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P00747

- PLMN_HUMAN

UniProt

P00747 - PLMN_HUMAN

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Protein

Plasminogen

Gene

PLG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication
Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.1 Publication

Catalytic activityi

Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.1 Publication

Enzyme regulationi

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 SERPINE2.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei78 – 792Cleavage; by stromelysin-1
Binding sitei134 – 1341Fibrin
Binding sitei136 – 1361Fibrin
Binding sitei136 – 1361Omega-aminocarboxylic acids
Binding sitei158 – 1581Omega-aminocarboxylic acids
Binding sitei172 – 1721Omega-aminocarboxylic acids
Binding sitei432 – 4321Omega-aminocarboxylic acids
Binding sitei445 – 4451Omega-aminocarboxylic acids
Sitei466 – 4672Cleavage; by stromelysin-19
Sitei580 – 5812Cleavage; by plasminogen activator
Active sitei622 – 6221Charge relay system
Active sitei665 – 6651Charge relay system
Active sitei760 – 7601Charge relay system

GO - Molecular functioni

  1. apolipoprotein binding Source: BHF-UCL
  2. protein domain specific binding Source: UniProtKB
  3. serine-type endopeptidase activity Source: BHF-UCL
  4. serine-type peptidase activity Source: AgBase

GO - Biological processi

  1. blood coagulation Source: HGNC
  2. cellular protein metabolic process Source: Reactome
  3. extracellular matrix disassembly Source: BHF-UCL
  4. extracellular matrix organization Source: Reactome
  5. fibrinolysis Source: Reactome
  6. negative regulation of cell-cell adhesion mediated by cadherin Source: BHF-UCL
  7. negative regulation of cell proliferation Source: ProtInc
  8. negative regulation of cell-substrate adhesion Source: BHF-UCL
  9. negative regulation of fibrinolysis Source: BHF-UCL
  10. platelet activation Source: Reactome
  11. platelet degranulation Source: Reactome
  12. positive regulation of fibrinolysis Source: BHF-UCL
  13. tissue remodeling Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis, Tissue remodeling

Enzyme and pathway databases

BioCyciMetaCyc:HS04553-MONOMER.
ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_16888. Signaling by PDGF.
REACT_641. Dissolution of Fibrin Clot.
SABIO-RKP00747.

Protein family/group databases

MEROPSiS01.233.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:PLG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9071. PLG.

Subcellular locationi

Secreted 2 Publications
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.

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. cell surface Source: BHF-UCL
  3. extracellular region Source: Reactome
  4. extracellular space Source: BHF-UCL
  5. extracellular vesicular exosome Source: UniProtKB
  6. extrinsic component of external side of plasma membrane Source: BHF-UCL
  7. plasma membrane Source: Reactome
  8. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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.8 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381K → E in PLGD; common mutation. 1 Publication
Corresponds to variant rs73015965 [ dbSNP | Ensembl ].
VAR_018657
Natural varianti147 – 1471L → P in PLGD. 1 Publication
VAR_018658
Natural varianti235 – 2351R → H in PLGD; severe type 1 deficiency. 1 Publication
VAR_018659
Natural varianti374 – 3741V → F in PLGD; Nagoya-1. 1 Publication
Corresponds to variant rs121918028 [ dbSNP | Ensembl ].
VAR_006627
Natural varianti532 – 5321R → H in PLGD. 1 Publication
VAR_018660
Natural varianti591 – 5911S → P in PLGD; may be associated with susceptibility to thrombosis. 1 Publication
VAR_006628
Natural varianti620 – 6201A → T in PLGD; type 2 plasminogen deficiency; decreased activity; Nagoya-2/Tochigi/Kagoshima; may be associated with susceptibility to thrombosis. 4 Publications
Corresponds to variant rs121918027 [ dbSNP | Ensembl ].
VAR_006629
Natural varianti751 – 7511G → R in PLGD; Kanagawa-1; 50% activity. 1 Publication
VAR_006630

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi741 – 7411S → A: Proteolytically cleaved, but abolishes plasmin activity and cell detachment. 1 Publication

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

MIMi217090. phenotype.
Orphaneti722. Hypoplasminogenemia.
97231. Ligneous conjunctivitis.
PharmGKBiPA33405.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19192 PublicationsAdd
BLAST
Chaini20 – 810791PlasminogenPRO_0000028053Add
BLAST
Chaini20 – 580561Plasmin heavy chain APRO_0000028054Add
BLAST
Peptidei20 – 9778Activation peptidePRO_0000028055Add
BLAST
Chaini79 – 466388AngiostatinPRO_0000028057Add
BLAST
Chaini98 – 580483Plasmin heavy chain A, short formPRO_0000028056Add
BLAST
Chaini581 – 810230Plasmin light chain BPRO_0000028058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 73
Disulfide bondi53 ↔ 61
Disulfide bondi103 ↔ 181
Disulfide bondi124 ↔ 164
Disulfide bondi152 ↔ 176
Disulfide bondi185 ↔ 262
Disulfide bondi188 ↔ 316
Disulfide bondi206 ↔ 245
Disulfide bondi234 ↔ 257
Glycosylationi268 – 2681O-linked (GalNAc...)2 PublicationsCAR_000016
Disulfide bondi275 ↔ 352
Disulfide bondi296 ↔ 335
Glycosylationi308 – 3081N-linked (GlcNAc...)2 PublicationsCAR_000017
Disulfide bondi324 ↔ 347
Glycosylationi365 – 3651O-linked (GalNAc...)1 PublicationCAR_000018
Disulfide bondi377 ↔ 454
Disulfide bondi398 ↔ 437
Disulfide bondi426 ↔ 449
Disulfide bondi481 ↔ 560
Disulfide bondi502 ↔ 543
Disulfide bondi531 ↔ 555
Disulfide bondi567 ↔ 685Interchain (between A and B chains)
Disulfide bondi577 ↔ 585Interchain (between A and B chains)
Modified residuei597 – 5971Phosphoserine1 Publication
Disulfide bondi607 ↔ 623
Disulfide bondi699 ↔ 766
Disulfide bondi729 ↔ 745
Disulfide bondi756 ↔ 784

Post-translational modificationi

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).3 Publications
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.2 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP00747.
PeptideAtlasiP00747.
PRIDEiP00747.

2D gel databases

SWISS-2DPAGEP00747.

PTM databases

PhosphoSiteiP00747.
UniCarbKBiP00747.

Miscellaneous databases

PMAP-CutDBP00747.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP00747.
CleanExiHS_PLG.
ExpressionAtlasiP00747. baseline and differential.
GenevestigatoriP00747.

Organism-specific databases

HPAiCAB000668.
CAB016678.
HPA021602.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
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.
APOHP027492EBI-999394,EBI-2114682
sakQ99SU77EBI-999394,EBI-7689378From a different organism.
skcP007792EBI-999394,EBI-1035089From a different organism.

Protein-protein interaction databases

BioGridi111356. 34 interactions.
IntActiP00747. 30 interactions.
STRINGi9606.ENSP00000308938.

Structurei

Secondary structure

1
810
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 339
Beta strandi36 – 427
Helixi46 – 5510
Beta strandi57 – 593
Beta strandi63 – 675
Turni68 – 714
Beta strandi72 – 776
Turni80 – 823
Beta strandi85 – 9612
Helixi97 – 993
Beta strandi102 – 1043
Beta strandi105 – 1106
Helixi113 – 1153
Turni119 – 1213
Beta strandi131 – 1333
Turni139 – 1413
Helixi143 – 1453
Beta strandi148 – 1503
Beta strandi155 – 1573
Beta strandi163 – 1675
Beta strandi172 – 1754
Beta strandi180 – 1823
Beta strandi184 – 1863
Beta strandi205 – 2073
Beta strandi209 – 2113
Beta strandi213 – 2153
Turni221 – 2233
Helixi225 – 2273
Beta strandi237 – 2393
Beta strandi244 – 2485
Beta strandi253 – 2564
Beta strandi273 – 2764
Beta strandi281 – 2833
Beta strandi291 – 2933
Beta strandi295 – 2973
Beta strandi303 – 3053
Turni311 – 3133
Helixi315 – 3173
Beta strandi334 – 3396
Beta strandi343 – 3464
Beta strandi377 – 3793
Beta strandi382 – 3843
Beta strandi405 – 4073
Turni413 – 4153
Turni417 – 4193
Beta strandi429 – 4313
Beta strandi436 – 4416
Beta strandi446 – 4505
Beta strandi481 – 4833
Beta strandi487 – 4893
Beta strandi509 – 5113
Beta strandi514 – 5163
Turni518 – 5203
Turni522 – 5254
Beta strandi542 – 5465
Beta strandi552 – 5543
Beta strandi582 – 5865
Beta strandi595 – 5995
Beta strandi605 – 6139
Beta strandi616 – 6194
Helixi621 – 6244
Helixi630 – 6323
Beta strandi634 – 6385
Beta strandi640 – 6445
Beta strandi650 – 65910
Turni661 – 6633
Beta strandi667 – 6737
Beta strandi698 – 7036
Beta strandi708 – 7103
Turni711 – 7144
Beta strandi717 – 7248
Helixi726 – 7294
Turni732 – 7376
Beta strandi743 – 7475
Beta strandi749 – 7513
Beta strandi752 – 7543
Beta strandi763 – 7675
Beta strandi769 – 77810
Helixi780 – 7823
Beta strandi791 – 7955
Helixi796 – 7983
Helixi800 – 8089

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B2INMR-A181-263[»]
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/B184-262[»]
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[»]
2L0SNMR-A272-354[»]
2PK4X-ray2.25A375-454[»]
3UIRX-ray2.78A/B564-810[»]
4A5TX-ray3.49S20-810[»]
4CIKX-ray1.78A101-181[»]
4DCBX-ray2.03F576-585[»]
4DURX-ray2.45A/B20-810[»]
4DUUX-ray5.20A20-810[»]
5HPGX-ray1.66A/B480-563[»]
DisProtiDP00191.
ProteinModelPortaliP00747.
SMRiP00747. Positions 20-810.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00747.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9879PANPROSITE-ProRule annotationAdd
BLAST
Domaini103 – 18179Kringle 1PROSITE-ProRule annotationAdd
BLAST
Domaini184 – 26279Kringle 2PROSITE-ProRule annotationAdd
BLAST
Domaini275 – 35278Kringle 3PROSITE-ProRule annotationAdd
BLAST
Domaini377 – 45478Kringle 4PROSITE-ProRule annotationAdd
BLAST
Domaini481 – 56080Kringle 5PROSITE-ProRule annotationAdd
BLAST
Domaini581 – 808228Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Domaini

Kringle domains mediate interaction with CSPG4.1 Publication

Sequence similaritiesi

Belongs to the peptidase S1 family. Plasminogen subfamily.PROSITE-ProRule annotation
Contains 5 kringle domains.PROSITE-ProRule annotation
Contains 1 PAN domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

GeneTreeiENSGT00760000119133.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiP00747.
KOiK01315.
OMAiEGLEENY.
OrthoDBiEOG75B84T.
PhylomeDBiP00747.
TreeFamiTF329901.

Family and domain databases

Gene3Di2.40.20.10. 5 hits.
InterProiIPR000001. 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]
PfamiPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001150. Plasmin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 5 hits.
PROSITEiPS00021. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00747-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEHKEVVLLL LLFLKSGQGE PLDDYVNTQG ASLFSVTKKQ LGAGSIEECA
60 70 80 90 100
AKCEEDEEFT CRAFQYHSKE QQCVIMAENR KSSIIIRMRD VVLFEKKVYL
110 120 130 140 150
SECKTGNGKN YRGTMSKTKN GITCQKWSST SPHRPRFSPA THPSEGLEEN
160 170 180 190 200
YCRNPDNDPQ GPWCYTTDPE KRYDYCDILE CEEECMHCSG ENYDGKISKT
210 220 230 240 250
MSGLECQAWD SQSPHAHGYI PSKFPNKNLK KNYCRNPDRE LRPWCFTTDP
260 270 280 290 300
NKRWELCDIP RCTTPPPSSG PTYQCLKGTG ENYRGNVAVT VSGHTCQHWS
310 320 330 340 350
AQTPHTHNRT PENFPCKNLD ENYCRNPDGK RAPWCHTTNS QVRWEYCKIP
360 370 380 390 400
SCDSSPVSTE QLAPTAPPEL TPVVQDCYHG DGQSYRGTSS TTTTGKKCQS
410 420 430 440 450
WSSMTPHRHQ KTPENYPNAG LTMNYCRNPD ADKGPWCFTT DPSVRWEYCN
460 470 480 490 500
LKKCSGTEAS VVAPPPVVLL PDVETPSEED CMFGNGKGYR GKRATTVTGT
510 520 530 540 550
PCQDWAAQEP HRHSIFTPET NPRAGLEKNY CRNPDGDVGG PWCYTTNPRK
560 570 580 590 600
LYDYCDVPQC AAPSFDCGKP QVEPKKCPGR VVGGCVAHPH SWPWQVSLRT
610 620 630 640 650
RFGMHFCGGT LISPEWVLTA AHCLEKSPRP SSYKVILGAH QEVNLEPHVQ
660 670 680 690 700
EIEVSRLFLE PTRKDIALLK LSSPAVITDK VIPACLPSPN YVVADRTECF
710 720 730 740 750
ITGWGETQGT FGAGLLKEAQ LPVIENKVCN RYEFLNGRVQ STELCAGHLA
760 770 780 790 800
GGTDSCQGDS GGPLVCFEKD KYILQGVTSW GLGCARPNKP GVYVRVSRFV
810
TWIEGVMRNN
Length:810
Mass (Da):90,569
Last modified:July 1, 1989 - v2
Checksum:i8B31CB877CCB3AB6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501A → AQ AA sequence (PubMed:122932)Curated
Sequence conflicti72 – 721Q → E AA sequence 1 PublicationCurated
Sequence conflicti72 – 721Q → E AA sequence (PubMed:122932)Curated
Sequence conflicti86 – 861Missing AA sequence 1 PublicationCurated
Sequence conflicti86 – 861Missing AA sequence (PubMed:122932)Curated
Sequence conflicti361 – 3611Q → E AA sequence 1 PublicationCurated
Sequence conflicti361 – 3611Q → E AA sequence 1 PublicationCurated
Sequence conflicti701 – 7011I → V in AAA36451. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381K → E in PLGD; common mutation. 1 Publication
Corresponds to variant rs73015965 [ dbSNP | Ensembl ].
VAR_018657
Natural varianti46 – 461I → R.
Corresponds to variant rs1049573 [ dbSNP | Ensembl ].
VAR_011779
Natural varianti57 – 571E → K.1 Publication
Corresponds to variant rs4252070 [ dbSNP | Ensembl ].
VAR_016287
Natural varianti133 – 1331H → Q.1 Publication
Corresponds to variant rs4252186 [ dbSNP | Ensembl ].
VAR_016288
Natural varianti134 – 1341R → K.
Corresponds to variant rs2817 [ dbSNP | Ensembl ].
VAR_033653
Natural varianti147 – 1471L → P in PLGD. 1 Publication
VAR_018658
Natural varianti235 – 2351R → H in PLGD; severe type 1 deficiency. 1 Publication
VAR_018659
Natural varianti261 – 2611R → H.1 Publication
Corresponds to variant rs4252187 [ dbSNP | Ensembl ].
VAR_016289
Natural varianti374 – 3741V → F in PLGD; Nagoya-1. 1 Publication
Corresponds to variant rs121918028 [ dbSNP | Ensembl ].
VAR_006627
Natural varianti408 – 4081R → W.1 Publication
Corresponds to variant rs4252119 [ dbSNP | Ensembl ].
VAR_016290
Natural varianti453 – 4531K → I.
Corresponds to variant rs1804181 [ dbSNP | Ensembl ].
VAR_011780
Natural varianti472 – 4721D → N.4 Publications
Corresponds to variant rs4252125 [ dbSNP | Ensembl ].
VAR_016291
Natural varianti494 – 4941A → V.1 Publication
Corresponds to variant rs4252128 [ dbSNP | Ensembl ].
VAR_016292
Natural varianti523 – 5231R → W.1 Publication
Corresponds to variant rs4252129 [ dbSNP | Ensembl ].
VAR_016293
Natural varianti532 – 5321R → H in PLGD. 1 Publication
VAR_018660
Natural varianti591 – 5911S → P in PLGD; may be associated with susceptibility to thrombosis. 1 Publication
VAR_006628
Natural varianti620 – 6201A → T in PLGD; type 2 plasminogen deficiency; decreased activity; Nagoya-2/Tochigi/Kagoshima; may be associated with susceptibility to thrombosis. 4 Publications
Corresponds to variant rs121918027 [ dbSNP | Ensembl ].
VAR_006629
Natural varianti676 – 6761V → D.1 Publication
Corresponds to variant rs17857492 [ dbSNP | Ensembl ].
VAR_031213
Natural varianti751 – 7511G → R in PLGD; Kanagawa-1; 50% activity. 1 Publication
VAR_006630

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS5279.1.
PIRiA35229. PLHU.
RefSeqiNP_000292.1. NM_000301.3.
UniGeneiHs.143436.

Genome annotation databases

EnsembliENST00000308192; ENSP00000308938; ENSG00000122194.
GeneIDi5340.
KEGGihsa:5340.
UCSCiuc003qtm.4. human.

Polymorphism databases

DMDMi130316.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Plasmin entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS5279.1.
PIRi A35229. PLHU.
RefSeqi NP_000292.1. NM_000301.3.
UniGenei Hs.143436.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B2I NMR - A 181-263 [» ]
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 184-262 [» ]
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 [» ]
4CIK X-ray 1.78 A 101-181 [» ]
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 [» ]
DisProti DP00191.
ProteinModelPortali P00747.
SMRi P00747. Positions 20-810.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111356. 34 interactions.
IntActi P00747. 30 interactions.
STRINGi 9606.ENSP00000308938.

Chemistry

BindingDBi P00747.
ChEMBLi CHEMBL1801.
DrugBanki DB00009. Alteplase.
DB00513. Aminocaproic Acid.
DB00029. Anistreplase.
DB06692. Aprotinin.
DB00015. Reteplase.
DB00086. Streptokinase.
DB00031. Tenecteplase.
DB00302. Tranexamic Acid.
DB00013. Urokinase.
GuidetoPHARMACOLOGYi 2394.

Protein family/group databases

MEROPSi S01.233.

PTM databases

PhosphoSitei P00747.
UniCarbKBi P00747.

Polymorphism databases

DMDMi 130316.

2D gel databases

SWISS-2DPAGE P00747.

Proteomic databases

MaxQBi P00747.
PeptideAtlasi P00747.
PRIDEi P00747.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308192 ; ENSP00000308938 ; ENSG00000122194 .
GeneIDi 5340.
KEGGi hsa:5340.
UCSCi uc003qtm.4. human.

Organism-specific databases

CTDi 5340.
GeneCardsi GC06P161123.
HGNCi HGNC:9071. PLG.
HPAi CAB000668.
CAB016678.
HPA021602.
MIMi 173350. gene.
217090. phenotype.
neXtProti NX_P00747.
Orphaneti 722. Hypoplasminogenemia.
97231. Ligneous conjunctivitis.
PharmGKBi PA33405.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00760000119133.
HOGENOMi HOG000112892.
HOVERGENi HBG004381.
InParanoidi P00747.
KOi K01315.
OMAi EGLEENY.
OrthoDBi EOG75B84T.
PhylomeDBi P00747.
TreeFami TF329901.

Enzyme and pathway databases

BioCyci MetaCyc:HS04553-MONOMER.
Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_16888. Signaling by PDGF.
REACT_641. Dissolution of Fibrin Clot.
SABIO-RK P00747.

Miscellaneous databases

EvolutionaryTracei P00747.
GeneWikii Plasmin.
Plasminogen_activator.
GenomeRNAii 5340.
NextBioi 20698.
PMAP-CutDB P00747.
PROi P00747.
SOURCEi Search...

Gene expression databases

Bgeei P00747.
CleanExi HS_PLG.
ExpressionAtlasi P00747. baseline and differential.
Genevestigatori P00747.

Family and domain databases

Gene3Di 2.40.20.10. 5 hits.
InterProi 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 ]
Pfami PF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001150. Plasmin. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 5 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: GLYCOSYLATION AT SER-268; ASN-308 AND THR-365, 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. 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.
    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. "The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake."
    Millers E.K., Johnson L.A., Birrell G.W., Masci P.P., Lavin M.F., de Jersey J., Guddat L.W.
    PLoS ONE 8:E54104-E54104(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 564-810 IN COMPLEX WITH THE SNAKE VENOM PROTEASE INHIBITOR TEXTILININ-1, DISULFIDE BOND.
  44. "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.
  45. "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.
  46. "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.
  47. "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.
  48. "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.
  49. "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.
  50. 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)
  51. "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.
  52. "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.
  53. "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.
  54. "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.
  55. "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.
  56. "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.
  57. "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.

Entry informationi

Entry nameiPLMN_HUMAN
AccessioniPrimary (citable) accession number: P00747
Secondary accession number(s): Q15146, Q5TEH4, Q6PA00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 195 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3