P05121 (PAI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from expression pattern PubMed 11866539. Source: UniProtKB 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 fibrinolysis Traceable author statement. Source: Reactome negative regulation of apoptotic process Inferred from mutant phenotype PubMed 18835034. Source: BHF-UCL negative regulation of cell adhesion mediated by integrin Inferred from direct assay PubMed 8837777. 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 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 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: Compara 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 transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	extracellular matrix Inferred from direct assay PubMed 1632457. 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_function	serine-type endopeptidase inhibitor activity Inferred from direct assay PubMed 1695900. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ORM1	P02763	4	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Chain

24 – 402

379

Plasminogen activator inhibitor 1

PRO_0000032499

Sites

Site

369 – 370

2

Reactive bond

Amino acid modifications

Glycosylation

232

1

N-linked (GlcNAc...)

Glycosylation

288

1

N-linked (GlcNAc...)

Glycosylation

352

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

31 – 45

15

Missing in isoform 2.

VSP_045493

Natural variant

15

1

A → T. Ref.8 Ref.24 Ref.25
Corresponds to variant rs6092 [ dbSNP | Ensembl ].

VAR_007099

Natural variant

17

1

V → I. Ref.8 Ref.25
Corresponds to variant rs6090 [ dbSNP | Ensembl ].

VAR_011750

Natural variant

25

1

H → P. Ref.8
Corresponds to variant rs2227647 [ dbSNP | Ensembl ].

VAR_013086

Natural variant

209

1

R → H. Ref.8
Corresponds to variant rs2227669 [ dbSNP | Ensembl ].

VAR_013087

Natural variant

255

1

T → N. Ref.8
Corresponds to variant rs2227685 [ dbSNP | Ensembl ].

VAR_013088

Experimental info

Sequence conflict

53

1

R → A in CAA31208. Ref.7

Sequence conflict

55

1

V → L in AAA60009. Ref.2

Sequence conflict

75

1

G → V in CAA31208. Ref.7

Sequence conflict

138

1

R → K in CAA31208. Ref.7

Sequence conflict

226

1

A → V in BAH12656. Ref.9

Sequence conflict

280 – 282

3

QLI → HVM in CAA31208. Ref.7

Secondary structure

1

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402

Helix Strand Turn

Details...

Helix

27 – 49

23

Turn

50 – 52

3

Beta strand

55 – 57

3

Helix

59 – 72

14

Helix

75 – 85

11

Helix

94 – 106

13

Helix

108 – 110

3

Beta strand

111 – 123

13

Helix

132 – 140

9

Beta strand

145 – 147

3

Helix

149 – 151

3

Helix

152 – 165

14

Turn

166 – 169

4

Helix

176 – 179

4

Beta strand

186 – 200

15

Helix

204 – 206

3

Beta strand

209 – 213

5

Beta strand

216 – 218

3

Beta strand

219 – 237

19

Turn

239 – 241

3

Beta strand

243 – 251

9

Beta strand

254 – 265

12

Helix

271 – 274

4

Helix

279 – 288

10

Beta strand

290 – 299

10

Beta strand

301 – 308

8

Helix

310 – 315

6

Helix

320 – 322

3

Turn

324 – 326

3

Turn

330 – 332

3

Beta strand

334 – 336

3

Beta strand

340 – 351

12

Beta strand

353 – 368

16

Beta strand

374 – 376

3

Beta strand

380 – 387

8

Turn

388 – 391

4

Beta strand

392 – 400

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: A2E181ED28DD6082	FASTA	402	45,060
	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
	Isoform 2 [UniParc]. Checksum: 9BFE4D37D0F81361	FASTA	387	43,404
	10 20 30 40 50 60 MQMSPALTCL VLGLALVFGE GSAVHHPPSY VAQASKDRNV VFSPYGVASV LAMLQLTTGG 70 80 90 100 110 120 ETQQQIQAAM GFKIDDKGMA PALRHLYKEL MGPWNKDEIS TTDAIFVQRD LKLVQGFMPH 130 140 150 160 170 180 FFRLFRSTVK QVDFSEVERA RFIINDWVKT HTKGMISNLL GKGAVDQLTR LVLVNALYFN 190 200 210 220 230 240 GQWKTPFPDS STHRRLFHKS DGSTVSVPMM AQTNKFNYTE FTTPDGHYYD ILELPYHGDT 250 260 270 280 290 300 LSMFIAAPYE KEVPLSALTN ILSAQLISHW KGNMTRLPRL LVLPKFSLET EVDLRKPLEN 310 320 330 340 350 360 LGMTDMFRQF QADFTSLSDQ EPLHVAQALQ KVKIEVNESG TVASSSTAVI VSARMAPEEI 370 380 IMDRPFLFVV RHNPTGTVLF MGQVMEP

References

	« Hide 'large scale' referencesShow '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. , 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. , 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 , 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.

IPI

IPI00007118.
IPI00926949.

PIR

ITHUP1. A28107.

RefSeq

NP_000593.1. NM_000602.4.
NP_001158885.1. NM_001165413.2.

UniGene

Hs.414795.
Hs.713079.
Hs.741440.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A7C	X-ray	1.95	A	24-402	[»]
1B3K	X-ray	2.99	A/B/C/D	24-402	[»]
1C5G	X-ray	2.60	A	1-402	[»]
1DB2	X-ray	2.70	A/B	26-402	[»]
1DVM	X-ray	2.40	A/B/C/D	24-402	[»]
1DVN	X-ray	2.10	A	24-402	[»]
1LJ5	X-ray	1.80	A	24-402	[»]
1OC0	X-ray	2.28	A	24-402	[»]
3CVM	X-ray	2.02	A/B	21-402	[»]
3EOX	X-ray	2.61	A	24-402	[»]
3PB1	X-ray	2.30	I	24-402	[»]
3Q02	X-ray	2.30	A/B	24-402	[»]
3Q03	X-ray	2.64	A/B	24-402	[»]
3R4L	X-ray	2.70	A	24-402	[»]
3UT3	X-ray	2.42	A/B/C/D	28-402	[»]
4AQH	X-ray	2.40	A/B/C	24-402	[»]
9PAI	X-ray	2.70	A	24-369	[»]
			B	370-402	[»]

DisProt

DP00320.

ProteinModelPortal

P05121.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05121. 3 interactions.

MINT

MINT-202409.

STRING

9606.ENSP00000223095.

Protein family/group databases

MEROPS

I04.020.

PTM databases

PhosphoSite

P05121.

Polymorphism databases

DMDM

129576.

2D gel databases

OGP

P05121.

SWISS-2DPAGE

P05121.

Proteomic databases

PaxDb

P05121.

PRIDE

P05121.

Protocols and materials databases

DNASU

5054.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000223095; ENSP00000223095; ENSG00000106366.
ENST00000445463; ENSP00000396766; ENSG00000106366.

GeneID

5054.

KEGG

hsa:5054.

UCSC

uc003uxt.3. human.
uc011kkj.2. human.

Organism-specific databases

CTD

5054.

GeneCards

GC07P100770.

HGNC

HGNC:8583. SERPINE1.

HPA

HPA050039.

MIM

173360. gene.
613329. phenotype.

neXtProt

NX_P05121.

Orphanet

465. Congenital plasminogen activator inhibitor type 1 deficiency.

PharmGKB

PA261.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4826.

HOGENOM

HOG000238519.

HOVERGEN

HBG106493.

InParanoid

P05121.

KO

K03982.

OMA

GPWNKDE.

OrthoDB

EOG4X3H1K.

PhylomeDB

P05121.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_24941. Circadian Clock.
REACT_604. Hemostasis.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P05121.

Bgee

P05121.

CleanEx

HS_SERPINE1.

Genevestigator

P05121.

GermOnline

ENSG00000106366. Homo sapiens.

Family and domain databases

InterPro

IPR023795. Protease_inhib_I4_serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]

PANTHER

PTHR11461. PTHR11461. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

SUPFAM

SSF56574. Prot_inh_serpin. 1 hit.

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P05121.

ChEMBL

CHEMBL3475.

ChiTaRS

SERPINE1. human.

DrugBank

DB01076. Atorvastatin.
DB01093. Dimethyl sulfoxide.
DB00055. Drotrecogin alfa.
DB00641. Simvastatin.
DB00031. Tenecteplase.
DB00197. Troglitazone.
DB00013. Urokinase.

EvolutionaryTrace

P05121.

GenomeRNAi

5054.

NextBio

19480.

PMAP-CutDB

P05121.

SOURCE

Search...

Entry information

Entry name

PAI1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 165 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.