Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P08697

- A2AP_HUMAN

UniProt

P08697 - A2AP_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Alpha-2-antiplasmin

Gene

SERPINF2

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

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
Sitei39 – 402Cleavage; by prolyl endopeptidase FAP, antiplasmin-cleaving enzyme FAP soluble form2 Publications
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 homodimerization activity Source: BHF-UCL
  4. 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
Complete GO annotation...

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: UniProtKB
  6. fibrinogen complex Source: BHF-UCL
  7. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

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 – 39124 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

Post-translational modificationi

Proteolytically cleaved at Pro-39 by both the prolyl endopeptidase FAP form and antiplasmin-cleaving enzyme FAP soluble form to generate mature alpha-2-antiplasmin.2 Publications

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

BgeeiP08697.
CleanExiHS_SERPINF2.
ExpressionAtlasiP08697. baseline and differential.
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.
GeneTreeiENSGT00760000118839.
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

        10         20         30         40         50
MALLWGLLVL SWSCLQGPCS VFSPVSAMEP LGRQLTSGPN QEQVSPLTLL
60 70 80 90 100
KLGNQEPGGQ TALKSPPGVC SRDPTPEQTH RLARAMMAFT ADLFSLVAQT
110 120 130 140 150
STCPNLILSP LSVALALSHL ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR
160 170 180 190 200
LCQDLGPGAF RLAARMYLQK GFPIKEDFLE QSEQLFGAKP VSLTGKQEDD
210 220 230 240 250
LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF WRNKFDPSLT
260 270 280 290 300
QRDSFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV
310 320 330 340 350
LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT
360 370 380 390 400
LSQLGLQELF QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA
410 420 430 440 450
MSRMSLSSFS VNRPFLFFIF EDTTGLPLFV GSVRNPNPSA PRELKEQQDS
460 470 480 490
PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM EEDYPQFGSP K
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 DB08888. Ocriplasmin.

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 GC17P001646.
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.
GeneTreei ENSGT00760000118839.
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

Bgeei P08697.
CleanExi HS_SERPINF2.
ExpressionAtlasi P08697. baseline and differential.
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

« Hide 'large scale' publications
  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. "A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion."
    Lee K.N., Jackson K.W., Christiansen V.J., Chung K.H., McKee P.A.
    Blood 103:3783-3788(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY SOLUBLE FAP FORM, CLEAVAGE SITE.
  17. "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.
  18. "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.
  19. "Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation protein."
    Lee K.N., Jackson K.W., Christiansen V.J., Lee C.S., Chun J.G., McKee P.A.
    Blood 107:1397-1404(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY PLASMA MEMBRANE AND SOLUBLE FAP FORMS, CLEAVAGE SITE.
  20. "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.
  21. "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 29, 2014
This is version 164 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