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P08697

- A2AP_HUMAN

UniProt

P08697 - A2AP_HUMAN

Protein

Alpha-2-antiplasmin

Gene

SERPINF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 3 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei403 – 4042Reactive bond for plasmin
    Sitei404 – 4052Reactive bond for chymotrypsin

    GO - Molecular functioni

    1. endopeptidase inhibitor activity Source: ProtInc
    2. protease binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: BHF-UCL
    5. serine-type endopeptidase inhibitor activity Source: UniProtKB

    GO - Biological processi

    1. acute-phase response Source: UniProtKB-KW
    2. blood coagulation Source: Reactome
    3. blood vessel morphogenesis Source: BHF-UCL
    4. collagen fibril organization Source: BHF-UCL
    5. fibrinolysis Source: Reactome
    6. negative regulation of endopeptidase activity Source: RefGenome
    7. negative regulation of fibrinolysis Source: BHF-UCL
    8. negative regulation of plasminogen activation Source: BHF-UCL
    9. platelet activation Source: Reactome
    10. platelet degranulation Source: Reactome
    11. positive regulation of cell-cell adhesion mediated by cadherin Source: BHF-UCL
    12. positive regulation of cell differentiation Source: BHF-UCL
    13. positive regulation of collagen biosynthetic process Source: BHF-UCL
    14. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    15. positive regulation of JNK cascade Source: BHF-UCL
    16. positive regulation of smooth muscle cell proliferation Source: BHF-UCL
    17. positive regulation of stress fiber assembly Source: BHF-UCL
    18. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    19. positive regulation of transforming growth factor beta production Source: BHF-UCL
    20. regulation of blood vessel size by renin-angiotensin Source: BHF-UCL
    21. regulation of proteolysis Source: RefGenome
    22. response to organic substance Source: Ensembl

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Keywords - Biological processi

    Acute phase

    Enzyme and pathway databases

    ReactomeiREACT_641. Dissolution of Fibrin Clot.

    Protein family/group databases

    MEROPSiI04.023.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-2-antiplasmin
    Short name:
    Alpha-2-AP
    Alternative name(s):
    Alpha-2-plasmin inhibitor
    Short name:
    Alpha-2-PI
    Serpin F2
    Gene namesi
    Name:SERPINF2
    Synonyms:AAP, PLI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9075. SERPINF2.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cell surface Source: BHF-UCL
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: BHF-UCL
    5. extracellular vesicular exosome Source: UniProt
    6. fibrinogen complex Source: BHF-UCL
    7. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Alpha-2-plasmin inhibitor deficiency (APLID) [MIM:262850]: An autosomal recessive disorder resulting in severe hemorrhagic diathesis.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti176 – 1761Missing in APLID; variant Okinawa; probably blocks intracellular transport of alpha-2-plasmin inhibitor. 1 Publication
    VAR_013254
    Natural varianti411 – 4111V → M in APLID. 1 Publication
    VAR_013255

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi262850. phenotype.
    Orphaneti79. Congenital alpha2 antiplasmin deficiency.
    PharmGKBiPA35522.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27272 PublicationsAdd
    BLAST
    Propeptidei28 – 39122 PublicationsPRO_0000032511Add
    BLAST
    Chaini40 – 491452Alpha-2-antiplasminPRO_0000032512Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki41 – 41Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-322 in alpha-fibrinogen)
    Disulfide bondi70 ↔ 1431 Publication
    Glycosylationi126 – 1261N-linked (GlcNAc...)1 Publication
    Glycosylationi295 – 2951N-linked (GlcNAc...)1 Publication
    Glycosylationi309 – 3091N-linked (GlcNAc...)1 Publication
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Modified residuei484 – 4841Sulfotyrosine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Sulfation

    Proteomic databases

    MaxQBiP08697.
    PaxDbiP08697.
    PRIDEiP08697.

    2D gel databases

    SWISS-2DPAGEP08697.

    PTM databases

    PhosphoSiteiP08697.

    Miscellaneous databases

    PMAP-CutDBP08697.

    Expressioni

    Tissue specificityi

    Expressed by the liver and secreted in plasma.

    Gene expression databases

    ArrayExpressiP08697.
    BgeeiP08697.
    CleanExiHS_SERPINF2.
    GenevestigatoriP08697.

    Organism-specific databases

    HPAiCAB024863.
    HPA001885.

    Interactioni

    Subunit structurei

    Forms protease inhibiting heterodimer with TMPRSS7.

    Protein-protein interaction databases

    BioGridi111360. 10 interactions.
    IntActiP08697. 2 interactions.
    STRINGi9606.ENSP00000321853.

    Structurei

    3D structure databases

    ProteinModelPortaliP08697.
    SMRiP08697. Positions 74-446.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the serpin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4826.
    HOGENOMiHOG000231761.
    HOVERGENiHBG000043.
    InParanoidiP08697.
    KOiK03983.
    OMAiRWFLLEQ.
    PhylomeDBiP08697.
    TreeFamiTF317350.

    Family and domain databases

    InterProiIPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view]
    PANTHERiPTHR11461. PTHR11461. 1 hit.
    PfamiPF00079. Serpin. 1 hit.
    [Graphical view]
    SMARTiSM00093. SERPIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF56574. SSF56574. 1 hit.
    PROSITEiPS00284. SERPIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P08697-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALLWGLLVL SWSCLQGPCS VFSPVSAMEP LGRQLTSGPN QEQVSPLTLL    50
    KLGNQEPGGQ TALKSPPGVC SRDPTPEQTH RLARAMMAFT ADLFSLVAQT 100
    STCPNLILSP LSVALALSHL ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR 150
    LCQDLGPGAF RLAARMYLQK GFPIKEDFLE QSEQLFGAKP VSLTGKQEDD 200
    LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF WRNKFDPSLT 250
    QRDSFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV 300
    LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT 350
    LSQLGLQELF QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA 400
    MSRMSLSSFS VNRPFLFFIF EDTTGLPLFV GSVRNPNPSA PRELKEQQDS 450
    PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM EEDYPQFGSP K 491
    Length:491
    Mass (Da):54,566
    Last modified:November 1, 1990 - v3
    Checksum:i385A1C90E91A63CB
    GO
    Isoform 2 (identifier: P08697-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         56-119: Missing.
         120-122: LAL → VQP

    Show »
    Length:427
    Mass (Da):47,907
    Checksum:i1A5190EC32B5350A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491L → G AA sequence (PubMed:2440681)Curated
    Sequence conflicti105 – 1051N → D AA sequence (PubMed:2440681)Curated
    Sequence conflicti289 – 2891H → D in AAA35543. (PubMed:2433286)Curated
    Sequence conflicti408 – 4081S → G AA sequence (PubMed:2440681)Curated
    Sequence conflicti455 – 4551D → N AA sequence (PubMed:2440681)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21A → V.1 Publication
    Corresponds to variant rs2070862 [ dbSNP | Ensembl ].
    VAR_047951
    Natural varianti27 – 271A → V.1 Publication
    VAR_013252
    Natural varianti33 – 331R → W.1 Publication
    Corresponds to variant rs2070863 [ dbSNP | Ensembl ].
    VAR_013253
    Natural varianti98 – 981A → G.
    Corresponds to variant rs36021516 [ dbSNP | Ensembl ].
    VAR_051956
    Natural varianti176 – 1761Missing in APLID; variant Okinawa; probably blocks intracellular transport of alpha-2-plasmin inhibitor. 1 Publication
    VAR_013254
    Natural varianti411 – 4111V → M in APLID. 1 Publication
    VAR_013255
    Natural varianti434 – 4341R → K.1 Publication
    Corresponds to variant rs1057335 [ dbSNP | Ensembl ].
    VAR_013256
    Natural varianti451 – 4511P → S.
    Corresponds to variant rs57360598 [ dbSNP | Ensembl ].
    VAR_061792

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei56 – 11964Missing in isoform 2. 1 PublicationVSP_043833Add
    BLAST
    Alternative sequencei120 – 1223LAL → VQP in isoform 2. 1 PublicationVSP_043834

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00174 mRNA. Translation: BAA00124.1.
    M20786
    , M20782, M20783, M20784, M20785 Genomic DNA. Translation: AAA51554.1.
    AK303763 mRNA. Translation: BAG64729.1.
    AC130343 Genomic DNA. No translation available.
    BC031592 mRNA. Translation: AAH31592.1.
    J02654 mRNA. Translation: AAA35543.1.
    D00116 mRNA. Translation: BAA00070.1.
    CCDSiCCDS11011.1. [P08697-1]
    CCDS54064.1. [P08697-2]
    PIRiA31402. ITHUA2.
    RefSeqiNP_000925.2. NM_000934.3. [P08697-1]
    NP_001159392.1. NM_001165920.1. [P08697-1]
    NP_001159393.1. NM_001165921.1. [P08697-2]
    XP_005256758.1. XM_005256701.2. [P08697-1]
    UniGeneiHs.159509.

    Genome annotation databases

    EnsembliENST00000324015; ENSP00000321853; ENSG00000167711. [P08697-1]
    ENST00000382061; ENSP00000371493; ENSG00000167711. [P08697-1]
    ENST00000450523; ENSP00000403877; ENSG00000167711. [P08697-2]
    GeneIDi5345.
    KEGGihsa:5345.
    UCSCiuc002ftk.1. human. [P08697-1]
    uc010vqr.1. human. [P08697-2]

    Polymorphism databases

    DMDMi112907.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00174 mRNA. Translation: BAA00124.1 .
    M20786
    , M20782 , M20783 , M20784 , M20785 Genomic DNA. Translation: AAA51554.1 .
    AK303763 mRNA. Translation: BAG64729.1 .
    AC130343 Genomic DNA. No translation available.
    BC031592 mRNA. Translation: AAH31592.1 .
    J02654 mRNA. Translation: AAA35543.1 .
    D00116 mRNA. Translation: BAA00070.1 .
    CCDSi CCDS11011.1. [P08697-1 ]
    CCDS54064.1. [P08697-2 ]
    PIRi A31402. ITHUA2.
    RefSeqi NP_000925.2. NM_000934.3. [P08697-1 ]
    NP_001159392.1. NM_001165920.1. [P08697-1 ]
    NP_001159393.1. NM_001165921.1. [P08697-2 ]
    XP_005256758.1. XM_005256701.2. [P08697-1 ]
    UniGenei Hs.159509.

    3D structure databases

    ProteinModelPortali P08697.
    SMRi P08697. Positions 74-446.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111360. 10 interactions.
    IntActi P08697. 2 interactions.
    STRINGi 9606.ENSP00000321853.

    Chemistry

    DrugBanki DB00086. Streptokinase.

    Protein family/group databases

    MEROPSi I04.023.

    PTM databases

    PhosphoSitei P08697.

    Polymorphism databases

    DMDMi 112907.

    2D gel databases

    SWISS-2DPAGE P08697.

    Proteomic databases

    MaxQBi P08697.
    PaxDbi P08697.
    PRIDEi P08697.

    Protocols and materials databases

    DNASUi 5345.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324015 ; ENSP00000321853 ; ENSG00000167711 . [P08697-1 ]
    ENST00000382061 ; ENSP00000371493 ; ENSG00000167711 . [P08697-1 ]
    ENST00000450523 ; ENSP00000403877 ; ENSG00000167711 . [P08697-2 ]
    GeneIDi 5345.
    KEGGi hsa:5345.
    UCSCi uc002ftk.1. human. [P08697-1 ]
    uc010vqr.1. human. [P08697-2 ]

    Organism-specific databases

    CTDi 5345.
    GeneCardsi GC17P001593.
    H-InvDB HIX0013407.
    HGNCi HGNC:9075. SERPINF2.
    HPAi CAB024863.
    HPA001885.
    MIMi 262850. phenotype.
    613168. gene.
    neXtProti NX_P08697.
    Orphaneti 79. Congenital alpha2 antiplasmin deficiency.
    PharmGKBi PA35522.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4826.
    HOGENOMi HOG000231761.
    HOVERGENi HBG000043.
    InParanoidi P08697.
    KOi K03983.
    OMAi RWFLLEQ.
    PhylomeDBi P08697.
    TreeFami TF317350.

    Enzyme and pathway databases

    Reactomei REACT_641. Dissolution of Fibrin Clot.

    Miscellaneous databases

    ChiTaRSi SERPINF2. human.
    GeneWikii Alpha_2-antiplasmin.
    GenomeRNAii 5345.
    NextBioi 20714.
    PMAP-CutDB P08697.
    PROi P08697.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08697.
    Bgeei P08697.
    CleanExi HS_SERPINF2.
    Genevestigatori P08697.

    Family and domain databases

    InterProi IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view ]
    PANTHERi PTHR11461. PTHR11461. 1 hit.
    Pfami PF00079. Serpin. 1 hit.
    [Graphical view ]
    SMARTi SM00093. SERPIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56574. SSF56574. 1 hit.
    PROSITEi PS00284. SERPIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of human alpha 2-plasmin inhibitor deduced from the cDNA sequence."
      Tone M., Kikuno R., Kume-Iwaki A., Hashimoto-Gotoh T.
      J. Biochem. 102:1033-1041(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
    3. Erratum
      Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.
      Proc. Natl. Acad. Sci. U.S.A. 86:1612-1613(1989)
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Liver.
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [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] (ISOFORM 1), VARIANT VAL-2.
    7. "Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin)."
      Holmes W.E., Nelles L., Lijnen H.R., Collen D.
      J. Biol. Chem. 262:1659-1664(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-491 (ISOFORM 1).
    8. "Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma."
      Bangert K., Johnsen A.H., Christensen U., Thorsen S.
      Biochem. J. 291:623-625(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-58.
      Tissue: Plasma.
    9. "Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence."
      Christensen S., Sottrup-Jensen L.
      FEBS Lett. 312:100-104(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-52.
      Tissue: Plasma.
    10. Cited for: PROTEIN SEQUENCE OF 40-491.
    11. "Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma."
      Wiman B., Collen D.
      Eur. J. Biochem. 78:19-26(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 40-43.
    12. "Structure of the carboxyl-terminal half of human alpha 2-plasmin inhibitor deduced from that of cDNA."
      Sumi Y., Nakamura Y., Aoki N., Sakai M., Muramatsu M.
      J. Biochem. 100:1399-1402(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 218-491.
    13. "Sulfation of a tyrosine residue in the plasmin-binding domain of alpha 2-antiplasmin."
      Hortin G., Fok K.F., Toren P.C., Strauss A.W.
      J. Biol. Chem. 262:3082-3085(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 481-491, SULFATION AT TYR-484.
    14. "Alpha-2-antiplasmin: a serpin with two separate but overlapping reactive sites."
      Potempa J., Shieh B.-H., Travis J.
      Science 241:699-700(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: REACTIVE SITES.
    15. "Assignment of a single disulphide bridge in human alpha2-antiplasmin: implications for the structural and functional properties."
      Christensen S., Valnickova Z., Thogersen I.B., Olsen E.H., Enghild J.J.
      Biochem. J. 323:847-852(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BOND.
    16. "Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity."
      Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.
      Biochem. J. 390:231-242(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, HETERODIMER WITH TMPRSS7.
    17. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-295 AND ASN-309.
      Tissue: Plasma.
    18. "Hereditary alpha 2-plasmin inhibitor deficiency caused by a transport-deficient mutation (alpha 2-PI-Okinawa). Deletion of Glu137 by a trinucleotide deletion blocks intracellular transport."
      Miura O., Sugahara Y., Aoki N.
      J. Biol. Chem. 264:18213-18219(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT APLID GLU-176 DEL.
    19. "A novel missense mutation in the human plasmin inhibitor (alpha2-antiplasmin) gene associated with a bleeding tendency."
      Lind B., Thorsen S.
      Br. J. Haematol. 107:317-322(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT APLID MET-411, VARIANTS VAL-27; TRP-33 AND LYS-434.

    Entry informationi

    Entry nameiA2AP_HUMAN
    AccessioniPrimary (citable) accession number: P08697
    Secondary accession number(s): B4E1B7
    , Q8N5U7, Q9UCG2, Q9UCG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 163 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3