P00747 (PLMN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plasminogen
EC=3.4.21.7

Cleaved into the following 5 chains:

1. Plasmin heavy chain A
2. Activation peptide
3. Angiostatin
4. Plasmin heavy chain A, short form
5. Plasmin light chain B

Gene names

Name:

PLG

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	810 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	Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. Ref.26 Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo. Ref.26
Catalytic activity	Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products. Ref.29
Enzyme regulation	Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Activated with catalytic amounts of streptokinase. Plasmin activity inhibited by SERPINE2. Ref.26
Subunit structure	Interacts (both mature PLG and the angiostatin peptide) with CSPG4 and AMOT. Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation By similarity. Ref.19 Ref.24 Ref.25 Ref.27 Ref.30
Subcellular location	Secreted. Note: Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface. Ref.24 Ref.26
Tissue specificity	Present in plasma and many other extracellular fluids. It is synthesized in the liver.
Domain	Kringle domains mediate interaction with CSPG4. Ref.25
Post-translational modification	N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide modified with up to 2 sialic acid residues (microheterogeneity). In the presence of the inhibitor, the activation involves only cleavage after Arg-580, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide.
Involvement in disease	Plasminogen deficiency (PLGD) [MIM:217090]: A disorder characterized by decreased serum plasminogen activity. Two forms of the disorder are distinguished: type 1 deficiency is additionally characterized by decreased plasminogen antigen levels and clinical symptoms, whereas type 2 deficiency, also known as dysplasminogenemia, is characterized by normal, or slightly reduced antigen levels, and absence of clinical manifestations. Plasminogen deficiency type 1 results in markedly impaired extracellular fibrinolysis and chronic mucosal pseudomembranous lesions due to subepithelial fibrin deposition and inflammation. The most common clinical manifestation of type 1 deficiency is ligneous conjunctivitis in which pseudomembranes formation on the palpebral surfaces of the eye progresses to white, yellow-white, or red thick masses with a wood-like consistency that replace the normal mucosa. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.48 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56
Miscellaneous	Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot.
Sequence similarities	Belongs to the peptidase S1 family. Plasminogen subfamily. Contains 5 kringle domains. Contains 1 PAN domain. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Blood coagulation Fibrinolysis Hemostasis Tissue remodeling
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Thrombophilia
Domain	Kringle Repeat Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: Compara extracellular matrix disassembly Inferred from direct assay Ref.26. Source: BHF-UCL fibrinolysis Traceable author statement. Source: Reactome induction of apoptosis Inferred from electronic annotation. Source: Compara labyrinthine layer blood vessel development Inferred from electronic annotation. Source: Compara mononuclear cell migration Inferred from electronic annotation. Source: Compara muscle cell homeostasis Inferred from electronic annotation. Source: Compara myoblast differentiation Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Traceable author statement PubMed 8910613. Source: ProtInc negative regulation of cell-cell adhesion mediated by cadherin Traceable author statement PubMed 17203182. Source: BHF-UCL negative regulation of cell-substrate adhesion Inferred from direct assay Ref.26. Source: BHF-UCL negative regulation of fibrinolysis Inferred from direct assay PubMed 14726399. Source: BHF-UCL platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of fibrinolysis Inferred from direct assay PubMed 6438154. Source: BHF-UCL proteolysis involved in cellular protein catabolic process Inferred from electronic annotation. Source: Compara tissue regeneration Inferred from electronic annotation. Source: Compara tissue remodeling Inferred from electronic annotation. Source: UniProtKB-KW trophoblast giant cell differentiation Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Inferred from direct assay PubMed 6980881. Source: BHF-UCL extrinsic to external side of plasma membrane Inferred from direct assay Ref.26. Source: BHF-UCL platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	cell surface binding Inferred from direct assay Ref.26. Source: BHF-UCL serine-type endopeptidase activity Inferred from direct assay Ref.26. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q6V4L1	2	EBI-999394,EBI-984250	From a different organism.
	Q6V4L4	2	EBI-999394,EBI-984286	From a different organism.
	Q6V4L5	2	EBI-999394,EBI-984118	From a different organism.
	Q6V4L9	2	EBI-999394,EBI-984197	From a different organism.
skc	P00779	2	EBI-999394,EBI-1035089	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.7 Ref.8

Chain

20 – 810

791

Plasminogen

PRO_0000028053

Chain

20 – 580

561

Plasmin heavy chain A

PRO_0000028054

Peptide

20 – 97

78

Activation peptide

PRO_0000028055

Chain

79 – 466

388

Angiostatin

PRO_0000028057

Chain

98 – 580

483

Plasmin heavy chain A, short form

PRO_0000028056

Chain

581 – 810

230

Plasmin light chain B

PRO_0000028058

Regions

Domain

20 – 98

79

PAN

Domain

103 – 181

79

Kringle 1

Domain

184 – 262

79

Kringle 2

Domain

275 – 352

78

Kringle 3

Domain

377 – 454

78

Kringle 4

Domain

481 – 560

80

Kringle 5

Domain

581 – 808

228

Peptidase S1

Sites

Active site

622

1

Charge relay system Ref.13 Ref.14

Active site

665

1

Charge relay system Ref.13 Ref.14

Active site

760

1

Charge relay system Ref.13 Ref.14

Binding site

134

1

Fibrin

Binding site

136

1

Fibrin

Binding site

136

1

Omega-aminocarboxylic acids

Binding site

158

1

Omega-aminocarboxylic acids

Binding site

172

1

Omega-aminocarboxylic acids

Binding site

432

1

Omega-aminocarboxylic acids

Binding site

445

1

Omega-aminocarboxylic acids

Site

78 – 79

2

Cleavage; by stromelysin-1

Site

466 – 467

2

Cleavage; by stromelysin-19

Site

580 – 581

2

Cleavage; by plasminogen activator

Amino acid modifications

Modified residue

597

1

Phosphoserine Ref.17

Glycosylation

268

1

O-linked (GalNAc...) Ref.20

CAR_000016

Glycosylation

308

1

N-linked (GlcNAc...) Ref.28

CAR_000017

Glycosylation

365

1

O-linked (GalNAc...)

CAR_000018

Disulfide bond

49 ↔ 73

Ref.36 Ref.38 Ref.40

Disulfide bond

53 ↔ 61

Ref.36 Ref.38 Ref.40

Disulfide bond

103 ↔ 181

Ref.36 Ref.38 Ref.40

Disulfide bond

124 ↔ 164

Ref.36 Ref.38 Ref.40

Disulfide bond

152 ↔ 176

Ref.36 Ref.38 Ref.40

Disulfide bond

185 ↔ 262

Ref.36 Ref.38 Ref.40

Disulfide bond

188 ↔ 316

Ref.36 Ref.38 Ref.40

Disulfide bond

206 ↔ 245

Ref.36 Ref.38 Ref.40

Disulfide bond

234 ↔ 257

Ref.36 Ref.38 Ref.40

Disulfide bond

275 ↔ 352

Ref.36 Ref.38 Ref.40

Disulfide bond

296 ↔ 335

Ref.36 Ref.38 Ref.40

Disulfide bond

324 ↔ 347

Ref.36 Ref.38 Ref.40

Disulfide bond

377 ↔ 454

Ref.36 Ref.38 Ref.40

Disulfide bond

398 ↔ 437

Ref.36 Ref.38 Ref.40

Disulfide bond

426 ↔ 449

Ref.36 Ref.38 Ref.40

Disulfide bond

481 ↔ 560

Ref.36 Ref.38 Ref.40

Disulfide bond

502 ↔ 543

Ref.36 Ref.38 Ref.40

Disulfide bond

531 ↔ 555

Ref.36 Ref.38 Ref.40

Disulfide bond

567 ↔ 685

Interchain (between A and B chains) Ref.36 Ref.38 Ref.40

Disulfide bond

577 ↔ 585

Interchain (between A and B chains) Ref.36 Ref.38 Ref.40

Disulfide bond

607 ↔ 623

Ref.36 Ref.38 Ref.40

Disulfide bond

699 ↔ 766

Ref.36 Ref.38 Ref.40

Disulfide bond

729 ↔ 745

Ref.36 Ref.38 Ref.40

Disulfide bond

756 ↔ 784

Ref.36 Ref.38 Ref.40

Natural variations

Natural variant

38

1

K → E in PLGD; common mutation. Ref.56

VAR_018657

Natural variant

46

1

I → R.
Corresponds to variant rs1049573 [ dbSNP | Ensembl ].

VAR_011779

Natural variant

57

1

E → K. Ref.4
Corresponds to variant rs4252070 [ dbSNP | Ensembl ].

VAR_016287

Natural variant

133

1

H → Q. Ref.4
Corresponds to variant rs4252186 [ dbSNP | Ensembl ].

VAR_016288

Natural variant

134

1

R → K.
Corresponds to variant rs2817 [ dbSNP | Ensembl ].

VAR_033653

Natural variant

147

1

L → P in PLGD. Ref.56

VAR_018658

Natural variant

235

1

R → H in PLGD; severe type 1 deficiency. Ref.54

VAR_018659

Natural variant

261

1

R → H. Ref.4
Corresponds to variant rs4252187 [ dbSNP | Ensembl ].

VAR_016289

Natural variant

374

1

V → F in PLGD; Nagoya-1. Ref.48

VAR_006627

Natural variant

408

1

R → W. Ref.4
Corresponds to variant rs4252119 [ dbSNP | Ensembl ].

VAR_016290

Natural variant

453

1

K → I.
Corresponds to variant rs1804181 [ dbSNP | Ensembl ].

VAR_011780

Natural variant

472

1

D → N. Ref.1 Ref.4 Ref.7 Ref.9
Corresponds to variant rs4252125 [ dbSNP | Ensembl ].

VAR_016291

Natural variant

494

1

A → V. Ref.4
Corresponds to variant rs4252128 [ dbSNP | Ensembl ].

VAR_016292

Natural variant

523

1

R → W. Ref.4
Corresponds to variant rs4252129 [ dbSNP | Ensembl ].

VAR_016293

Natural variant

532

1

R → H in PLGD. Ref.56

VAR_018660

Natural variant

591

1

S → P in PLGD; may be associated with susceptibility to thrombosis. Ref.50

VAR_006628

Natural variant

620

1

A → T in PLGD; type 2 plasminogen deficiency; decreased activity; Nagoya-2/Tochigi/Kagoshima; may be associated with susceptibility to thrombosis. Ref.48 Ref.51 Ref.52 Ref.53

VAR_006629

Natural variant

676

1

V → D. Ref.6
Corresponds to variant rs17857492 [ dbSNP | Ensembl ].

VAR_031213

Natural variant

751

1

G → R in PLGD; Kanagawa-1; 50% activity. Ref.55

VAR_006630

Experimental info

Mutagenesis

741

1

S → A: Proteolytically cleaved, but abolishes plasmin activity and cell detachment. Ref.26

Sequence conflict

50

1

A → AQ AA sequence Ref.8

Sequence conflict

72

1

Q → E AA sequence Ref.7

Sequence conflict

72

1

Q → E AA sequence Ref.8

Sequence conflict

86

1

Missing AA sequence Ref.7

Sequence conflict

86

1

Missing AA sequence Ref.8

Sequence conflict

361

1

Q → E AA sequence Ref.7

Sequence conflict

361

1

Q → E AA sequence Ref.9

Sequence conflict

701

1

I → V in AAA36451. Ref.3

Secondary structure

1

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810

Helix Strand Turn

Details...

Beta strand

25 – 33

9

Beta strand

36 – 42

7

Helix

46 – 55

10

Beta strand

57 – 59

3

Beta strand

63 – 67

5

Turn

68 – 71

4

Beta strand

72 – 77

6

Turn

80 – 82

3

Beta strand

85 – 96

12

Helix

97 – 99

3

Beta strand

102 – 104

3

Beta strand

105 – 110

6

Helix

113 – 115

3

Turn

119 – 121

3

Beta strand

131 – 133

3

Turn

139 – 141

3

Helix

143 – 145

3

Beta strand

148 – 150

3

Beta strand

155 – 157

3

Beta strand

163 – 167

5

Beta strand

172 – 175

4

Beta strand

180 – 182

3

Beta strand

184 – 186

3

Beta strand

205 – 207

3

Beta strand

209 – 211

3

Beta strand

213 – 215

3

Turn

221 – 223

3

Helix

225 – 227

3

Beta strand

237 – 239

3

Beta strand

244 – 248

5

Beta strand

253 – 256

4

Beta strand

273 – 276

4

Beta strand

281 – 283

3

Beta strand

291 – 293

3

Beta strand

295 – 297

3

Beta strand

303 – 305

3

Turn

311 – 313

3

Helix

315 – 317

3

Beta strand

334 – 339

6

Beta strand

343 – 346

4

Beta strand

377 – 379

3

Beta strand

382 – 384

3

Beta strand

405 – 407

3

Turn

413 – 415

3

Turn

417 – 419

3

Beta strand

429 – 431

3

Beta strand

436 – 441

6

Beta strand

446 – 450

5

Beta strand

481 – 483

3

Beta strand

487 – 489

3

Beta strand

509 – 511

3

Beta strand

514 – 516

3

Turn

518 – 520

3

Turn

522 – 525

4

Beta strand

542 – 546

5

Beta strand

552 – 554

3

Beta strand

582 – 586

5

Beta strand

595 – 599

5

Beta strand

605 – 613

9

Beta strand

616 – 619

4

Helix

621 – 624

4

Helix

630 – 632

3

Beta strand

634 – 638

5

Beta strand

640 – 644

5

Beta strand

650 – 659

10

Turn

661 – 663

3

Beta strand

667 – 673

7

Beta strand

698 – 703

6

Beta strand

708 – 710

3

Turn

711 – 714

4

Beta strand

717 – 724

8

Helix

726 – 729

4

Turn

732 – 737

6

Beta strand

743 – 747

5

Beta strand

749 – 751

3

Beta strand

752 – 754

3

Beta strand

763 – 767

5

Beta strand

769 – 778

10

Helix

780 – 782

3

Beta strand

791 – 795

5

Helix

796 – 798

3

Helix

800 – 808

9

Sequences

	Sequence		Length	Mass (Da)
	P00747 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: 8B31CB877CCB3AB6	FASTA	810	90,569
	10 20 30 40 50 60 MEHKEVVLLL LLFLKSGQGE PLDDYVNTQG ASLFSVTKKQ LGAGSIEECA AKCEEDEEFT 70 80 90 100 110 120 CRAFQYHSKE QQCVIMAENR KSSIIIRMRD VVLFEKKVYL SECKTGNGKN YRGTMSKTKN 130 140 150 160 170 180 GITCQKWSST SPHRPRFSPA THPSEGLEEN YCRNPDNDPQ GPWCYTTDPE KRYDYCDILE 190 200 210 220 230 240 CEEECMHCSG ENYDGKISKT MSGLECQAWD SQSPHAHGYI PSKFPNKNLK KNYCRNPDRE 250 260 270 280 290 300 LRPWCFTTDP NKRWELCDIP RCTTPPPSSG PTYQCLKGTG ENYRGNVAVT VSGHTCQHWS 310 320 330 340 350 360 AQTPHTHNRT PENFPCKNLD ENYCRNPDGK RAPWCHTTNS QVRWEYCKIP SCDSSPVSTE 370 380 390 400 410 420 QLAPTAPPEL TPVVQDCYHG DGQSYRGTSS TTTTGKKCQS WSSMTPHRHQ KTPENYPNAG 430 440 450 460 470 480 LTMNYCRNPD ADKGPWCFTT DPSVRWEYCN LKKCSGTEAS VVAPPPVVLL PDVETPSEED 490 500 510 520 530 540 CMFGNGKGYR GKRATTVTGT PCQDWAAQEP HRHSIFTPET NPRAGLEKNY CRNPDGDVGG 550 560 570 580 590 600 PWCYTTNPRK LYDYCDVPQC AAPSFDCGKP QVEPKKCPGR VVGGCVAHPH SWPWQVSLRT 610 620 630 640 650 660 RFGMHFCGGT LISPEWVLTA AHCLEKSPRP SSYKVILGAH QEVNLEPHVQ EIEVSRLFLE 670 680 690 700 710 720 PTRKDIALLK LSSPAVITDK VIPACLPSPN YVVADRTECF ITGWGETQGT FGAGLLKEAQ 730 740 750 760 770 780 LPVIENKVCN RYEFLNGRVQ STELCAGHLA GGTDSCQGDS GGPLVCFEKD KYILQGVTSW 790 800 810 GLGCARPNKP GVYVRVSRFV TWIEGVMRNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the gene for human plasminogen, a key proenzyme in the fibrinolytic system." Petersen T.E., Martzen M.R., Ichinose A., Davie E.W. J. Biol. Chem. 265:6104-6111(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-472.
[2]	"Molecular cloning and characterization of a full-length cDNA clone for human plasminogen." Forsgren M., Raden B., Israelsson M., Larsson K., Heden L.-O. FEBS Lett. 213:254-260(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Expression of recombinant human plasminogen and aglycoplasminogen in HeLa cells." Browne M.J., Chapman C.G., Dodd I., Carey J.E., Lawrence G.M.P., Mitchell D., Robinson J.H. Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	SeattleSNPs variation discovery resource Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-57; GLN-133; HIS-261; TRP-408; ASN-472; VAL-494 AND TRP-523.
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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], VARIANT ASP-676. Tissue: Kidney.
[7]	Sottrup-Jensen L., Petersen T.E., Magnusson S. Submitted (JUL-1977) to the PIR data bank Cited for: PROTEIN SEQUENCE OF 20-810, VARIANT ASN-472.
[8]	"Structural relationship between 'glutamic acid' and 'lysine' forms of human plasminogen and their interaction with the NH2-terminal activation peptide as studied by affinity chromatography." Wiman B., Wallen P. Eur. J. Biochem. 50:489-494(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-100.
[9]	"The primary structure of human plasminogen." Sottrup-Jensen L., Claeys H., Zajdel M., Petersen T.E., Magnusson S. (In) Davidson J.F., Rowan R.M., Samama M.M., Desnoyers P.C. (eds.); Progress in chemical fibrinolysis and thrombolysis, pp.3:191-209, Raven Press, New York (1978) Cited for: PROTEIN SEQUENCE OF 95-580; 581-626; 657-700 AND 732-810, VARIANT ASN-472.
[10]	"Characterization of a complementary deoxyribonucleic acid coding for human and bovine plasminogen." Malinowski D.P., Sadler J.E., Davie E.W. Biochemistry 23:4243-4250(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 292-810.
[11]	"Amino-acid sequence of the cyanogen-bromide fragment from human plasminogen that forms the linkage between the plasmin chains." Wiman B., Wallen P. Eur. J. Biochem. 58:539-547(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 483-604.
[12]	"Primary structure of the B-chain of human plasmin." Wiman B. Eur. J. Biochem. 76:129-137(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 581-810.
[13]	"The primary structure of human plasminogen. II. The histidine loop of human plasmin: light (B) chain active center histidine sequence." Robbins K.C., Bernabe P., Arzadon L., Summaria L. J. Biol. Chem. 248:1631-1633(1973) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE.
[14]	"Studies on the active center of human plasmin. Partial amino acid sequence of a peptide containing the active center serine residue." Groskopf W.R., Summaria L., Robbins K.C. J. Biol. Chem. 244:3590-3597(1969) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE.
[15]	"Structure of the omega-aminocarboxylic acid-binding sites of human plasminogen. Arginine 70 and aspartic acid 56 are essential for binding of ligand by kringle 4." Trexler M., Vali Z., Patthy L. J. Biol. Chem. 257:7401-7406(1982) [PubMed] [Europe PMC] [Abstract] Cited for: OMEGA-AMINOCARBOXYLIC ACID-BINDING SITES.
[16]	"The fibrin-binding site of human plasminogen. Arginines 32 and 34 are essential for fibrin affinity of the kringle 1 domain." Vali Z., Patthy L. J. Biol. Chem. 259:13690-13694(1984) [PubMed] [Europe PMC] [Abstract] Cited for: FIBRIN AND OMEGA-AMINOCARBOXYLIC ACID BINDING SITES.
[17]	"Serine-578 is a major phosphorylation locus in human plasma plasminogen." Wang H., Prorok M., Bretthauer R.K., Castellino F.J. Biochemistry 36:8100-8106(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-597.
[18]	"The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen. Species specificity in relation to sialylation and fucosylation patterns." Marti T., Schaller J., Rickli E.E., Schmid K., Kamerling J.P., Gerwig G.J., van Halbeek H., Vliegenthart J.F.G. Eur. J. Biochem. 173:57-63(1988) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATES.
[19]	"Acceleration of plasminogen activation by tissue plasminogen activator on surface-bound histidine-proline-rich glycoprotein." Borza D.B., Morgan W.T. J. Biol. Chem. 272:5718-5726(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HRG.
[20]	"Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2." Pirie-Shepherd S.R., Stevens R.D., Andon N.L., Enghild J.J., Pizzo S.V. J. Biol. Chem. 272:7408-7411(1997) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-268.
[21]	"Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma." O'Reilly M.S., Holmgren L., Shing Y., Chen C., Rosenthal R.A., Moses M., Lane W.S., Cao Y., Sage E.H., Folkman J. Cell 79:315-328(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF ANGIOSTATIN, PARTIAL PROTEIN SEQUENCE.
[22]	"A recombinant human angiostatin protein inhibits experimental primary and metastatic cancer." Sim B.K., O'Reilly M.S., Liang H., Fortier A.H., He W., Madsen J.W., Lapcevich R., Nacy C.A. Cancer Res. 57:1329-1334(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF ANGIOSTATIN.
[23]	"Generation of an angiostatin-like fragment from plasminogen by stromelysin-1 (MMP-3)." Lijnen H.R., Ugwu F., Bini A., Collen D. Biochemistry 37:4699-4702(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC CLEAVAGE.
[24]	"Angiostatin binds ATP synthase on the surface of human endothelial cells." Moser T.L., Stack M.S., Asplin I., Enghild J.J., Hojrup P., Everitt L., Hubchak S., Schnaper H.W., Pizzo S.V. Proc. Natl. Acad. Sci. U.S.A. 96:2811-2816(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATP5A1, SUBCELLULAR LOCATION.
[25]	"Binding of the NG2 proteoglycan to kringle domains modulates the functional properties of angiostatin and plasmin(ogen)." Goretzki L., Lombardo C.R., Stallcup W.B. J. Biol. Chem. 275:28625-28633(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CSPG4, DOMAIN.
[26]	"Protease nexin-1 inhibits plasminogen activation-induced apoptosis of adherent cells." Rossignol P., Ho-Tin-Noe B., Vranckx R., Bouton M.C., Meilhac O., Lijnen H.R., Guillin M.C., Michel J.B., Angles-Cano E. J. Biol. Chem. 279:10346-10356(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING, ENZYME REGULATION, SUBCELLULAR LOCATION, FUNCTION OF PLASMIN, MUTAGENESIS OF SER-741.
[27]	"Angiomotin regulates endothelial cell-cell junctions and cell motility." Bratt A., Birot O., Sinha I., Veitonmaeki N., Aase K., Ernkvist M., Holmgren L. J. Biol. Chem. 280:34859-34869(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AMOT.
[28]	"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry." Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F. Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308, MASS SPECTROMETRY. Tissue: Milk.
[29]	"A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule." Kirschbaum N.E., Budzynski A.Z. J. Biol. Chem. 265:13669-13676(1990) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY.
[30]	"Regulation of histidine-rich glycoprotein (HRG) function via plasmin-mediated proteolytic cleavage." Poon I.K., Olsson A.K., Hulett M.D., Parish C.R. Biochem. J. 424:27-37(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HRG.
[31]	"Crystal and molecular structure of human plasminogen kringle 4 refined at 1.9-A resolution." Mulichak A.M., Tulinsky A., Ravichandran K.G. Biochemistry 30:10576-10588(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 374-461.
[32]	"The refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4." Wu T.-P., Padmanabhan K., Tulinsky A., Mulichak A.M. Biochemistry 30:10589-10594(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 374-461.
[33]	"The structure of recombinant plasminogen kringle 1 and the fibrin binding site." Wu T.-P., Padmanabhan K.P., Tulinsky A. Blood Coagul. Fibrinolysis 5:157-166(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 101-181.
[34]	"Crystal structures of the recombinant kringle 1 domain of human plasminogen in complexes with the ligands epsilon-aminocaproic acid and trans-4-(aminomethyl)cyclohexane-1-carboxylic Acid." Mathews I.I., Vanderhoff-Hanaver P., Castellino F.J., Tulinsky A. Biochemistry 35:2567-2576(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 102-181.
[35]	"Structure of human plasminogen kringle 4 at 1.68 Angstrom and 277 K. A possible structural role of disordered residues." Stec B., Yamano A., Whitlow M., Teeter M.M. Acta Crystallogr. D 53:169-178(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 376-454.
[36]	"The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action." Parry M.A., Fernandez-Catalan C., Bergner A., Huber R., Hopfner K.P., Schlott B., Guehrs K.H., Bode W. Nat. Struct. Biol. 5:917-923(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 561-810, DISULFIDE BONDS.
[37]	"Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen." Chang Y., Mochalkin I., McCance S.G., Cheng B., Tulinsky A., Castellino F.J. Biochemistry 37:3258-3271(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 480-563.
[38]	"Human plasminogen catalytic domain undergoes an unusual conformational change upon activation." Wang X., Terzyan S., Tang J., Loy J.A., Lin X., Zhang X.C. J. Mol. Biol. 295:903-914(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 564-810, DISULFIDE BONDS.
[39]	"Structure and binding determinants of the recombinant kringle-2 domain of human plasminogen to an internal peptide from a group A Streptococcal surface protein." Rios-Steiner J.L., Schenone M., Mochalkin I., Tulinsky A., Castellino F.J. J. Mol. Biol. 308:705-719(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 183-262.
[40]	"The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin." Abad M.C., Arni R.K., Grella D.K., Castellino F.J., Tulinsky A., Geiger J.H. J. Mol. Biol. 318:1009-1017(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 100-352, DISULFIDE BONDS.
[41]	"Effects of deletion of streptokinase residues 48-59 on plasminogen activation." Wakeham N., Terzyan S., Zhai P., Loy J.A., Tang J., Zhang X.C. Protein Eng. 15:753-761(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 562-810.
[42]	"Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain." Terzyan S., Wakeham N., Zhai P., Rodgers K., Zhang X.C. Proteins 56:277-284(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 564-810.
[43]	"Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry." Atkinson R.A., Williams R.J.P. J. Mol. Biol. 212:541-552(1990) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 374-461.
[44]	"1H-NMR assignments and secondary structure of human plasminogen kringle 1." Rejante M.R., Llinas M. Eur. J. Biochem. 221:927-937(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 96-184.
[45]	"Solution structure of the epsilon-aminohexanoic acid complex of human plasminogen kringle 1." Rejante M.R., Llinas M. Eur. J. Biochem. 221:939-949(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 96-184.
[46]	"Recombinant gene expression and 1H NMR characteristics of the kringle (2 + 3) supermodule: spectroscopic/functional individuality of plasminogen kringle domains." Soehndel S., Hu C.-K., Marti D., Affolter M., Schaller J., Llinas M., Rickli E.E. Biochemistry 35:2357-2364(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 183-354.
[47]	"Ligand preferences of kringle 2 and homologous domains of human plasminogen: canvassing weak, intermediate, and high-affinity binding sites by 1H-NMR." Marti D.N., Hu C.K., An S.S., von Haller P., Schaller J., Llinas M. Biochemistry 36:11591-11604(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 183-263.
[48]	"Two types of abnormal genes for plasminogen in families with a predisposition for thrombosis." Ichinose A., Espling E.S., Takamatsu J., Saito H., Shinmyozu K., Maruyama I., Petersen T.E., Davie E.W. Proc. Natl. Acad. Sci. U.S.A. 88:115-119(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PLGD PHE-374 AND THR-620.
[49]	Erratum Ichinose A., Espling E.S., Takamatsu J., Saito H., Shinmyozu K., Maruyama I., Petersen T.E., Davie E.W. Proc. Natl. Acad. Sci. U.S.A. 88:2067-2067(1991)
[50]	"Congenital plasminogen deficiency caused by a Ser-572 to Pro mutation." Azuma H., Uno Y., Shigekiyo T., Saito S. Blood 82:475-480(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PLGD PRO-591.
[51]	"Plasminogen Tochigi: inactive plasmin resulting from replacement of alanine-600 by threonine in the active site." Miyata T., Iwanaga S., Sakata Y., Aoki N. Proc. Natl. Acad. Sci. U.S.A. 79:6132-6136(1982) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PLGD THR-620.
[52]	"Plasminogens Tochigi II and Nagoya: two additional molecular defects with Ala-600-->Thr replacement found in plasmin light chain variants." Miyata T., Iwanaga S., Sakata Y., Aoki N., Takamatsu J., Kamiya T. J. Biochem. 96:277-287(1984) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PLGD THR-620.
[53]	"Plasminogen with type-I mutation is polymorphic in the Japanese population." Kikuchi S., Yamanouchi Y., Li L., Kobayashi K., Ijima H., Miyazaki R., Tsuchiya S., Hamaguchi H. Hum. Genet. 90:7-11(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PLGD THR-620.
[54]	"Homozygous mutations in the plasminogen gene of two unrelated girls with ligneous conjunctivitis." Schuster V., Mingers A.-M., Seidenspinner S., Nuessgens Z., Pukrop T., Kreth H.W. Blood 90:958-966(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PLGD HIS-235.
[55]	"Plasminogen Kanagawa-I, a novel missense mutation, is caused by the amino acid substitution G732R." Higuchi Y., Furihata K., Ueno I., Ishikawa S., Okumura N., Tozuka M., Sakurai N. Br. J. Haematol. 103:867-870(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PLGD ARG-751.
[56]	"Compound-heterozygous mutations in the plasminogen gene predispose to the development of ligneous conjunctivitis." Schuster V., Seidenspinner S., Zeitler P., Escher C., Pleyer U., Bernauer W., Stiehm E.R., Isenberg S., Seregard S., Olsson T., Mingers A.-M., Schambeck C., Kreth H.W. Blood 93:3457-3466(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PLGD GLU-38; PRO-147 AND HIS-532.
+	Additional computationally mapped references.

Web resources

Wikipedia

Plasmin entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34276 , M33272, M33274, M33275, M33278, M33279, M33280, M33282, M33283, M33284, M33285, M33286, M33287, M33288, M33289, M33290, M34272, M34273, M34275 Genomic DNA. Translation: AAA60113.1.
X05199 mRNA. Translation: CAA28831.1.
M74220 mRNA. Translation: AAA36451.1.
AY192161 Genomic DNA. Translation: AAN85555.1.
AL109933 Genomic DNA. Translation: CAI22908.1.
BC060513 mRNA. Translation: AAH60513.1.
K02922 mRNA. Translation: AAA60124.1.

IPI

IPI00019580.

PIR

PLHU. A35229.

RefSeq

NP_000292.1. NM_000301.3.

UniGene

Hs.143436.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B2I	NMR	-	A	183-263	[»]
1BML	X-ray	2.90	A/B	561-810	[»]
1BUI	X-ray	2.65	A/B	561-810	[»]
1CEA	X-ray	2.06	A/B	100-187	[»]
1CEB	X-ray	2.07	A/B	100-187	[»]
1DDJ	X-ray	2.00	A/B/C/D	564-810	[»]
1HPJ	NMR	-	A	103-181	[»]
1HPK	NMR	-	A	103-181	[»]
1I5K	X-ray	2.70	A/B	183-262	[»]
1KI0	X-ray	1.75	A	100-352	[»]
1KRN	X-ray	1.67	A	374-461	[»]
1L4D	X-ray	2.30	A	562-810	[»]
1L4Z	X-ray	2.80	A	563-810	[»]
1PK4	X-ray	1.90	A	376-454	[»]
1PKR	X-ray	2.48	A	101-181	[»]
1PMK	X-ray	2.25	A/B	374-461	[»]
1QRZ	X-ray	2.00	A/B/C/D	565-810	[»]
1RJX	X-ray	2.30	B	564-810	[»]
2DOH	X-ray	2.30	X	100-333	[»]
2DOI	X-ray	3.10	A/X	100-333	[»]
2KNF	NMR	-	A	480-562	[»]
2L0S	NMR	-	A	272-354	[»]
2PK4	X-ray	2.25	A	375-454	[»]
3UIR	X-ray	2.78	A/B	564-810	[»]
4A5T	X-ray	3.49	S	20-810	[»]
4DCB	X-ray	2.03	F	576-585	[»]
4DUR	X-ray	2.45	A/B	20-810	[»]
4DUU	X-ray	5.20	A	20-810	[»]
5HPG	X-ray	1.66	A/B	480-563	[»]

DisProt

DP00191.

ProteinModelPortal

P00747.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00747. 22 interactions.

STRING

9606.ENSP00000308938.

Protein family/group databases

MEROPS

S01.233.

PTM databases

GlycoSuiteDB

P00747.

PhosphoSite

P00747.

Polymorphism databases

DMDM

130316.

2D gel databases

SWISS-2DPAGE

P00747.

Proteomic databases

PeptideAtlas

P00747.

PRIDE

P00747.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000308192; ENSP00000308938; ENSG00000122194.

GeneID

5340.

KEGG

hsa:5340.

UCSC

uc003qtm.4. human.

Organism-specific databases

CTD

5340.

GeneCards

GC06P161123.

HGNC

HGNC:9071. PLG.

HPA

CAB000668.
CAB016678.
HPA021602.

MIM

173350. gene.
217090. phenotype.

neXtProt

NX_P00747.

Orphanet

722. Hypoplasminogenemia.
97231. Ligneous conjunctivitis.

PharmGKB

PA33405.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HOG000112892.

HOVERGEN

HBG004381.

InParanoid

P00747.

KO

K01315.

OMA

PSKFPNK.

OrthoDB

EOG4RR6GQ.

PhylomeDB

P00747.

Enzyme and pathway databases

BioCyc

MetaCyc:HS04553-MONOMER.

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
p75ntrpathway. p75(NTR)-mediated signaling.
syndecan_4_pathway. Syndecan-4-mediated signaling events.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P00747.

Bgee

P00747.

CleanEx

HS_PLG.

Genevestigator

P00747.

GermOnline

ENSG00000122194. Homo sapiens.

Family and domain databases

Gene3D

2.40.20.10. 5 hits.

InterPro

IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR023317. Pept_S1A_plasmin.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]

PIRSF

PIRSF001150. Plasmin. 1 hit.

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF57440. Kringle-like. 5 hits.
SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS00021. KRINGLE_1. 5 hits.
PS50070. KRINGLE_2. 5 hits.
PS50948. PAN. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00747.

ChEMBL

CHEMBL1801.

DrugBank

DB00513. Aminocaproic Acid.
DB00086. Streptokinase.
DB00302. Tranexamic Acid.
DB00013. Urokinase.

EvolutionaryTrace

P00747.

GenomeRNAi

5340.

NextBio

20698.

PMAP-CutDB

P00747.

SOURCE

Search...

Entry information

Entry name

PLMN_HUMAN

Accession

Primary (citable) accession number: P00747
Secondary accession number(s): Q15146, Q5TEH4, Q6PA00

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 178 of the entry and version 2 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.