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Protein

Perilipin-5

Gene

Plin5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE.7 Publications

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • lipase binding Source: UniProtKB

GO - Biological processi

  • lipid metabolic process Source: UniProtKB-KW
  • lipid particle organization Source: UniProtKB
  • lipid storage Source: UniProtKB
  • mitochondrion localization Source: UniProtKB
  • negative regulation of fatty acid beta-oxidation Source: UniProtKB
  • negative regulation of lipase activity Source: UniProtKB
  • negative regulation of lipid catabolic process Source: UniProtKB
  • negative regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
  • negative regulation of reactive oxygen species metabolic process Source: UniProtKB
  • negative regulation of triglyceride catabolic process Source: UniProtKB
  • positive regulation of fatty acid beta-oxidation Source: UniProtKB
  • positive regulation of lipase activity Source: UniProtKB
  • positive regulation of lipid storage Source: UniProtKB
  • positive regulation of sequestering of triglyceride Source: UniProtKB
  • positive regulation of triglyceride biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Perilipin-5
Alternative name(s):
Lipid droplet-associated protein PAT-1
Lipid storage droplet protein 5
Myocardial LD protein
Gene namesi
Name:Plin5
Synonyms:Lsdp5, Mldp, Oxpat, Pat1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1914218. Plin5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: MGI
  • lipid particle Source: UniProtKB
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lipid droplet, Mitochondrion

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice lack detectable lipid droplets in heart. The triacylglycerol and fatty acid content in heart is lower.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Perilipin-5PRO_0000338983Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei163 – 1631PhosphoserineCombined sources
Modified residuei337 – 3371PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by PKA. Phosphorylated on serine in skeletal muscle at rest or with lipolytic stimulation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BVZ1.
MaxQBiQ8BVZ1.
PaxDbiQ8BVZ1.
PRIDEiQ8BVZ1.

PTM databases

iPTMnetiQ8BVZ1.
PhosphoSiteiQ8BVZ1.

Expressioni

Tissue specificityi

Highly expressed in oxidative tissues, including heart, liver, brown adipose tissue (BAT) and slow-twitch fibers of skeletal muscle. Lower expression in epididymal white adipose tissue and anterior tibialis and quadriceps. Expressed in adrenal glands. Isoform 2 has the highest expression in heart.3 Publications

Inductioni

Up-regulated by fasting, PPARD, PPARA and PLIN4. Increased in muscle of high-fat diet fed mice. Induced by unsaturated long chain fatty acid in muscle.5 Publications

Gene expression databases

BgeeiQ8BVZ1.
GenevisibleiQ8BVZ1. MM.

Interactioni

Subunit structurei

Homooligomer. Interacts with PNPLA2; prevents interaction of PNPLA2 with ABHD5. Interacts with ABHD5; targets ABHD5 to lipid droplets and promotes interaction of ABHD5 with PNPLA2. Interacts with LIPE.4 Publications

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • lipase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi211843. 1 interaction.
STRINGi10090.ENSMUSP00000019808.

Structurei

3D structure databases

ProteinModelPortaliQ8BVZ1.
SMRiQ8BVZ1. Positions 181-399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 188188Essential for lipid droplet targetingAdd
BLAST
Regioni1 – 123123Interaction with LIPEAdd
BLAST
Regioni200 – 463264Interaction with PNPLA2 and ABHD5Add
BLAST
Regioni444 – 46320Necessary for mitochondria recruitment at the lipid droplet surfaceAdd
BLAST

Sequence similaritiesi

Belongs to the perilipin family.Curated

Phylogenomic databases

eggNOGiENOG410IM0T. Eukaryota.
ENOG410XS97. LUCA.
GeneTreeiENSGT00500000044795.
HOGENOMiHOG000033816.
HOVERGENiHBG002935.
InParanoidiQ8BVZ1.
OMAiSKHRAQD.
OrthoDBiEOG7SN8CD.
PhylomeDBiQ8BVZ1.
TreeFamiTF328397.

Family and domain databases

InterProiIPR004279. Perilipin.
[Graphical view]
PANTHERiPTHR14024. PTHR14024. 1 hit.
PfamiPF03036. Perilipin. 1 hit.
[Graphical view]
PIRSFiPIRSF036881. PAT. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q8BVZ1-1) [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
MDQRGEDTTL APHSRMSGDQ TAQDPGSSLG ELDQQNVVNR VVALPLVKAT
60 70 80 90 100
CTAVSSAYNS AKDRHPLLGS ACRLAEHCVC SVTTCALDHA QPLLEHLQPQ
110 120 130 140 150
LATVNDLACR GLDKLEEKLP FLQQPSDMVV TSAKDTVAKS VTGMVDLAQR
160 170 180 190 200
GRRWSGELRR SMSQAMDMVL GKSEKLVDRF LPMTEAELAV LAAEAEGPEV
210 220 230 240 250
GTVEEQRQQQ GYFVRLGSLS ARLRHLAYEH SLGKLRQSKH RTQEMLAQLQ
260 270 280 290 300
ETLELIQHMQ RGASPSPTFH PPKTQELWGS WSPCLENGRS HSEVELETLA
310 320 330 340 350
LSRSLTLELQ NAVDALAGCV RGLPPSAQAK VAEVQRSVDA LQATFADAHC
360 370 380 390 400
LGDVAPTALA EGRGSVARAH ACVDEFLDLV LRAMPLPWLV GPFAPILVEQ
410 420 430 440 450
SEPLINLATC VDEVVGDPDP RWAHMDWPAQ KRAWEAESAD PGGQEAEPPR
460
GQGKHTMMPE LDF
Length:463
Mass (Da):50,474
Last modified:March 1, 2003 - v1
Checksum:iE232342603E3F303
GO
Isoform 2 (identifier: Q8BVZ1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: Missing.

Show »
Length:448
Mass (Da):48,778
Checksum:iB14F60ABD8584CB5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515Missing in isoform 2. 1 PublicationVSP_034085Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ473305 mRNA. Translation: ABF13218.1.
AY919875 mRNA. Translation: AAX12443.1.
AK075872 mRNA. Translation: BAC36019.1.
BC024138 mRNA. Translation: AAH24138.2.
CCDSiCCDS37662.1. [Q8BVZ1-1]
RefSeqiNP_001070816.1. NM_001077348.1. [Q8BVZ1-1]
NP_080150.2. NM_025874.3. [Q8BVZ1-1]
UniGeneiMm.254985.

Genome annotation databases

EnsembliENSMUST00000019808; ENSMUSP00000019808; ENSMUSG00000011305. [Q8BVZ1-1]
ENSMUST00000113072; ENSMUSP00000108695; ENSMUSG00000011305. [Q8BVZ1-1]
GeneIDi66968.
KEGGimmu:66968.
UCSCiuc008daz.1. mouse. [Q8BVZ1-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ473305 mRNA. Translation: ABF13218.1.
AY919875 mRNA. Translation: AAX12443.1.
AK075872 mRNA. Translation: BAC36019.1.
BC024138 mRNA. Translation: AAH24138.2.
CCDSiCCDS37662.1. [Q8BVZ1-1]
RefSeqiNP_001070816.1. NM_001077348.1. [Q8BVZ1-1]
NP_080150.2. NM_025874.3. [Q8BVZ1-1]
UniGeneiMm.254985.

3D structure databases

ProteinModelPortaliQ8BVZ1.
SMRiQ8BVZ1. Positions 181-399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211843. 1 interaction.
STRINGi10090.ENSMUSP00000019808.

PTM databases

iPTMnetiQ8BVZ1.
PhosphoSiteiQ8BVZ1.

Proteomic databases

EPDiQ8BVZ1.
MaxQBiQ8BVZ1.
PaxDbiQ8BVZ1.
PRIDEiQ8BVZ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019808; ENSMUSP00000019808; ENSMUSG00000011305. [Q8BVZ1-1]
ENSMUST00000113072; ENSMUSP00000108695; ENSMUSG00000011305. [Q8BVZ1-1]
GeneIDi66968.
KEGGimmu:66968.
UCSCiuc008daz.1. mouse. [Q8BVZ1-1]

Organism-specific databases

CTDi440503.
MGIiMGI:1914218. Plin5.

Phylogenomic databases

eggNOGiENOG410IM0T. Eukaryota.
ENOG410XS97. LUCA.
GeneTreeiENSGT00500000044795.
HOGENOMiHOG000033816.
HOVERGENiHBG002935.
InParanoidiQ8BVZ1.
OMAiSKHRAQD.
OrthoDBiEOG7SN8CD.
PhylomeDBiQ8BVZ1.
TreeFamiTF328397.

Miscellaneous databases

PROiQ8BVZ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BVZ1.
GenevisibleiQ8BVZ1. MM.

Family and domain databases

InterProiIPR004279. Perilipin.
[Graphical view]
PANTHERiPTHR14024. PTHR14024. 1 hit.
PfamiPF03036. Perilipin. 1 hit.
[Graphical view]
PIRSFiPIRSF036881. PAT. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "LSDP5 is a PAT protein specifically expressed in fatty acid oxidizing tissues."
    Dalen K.T., Dahl T., Holter E., Arntsen B., Londos C., Sztalryd C., Nebb H.I.
    Biochim. Biophys. Acta 1771:210-227(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, ALTERNATIVE INITIATION.
    Strain: C57BL/6J.
  2. Tansey J.T., Kimmel A.R., Hlavin E.M., Dickey L.O., Londos C.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Tongue.
  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].
    Strain: FVB/N.
    Tissue: Liver.
  5. "OXPAT/PAT-1 is a PPAR-induced lipid droplet protein that promotes fatty acid utilization."
    Wolins N.E., Quaynor B.K., Skinner J.R., Tzekov A., Croce M.A., Gropler M.C., Varma V., Yao-Borengasser A., Rasouli N., Kern P.A., Finck B.N., Bickel P.E.
    Diabetes 55:3418-3428(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIPOLYSIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  6. "MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha."
    Yamaguchi T., Matsushita S., Motojima K., Hirose F., Osumi T.
    J. Biol. Chem. 281:14232-14240(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Functional interactions between Mldp (LSDP5) and Abhd5 in the control of intracellular lipid accumulation."
    Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z.
    J. Biol. Chem. 284:3049-3057(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIPOLYSIS, INTERACTION WITH ABHD5.
  9. "Activation of hormone-sensitive lipase requires two steps, protein phosphorylation and binding to the PAT-1 domain of lipid droplet coat proteins."
    Wang H., Hu L., Dalen K., Dorward H., Marcinkiewicz A., Russell D., Gong D., Londos C., Yamaguchi T., Holm C., Rizzo M.A., Brasaemle D., Sztalryd C.
    J. Biol. Chem. 284:32116-32125(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIPE, SUBCELLULAR LOCATION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Liver and Lung.
  11. "Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase."
    Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z., Zhou L.
    J. Biol. Chem. 286:5126-5135(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ABHD5 AND PNPLA2, REGION, HOMOOLIGOMERIZATION.
  12. "Unique regulation of adipose triglyceride lipase (ATGL) by perilipin 5, a lipid droplet-associated protein."
    Wang H., Bell M., Sreenivasan U., Sreenevasan U., Hu H., Liu J., Dalen K., Londos C., Yamaguchi T., Rizzo M.A., Coleman R., Gong D., Brasaemle D., Sztalryd C.
    J. Biol. Chem. 286:15707-15715(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIPOLYSIS, INTERACTION WITH PNPLA2, REGION, PHOSPHORYLATION BY PKA.
  13. "Perilipin 5, a lipid droplet-associated protein, provides physical and metabolic linkage to mitochondria."
    Wang H., Sreenivasan U., Sreenevasan U., Hu H., Saladino A., Polster B.M., Lund L.M., Gong D.W., Stanley W.C., Sztalryd C.
    J. Lipid Res. 52:2159-2168(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIPID HOMEOSTASIS, REGION.
  14. "Perilipin 5, a lipid droplet-binding protein, protects heart from oxidative burden by sequestering fatty acid from excessive oxidation."
    Kuramoto K., Okamura T., Yamaguchi T., Nakamura T.Y., Wakabayashi S., Morinaga H., Nomura M., Yanase T., Otsu K., Usuda N., Matsumura S., Inoue K., Fushiki T., Kojima Y., Hashimoto T., Sakai F., Hirose F., Osumi T.
    J. Biol. Chem. 287:23852-23863(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIPOGENESIS, DISRUPTION PHENOTYPE.
  15. "LSDP5 enhances triglyceride storage in hepatocytes by influencing lipolysis and fatty acid beta-oxidation of lipid droplets."
    Li H., Song Y., Zhang L.J., Gu Y., Li F.F., Pan S.Y., Jiang L.N., Liu F., Ye J., Li Q.
    PLoS ONE 7:E36712-E36712(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIPID STORAGE, REGION.
  16. "Inactivation of Plin4 downregulates Plin5 and reduces cardiac lipid accumulation in mice."
    Chen W., Chang B., Wu X., Li L., Sleeman M., Chan L.
    Am. J. Physiol. 304:E770-E779(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  17. "Cardiomyocyte-specific perilipin 5 overexpression leads to myocardial steatosis and modest cardiac dysfunction."
    Wang H., Sreenivasan U., Gong D.W., O'Connell K.A., Dabkowski E.R., Hecker P.A., Ionica N., Konig M., Mahurkar A., Sun Y., Stanley W.C., Sztalryd C.
    J. Lipid Res. 54:953-965(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LYPOLYSIS, SUBCELLULAR LOCATION.
  18. "Fatty acids regulate perilipin5 in muscle by activating PPARdelta."
    Bindesboll C., Berg O., Arntsen B., Nebb H.I., Dalen K.T.
    J. Lipid Res. 54:1949-1963(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiPLIN5_MOUSE
AccessioniPrimary (citable) accession number: Q8BVZ1
Secondary accession number(s): Q78IK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.