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P30740

- ILEU_HUMAN

UniProt

P30740 - ILEU_HUMAN

Protein

Leukocyte elastase inhibitor

Gene

SERPINB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Also functions as a potent intracellular inhibitor of granzyme H.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei343 – 3442Reactive bond 1
    Sitei344 – 3452Reactive bond 2

    GO - Molecular functioni

    1. serine-type endopeptidase inhibitor activity Source: UniProtKB

    GO - Biological processi

    1. negative regulation of endopeptidase activity Source: RefGenome
    2. regulation of proteolysis Source: RefGenome

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Protein family/group databases

    MEROPSiI04.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leukocyte elastase inhibitor
    Short name:
    LEI
    Alternative name(s):
    Monocyte/neutrophil elastase inhibitor
    Short name:
    EI
    Short name:
    M/NEI
    Peptidase inhibitor 2
    Short name:
    PI-2
    Serpin B1
    Gene namesi
    Name:SERPINB1
    Synonyms:ELANH2, MNEI, PI2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:3311. SERPINB1.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmic granule 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35046.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 379379Leukocyte elastase inhibitorPRO_0000094101Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei137 – 1371N6-acetyllysine1 Publication
    Modified residuei177 – 1771N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP30740.
    PaxDbiP30740.
    PeptideAtlasiP30740.
    PRIDEiP30740.

    2D gel databases

    OGPiP30740.
    REPRODUCTION-2DPAGEIPI00027444.

    PTM databases

    PhosphoSiteiP30740.

    Miscellaneous databases

    PMAP-CutDBP30740.

    Expressioni

    Gene expression databases

    ArrayExpressiP30740.
    BgeeiP30740.
    CleanExiHS_SERPINB1.
    GenevestigatoriP30740.

    Organism-specific databases

    HPAiHPA018871.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi108307. 6 interactions.
    IntActiP30740. 2 interactions.
    MINTiMINT-4999893.
    STRINGi9606.ENSP00000370115.

    Structurei

    Secondary structure

    1
    379
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 2220
    Beta strandi24 – 263
    Beta strandi28 – 303
    Helixi32 – 4312
    Helixi48 – 5710
    Helixi60 – 623
    Helixi66 – 7712
    Beta strandi83 – 9513
    Helixi102 – 11110
    Beta strandi116 – 1194
    Helixi121 – 13919
    Turni140 – 1423
    Beta strandi159 – 16810
    Beta strandi171 – 1733
    Turni177 – 1793
    Beta strandi181 – 1888
    Beta strandi191 – 20919
    Turni210 – 2134
    Beta strandi214 – 2218
    Beta strandi224 – 23512
    Beta strandi238 – 2425
    Helixi244 – 2496
    Helixi252 – 2598
    Helixi261 – 2633
    Beta strandi265 – 27410
    Beta strandi276 – 2838
    Helixi285 – 2906
    Helixi295 – 2973
    Turni299 – 3013
    Turni305 – 3073
    Beta strandi315 – 32612
    Beta strandi345 – 3473
    Beta strandi349 – 3535
    Beta strandi358 – 3647
    Turni365 – 3684
    Beta strandi369 – 3768

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GA7X-ray2.90A/B1-379[»]
    ProteinModelPortaliP30740.
    SMRiP30740. Positions 1-379.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    Reactive bond 1 is specific for reaction with chymotrypsin-like protease such as cathepsin G, chymotrypsin, chymase or granzyme H, while reactive bond 2 is specific for reaction with elastase-like protease such as neutrophil elastase, proteinase-3, pancreatic elastase or PSA.

    Sequence similaritiesi

    Belongs to the serpin family. Ov-serpin subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG4826.
    HOGENOMiHOG000238519.
    HOVERGENiHBG005957.
    InParanoidiP30740.
    KOiK13963.
    OMAiMHEENFV.
    OrthoDBiEOG7327PB.
    PhylomeDBiP30740.
    TreeFamiTF352619.

    Family and domain databases

    InterProiIPR015557. Serpin_B1.
    IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view]
    PANTHERiPTHR11461. PTHR11461. 1 hit.
    PTHR11461:SF142. PTHR11461:SF142. 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.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30740-1) [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

    MEQLSSANTR FALDLFLALS ENNPAGNIFI SPFSISSAMA MVFLGTRGNT    50
    AAQLSKTFHF NTVEEVHSRF QSLNADINKR GASYILKLAN RLYGEKTYNF 100
    LPEFLVSTQK TYGADLASVD FQHASEDARK TINQWVKGQT EGKIPELLAS 150
    GMVDNMTKLV LVNAIYFKGN WKDKFMKEAT TNAPFRLNKK DRKTVKMMYQ 200
    KKKFAYGYIE DLKCRVLELP YQGEELSMVI LLPDDIEDES TGLKKIEEQL 250
    TLEKLHEWTK PENLDFIEVN VSLPRFKLEE SYTLNSDLAR LGVQDLFNSS 300
    KADLSGMSGA RDIFISKIVH KSFVEVNEEG TEAAAATAGI ATFCMLMPEE 350
    NFTADHPFLF FIRHNSSGSI LFLGRFSSP 379
    Length:379
    Mass (Da):42,742
    Last modified:April 1, 1993 - v1
    Checksum:iBAAE08DFCBCD8CD3
    GO
    Isoform 2 (identifier: P30740-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-151: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:228
    Mass (Da):26,073
    Checksum:iEDA3D9952C365A47
    GO

    Sequence cautioni

    The sequence BAD97090.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371K → R in AAP35574. 1 PublicationCurated
    Sequence conflicti149 – 1491A → V in BAF84016. (PubMed:14702039)Curated
    Sequence conflicti264 – 2641L → F in BAF84016. (PubMed:14702039)Curated
    Sequence conflicti272 – 2721Missing AA sequence (PubMed:7578269)Curated
    Sequence conflicti329 – 3291E → K in BAF84016. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti82 – 821A → V.
    Corresponds to variant rs34825616 [ dbSNP | Ensembl ].
    VAR_051945

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 151151Missing in isoform 2. 1 PublicationVSP_056511Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93056 mRNA. No translation available.
    AF053630 Genomic DNA. Translation: AAC31394.1.
    AK291327 mRNA. Translation: BAF84016.1.
    AK298044 mRNA. Translation: BAG60342.1.
    BT006928 mRNA. Translation: AAP35574.1.
    AK223370 mRNA. Translation: BAD97090.1. Different initiation.
    AL139092 Genomic DNA. Translation: CAH73667.1.
    BC009015 mRNA. Translation: AAH09015.1.
    CCDSiCCDS4477.1.
    PIRiS27383.
    RefSeqiNP_109591.1. NM_030666.3.
    XP_006715071.1. XM_006715008.1.
    UniGeneiHs.381167.

    Genome annotation databases

    EnsembliENST00000380739; ENSP00000370115; ENSG00000021355.
    ENST00000537185; ENSP00000444543; ENSG00000021355.
    GeneIDi1992.
    KEGGihsa:1992.
    UCSCiuc003mub.4. human.

    Polymorphism databases

    DMDMi266344.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93056 mRNA. No translation available.
    AF053630 Genomic DNA. Translation: AAC31394.1 .
    AK291327 mRNA. Translation: BAF84016.1 .
    AK298044 mRNA. Translation: BAG60342.1 .
    BT006928 mRNA. Translation: AAP35574.1 .
    AK223370 mRNA. Translation: BAD97090.1 . Different initiation.
    AL139092 Genomic DNA. Translation: CAH73667.1 .
    BC009015 mRNA. Translation: AAH09015.1 .
    CCDSi CCDS4477.1.
    PIRi S27383.
    RefSeqi NP_109591.1. NM_030666.3.
    XP_006715071.1. XM_006715008.1.
    UniGenei Hs.381167.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GA7 X-ray 2.90 A/B 1-379 [» ]
    ProteinModelPortali P30740.
    SMRi P30740. Positions 1-379.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108307. 6 interactions.
    IntActi P30740. 2 interactions.
    MINTi MINT-4999893.
    STRINGi 9606.ENSP00000370115.

    Protein family/group databases

    MEROPSi I04.006.

    PTM databases

    PhosphoSitei P30740.

    Polymorphism databases

    DMDMi 266344.

    2D gel databases

    OGPi P30740.
    REPRODUCTION-2DPAGE IPI00027444.

    Proteomic databases

    MaxQBi P30740.
    PaxDbi P30740.
    PeptideAtlasi P30740.
    PRIDEi P30740.

    Protocols and materials databases

    DNASUi 1992.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380739 ; ENSP00000370115 ; ENSG00000021355 .
    ENST00000537185 ; ENSP00000444543 ; ENSG00000021355 .
    GeneIDi 1992.
    KEGGi hsa:1992.
    UCSCi uc003mub.4. human.

    Organism-specific databases

    CTDi 1992.
    GeneCardsi GC06M002833.
    HGNCi HGNC:3311. SERPINB1.
    HPAi HPA018871.
    MIMi 130135. gene.
    neXtProti NX_P30740.
    PharmGKBi PA35046.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4826.
    HOGENOMi HOG000238519.
    HOVERGENi HBG005957.
    InParanoidi P30740.
    KOi K13963.
    OMAi MHEENFV.
    OrthoDBi EOG7327PB.
    PhylomeDBi P30740.
    TreeFami TF352619.

    Miscellaneous databases

    ChiTaRSi SERPINB1. human.
    GeneWikii SERPINB1.
    GenomeRNAii 1992.
    NextBioi 8055.
    PMAP-CutDB P30740.
    PROi P30740.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30740.
    Bgeei P30740.
    CleanExi HS_SERPINB1.
    Genevestigatori P30740.

    Family and domain databases

    InterProi IPR015557. Serpin_B1.
    IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view ]
    PANTHERi PTHR11461. PTHR11461. 1 hit.
    PTHR11461:SF142. PTHR11461:SF142. 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. "Sequence and molecular characterization of human monocyte/neutrophil elastase inhibitor."
      Remold-O'Donnell E., Chin J., Alberts M.
      Proc. Natl. Acad. Sci. U.S.A. 89:5635-5639(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structure and sequence of human M/NEI (monocyte/neutrophil elastase inhibitor), an Ov-serpin family gene."
      Zeng W., Silverman G.A., Remold-O'Donnell E.
      Gene 213:179-187(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Lung and Tongue.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Small intestine.
    6. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
      Tissue: Cervix.
    8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10, ACETYLATION AT MET-1.
      Tissue: Platelet.
    9. "A serpin from human tumor cells with direct lymphoid immunomodulatory activity: mitogenic stimulation of human tumor-infiltrating lymphocytes."
      Packard B.Z., Lee S.S., Remold-O'Donnell E., Komoriya A.
      Biochim. Biophys. Acta 1269:41-50(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 111-129; 216-244 AND 255-274.
    10. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 178-185; 204-210 AND 364-371.
      Tissue: Keratinocyte.
    11. "The serpin MNEI inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites."
      Cooley J., Takayama T.K., Shapiro S.D., Schechter N.M., Remold-O'Donnell E.
      Biochemistry 40:15762-15770(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, REACTIVE SITES, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137 AND LYS-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Identification of SERPINB1 as a physiological inhibitor of human granzyme H."
      Wang L., Li Q., Wu L., Liu S., Zhang Y., Yang X., Zhu P., Zhang H., Zhang K., Lou J., Liu P., Tong L., Sun F., Fan Z.
      J. Immunol. 190:1319-1330(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH GZMH, SUBCELLULAR LOCATION, SUBUNIT.

    Entry informationi

    Entry nameiILEU_HUMAN
    AccessioniPrimary (citable) accession number: P30740
    Secondary accession number(s): A8K5L2
    , B4DNT0, Q53FB9, Q5W0E1, Q9UDF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 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

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

    Documents

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

    External Data

    Dasty 3