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Protein

Cocaine esterase

Gene

CES2

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

Functioni

Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine.1 Publication

Catalytic activityi

Cocaine + H2O = ecgonine methyl ester + benzoate.1 Publication
A carboxylic ester + H2O = an alcohol + a carboxylate.PROSITE-ProRule annotation1 Publication
4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate.1 Publication

Kineticsi

  1. KM=0.39 mM for cocaine1 Publication
  2. KM=0.15 mM for 4-methylumbelliferyl acetate1 Publication
  3. KM=6.8 mM for heroin1 Publication
  4. KM=0.13 mM for 6-monoacetylmorphine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei228 – 2281Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei345 – 3451Charge relay systemBy similarity
Active sitei457 – 4571Charge relay systemBy similarity

GO - Molecular functioni

  1. carboxylic ester hydrolase activity Source: ProtInc
  2. methylumbelliferyl-acetate deacetylase activity Source: UniProtKB-EC

GO - Biological processi

  1. catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.1.1. 2681.
3.1.1.84. 2681.
SABIO-RKO00748.

Protein family/group databases

MEROPSiS09.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Cocaine esterase (EC:3.1.1.84)
Alternative name(s):
Carboxylesterase 2 (EC:3.1.1.1)
Short name:
CE-2
Short name:
hCE-2
Methylumbelliferyl-acetate deacetylase 2 (EC:3.1.1.56)
Gene namesi
Name:CES2
Synonyms:ICE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:1864. CES2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: ProtInc
  2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  3. extracellular space Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 559533Cocaine esterasePRO_0000008572Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi95 ↔ 123By similarity
Glycosylationi111 – 1111N-linked (GlcNAc...)1 Publication
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi280 ↔ 291By similarity

Post-translational modificationi

Glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO00748.
PaxDbiO00748.
PRIDEiO00748.

PTM databases

PhosphoSiteiO00748.

Expressioni

Tissue specificityi

Preferentially expressed in intestine with moderate expression in liver. Within the intestine, highest expression is found in small intestine with lower expression in colon and rectum.1 Publication

Gene expression databases

BgeeiO00748.
CleanExiHS_CES2.
ExpressionAtlasiO00748. baseline and differential.
GenevestigatoriO00748.

Organism-specific databases

HPAiHPA018897.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiO00748. 1 interaction.
STRINGi9606.ENSP00000317842.

Structurei

3D structure databases

ProteinModelPortaliO00748.
SMRiO00748. Positions 39-544.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi556 – 5594Prevents secretion from ERSequence Analysis

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiO00748.
KOiK03927.
OrthoDBiEOG7RBZ7R.
PhylomeDBiO00748.
TreeFamiTF315470.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 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. AlignAdd to basket

Isoform 1 (identifier: O00748-1) [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
MRLHRLRARL SAVACGLLLL LVRGQGQDSA SPIRTTHTGQ VLGSLVHVKG
60 70 80 90 100
ANAGVQTFLG IPFAKPPLGP LRFAPPEPPE SWSGVRDGTT HPAMCLQDLT
110 120 130 140 150
AVESEFLSQF NMTFPSDSMS EDCLYLSIYT PAHSHEGSNL PVMVWIHGGA
160 170 180 190 200
LVFGMASLYD GSMLAALENV VVVIIQYRLG VLGFFSTGDK HATGNWGYLD
210 220 230 240 250
QVAALRWVQQ NIAHFGGNPD RVTIFGESAG GTSVSSLVVS PISQGLFHGA
260 270 280 290 300
IMESGVALLP GLIASSADVI STVVANLSAC DQVDSEALVG CLRGKSKEEI
310 320 330 340 350
LAINKPFKMI PGVVDGVFLP RHPQELLASA DFQPVPSIVG VNNNEFGWLI
360 370 380 390 400
PKVMRIYDTQ KEMDREASQA ALQKMLTLLM LPPTFGDLLR EEYIGDNGDP
410 420 430 440 450
QTLQAQFQEM MADSMFVIPA LQVAHFQCSR APVYFYEFQH QPSWLKNIRP
460 470 480 490 500
PHMKADHGDE LPFVFRSFFG GNYIKFTEEE EQLSRKMMKY WANFARNGNP
510 520 530 540 550
NGEGLPHWPL FDQEEQYLQL NLQPAVGRAL KAHRLQFWKK ALPQKIQELE

EPEERHTEL
Length:559
Mass (Da):61,807
Last modified:July 1, 1997 - v1
Checksum:iE2EBCABA2995339A
GO
Isoform 2 (identifier: O00748-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     458-474: GDELPFVFRSFFGGNYI → V

Show »
Length:543
Mass (Da):59,959
Checksum:i4F14FE06766F0F7E
GO

Sequence cautioni

The sequence AAH32095.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAW29943.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAD28531.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAD98009.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 109Missing AA sequence (PubMed:9169443).Curated
Sequence conflicti180 – 1801G → S in BAF83171 (PubMed:14702039).Curated
Sequence conflicti239 – 2391V → M in BAF83171 (PubMed:14702039).Curated
Sequence conflicti385 – 3851F → S in CAD98009 (PubMed:17974005).Curated
Sequence conflicti519 – 5191Q → R in CAD98009 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341R → W.1 Publication
VAR_018396
Natural varianti206 – 2061R → H.1 Publication
VAR_018397

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei458 – 47417GDELP…GGNYI → V in isoform 2. 1 PublicationVSP_010161Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09616 mRNA. Translation: CAA70831.1.
D50579 mRNA. Translation: BAA23606.1.
U60553 mRNA. Translation: AAB03611.1.
AL713761 mRNA. Translation: CAD28531.1. Different initiation.
AK290482 mRNA. Translation: BAF83171.1.
BX538086 mRNA. Translation: CAD98009.1. Different initiation.
AY851164 Genomic DNA. Translation: AAW29943.1. Different initiation.
AC009084 Genomic DNA. No translation available.
BC032095 mRNA. Translation: AAH32095.1. Different initiation.
PIRiJC5408.
RefSeqiNP_003860.2. NM_003869.5.
NP_932327.1. NM_198061.2.
UniGeneiHs.282975.

Genome annotation databases

EnsembliENST00000417689; ENSP00000394452; ENSG00000172831.
GeneIDi8824.
KEGGihsa:8824.
UCSCiuc002eqs.3. human. [O00748-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09616 mRNA. Translation: CAA70831.1.
D50579 mRNA. Translation: BAA23606.1.
U60553 mRNA. Translation: AAB03611.1.
AL713761 mRNA. Translation: CAD28531.1. Different initiation.
AK290482 mRNA. Translation: BAF83171.1.
BX538086 mRNA. Translation: CAD98009.1. Different initiation.
AY851164 Genomic DNA. Translation: AAW29943.1. Different initiation.
AC009084 Genomic DNA. No translation available.
BC032095 mRNA. Translation: AAH32095.1. Different initiation.
PIRiJC5408.
RefSeqiNP_003860.2. NM_003869.5.
NP_932327.1. NM_198061.2.
UniGeneiHs.282975.

3D structure databases

ProteinModelPortaliO00748.
SMRiO00748. Positions 39-544.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO00748. 1 interaction.
STRINGi9606.ENSP00000317842.

Chemistry

BindingDBiO00748.
ChEMBLiCHEMBL3180.
DrugBankiDB06695. Dabigatran etexilate.
DB00762. Irinotecan.
DB00688. Mycophenolate mofetil.
DB06209. Prasugrel.

Protein family/group databases

MEROPSiS09.984.

PTM databases

PhosphoSiteiO00748.

Proteomic databases

MaxQBiO00748.
PaxDbiO00748.
PRIDEiO00748.

Protocols and materials databases

DNASUi8824.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000417689; ENSP00000394452; ENSG00000172831.
GeneIDi8824.
KEGGihsa:8824.
UCSCiuc002eqs.3. human. [O00748-1]

Organism-specific databases

CTDi8824.
GeneCardsiGC16P066969.
HGNCiHGNC:1864. CES2.
HPAiHPA018897.
MIMi605278. gene.
neXtProtiNX_O00748.
PharmGKBiPA377.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2272.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiO00748.
KOiK03927.
OrthoDBiEOG7RBZ7R.
PhylomeDBiO00748.
TreeFamiTF315470.

Enzyme and pathway databases

BRENDAi3.1.1.1. 2681.
3.1.1.84. 2681.
SABIO-RKO00748.

Miscellaneous databases

ChiTaRSiCES2. human.
GeneWikiiCarboxylesterase_2.
GenomeRNAii8824.
NextBioi33104.
PROiO00748.
SOURCEiSearch...

Gene expression databases

BgeeiO00748.
CleanExiHS_CES2.
ExpressionAtlasiO00748. baseline and differential.
GenevestigatoriO00748.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver."
    Schwer H., Langmann T., Daig R., Becker A., Aslanidis C., Schmitz G.
    Biochem. Biophys. Res. Commun. 233:117-120(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Small intestine.
  2. "Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin."
    Pindel E.V., Kedishvili N.Y., Abraham T.L., Brzezinski M.R., Zhang J., Dean R.A., Bosron W.F.
    J. Biol. Chem. 272:14769-14775(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 27-34; 57-70; 227-235; 300-305; 346-351; 447-454; 458-466; 535-540 AND 546-551, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Liver.
  3. "Molecular cloning and expression of a human liver cDNA encoding a novel carboxylesterase."
    Sone T., Ishida Y., Takabatake E., Wang C., Pohl L., Isobe M.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Endometrial adenocarcinoma and Testis.
  6. NIEHS SNPs program
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Skin.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111.
    Tissue: Liver.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population."
    Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., Nakamura Y.
    J. Hum. Genet. 48:249-270(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-206.
  13. "Twelve novel single nucleotide polymorphisms in the CES2 gene encoding human carboxylesterase 2 (hCE-2)."
    Kim S.-R., Nakamura T., Saito Y., Sai K., Nakajima T., Saito H., Shirao K., Minami H., Ohtsu A., Yoshida T., Saijo N., Ozawa S., Sawada J.
    Drug Metab. Pharmacokinet. 18:327-332(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TRP-34.

Entry informationi

Entry nameiEST2_HUMAN
AccessioniPrimary (citable) accession number: O00748
Secondary accession number(s): A8K367
, Q16859, Q5MAB8, Q7Z366, Q8IUP4, Q8TCP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: July 1, 1997
Last modified: April 1, 2015
This is version 128 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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

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.