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P30740

- ILEU_HUMAN

UniProt

P30740 - ILEU_HUMAN

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Protein

Leukocyte elastase inhibitor

Gene

SERPINB1

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

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
Complete GO annotation...

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-KW
  2. extracellular space Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
Complete GO annotation...

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

BgeeiP30740.
CleanExiHS_SERPINB1.
ExpressionAtlasiP30740. baseline and differential.
GenevestigatoriP30740.

Organism-specific databases

HPAiHPA018871.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi108307. 10 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 – 2220Combined sources
Beta strandi24 – 263Combined sources
Beta strandi28 – 303Combined sources
Helixi32 – 4312Combined sources
Helixi48 – 5710Combined sources
Helixi60 – 623Combined sources
Helixi66 – 7712Combined sources
Beta strandi83 – 9513Combined sources
Helixi102 – 11110Combined sources
Beta strandi116 – 1194Combined sources
Helixi121 – 13919Combined sources
Turni140 – 1423Combined sources
Beta strandi159 – 16810Combined sources
Beta strandi171 – 1733Combined sources
Turni177 – 1793Combined sources
Beta strandi181 – 1888Combined sources
Beta strandi191 – 20919Combined sources
Turni210 – 2134Combined sources
Beta strandi214 – 2218Combined sources
Beta strandi224 – 23512Combined sources
Beta strandi238 – 2425Combined sources
Helixi244 – 2496Combined sources
Helixi252 – 2598Combined sources
Helixi261 – 2633Combined sources
Beta strandi265 – 27410Combined sources
Beta strandi276 – 2838Combined sources
Helixi285 – 2906Combined sources
Helixi295 – 2973Combined sources
Turni299 – 3013Combined sources
Turni305 – 3073Combined sources
Beta strandi315 – 32612Combined sources
Beta strandi345 – 3473Combined sources
Beta strandi349 – 3535Combined sources
Beta strandi358 – 3647Combined sources
Turni365 – 3684Combined sources
Beta strandi369 – 3768Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GA7X-ray2.90A/B1-379[»]
ProteinModelPortaliP30740.
SMRiP30740. Positions 1-327, 349-379.
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

        10         20         30         40         50
MEQLSSANTR FALDLFLALS ENNPAGNIFI SPFSISSAMA MVFLGTRGNT
60 70 80 90 100
AAQLSKTFHF NTVEEVHSRF QSLNADINKR GASYILKLAN RLYGEKTYNF
110 120 130 140 150
LPEFLVSTQK TYGADLASVD FQHASEDARK TINQWVKGQT EGKIPELLAS
160 170 180 190 200
GMVDNMTKLV LVNAIYFKGN WKDKFMKEAT TNAPFRLNKK DRKTVKMMYQ
210 220 230 240 250
KKKFAYGYIE DLKCRVLELP YQGEELSMVI LLPDDIEDES TGLKKIEEQL
260 270 280 290 300
TLEKLHEWTK PENLDFIEVN VSLPRFKLEE SYTLNSDLAR LGVQDLFNSS
310 320 330 340 350
KADLSGMSGA RDIFISKIVH KSFVEVNEEG TEAAAATAGI ATFCMLMPEE
360 370
NFTADHPFLF FIRHNSSGSI LFLGRFSSP
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. Curated

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:
EMBLi
GenBanki
DDBJi
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. [P30740-1]
PIRiS27383.
RefSeqiNP_109591.1. NM_030666.3. [P30740-1]
XP_006715071.1. XM_006715008.1. [P30740-1]
UniGeneiHs.381167.

Genome annotation databases

EnsembliENST00000380739; ENSP00000370115; ENSG00000021355. [P30740-1]
GeneIDi1992.
KEGGihsa:1992.
UCSCiuc003mub.4. human. [P30740-1]

Polymorphism databases

DMDMi266344.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P30740-1 ]
PIRi S27383.
RefSeqi NP_109591.1. NM_030666.3. [P30740-1 ]
XP_006715071.1. XM_006715008.1. [P30740-1 ]
UniGenei Hs.381167.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4GA7 X-ray 2.90 A/B 1-379 [» ]
ProteinModelPortali P30740.
SMRi P30740. Positions 1-327, 349-379.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108307. 10 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 . [P30740-1 ]
GeneIDi 1992.
KEGGi hsa:1992.
UCSCi uc003mub.4. human. [P30740-1 ]

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 35473693.
PMAP-CutDB P30740.
PROi P30740.
SOURCEi Search...

Gene expression databases

Bgeei P30740.
CleanExi HS_SERPINB1.
ExpressionAtlasi P30740. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 144 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

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