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Protein

Patatin-like phospholipase domain-containing protein 2

Gene

PNPLA2

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

Functioni

Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion.3 Publications

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Enzyme regulationi

Inhibited by BEL ((E)-6-(bromomethylene)-3-(1-naphthalenyl)-2H-tetrahydropyran-2-one), a suicide substrate inhibitor. No differences in enzymatic activity that uses (1,2-dilinoleoyl)-phosphatidylcholine as substrate was detected in the presence or absence of ATP. Activated by ABHD5 and SERPINF1.2 Publications

pH dependencei

Optimum pH is 7.5 with (1,2-dilinoleoyl)-phosphatidylcholine as substrate.1 Publication

Pathway: triacylglycerol degradation

This protein is involved in the pathway triacylglycerol degradation, which is part of Glycerolipid metabolism.
View all proteins of this organism that are known to be involved in the pathway triacylglycerol degradation and in Glycerolipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei47 – 471

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_121122. Acyl chain remodeling of DAG and TAG.
UniPathwayiUPA00256.

Names & Taxonomyi

Protein namesi
Recommended name:
Patatin-like phospholipase domain-containing protein 2 (EC:3.1.1.3)
Alternative name(s):
Adipose triglyceride lipase
Calcium-independent phospholipase A2
Desnutrin
IPLA2-zeta
Pigment epithelium-derived factor
TTS2.2
Transport-secretion protein 2
Short name:
TTS2
Gene namesi
Name:PNPLA2
Synonyms:ATGL
ORF Names:FP17548
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:30802. PNPLA2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence Analysis
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 504475LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Lipid droplet, Membrane

Pathology & Biotechi

Involvement in diseasei

Genetic variations in PNPLA2 may be associated with risk of diabetes mellitus type 2.

Neutral lipid storage disease with myopathy (NLSDM)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionNeutral lipid storage disorder (NLSD) with myopathy but without ichthyosis. NLSDs are characterized by the presence of triglyceride-containing cytoplasmic droplets in leukocytes and in other tissues, including bone marrow, skin, and muscle. Individuals with NLSDM did not show obesity, in spite of a defect in triglyceride degradation in fibroblasts and in marked triglyceride storage in liver, muscles, and other visceral cells.

See also OMIM:610717
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti195 – 1951P → L in NLSDM. 1 Publication
VAR_032995

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471S → A: Reduces rate of lipid hydrolysis; does not affect the localization around the rim of the adiposomes. 2 Publications

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi610717. phenotype.
Orphaneti98908. Neutral lipid storage myopathy.
PharmGKBiPA134903083.

Polymorphism and mutation databases

BioMutaiPNPLA2.
DMDMi74731110.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504Patatin-like phospholipase domain-containing protein 2PRO_0000292527Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
Modified residuei372 – 3721Phosphoserine; in vitroBy similarity
Modified residuei404 – 4041Phosphoserine; by PKA1 Publication
Modified residuei428 – 4281Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation at Ser-404 by PKA is increased during fasting and moderate intensity exercise, and moderately increases lipolytic activity (By similarity). Phosphorylation at Ser-404 is increased upon beta-adrenergic stimulation.By similarity1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ96AD5.
PaxDbiQ96AD5.
PRIDEiQ96AD5.

PTM databases

PhosphoSiteiQ96AD5.

Expressioni

Tissue specificityi

Highest expression in adipose tissue. Also detected in heart, skeletal muscle, and portions of the gastrointestinal tract. Detected in normal retina and retinoblastoma cells. Detected in retinal pigment epithelium and, at lower intensity, in the inner segments of photoreceptors and in the ganglion cell layer of the neural retina (at protein level).4 Publications

Developmental stagei

Induced during differentiation of primary preadipocytes to adipocytes. Expression increased from fetal to adult in retinal pigment epithelium.3 Publications

Gene expression databases

BgeeiQ96AD5.
CleanExiHS_PNPLA2.
ExpressionAtlasiQ96AD5. baseline and differential.
GenevisibleiQ96AD5. HS.

Interactioni

Subunit structurei

Interacts with ABHD5; this association stimulates PNPLA2 triglyceride hydrolase activity (By similarity). Interacts with SERPINF1; interacts at one site of interaction. Despite a colocalization in lipid droplets, it probably does not interact with PLIN (By similarity). Interacts with PLIN5; prevents interaction with ABHD5 (By similarity).By similarity

Protein-protein interaction databases

BioGridi121370. 16 interactions.
IntActiQ96AD5. 7 interactions.
MINTiMINT-1184430.
STRINGi9606.ENSP00000337701.

Structurei

3D structure databases

ProteinModelPortaliQ96AD5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 179170PatatinAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 495GXSXG

Sequence similaritiesi

Contains 1 patatin domain.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG261571.
GeneTreeiENSGT00390000005295.
HOVERGENiHBG007046.
InParanoidiQ96AD5.
KOiK16816.
OMAiDMCKQGY.
OrthoDBiEOG7J9VQR.
PhylomeDBiQ96AD5.
TreeFamiTF314272.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002641. Patatin/PLipase_A2-rel.
[Graphical view]
PfamiPF01734. Patatin. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96AD5-1) [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
MFPREKTWNI SFAGCGFLGV YYVGVASCLR EHAPFLVANA THIYGASAGA
60 70 80 90 100
LTATALVTGV CLGEAGAKFI EVSKEARKRF LGPLHPSFNL VKIIRSFLLK
110 120 130 140 150
VLPADSHEHA SGRLGISLTR VSDGENVIIS HFNSKDELIQ ANVCSGFIPV
160 170 180 190 200
YCGLIPPSLQ GVRYVDGGIS DNLPLYELKN TITVSPFSGE SDICPQDSST
210 220 230 240 250
NIHELRVTNT SIQFNLRNLY RLSKALFPPE PLVLREMCKQ GYRDGLRFLQ
260 270 280 290 300
RNGLLNRPNP LLALPPARPH GPEDKDQAVE SAQAEDYSQL PGEDHILEHL
310 320 330 340 350
PARLNEALLE ACVEPTDLLT TLSNMLPVRL ATAMMVPYTL PLESALSFTI
360 370 380 390 400
RLLEWLPDVP EDIRWMKEQT GSICQYLVMR AKRKLGRHLP SRLPEQVELR
410 420 430 440 450
RVQSLPSVPL SCAAYREALP GWMRNNLSLG DALAKWEECQ RQLLLGLFCT
460 470 480 490 500
NVAFPPEALR MRAPADPAPA PADPASPQHQ LAGPAPLLST PAPEARPVIG

ALGL
Length:504
Mass (Da):55,316
Last modified:December 1, 2001 - v1
Checksum:iD9C16F942AB0B3C7
GO
Isoform 2 (identifier: Q96AD5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-324: Missing.

Note: No experimental confirmation available.
Show »
Length:180
Mass (Da):19,875
Checksum:i00655EB8A70EF89A
GO

Sequence cautioni

The sequence AAP34448.1 differs from that shown. Reason: Frameshift at position 501. Curated
The sequence CAC01131.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC01132.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631R → G in AAC09354 (Ref. 5) Curated
Sequence conflicti296 – 2961I → V in AAW81962 (PubMed:15550674).Curated
Sequence conflicti333 – 3331A → G in AAP34448 (PubMed:15498874).Curated
Sequence conflicti351 – 3511R → C in AAW81962 (PubMed:15550674).Curated
Sequence conflicti402 – 4021V → L in CAC01131 (Ref. 2) Curated
Sequence conflicti402 – 4021V → L in CAC01132 (Ref. 2) Curated
Sequence conflicti419 – 4191L → P in AAW81962 (PubMed:15550674).Curated

Polymorphismi

Genetic variations in PNPLA2 may be associated with plasma free fatty acids, triglycerides levels, and fasting glucose concentrations.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti195 – 1951P → L in NLSDM. 1 Publication
VAR_032995
Natural varianti219 – 2191L → F.1 Publication
VAR_032996
Natural varianti252 – 2521N → K.1 Publication
Corresponds to variant rs140201358 [ dbSNP | Ensembl ].
VAR_032997
Natural varianti481 – 4811L → P.3 Publications
Corresponds to variant rs1138693 [ dbSNP | Ensembl ].
VAR_032998

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 324324Missing in isoform 2. 1 PublicationVSP_026421Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY894804 mRNA. Translation: AAW81962.1.
AJ278475 mRNA. Translation: CAC01131.1. Different initiation.
AJ278476 mRNA. Translation: CAC01132.1. Different initiation.
AY203925 mRNA. Translation: AAP34448.1. Frameshift.
BC011958 mRNA. Translation: AAH11958.1.
BC017280 mRNA. Translation: AAH17280.1.
AF055000 mRNA. Translation: AAC09354.1.
CCDSiCCDS7718.1. [Q96AD5-1]
RefSeqiNP_065109.1. NM_020376.3. [Q96AD5-1]
UniGeneiHs.654697.

Genome annotation databases

EnsembliENST00000336615; ENSP00000337701; ENSG00000177666. [Q96AD5-1]
GeneIDi57104.
KEGGihsa:57104.
UCSCiuc001lrt.3. human. [Q96AD5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY894804 mRNA. Translation: AAW81962.1.
AJ278475 mRNA. Translation: CAC01131.1. Different initiation.
AJ278476 mRNA. Translation: CAC01132.1. Different initiation.
AY203925 mRNA. Translation: AAP34448.1. Frameshift.
BC011958 mRNA. Translation: AAH11958.1.
BC017280 mRNA. Translation: AAH17280.1.
AF055000 mRNA. Translation: AAC09354.1.
CCDSiCCDS7718.1. [Q96AD5-1]
RefSeqiNP_065109.1. NM_020376.3. [Q96AD5-1]
UniGeneiHs.654697.

3D structure databases

ProteinModelPortaliQ96AD5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121370. 16 interactions.
IntActiQ96AD5. 7 interactions.
MINTiMINT-1184430.
STRINGi9606.ENSP00000337701.

PTM databases

PhosphoSiteiQ96AD5.

Polymorphism and mutation databases

BioMutaiPNPLA2.
DMDMi74731110.

Proteomic databases

MaxQBiQ96AD5.
PaxDbiQ96AD5.
PRIDEiQ96AD5.

Protocols and materials databases

DNASUi57104.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336615; ENSP00000337701; ENSG00000177666. [Q96AD5-1]
GeneIDi57104.
KEGGihsa:57104.
UCSCiuc001lrt.3. human. [Q96AD5-1]

Organism-specific databases

CTDi57104.
GeneCardsiGC11P000821.
HGNCiHGNC:30802. PNPLA2.
MIMi609059. gene.
610717. phenotype.
neXtProtiNX_Q96AD5.
Orphaneti98908. Neutral lipid storage myopathy.
PharmGKBiPA134903083.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG261571.
GeneTreeiENSGT00390000005295.
HOVERGENiHBG007046.
InParanoidiQ96AD5.
KOiK16816.
OMAiDMCKQGY.
OrthoDBiEOG7J9VQR.
PhylomeDBiQ96AD5.
TreeFamiTF314272.

Enzyme and pathway databases

UniPathwayiUPA00256.
ReactomeiREACT_121122. Acyl chain remodeling of DAG and TAG.

Miscellaneous databases

ChiTaRSiPNPLA2. human.
GeneWikiiPNPLA2.
GenomeRNAii57104.
NextBioi62941.
PROiQ96AD5.
SOURCEiSearch...

Gene expression databases

BgeeiQ96AD5.
CleanExiHS_PNPLA2.
ExpressionAtlasiQ96AD5. baseline and differential.
GenevisibleiQ96AD5. HS.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002641. Patatin/PLipase_A2-rel.
[Graphical view]
PfamiPF01734. Patatin. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  2. "TTS-2, a novel protein implicated in vesicular transport of the cell surface receptor ICAM-3."
    Strahl T., Shingler W.H., Lammiman M., Gregory C.D., Leach L., Matthias P., Nielsen P.J., Shaw P.E.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-481.
  3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-481.
    Tissue: Brain and Eye.
  5. Yu W., Gibbs R.A.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 94-504 (ISOFORM 1).
    Tissue: Brain.
  6. "Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities."
    Jenkins C.M., Mancuso D.J., Yan W., Sims H.F., Gibson B., Gross R.W.
    J. Biol. Chem. 279:48968-48975(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  7. Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  8. "Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members."
    Lake A.C., Sun Y., Li J.-L., Kim J.E., Johnson J.W., Li D., Revett T., Shih H.H., Liu W., Paulsen J.E., Gimeno R.E.
    J. Lipid Res. 46:2477-2487(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF SER-47.
  9. "The adipose tissue triglyceride lipase ATGL/PNPLA2 is downregulated by insulin and TNF-alpha in 3T3-L1 adipocytes and is a target for transactivation by PPARgamma."
    Kim J.Y., Tillison K., Lee J.-H., Rearick D.A., Smas C.M.
    Am. J. Physiol. 291:E115-E127(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  10. "ATGL has a key role in lipid droplet/adiposome degradation in mammalian cells."
    Smirnova E., Goldberg E.B., Makarova K.S., Lin L., Brown W.J., Jackson C.L.
    EMBO Rep. 7:106-113(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-47.
  11. Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH SERPINF1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Identification and functional characterization of protein kinase A phosphorylation sites in the major lipolytic protein, adipose triglyceride lipase."
    Pagnon J., Matzaris M., Stark R., Meex R.C., Macaulay S.L., Brown W., O'Brien P.E., Tiganis T., Watt M.J.
    Endocrinology 153:4278-4289(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-404.
  15. "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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "The ATGL gene is associated with free fatty acids, triglycerides, and type 2 diabetes."
    Schoenborn V., Heid I.M., Vollmert C., Lingenhel A., Adams T.D., Hopkins P.N., Illig T., Zimmermann R., Zechner R., Hunt S.C., Kronenberg F.
    Diabetes 55:1270-1275(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PHE-219; LYS-252 AND PRO-481, POLYMORPHISM, ASSOCIATION WITH DIABETES MELLITUS TYPE 2.
  17. "The gene encoding adipose triglyceride lipase (PNPLA2) is mutated in neutral lipid storage disease with myopathy."
    Fischer J., Lefevre C., Morava E., Mussini J.-M., Laforet P., Negre-Salvayre A., Lathrop M., Salvayre R.
    Nat. Genet. 39:28-30(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NLSDM LEU-195.

Entry informationi

Entry nameiPLPL2_HUMAN
AccessioniPrimary (citable) accession number: Q96AD5
Secondary accession number(s): O60643
, Q5EFF5, Q6XYE5, Q96ET6, Q9NQ61, Q9NQ62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 105 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.