-1 gene. Promoter and structural gene nucleotide sequences."
Bosma P.J., van den Berg E.A., Kooistra T., Siemieniak D.R., Slightom J.L.
J. Biol. Chem. 263:9129-9141(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]Pannekoek H.
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[8]SeattleSNPs variation discovery resource
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-15; ILE-17; PRO-25; HIS-209 AND ASN-255.
[9]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[10]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[12]"Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor."
Ny T., Sawdey M., Lawrence D., Millan J.L., Loskutoff D.J.
Proc. Natl. Acad. Sci. U.S.A. 83:6776-6780(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-402 (ISOFORM 1).
[13]"Plasminogen activator inhibitor type-1: reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing."
Andreasen P.A., Riccio A., Welinder K.G., Douglas R., Sartorio R., Nielsen L.S., Oppenheimer C., Blasi F., Danoe K.
FEBS Lett. 209:213-218(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 AND 364-402 (ISOFORM 1).
[14]"cDNA cloning and expression in E. coli of a plasminogen activator inhibitor (PAI) related to a PAI produced by Hep G2 hepatoma cell."
Wun T.C., Kretzmer K.K.
FEBS Lett. 210:11-16(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-402 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
Tissue: Placenta.
[15]"Identification of a PAI-1 binding site in vitronectin."
Sigurdardottir O., Wiman B.
Biochim. Biophys. Acta 1208:104-110(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VTN.
[16]"Human plasminogen activator inhibitor-1 (PAI-1) deficiency: characterization of a large kindred with a null mutation in the PAI-1 gene."
Fay W.P., Parker A.C., Condrey L.R., Shapiro A.D.
Blood 90:204-208(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PAI-1D.
[17]"The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein."
Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.
J. Biol. Chem. 276:28889-28896(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRP1B.
[18]"Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity."
Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.
Biochem. J. 390:231-242(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, HETERODIMER WITH TMPRSS7.
[19]"Structural basis of latency in plasminogen activator inhibitor-1."
Mottonen J., Strand A., Symersky J., Sweet R.M., Danley D.E., Geoghegan K.F., Gerard R.D., Goldsmith E.J.
Nature 355:270-273(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[20]"Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1."
Aertgeerts K., de Bondt H.L., de Ranter C.J., Declerck P.J.
Nat. Struct. Biol. 2:891-897(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[21]"Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide."
Xue Y., Bjoerquist P., Inghardt T., Linschoten M., Musil D., Sjoelin L., Deinum J.
Structure 6:627-636(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[22]"The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion."
Sharp A.M., Stein P.E., Pannu N.S., Carrell R.W., Berkenpas M.B., Ginsburg D., Lawrence D.A., Read R.J.
Structure 7:111-118(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS).
[23]"Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation."
Nar H., Bauer M., Stassen J.M., Lang D., Gils A., Declerck P.J.
J. Mol. Biol. 297:683-695(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[24]"Mutational analysis of the genes encoding urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer."
Turkmen B., Schmitt M., Schmalfeldt B., Trommler P., Hell W., Creutzburg S., Graeff H., Magdolen V.
Electrophoresis 18:686-689(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-15.
[25]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-15 AND ILE-17.
[26]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Plasminogen activator inhibitor-1 entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04429 mRNA. Translation: CAA28025.1.
M14083 mRNA. Translation: AAA60008.1.
X04729 mRNA. Translation: CAA28438.1.
X04731 mRNA. Translation: CAA28442.1.
M16006 mRNA. Translation: AAA60003.1.
M22321 expand/collapse EMBL AC list , M22314, M22315, M22316, M22317, M22318, M22319, M22320 Genomic DNA. Translation: AAA60009.1.
X13323 Genomic DNA. No translation available.
X13338 Genomic DNA. Translation: CAA31722.1.
X13339 Genomic DNA. Translation: CAB51639.1.
X13340 Genomic DNA. Translation: CAB51737.1.
X13341 Genomic DNA. Translation: CAB51606.1.
X13342 Genomic DNA. Translation: CAB51607.1.
X13343 Genomic DNA. Translation: CAB51738.1.
X13344 Genomic DNA. Translation: CAB51739.1.
X13345 Genomic DNA. Translation: CAA31729.1.
J03764 Genomic DNA. Translation: AAA60007.1.
X12701 mRNA. Translation: CAA31208.1.
AF386492 Genomic DNA. Translation: AAK60338.1.
AK297728 mRNA. Translation: BAH12656.1.
AC004876 Genomic DNA. Translation: AAD45828.1.
BC010860 mRNA. Translation: AAH10860.1.
X04744 mRNA. Translation: CAA28444.1.
PIRITHUP1. A28107.
RefSeqNP_000593.1. NM_000602.4.
UniGeneHs.414795.
Hs.713079.
Hs.741440.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7CX-ray1.95A24-402[»]
1B3KX-ray2.99A/B/C/D24-402[»]
1C5GX-ray2.60A1-402[»]
1DB2X-ray2.70A/B26-402[»]
1DVMX-ray2.40A/B/C/D24-402[»]
1DVNX-ray2.10A24-402[»]
1LJ5X-ray1.80A24-402[»]
1OC0X-ray2.28A24-402[»]
3CVMX-ray2.02A/B21-402[»]
3EOXX-ray2.61A24-402[»]
3PB1X-ray2.30I24-402[»]
3Q02X-ray2.30A/B24-402[»]
3Q03X-ray2.64A/B24-402[»]
3R4LX-ray2.70A24-402[»]
3UT3X-ray2.42A/B/C/D28-402[»]
4AQHX-ray2.40A/B/C24-402[»]
4G8OX-ray2.71A/B/C/D28-402[»]
4G8RX-ray2.19A/B28-402[»]
4IC0X-ray2.32A/B/C/D24-402[»]
9PAIX-ray2.70A24-369[»]
B370-402[»]
DisProtDP00320.
ProteinModelPortalP05121.
SMRP05121. Positions 24-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111091. 14 interactions.
IntActP05121. 6 interactions.
MINTMINT-202409.
STRING9606.ENSP00000223095.

Chemistry

BindingDBP05121.
ChEMBLCHEMBL3475.
DrugBankDB01076. Atorvastatin.
DB01093. Dimethyl sulfoxide.
DB00055. Drotrecogin alfa.
DB00641. Simvastatin.
DB00031. Tenecteplase.
DB00197. Troglitazone.
DB00013. Urokinase.

Protein family/group databases

MEROPSI04.020.

PTM databases

PhosphoSiteP05121.

Polymorphism databases

DMDM129576.

2D gel databases

OGPP05121.
SWISS-2DPAGEP05121.

Proteomic databases

PaxDbP05121.
PRIDEP05121.

Protocols and materials databases

DNASU5054.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000223095; ENSP00000223095; ENSG00000106366. [P05121-1]
ENST00000445463; ENSP00000396766; ENSG00000106366. [P05121-2]
GeneID5054.
KEGGhsa:5054.
UCSCuc003uxt.4. human. [P05121-1]

Organism-specific databases

CTD5054.
GeneCardsGC07P100770.
HGNCHGNC:8583. SERPINE1.
HPAHPA050039.
MIM173360. gene.
613329. phenotype.
neXtProtNX_P05121.
Orphanet465. Congenital plasminogen activator inhibitor type 1 deficiency.
PharmGKBPA261.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4826.
HOGENOMHOG000238519.
HOVERGENHBG106493.
InParanoidP05121.
KOK03982.
OMAFVQRDLK.
OrthoDBEOG7327PB.
PhylomeDBP05121.
TreeFamTF352620.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.
REACT_24941. Circadian Clock.
REACT_604. Hemostasis.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP05121.
BgeeP05121.
CleanExHS_SERPINE1.
GenevestigatorP05121.

Family and domain databases

InterProIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 1 hit.
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSERPINE1. human.
EvolutionaryTraceP05121.
GeneWikiPlasminogen_activator_inhibitor-1.
GenomeRNAi5054.
NextBio19480.
PMAP-CutDBP05121.
PROP05121.
SOURCESearch...

Entry information

Entry namePAI1_HUMAN
AccessionPrimary (citable) accession number: P05121
Secondary accession number(s): B7Z4S0, F8WD53
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 175 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM