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Reviewed, UniProtKB/Swiss-Prot P00747 (PLMN_HUMAN)

Last modified January 19, 2010. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Plasminogen
    EC=3.4.21.7
Cleaved into the following 5 chains:
    1- Recommended name:
            Plasmin heavy chain A
    2- Recommended name:
            Activation peptide
    3- Recommended name:
            Angiostatin
    4- Recommended name:
            Plasmin heavy chain A, short form
    5- Recommended name:
            Plasmin light chain B
Gene names
Name: PLG
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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 it weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. It cleaves fibrin, fibronectin, thrombospondin, laminin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4.

Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.

Catalytic activity

Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.

Enzyme regulation

Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Activated with catalytic amounts of streptokinase.

Subunit structure

Interacts with AMOT and CSPG4 (also true for angiostatin). Ref.23 Ref.24

Subcellular location

Secreted.

Tissue specificity

Present in plasma and many other extracellular fluids. It is synthesized in the liver.

Domain

Kringle domains mediate interaction with CSPG4. Ref.23

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

Defects in PLG are a cause of thrombophilia [MIM:188050]; a form of recurrent thrombosis. Ref.43 Ref.45 Ref.46 Ref.47 Ref.48

Defects in PLG may be associated with ligneous conjunctivitis [MIM:217090]. Ligneous conjunctivitis is an unusual and rare form of chronic conjunctivitis, characterized by chronic tearing and redness of the conjunctivae. Initially, pseudomembranes form on the palpebral surfaces which then progress to thick nodular masses that replace the normal mucosa. Because the pseudomembranes have a woodlike consistency, the disease is termed "ligneous" conjunctivitis. The disease may be associated with pseudomembranous lesions of other mucous membranes in the mouth, nasopharynx, trachea, and female genital tract.

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.

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Ontologies

Keywords
   Biological processBlood coagulation
Fibrinolysis
Tissue remodeling
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Thrombophilia
   DomainKringle
Repeat
Signal
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processblood coagulation Ref.43

Inferred from mutant phenotype. Source: HGNC

fibrinolysis

Inferred from electronic annotation. Source: UniProtKB-KW

induction of apoptosis

Traceable author statement. Source: HGNC

negative regulation of angiogenesis

Traceable author statement. Source: HGNC

negative regulation of blood vessel endothelial cell migration

Traceable author statement. Source: HGNC

negative regulation of cell proliferation

Traceable author statement. Source: ProtInc

negative regulation of fibrinolysis

Inferred from direct assay. Source: UniProtKB

positive regulation of fibrinolysis

Inferred from direct assay. Source: UniProtKB

tissue remodeling

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular space Ref.46

Inferred from direct assay. Source: HGNC

   Molecular functionapolipoprotein binding

Inferred from physical interaction. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

serine-type endopeptidase activity Ref.1 Ref.49

Inferred from Experiment. Source: Reactome

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q6V4K91EBI-999394,EBI-984399From a different organism.
Q6V4L12EBI-999394,EBI-984250From a different organism.
Q6V4L42EBI-999394,EBI-984286From a different organism.
Q6V4L52EBI-999394,EBI-984118From a different organism.
Q6V4L92EBI-999394,EBI-984197From a different organism.
skcP007791EBI-999394,EBI-1035089From a different organism.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.7 Ref.8
Chain20 – 810791Plasminogen
PRO_0000028053
Chain20 – 580561Plasmin heavy chain A
PRO_0000028054
Peptide20 – 9778Activation peptide
PRO_0000028055
Chain79 – 466388Angiostatin
PRO_0000028057
Chain98 – 580483Plasmin heavy chain A, short form
PRO_0000028056
Chain581 – 810230Plasmin light chain B
PRO_0000028058

Regions

Domain20 – 9879PAN
Domain103 – 18179Kringle 1
Domain184 – 26279Kringle 2
Domain275 – 35278Kringle 3
Domain377 – 45478Kringle 4
Domain481 – 56080Kringle 5
Domain581 – 808228Peptidase S1

Sites

Active site6221Charge relay system Ref.13 Ref.14
Active site6651Charge relay system Ref.13 Ref.14
Active site7601Charge relay system Ref.13 Ref.14
Binding site1341Fibrin
Binding site1361Fibrin
Binding site1361Omega-aminocarboxylic acids
Binding site1581Omega-aminocarboxylic acids
Binding site1721Omega-aminocarboxylic acids
Binding site4321Omega-aminocarboxylic acids
Binding site4451Omega-aminocarboxylic acids
Site78 – 792Cleavage; by stromelysin-1
Site466 – 4672Cleavage; by stromelysin-19
Site580 – 5812Cleavage; by plasminogen activator

Amino acid modifications

Modified residue5971Phosphoserine Ref.17
Glycosylation2681O-linked (GalNAc...) Ref.19
CAR_000016
Glycosylation3081N-linked (GlcNAc...) Ref.25
CAR_000017
Glycosylation3651O-linked (GalNAc...)
CAR_000018
Disulfide bond49 ↔ 73 Ref.31 Ref.33 Ref.35
Disulfide bond53 ↔ 61 Ref.31 Ref.33 Ref.35
Disulfide bond103 ↔ 181 Ref.31 Ref.33 Ref.35
Disulfide bond124 ↔ 164 Ref.31 Ref.33 Ref.35
Disulfide bond152 ↔ 176 Ref.31 Ref.33 Ref.35
Disulfide bond185 ↔ 262 Ref.31 Ref.33 Ref.35
Disulfide bond188 ↔ 316 Ref.31 Ref.33 Ref.35
Disulfide bond206 ↔ 245 Ref.31 Ref.33 Ref.35
Disulfide bond234 ↔ 257 Ref.31 Ref.33 Ref.35
Disulfide bond275 ↔ 352 Ref.31 Ref.33 Ref.35
Disulfide bond296 ↔ 335 Ref.31 Ref.33 Ref.35
Disulfide bond324 ↔ 347 Ref.31 Ref.33 Ref.35
Disulfide bond377 ↔ 454 Ref.31 Ref.33 Ref.35
Disulfide bond398 ↔ 437 Ref.31 Ref.33 Ref.35
Disulfide bond426 ↔ 449 Ref.31 Ref.33 Ref.35
Disulfide bond481 ↔ 560 Ref.31 Ref.33 Ref.35
Disulfide bond502 ↔ 543 Ref.31 Ref.33 Ref.35
Disulfide bond531 ↔ 555 Ref.31 Ref.33 Ref.35
Disulfide bond567 ↔ 685Interchain (between A and B chains) Ref.31 Ref.33 Ref.35
Disulfide bond577 ↔ 585Interchain (between A and B chains) Ref.31 Ref.33 Ref.35
Disulfide bond607 ↔ 623 Ref.31 Ref.33 Ref.35
Disulfide bond699 ↔ 766 Ref.31 Ref.33 Ref.35
Disulfide bond729 ↔ 745 Ref.31 Ref.33 Ref.35
Disulfide bond756 ↔ 784 Ref.31 Ref.33 Ref.35

Natural variations

Natural variant381K → E in ligneous conjonctivitis. Ref.51
VAR_018657
Natural variant461I → R: dbSNP rs1049573.
VAR_011779
Natural variant571E → K: dbSNP rs4252070. Ref.4
VAR_016287
Natural variant1331H → Q: dbSNP rs4252186. Ref.4
VAR_016288
Natural variant1341R → K: dbSNP rs2817.
VAR_033653
Natural variant1471L → P in ligneous conjonctivitis. Ref.51
VAR_018658
Natural variant2351R → H in ligneous conjunctivitis. Ref.49
VAR_018659
Natural variant2611R → H: dbSNP rs4252187. Ref.4
VAR_016289
Natural variant3741V → F in thrombophilia; Nagoya-1. Ref.43
VAR_006627
Natural variant4081R → W: dbSNP rs4252119. Ref.4
VAR_016290
Natural variant4531K → I: dbSNP rs1804181.
VAR_011780
Natural variant4721D → N: dbSNP rs4252125. Ref.7 Ref.4 Ref.1 Ref.9
VAR_016291
Natural variant4941A → V: dbSNP rs4252128. Ref.4
VAR_016292
Natural variant5231R → W: dbSNP rs4252129. Ref.4
VAR_016293
Natural variant5321R → H in ligneous conjonctivitis. Ref.51
VAR_018660
Natural variant5911S → P in thrombophilia. Ref.45
VAR_006628
Natural variant6201A → T in thrombophilia; inactive; Nagoya-2/Tochigi/Kagoshima. Ref.43 Ref.46 Ref.47 Ref.48
VAR_006629
Natural variant6761V → D: dbSNP rs17857492. Ref.6
VAR_031213
Natural variant7511G → R in Kanagawa-1; 50% activity. Ref.50
VAR_006630

Experimental info

Sequence conflict501A → AQ AA sequence Ref.8
Sequence conflict721Q → E AA sequence Ref.7
Sequence conflict721Q → E AA sequence Ref.8
Sequence conflict861Missing AA sequence Ref.7
Sequence conflict861Missing AA sequence Ref.8
Sequence conflict3611Q → E AA sequence Ref.7
Sequence conflict3611Q → E AA sequence Ref.9
Sequence conflict7011I → V in AAA36451. Ref.3

Secondary structure

1 ............................................................................................. 810
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00747-1 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 8B31CB877CCB3AB6

FASTA81090,569
        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

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References

« Hide '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: 2318848] [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: 3030813] [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. expand/collapse author list , 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: 14574404] [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: 15489334] [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: 122932] [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: 6148961] [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: 126863] [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: 142009] [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: 4694729] [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: 4240117] [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: 6919539] [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: 6094526] [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: 9201958] [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: 3356193] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
[19]"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: 9054441] [Abstract]
Cited for: GLYCOSYLATION AT SER-268.
[20]"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: 7525077] [Abstract]
Cited for: CHARACTERIZATION OF ANGIOSTATIN, PARTIAL PROTEIN SEQUENCE.
[21]"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: 9102221] [Abstract]
Cited for: CHARACTERIZATION OF ANGIOSTATIN.
[22]"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: 9548733] [Abstract]
Cited for: PROTEOLYTIC CLEAVAGE.
[23]"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: 10889192] [Abstract]
Cited for: INTERACTION WITH CSPG4, DOMAIN.
[24]"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: 16043488] [Abstract]
Cited for: INTERACTION WITH AMOT.
[25]"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: 18780401] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308, MASS SPECTROMETRY.
Tissue: Milk.
[26]"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: 1657148] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 374-461.
[27]"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: 1657149] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 374-461.
[28]"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: 8054447] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 101-181.
[29]"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: 8611560] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 102-181.
[30]"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: 15299951] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 376-454.
[31]"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: 9783753] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 561-810, DISULFIDE BONDS.
[32]"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: 9521645] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 480-563.
[33]"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: 10656799] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 564-810, DISULFIDE BONDS.
[34]"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: 11350170] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 183-262.
[35]"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: 12054798] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 100-352, DISULFIDE BONDS.
[36]"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: 12456874] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 562-810.
[37]"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: 15211511] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 564-810.
[38]"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: 2157850] [Abstract]
Cited for: STRUCTURE BY NMR OF 374-461.
[39]"1H-NMR assignments and secondary structure of human plasminogen kringle 1."
Rejante M.R., Llinas M.
Eur. J. Biochem. 221:927-937(1994) [PubMed: 8181475] [Abstract]
Cited for: STRUCTURE BY NMR OF 96-184.
[40]"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: 8181476] [Abstract]
Cited for: STRUCTURE BY NMR OF 96-184.
[41]"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: 8652577] [Abstract]
Cited for: STRUCTURE BY NMR OF 183-354.
[42]"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: 9305949] [Abstract]
Cited for: STRUCTURE BY NMR OF 183-263.
[43]"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: 1986355] [Abstract]
Cited for: VARIANTS THROMBOPHILIA PHE-374 AND THR-620.
[44]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)
[45]"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: 8392398] [Abstract]
Cited for: VARIANT THROMBOPHILIA PRO-591.
[46]"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: 6216475] [Abstract]
Cited for: VARIANT THROMBOPHILIA THR-620.
[47]"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: 6238949] [Abstract]
Cited for: VARIANT THROMBOPHILIA THR-620.
[48]"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: 1427790] [Abstract]
Cited for: VARIANT THROMBOPHILIA THR-620.
[49]"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: 9242524] [Abstract]
Cited for: VARIANT LIGNEOUS CONJUNCTIVITIS HIS-235.
[50]"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: 9858247] [Abstract]
Cited for: VARIANT KANAGAWA-1 ARG-751.
[51]"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: 10233898] [Abstract]
Cited for: VARIANTS LIGNEOUS CONJONCTIVITIS GLU-38; PRO-147 AND HIS-532.
+Additional computationally mapped references.

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Web resources

Wikipedia

Plasmin entry

SeattleSNPs

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M34276 expand/collapse EMBL AC list , 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.
IPIIPI00019580.
PIRPLHU. A35229.
RefSeqNP_000292.1.
UniGeneHs.143436

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B2INMR-A183-263[»]
1BMLX-ray2.90A/B561-810[»]
1BUIX-ray2.65A/B561-810[»]
1CEAX-ray2.06A/B100-187[»]
1CEBX-ray2.07A/B100-187[»]
1DDJX-ray2.00A/B/C/D564-810[»]
1HPJNMR-A103-181[»]
1HPKNMR-A103-181[»]
1I5KX-ray2.70A/B183-262[»]
1KI0X-ray1.75A100-352[»]
1KRNX-ray1.67A374-461[»]
1L4DX-ray2.30A562-810[»]
1L4ZX-ray2.80A563-810[»]
1PK4X-ray1.90A376-454[»]
1PKRX-ray2.48A101-181[»]
1PMKX-ray2.25A/B374-461[»]
1QRZX-ray2.00A/B/C/D565-810[»]
1RJXX-ray2.30B564-810[»]
2DOHX-ray2.30X100-333[»]
2DOIX-ray3.10A/X100-333[»]
2KNFNMR-A480-562[»]
2PK4X-ray2.25A375-454[»]
5HPGX-ray1.66A/B480-563[»]
SMRP00747. Positions 19-184, 310-459, 458-809.
DisProtDP00191.
ModBaseSearch...

Protein-protein interaction databases

IntActP00747. 9 interactions.
STRINGP00747.

Protein family/group databases

MEROPSS01.233.

PTM databases

GlycoSuiteDBP00747.
PhosphoSiteP00747.

2-D gel databases

SWISS-2DPAGEP00747.

Proteomic databases

PeptideAtlasP00747.
PRIDEP00747.

Genome annotation databases

EnsemblENST00000308192; ENSP00000308938; ENSG00000122194; Homo sapiens. [Genome view]
GeneID5340.
KEGGhsa:5340.
UCSCuc003qtm.2. human.

Organism-specific databases

CTD5340.
GeneCardsGC06P161093.
H-InvDBHIX0032909.
HGNCHGNC:9071. PLG.
HPACAB000668.
CAB016678.
HPA021602.
MIM173350. gene+phenotype.
188050. phenotype.
217090. phenotype.
Orphanet722. Hypoplasminogenemia.
97231. Ligneous conjunctivitis.
PharmGKBPA33405.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG15519.
HOGENOMHBG755338.
HOVERGENP00747.
InParanoidP00747.
OMAENKVCNR.
OrthoDBEOG9C2KVW.
PhylomeDBP00747.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12950.
BRENDA3.4.21.7. 247.
Pathway_Interaction_DBamb2_neutrophils_pathway. amb2 Integrin signaling.
p75ntrpathway. p75(NTR)-mediated signaling.
syndecan_4_pathway. Syndecan-4-mediated signaling events.
ReactomeREACT_15380. Diabetes pathways.
REACT_16888. Signaling by PDGF.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP00747.
BgeeP00747.
CleanExHS_PLG.
GenevestigatorP00747.
GermOnlineENSG00000122194. Homo sapiens.

Family and domain databases

InterProIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR011358. Pept_S1A_Plasmin.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR003966. Peptidase_S1A_prothrombin.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 5 hits.
PfamPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001150. Plasmin. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00018. KRINGLE.
PR01505. PROTHROMBIN.
SMARTSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS00021. 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]
ProtoNetSearch...

Other Resources

DrugBankDB00513. Aminocaproic Acid.
DB00086. Streptokinase.
DB00302. Tranexamic Acid.
DB00013. Urokinase.
NextBio20698.
PMAP-CutDBP00747.
SOURCESearch...

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Entry information

Entry namePLMN_HUMAN
AccessionPrimary (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: January 19, 2010
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents