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P00747 (PLMN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 192. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.49 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57

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 processBlood coagulation
Fibrinolysis
Hemostasis
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
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from mutant phenotype Ref.49. Source: HGNC

cellular protein metabolic process

Traceable author statement. Source: Reactome

extracellular matrix disassembly

Inferred from direct assay Ref.26. Source: BHF-UCL

extracellular matrix organization

Traceable author statement. Source: Reactome

fibrinolysis

Traceable author statement. Source: Reactome

labyrinthine layer blood vessel development

Inferred from electronic annotation. Source: Ensembl

mononuclear cell migration

Inferred from electronic annotation. Source: Ensembl

muscle cell cellular homeostasis

Inferred from electronic annotation. Source: Ensembl

myoblast differentiation

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

tissue regeneration

Inferred from electronic annotation. Source: Ensembl

tissue remodeling

Inferred from electronic annotation. Source: UniProtKB-KW

trophoblast giant cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cell surface

Inferred from direct assay Ref.26. Source: BHF-UCL

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 6980881. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 23376485. Source: UniProt

extrinsic component of external side of plasma membrane

Inferred from direct assay Ref.26. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionapolipoprotein binding

Inferred from physical interaction PubMed 16480936. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.30Ref.19. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 9786936. Source: UniProtKB

serine-type endopeptidase activity

Inferred from direct assay Ref.26. Source: BHF-UCL

serine-type peptidase activity

Traceable author statement PubMed 24263861. Source: AgBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.
sakQ99SU77EBI-999394,EBI-7689378From a different organism.
skcP007792EBI-999394,EBI-1035089From a different organism.

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.18 Ref.20
CAR_000016
Glycosylation3081N-linked (GlcNAc...) Ref.18 Ref.28
CAR_000017
Glycosylation3651O-linked (GalNAc...) Ref.18
CAR_000018
Disulfide bond49 ↔ 73 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond53 ↔ 61 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond103 ↔ 181 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond124 ↔ 164 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond152 ↔ 176 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond185 ↔ 262 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond188 ↔ 316 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond206 ↔ 245 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond234 ↔ 257 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond275 ↔ 352 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond296 ↔ 335 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond324 ↔ 347 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond377 ↔ 454 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond398 ↔ 437 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond426 ↔ 449 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond481 ↔ 560 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond502 ↔ 543 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond531 ↔ 555 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond567 ↔ 685Interchain (between A and B chains) Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond577 ↔ 585Interchain (between A and B chains) Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond607 ↔ 623 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond699 ↔ 766 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond729 ↔ 745 Ref.36 Ref.38 Ref.40 Ref.43
Disulfide bond756 ↔ 784 Ref.36 Ref.38 Ref.40 Ref.43

Natural variations

Natural variant381K → E in PLGD; common mutation. Ref.57
Corresponds to variant rs73015965 [ dbSNP | Ensembl ].
VAR_018657
Natural variant461I → R.
Corresponds to variant rs1049573 [ dbSNP | Ensembl ].
VAR_011779
Natural variant571E → K. Ref.4
Corresponds to variant rs4252070 [ dbSNP | Ensembl ].
VAR_016287
Natural variant1331H → Q. Ref.4
Corresponds to variant rs4252186 [ dbSNP | Ensembl ].
VAR_016288
Natural variant1341R → K.
Corresponds to variant rs2817 [ dbSNP | Ensembl ].
VAR_033653
Natural variant1471L → P in PLGD. Ref.57
VAR_018658
Natural variant2351R → H in PLGD; severe type 1 deficiency. Ref.55
VAR_018659
Natural variant2611R → H. Ref.4
Corresponds to variant rs4252187 [ dbSNP | Ensembl ].
VAR_016289
Natural variant3741V → F in PLGD; Nagoya-1. Ref.49
Corresponds to variant rs121918028 [ dbSNP | Ensembl ].
VAR_006627
Natural variant4081R → W. Ref.4
Corresponds to variant rs4252119 [ dbSNP | Ensembl ].
VAR_016290
Natural variant4531K → I.
Corresponds to variant rs1804181 [ dbSNP | Ensembl ].
VAR_011780
Natural variant4721D → N. Ref.1 Ref.4 Ref.7 Ref.9
Corresponds to variant rs4252125 [ dbSNP | Ensembl ].
VAR_016291
Natural variant4941A → V. Ref.4
Corresponds to variant rs4252128 [ dbSNP | Ensembl ].
VAR_016292
Natural variant5231R → W. Ref.4
Corresponds to variant rs4252129 [ dbSNP | Ensembl ].
VAR_016293
Natural variant5321R → H in PLGD. Ref.57
VAR_018660
Natural variant5911S → P in PLGD; may be associated with susceptibility to thrombosis. Ref.51
VAR_006628
Natural variant6201A → T in PLGD; type 2 plasminogen deficiency; decreased activity; Nagoya-2/Tochigi/Kagoshima; may be associated with susceptibility to thrombosis. Ref.49 Ref.52 Ref.53 Ref.54
Corresponds to variant rs121918027 [ dbSNP | Ensembl ].
VAR_006629
Natural variant6761V → D. Ref.6
Corresponds to variant rs17857492 [ dbSNP | Ensembl ].
VAR_031213
Natural variant7511G → R in PLGD; Kanagawa-1; 50% activity. Ref.56
VAR_006630

Experimental info

Mutagenesis7411S → A: Proteolytically cleaved, but abolishes plasmin activity and cell detachment. Ref.26
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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00747 [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 

« Hide

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] [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. 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] [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]"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.
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.
+Additional computationally mapped references.

Web resources

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.
CCDSCCDS5279.1.
PIRPLHU. A35229.
RefSeqNP_000292.1. NM_000301.3.
UniGeneHs.143436.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
4DCBX-ray2.03F576-585[»]
4DURX-ray2.45A/B20-810[»]
4DUUX-ray5.20A20-810[»]
5HPGX-ray1.66A/B480-563[»]
DisProtDP00191.
ProteinModelPortalP00747.
SMRP00747. Positions 20-810.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111356. 34 interactions.
IntActP00747. 29 interactions.
STRING9606.ENSP00000308938.

Chemistry

BindingDBP00747.
ChEMBLCHEMBL1801.
DrugBankDB00513. Aminocaproic Acid.
DB00086. Streptokinase.
DB00302. Tranexamic Acid.
DB00013. Urokinase.
GuidetoPHARMACOLOGY2394.

Protein family/group databases

MEROPSS01.233.

PTM databases

PhosphoSiteP00747.
UniCarbKBP00747.

Polymorphism databases

DMDM130316.

2D gel databases

SWISS-2DPAGEP00747.

Proteomic databases

MaxQBP00747.
PeptideAtlasP00747.
PRIDEP00747.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308192; ENSP00000308938; ENSG00000122194.
GeneID5340.
KEGGhsa:5340.
UCSCuc003qtm.4. human.

Organism-specific databases

CTD5340.
GeneCardsGC06P161123.
HGNCHGNC:9071. PLG.
HPACAB000668.
CAB016678.
HPA021602.
MIM173350. gene.
217090. phenotype.
neXtProtNX_P00747.
Orphanet722. Hypoplasminogenemia.
97231. Ligneous conjunctivitis.
PharmGKBPA33405.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000112892.
HOVERGENHBG004381.
InParanoidP00747.
KOK01315.
OMAEGLEENY.
OrthoDBEOG75B84T.
PhylomeDBP00747.
TreeFamTF329901.

Enzyme and pathway databases

BioCycMetaCyc:HS04553-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
SABIO-RKP00747.

Gene expression databases

ArrayExpressP00747.
BgeeP00747.
CleanExHS_PLG.
GenevestigatorP00747.

Family and domain databases

Gene3D2.40.20.10. 5 hits.
InterProIPR000001. 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]
PfamPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001150. Plasmin. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 5 hits.
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

EvolutionaryTraceP00747.
GeneWikiPlasmin.
Plasminogen_activator.
GenomeRNAi5340.
NextBio20698.
PMAP-CutDBP00747.
PROP00747.
SOURCESearch...

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: July 9, 2014
This is version 192 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

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