endopeptidase inhibitor activity

endopeptidase inhibitor activity

Item
http://www.wikidata.org/entity/Q14861841
Serine (or cysteine) peptidase inhibitor, clade A, member 1AComplement component 3Hemolytic complementCST3Cystatin CPregnancy zone proteinSecretory leukocyte peptidase inhibitorProteasome inhibitor subunit 1Complement C4A (Rodgers blood group)Complement component 4B (Chido blood group), copy 2Cystatin FSerine peptidase inhibitor Kazal type 2Cystatin ACystatin BPutative protein C3P1Ubiquitin C-terminal hydrolase L5Reversion inducing cysteine rich protein with kazal motifsApolipoprotein(a)Serine peptidase inhibitor Kazal type 1Alpha-2-macroglobulin like 1C3 and PZP like alpha-2-macroglobulin domain containing 8Serine peptidase inhibitor, Kunitz type 2Inter-alpha-trypsin inhibitor heavy chain 2Inter-alpha-trypsin inhibitor heavy chain 3Secreted phosphoprotein 2Submaxillary gland androgen regulated protein 3BSubmaxillary gland androgen regulated protein 3AUbiquitin specific peptidase 14CD109 moleculeCalpastatinProprotein convertase subtilisin/kexin type 1 inhibitorInter-alpha-trypsin inhibitor heavy chain 4Ovostatin homolog 2WAP four-disulfide core domain 2Alpha-2-macroglobulin-like protein 1Alpha 2-HS glycoproteinPregnancy zone proteinOpiorphin prepropeptideStefin A3Stefin A2
P680
Human inter-alpha-trypsin inhibitor heavy chain H3 gene. Genomic organization, promoter analysis, and gene linkageCloning a synthetic gene for human stefin B and its expression in E. coliThe alpha-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian alpha-macroglobulinsAnalysis of inter-alpha-trypsin inhibitor and a novel trypsin inhibitor, pre-alpha-trypsin inhibitor, from human plasma. Polypeptide chain stoichiometry and assembly by glycanPurification and characterization of a tumor-associated trypsin inhibitor from the urine of a patient with ovarian cancerLeukocystatin, a new Class II cystatin expressed selectively by hematopoietic cellsIsolation and molecular cloning of a novel bone phosphoprotein related in sequence to the cystatin family of thiol protease inhibitorsProtein S binds to and inhibits factor XaIdentification and cloning of human placental bikunin, a novel serine protease inhibitor containing two Kunitz domainsElafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequenceOrganization and sequence of the gene encoding the human acrosin-trypsin inhibitor (HUSI-II)Autoantibodies to calpastatin (an endogenous inhibitor for calcium-dependent neutral protease, calpain) in systemic rheumatic diseasesHeparin cofactor IIOslo. Mutation of Arg-189 to His decreases the affinity for dermatan sulfateHuman plasma inter-alpha-trypsin inhibitor is encoded by four genes on three chromosomesStructure of human alpha 2-plasmin inhibitor deduced from the cDNA sequence
P921
Q14861844-942473E5-B61B-45A3-988A-0D55B0C78BD6Q14874319-33997FE1-BB6E-451B-832F-C75B09F71E52Q14905308-6187C9E0-C12D-4A3F-80B0-A231BD048D8AQ14913588-926B5BE6-CCB1-438F-BA1B-71A3E8B76F1EQ14913600-084416A7-6CC7-47B5-B10A-9FBF9BC8805CQ14913600-A6AB3351-ED76-4997-B931-4680B6A18A69Q15997057-5DAC9F53-FD90-48B5-A5A8-8DB25C0D0C0DQ15997057-9C4AF66C-F5D5-4676-A290-20516A633CA0Q21101249-663D6A8B-031A-474D-80C0-30C3C5EAEEBCQ21101249-6FEDA21F-9A30-449C-B9F1-BC2B6E70F378Q21101367-9B8598DA-9B8C-42DF-BE3B-081AC8EB3C7FQ21102477-D37636F7-A743-4868-9007-109BE4FA2D9CQ21102479-A6A79C7F-5B67-4868-893C-778AEF99761EQ21105609-5C964586-AE1C-4469-BACA-874834D3544BQ21106570-EEC44B16-134D-4DAD-AB99-DDB8E80554A5Q21109999-569545E5-E43D-4720-9D1D-33075C0289E4Q21110000-9B5ED4FD-A7A1-4189-9D98-AA91EC0CBF75Q21110516-A49C4686-F94D-49BF-BC9D-EBA986F23EEFQ21111236-FC0F5709-AB91-4F77-9B5A-226CF91CFCB1Q21112326-C5F75461-DBDF-4087-84CC-21C98540CE92Q21112326-F10957E5-3768-4221-A919-F860DB35A922Q21112670-DA167843-EA97-4FD7-A637-CE610F95CFA8Q21114753-9DB67AE8-057E-488A-9AA8-7220BA71EF29Q21115074-86A4834F-43B0-47C5-B70A-E6AC8C93F1A5Q21115702-CF70924E-9B1C-4CDA-BA7F-70268D837859Q21117803-29736C51-6292-40C4-ABC7-DB1AEB634900Q21121468-48B603E2-1FED-45FF-BB8F-D01DCC44F760Q21121473-5C6751A3-5CD2-4F29-90B4-F610070D6734Q21122088-CF288E60-1B50-4B10-A22F-1C96F5A8CB08Q21123427-1A9AD60A-5849-4369-B9F4-59723AC88648Q21123435-F07127C5-EE7D-4C54-95F8-F30EAE0FDEFCQ21126856-0AAD49D1-9B81-43CC-ACE9-22A9360B4F8BQ21132174-139DDDF9-46BE-4B37-88FC-30310D8BA038Q21133155-40817FD5-05BB-409F-8A24-2EE5D980A09AQ21133341-756794B5-DD59-494E-BB49-24DE7A0692FEQ21133341-8C37EEFB-4F32-4127-8230-752F36EAA22FQ21133646-A2A11FD9-DA1E-4ECC-B25C-F0F71EB66068Q21133871-7A36973B-5524-4ADC-B4D2-BBB9E49EEB59Q21136674-65F6650B-9CC5-4AE1-BE14-E78DB25057C7Q21152284-00140114-4330-4CF7-A0FE-8B511C98E807
P680

endopeptidase inhibitor activity

Item
http://www.wikidata.org/entity/Q14861841
description
Stops, prevents or reduces the ...... peptide bonds in polypeptides.
@en
biologisch proces
@nl
name
endopeptidase inhibitor activity
@en
type
label
endopeptidase inhibitor activity
@en
altLabel
GO:0004866
@en
prefLabel
endopeptidase inhibitor activity
@en
P128
P279
P2888
P31
P361
P686
P128
P279
P2888
P31
P361
P686