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Protein

Pancreatic triacylglycerol lipase

Gene

PNLIP

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

Functioni

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei169 – 1691Nucleophile
Active sitei193 – 1931Charge relay system
Metal bindingi204 – 2041Calcium; via carbonyl oxygen
Metal bindingi207 – 2071Calcium; via carbonyl oxygen
Metal bindingi209 – 2091Calcium
Metal bindingi212 – 2121Calcium
Active sitei280 – 2801Charge relay system

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. triglyceride lipase activity Source: ProtInc

GO - Biological processi

  1. intestinal cholesterol absorption Source: Ensembl
  2. lipid catabolic process Source: UniProtKB-KW
  3. lipid digestion Source: Reactome
  4. phototransduction, visible light Source: Reactome
  5. retinoid metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10947-MONOMER.
ReactomeiREACT_24968. Retinoid metabolism and transport.
REACT_9518. Digestion of dietary lipid.
SABIO-RKP16233.

Names & Taxonomyi

Protein namesi
Recommended name:
Pancreatic triacylglycerol lipase (EC:3.1.1.3)
Short name:
PL
Short name:
PTL
Short name:
Pancreatic lipase
Gene namesi
Name:PNLIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9155. PNLIP.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

MIMi246600. gene+phenotype.
PharmGKBiPA33478.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Add
BLAST
Chaini17 – 465449Pancreatic triacylglycerol lipasePRO_0000017785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 26
Disulfide bondi107 ↔ 118
Glycosylationi183 – 1831N-linked (GlcNAc...)
Disulfide bondi254 ↔ 278
Disulfide bondi302 ↔ 313
Disulfide bondi316 ↔ 321
Disulfide bondi449 ↔ 465

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP16233.
PRIDEiP16233.

PTM databases

PhosphoSiteiP16233.

Expressioni

Inductioni

By colipase/CLPS in the presence of bile salts.

Gene expression databases

BgeeiP16233.
CleanExiHS_PNLIP.
GenevestigatoriP16233.

Organism-specific databases

HPAiHPA062430.
HPA062494.

Interactioni

Protein-protein interaction databases

BioGridi111407. 2 interactions.
IntActiP16233. 1 interaction.
MINTiMINT-1179407.
STRINGi9606.ENSP00000358223.

Structurei

Secondary structure

1
465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 214Combined sources
Turni22 – 243Combined sources
Beta strandi25 – 284Combined sources
Turni31 – 333Combined sources
Beta strandi34 – 385Combined sources
Helixi48 – 514Combined sources
Beta strandi54 – 585Combined sources
Beta strandi60 – 656Combined sources
Beta strandi67 – 693Combined sources
Helixi73 – 786Combined sources
Beta strandi87 – 915Combined sources
Helixi101 – 11010Combined sources
Turni111 – 1133Combined sources
Beta strandi117 – 1226Combined sources
Helixi124 – 1274Combined sources
Helixi131 – 15626Combined sources
Helixi160 – 1623Combined sources
Beta strandi163 – 1686Combined sources
Helixi170 – 18011Combined sources
Turni181 – 1844Combined sources
Beta strandi186 – 1938Combined sources
Turni197 – 2015Combined sources
Turni204 – 2063Combined sources
Helixi210 – 2123Combined sources
Beta strandi216 – 2194Combined sources
Turni227 – 2293Combined sources
Beta strandi239 – 2457Combined sources
Beta strandi248 – 2503Combined sources
Helixi258 – 2625Combined sources
Helixi268 – 29124Combined sources
Turni294 – 2974Combined sources
Helixi305 – 3095Combined sources
Beta strandi323 – 3253Combined sources
Helixi328 – 3303Combined sources
Turni332 – 3354Combined sources
Beta strandi336 – 3449Combined sources
Beta strandi348 – 3514Combined sources
Beta strandi355 – 36511Combined sources
Beta strandi368 – 37811Combined sources
Beta strandi386 – 3938Combined sources
Beta strandi398 – 40710Combined sources
Beta strandi411 – 42010Combined sources
Beta strandi431 – 44010Combined sources
Beta strandi445 – 4495Combined sources
Beta strandi460 – 4645Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LPAX-ray3.04B17-465[»]
1LPBX-ray2.46B17-465[»]
1N8SX-ray3.04A17-465[»]
ProteinModelPortaliP16233.
SMRiP16233. Positions 17-465.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16233.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini355 – 465111PLATPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiP16233.
KOiK14073.
OMAiMSQVVGH.
OrthoDBiEOG7KSX8B.
PhylomeDBiP16233.
TreeFamiTF324997.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16233-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGITERP LHILPWSPKD
60 70 80 90 100
VNTRFLLYTN ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE
110 120 130 140 150
NWLANVCKNL FKVESVNCIC VDWKGGSRTG YTQASQNIRI VGAEVAYFVE
160 170 180 190 200
FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR RTNGTIGRIT GLDPAEPCFQ
210 220 230 240 250
GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH LDFFPNGGVE
260 270 280 290 300
MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF
310 320 330 340 350
PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS
360 370 380 390 400
NFARWRYKVS VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS
410 420 430 440 450
NEFDSDVDVG DLQMVKFIWY NNVINPTLPR VGASKIIVET NVGKQFNFCS
460
PETVREEVLL TLTPC
Length:465
Mass (Da):51,157
Last modified:April 1, 1990 - v1
Checksum:i2BC49CC7F0E2DF52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05125 mRNA. Translation: AAA36740.1.
M93285 mRNA. Translation: AAA60129.1.
L24529
, L11242, L24502, L24522, L24523, L24525, L24526, L24527, L24528 Genomic DNA. Translation: AAA99053.1.
AK313941 mRNA. Translation: BAG36659.1.
AL731653 Genomic DNA. Translation: CAH72667.1.
CH471066 Genomic DNA. Translation: EAW49451.1.
BC014309 mRNA. Translation: AAH14309.1.
CCDSiCCDS7594.1.
PIRiC43357.
RefSeqiNP_000927.1. NM_000936.2.
UniGeneiHs.501135.

Genome annotation databases

EnsembliENST00000369221; ENSP00000358223; ENSG00000175535.
GeneIDi5406.
KEGGihsa:5406.
UCSCiuc001lcm.3. human.

Polymorphism databases

DMDMi126318.

Cross-referencesi

Web resourcesi

Wikipedia

Pancreatic lipase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05125 mRNA. Translation: AAA36740.1.
M93285 mRNA. Translation: AAA60129.1.
L24529
, L11242, L24502, L24522, L24523, L24525, L24526, L24527, L24528 Genomic DNA. Translation: AAA99053.1.
AK313941 mRNA. Translation: BAG36659.1.
AL731653 Genomic DNA. Translation: CAH72667.1.
CH471066 Genomic DNA. Translation: EAW49451.1.
BC014309 mRNA. Translation: AAH14309.1.
CCDSiCCDS7594.1.
PIRiC43357.
RefSeqiNP_000927.1. NM_000936.2.
UniGeneiHs.501135.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LPAX-ray3.04B17-465[»]
1LPBX-ray2.46B17-465[»]
1N8SX-ray3.04A17-465[»]
ProteinModelPortaliP16233.
SMRiP16233. Positions 17-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111407. 2 interactions.
IntActiP16233. 1 interaction.
MINTiMINT-1179407.
STRINGi9606.ENSP00000358223.

Chemistry

BindingDBiP16233.
ChEMBLiCHEMBL1812.
DrugBankiDB08909. Glycerol Phenylbutyrate.
DB01083. Orlistat.
GuidetoPHARMACOLOGYi2590.

PTM databases

PhosphoSiteiP16233.

Polymorphism databases

DMDMi126318.

Proteomic databases

PaxDbiP16233.
PRIDEiP16233.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369221; ENSP00000358223; ENSG00000175535.
GeneIDi5406.
KEGGihsa:5406.
UCSCiuc001lcm.3. human.

Organism-specific databases

CTDi5406.
GeneCardsiGC10P118305.
HGNCiHGNC:9155. PNLIP.
HPAiHPA062430.
HPA062494.
MIMi246600. gene+phenotype.
neXtProtiNX_P16233.
PharmGKBiPA33478.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiP16233.
KOiK14073.
OMAiMSQVVGH.
OrthoDBiEOG7KSX8B.
PhylomeDBiP16233.
TreeFamiTF324997.

Enzyme and pathway databases

BioCyciMetaCyc:HS10947-MONOMER.
ReactomeiREACT_24968. Retinoid metabolism and transport.
REACT_9518. Digestion of dietary lipid.
SABIO-RKP16233.

Miscellaneous databases

ChiTaRSiPNLIP. human.
EvolutionaryTraceiP16233.
GeneWikiiPancreatic_lipase.
GenomeRNAii5406.
NextBioi20931.
PROiP16233.
SOURCEiSearch...

Gene expression databases

BgeeiP16233.
CleanExiHS_PNLIP.
GenevestigatoriP16233.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of human pancreatic lipase cDNA."
    Lowe M.E., Rosenblum J.L., Strauss A.W.
    J. Biol. Chem. 264:20042-20048(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity."
    Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.
    J. Biol. Chem. 267:16509-16516(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pancreas.
  3. "The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family."
    Sims H.F., Jennens M.L., Lowe M.E.
    Gene 131:281-285(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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].
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  8. "Hydrolysis of retinyl esters by pancreatic triglyceride lipase."
    van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.
    Biochemistry 39:4900-4906(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  10. "Structure of the pancreatic lipase-procolipase complex."
    van Tilbeurgh H., Sarda L., Verger R., Cambillau C.
    Nature 359:159-162(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
  11. "Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography."
    van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R., Cambillau C.
    Nature 362:814-820(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
  12. "Structure-function relationships in naturally occurring mutants of pancreatic lipase."
    Carriere F., Thirstrup K., Boel E., Verger R., Thim L.
    Protein Eng. 7:563-569(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 354-465.

Entry informationi

Entry nameiLIPP_HUMAN
AccessioniPrimary (citable) accession number: P16233
Secondary accession number(s): Q5VSQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: March 4, 2015
This is version 160 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, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.