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Protein

Chymotrypsin-like elastase family member 2B

Gene

CELA2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Acts upon elastin.

Catalytic activityi

Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731Charge relay systemBy similarity
Active sitei121 – 1211Charge relay systemBy similarity
Active sitei216 – 2161Charge relay systemBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.206.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsin-like elastase family member 2B (EC:3.4.21.71)
Alternative name(s):
Elastase-2B
Gene namesi
Name:CELA2B
Synonyms:ELA2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29995. CELA2B.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165750841.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Add
BLAST
Propeptidei17 – 2812Activation peptidePRO_0000027695Add
BLAST
Chaini29 – 269241Chymotrypsin-like elastase family member 2BPRO_0000027696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 74PROSITE-ProRule annotation
Disulfide bondi155 ↔ 222PROSITE-ProRule annotation
Disulfide bondi186 ↔ 202PROSITE-ProRule annotation
Disulfide bondi212 ↔ 243PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP08218.
PRIDEiP08218.

Miscellaneous databases

PMAP-CutDBP08218.

Expressioni

Tissue specificityi

Pancreas.

Gene expression databases

BgeeiP08218.
ExpressionAtlasiP08218. baseline and differential.
GenevestigatoriP08218.

Interactioni

Protein-protein interaction databases

BioGridi119238. 15 interactions.
STRINGi9606.ENSP00000365075.

Structurei

3D structure databases

ProteinModelPortaliP08218.
SMRiP08218. Positions 29-269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 267239Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119027.
HOGENOMiHOG000251820.
InParanoidiP08218.
KOiK01346.
OMAiHILHENW.
OrthoDBiEOG75B84T.
PhylomeDBiP08218.
TreeFamiTF330455.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRTLLLSTL VAGALSCGVS TYAPDMSRML GGEEARPNSW PWQVSLQYSS
60 70 80 90 100
NGQWYHTCGG SLIANSWVLT AAHCISSSGI YRVMLGQHNL YVAESGSLAV
110 120 130 140 150
SVSKIVVHKD WNSDQVSKGN DIALLKLANP VSLTDKIQLA CLPPAGTILP
160 170 180 190 200
NNYPCYVTGW GRLQTNGALP DDLKQGQLLV VDYATCSSSG WWGSTVKTNM
210 220 230 240 250
ICAGGDGVIC TCNGDSGGPL NCQASDGRWE VHGIGSLTSV LGCNYYYKPS
260
IFTRVSNYND WINSVIANN
Length:269
Mass (Da):28,810
Last modified:July 22, 2008 - v2
Checksum:iCC81C1D18B918B5F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791G → R.2 Publications
Corresponds to variant rs3820071 [ dbSNP | Ensembl ].
VAR_044534
Natural varianti114 – 1141D → N.2 Publications
Corresponds to variant rs3766160 [ dbSNP | Ensembl ].
VAR_044535
Natural varianti177 – 1771Q → R.2 Publications
Corresponds to variant rs6429745 [ dbSNP | Ensembl ].
VAR_044536
Natural varianti235 – 2351G → S.
Corresponds to variant rs3737703 [ dbSNP | Ensembl ].
VAR_044537

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16653 mRNA. Translation: AAA52381.1.
AL512883 Genomic DNA. Translation: CAC42422.1.
CH471167 Genomic DNA. Translation: EAW51728.1.
BC069455 mRNA. Translation: AAH69455.1.
BC113540 mRNA. Translation: AAI13541.1.
BC113542 mRNA. Translation: AAI13543.1.
CCDSiCCDS30605.1.
PIRiC26823.
RefSeqiNP_056933.2. NM_015849.2.
UniGeneiHs.631871.

Genome annotation databases

EnsembliENST00000375910; ENSP00000365075; ENSG00000215704.
GeneIDi51032.
KEGGihsa:51032.
UCSCiuc001awl.3. human.

Polymorphism databases

DMDMi212288098.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16653 mRNA. Translation: AAA52381.1.
AL512883 Genomic DNA. Translation: CAC42422.1.
CH471167 Genomic DNA. Translation: EAW51728.1.
BC069455 mRNA. Translation: AAH69455.1.
BC113540 mRNA. Translation: AAI13541.1.
BC113542 mRNA. Translation: AAI13543.1.
CCDSiCCDS30605.1.
PIRiC26823.
RefSeqiNP_056933.2. NM_015849.2.
UniGeneiHs.631871.

3D structure databases

ProteinModelPortaliP08218.
SMRiP08218. Positions 29-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119238. 15 interactions.
STRINGi9606.ENSP00000365075.

Protein family/group databases

MEROPSiS01.206.

Polymorphism databases

DMDMi212288098.

Proteomic databases

PaxDbiP08218.
PRIDEiP08218.

Protocols and materials databases

DNASUi51032.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375910; ENSP00000365075; ENSG00000215704.
GeneIDi51032.
KEGGihsa:51032.
UCSCiuc001awl.3. human.

Organism-specific databases

CTDi51032.
GeneCardsiGC01P015792.
HGNCiHGNC:29995. CELA2B.
MIMi609444. gene.
neXtProtiNX_P08218.
PharmGKBiPA165750841.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119027.
HOGENOMiHOG000251820.
InParanoidiP08218.
KOiK01346.
OMAiHILHENW.
OrthoDBiEOG75B84T.
PhylomeDBiP08218.
TreeFamiTF330455.

Miscellaneous databases

GeneWikiiCELA2B.
GenomeRNAii51032.
NextBioi53589.
PMAP-CutDBP08218.
PROiP08218.
SOURCEiSearch...

Gene expression databases

BgeeiP08218.
ExpressionAtlasiP08218. baseline and differential.
GenevestigatoriP08218.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs are expressed in human pancreas."
    Kawashima I., Tani T., Shimoda K., Takiguchi Y.
    DNA 6:163-172(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-79; ASN-114 AND ARG-177.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-79; ASN-114 AND ARG-177.

Entry informationi

Entry nameiCEL2B_HUMAN
AccessioniPrimary (citable) accession number: P08218
Secondary accession number(s): Q14D16, Q6ISM5, Q96QV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 22, 2008
Last modified: March 4, 2015
This is version 135 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.