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Protein

Junctophilin-2

Gene

JPH2

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

Functioni

Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH2 is necessary for proper intracellular Ca2+ signaling in cardiac myocytes via its involvement in ryanodine receptor-mediated calcium ion release. Contributes to the construction of skeletal muscle triad junctions.1 Publication

GO - Molecular functioni

  1. calcium-release channel activity Source: UniProtKB
  2. phosphatidic acid binding Source: UniProtKB
  3. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  4. phosphatidylinositol-3,5-bisphosphate binding Source: UniProtKB
  5. phosphatidylinositol-3-phosphate binding Source: UniProtKB
  6. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  7. phosphatidylinositol-4-phosphate binding Source: UniProtKB
  8. phosphatidylinositol-5-phosphate binding Source: UniProtKB
  9. phosphatidylserine binding Source: UniProtKB

GO - Biological processi

  1. calcium ion homeostasis Source: UniProtKB
  2. calcium ion transmembrane transport Source: GOC
  3. calcium ion transport into cytosol Source: BHF-UCL
  4. positive regulation of ryanodine-sensitive calcium-release channel activity Source: UniProtKB
  5. regulation of cardiac muscle tissue development Source: Ensembl
  6. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Junctophilin-2
Short name:
JP-2
Alternative name(s):
Junctophilin type 2
Gene namesi
Name:JPH2
Synonyms:JP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:14202. JPH2.

Subcellular locationi

Cell membrane By similarity; Peripheral membrane protein By similarity. Endoplasmic reticulum membrane By similarity; Single-pass type IV membrane protein By similarity. Sarcoplasmic reticulum membrane By similarity; Single-pass type IV membrane protein By similarity
Note: Localized predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic/sarcoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane. In heart cells, it predominantly associates along Z lines within myocytes. In skeletal muscle, it is specifically localized at the junction of A and I bands (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 674674CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei675 – 69521Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. junctional membrane complex Source: Ensembl
  3. junctional sarcoplasmic reticulum membrane Source: BHF-UCL
  4. plasma membrane Source: UniProtKB-SubCell
  5. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Cardiomyopathy, familial hypertrophic 171 Publication

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

Disease descriptionA hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.

See also OMIM:613873
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011S → R in CMH17; modifies the secondary structure of the protein which is more flexible but does not undergo structural transition upon binding to membrane lipids; increases the affinity for phosphatidylserine; affects intracellular calcium handling and homeostasis. 2 Publications
VAR_065471
Natural varianti141 – 1411Y → H in CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. 1 Publication
VAR_065472
Natural varianti165 – 1651S → F in CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. Greatly reduced phosphorylation. Increased myotube diameter. Reduced RYR1 activity and EC gain. Disruption of interaction with TRPC3. 2 Publications
VAR_065473

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

MIMi613873. phenotype.
Orphaneti155. Familial isolated hypertrophic cardiomyopathy.
PharmGKBiPA29999.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 696696Junctophilin-2PRO_0000159847Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei165 – 1651Phosphoserine1 Publication
Modified residuei469 – 4691Phosphoserine1 Publication
Modified residuei484 – 4841Phosphoserine1 Publication
Modified residuei486 – 4861Phosphoserine1 Publication
Modified residuei490 – 4901Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylation on Ser-165, probably by PKC, affects RYR1-mediated calcium ion release, interaction with TRPC3, and skeletal muscle myotubule development.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BR39.
PaxDbiQ9BR39.
PRIDEiQ9BR39.

PTM databases

PhosphoSiteiQ9BR39.

Expressioni

Tissue specificityi

Specifically expressed in skeletal muscle and heart.1 Publication

Gene expression databases

BgeeiQ9BR39.
CleanExiHS_JPH2.
ExpressionAtlasiQ9BR39. baseline and differential.
GenevestigatoriQ9BR39.

Organism-specific databases

HPAiHPA052646.

Interactioni

Protein-protein interaction databases

BioGridi121414. 1 interaction.
STRINGi9606.ENSP00000362071.

Structurei

3D structure databases

ProteinModelPortaliQ9BR39.
SMRiQ9BR39. Positions 8-45, 53-144, 318-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati14 – 3623MORN 1Add
BLAST
Repeati38 – 5922MORN 2Add
BLAST
Repeati60 – 7920MORN 3Add
BLAST
Repeati82 – 10423MORN 4Add
BLAST
Repeati106 – 12823MORN 5Add
BLAST
Repeati129 – 15123MORN 6Add
BLAST
Repeati291 – 31323MORN 7Add
BLAST
Repeati314 – 33623MORN 8Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 142140Gly-richAdd
BLAST
Compositional biasi373 – 40836Ala-richAdd
BLAST
Compositional biasi452 – 633182Pro-richAdd
BLAST

Domaini

The MORN (membrane occupation and recognition nexus) repeats contribute to the plasma membrane binding, by interacting with phospholipids. Has affinity for phosphatidylserine, and phosphorylated phosphatidylinositols including PtdIns3P, PtdIns4P, PtdIns5P, PtdIns(3,5)P2 and PtdIns(3,4,5)P3.1 Publication

Sequence similaritiesi

Belongs to the junctophilin family.Curated
Contains 8 MORN repeats.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG324165.
GeneTreeiENSGT00730000110639.
HOGENOMiHOG000264244.
HOVERGENiHBG031648.
InParanoidiQ9BR39.
OMAiHERETPR.
OrthoDBiEOG7J4463.
PhylomeDBiQ9BR39.
TreeFamiTF317210.

Family and domain databases

InterProiIPR017191. Junctophilin.
IPR003409. MORN.
[Graphical view]
PfamiPF02493. MORN. 8 hits.
[Graphical view]
PIRSFiPIRSF037387. Junctophilin. 1 hit.
SMARTiSM00698. MORN. 6 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BR39-1) [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
MSGGRFDFDD GGAYCGGWEG GKAHGHGLCT GPKGQGEYSG SWNFGFEVAG
60 70 80 90 100
VYTWPSGNTF EGYWSQGKRH GLGIETKGRW LYKGEWTHGF KGRYGIRQSS
110 120 130 140 150
SSGAKYEGTW NNGLQDGYGT ETYADGGTYQ GQFTNGMRHG YGVRQSVPYG
160 170 180 190 200
MAVVVRSPLR TSLSSLRSEH SNGTVAPDSP ASPASDGPAL PSPAIPRGGF
210 220 230 240 250
ALSLLANAEA AARAPKGGGL FQRGALLGKL RRAESRTSVG SQRSRVSFLK
260 270 280 290 300
SDLSSGASDA ASTASLGEAA EGADEAAPFE ADIDATTTET YMGEWKNDKR
310 320 330 340 350
SGFGVSERSS GLRYEGEWLD NLRHGYGCTT LPDGHREEGK YRHNVLVKDT
360 370 380 390 400
KRRMLQLKSN KVRQKVEHSV EGAQRAAAIA RQKAEIAASR TSHAKAKAEA
410 420 430 440 450
AEQAALAANQ ESNIARTLAR ELAPDFYQPG PEYQKRRLLQ EILENSESLL
460 470 480 490 500
EPPDRGAGAA GLPQPPRESP QLHERETPRP EGGSPSPAGT PPQPKRPRPG
510 520 530 540 550
VSKDGLLSPG AWNGEPSGEG SRSVTPSEGA GRRSPARPAT ERMAIEALQA
560 570 580 590 600
PPAPSREPEV ALYQGYHSYA VRTTPPEPPP FEDQPEPEVS GSESAPSSPA
610 620 630 640 650
TAPLQAPTLR GPEPARETPA KLEPKPIIPK AEPRAKARKT EARGLTKAGA
660 670 680 690
KKKARKEAAL AAEAEVEVEE VPNTILICMV ILLNIGLAIL FVHLLT
Length:696
Mass (Da):74,222
Last modified:January 17, 2003 - v2
Checksum:i80D62652CE48548B
GO
Isoform 2 (identifier: Q9BR39-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     128-129: TY → MC
     130-696: Missing.

Note: No experimental confirmation available.

Show »
Length:129
Mass (Da):13,951
Checksum:iF2008165B64B104B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011S → R in CMH17; modifies the secondary structure of the protein which is more flexible but does not undergo structural transition upon binding to membrane lipids; increases the affinity for phosphatidylserine; affects intracellular calcium handling and homeostasis. 2 Publications
VAR_065471
Natural varianti141 – 1411Y → H in CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. 1 Publication
VAR_065472
Natural varianti165 – 1651S → F in CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. Greatly reduced phosphorylation. Increased myotube diameter. Reduced RYR1 activity and EC gain. Disruption of interaction with TRPC3. 2 Publications
VAR_065473
Natural varianti396 – 3961A → T.
Corresponds to variant rs3810510 [ dbSNP | Ensembl ].
VAR_053447
Natural varianti436 – 4361R → C.1 Publication
VAR_065474
Natural varianti505 – 5051G → S in patients with cardiomyopathy; does not affect protein conformation as shown by circular dichroism; a patient with cardiomyopathy also carries V-26 and C-513 in MYH7. 1 Publication
Corresponds to variant rs140740776 [ dbSNP | Ensembl ].
VAR_065475

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei128 – 1292TY → MC in isoform 2. 1 PublicationVSP_002785
Alternative sequencei130 – 696567Missing in isoform 2. 1 PublicationVSP_002786Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132999 mRNA. Translation: CAB61347.1.
AL035447, AL034419 Genomic DNA. Translation: CAI19380.1.
AL034419, AL035447 Genomic DNA. Translation: CAI42199.1.
AL035447 Genomic DNA. Translation: CAC18785.1.
CH471077 Genomic DNA. Translation: EAW75940.1.
CH471077 Genomic DNA. Translation: EAW75943.1.
CCDSiCCDS13325.1. [Q9BR39-1]
CCDS13326.1. [Q9BR39-2]
RefSeqiNP_065166.2. NM_020433.4. [Q9BR39-1]
NP_787109.2. NM_175913.3. [Q9BR39-2]
XP_006723895.1. XM_006723832.1. [Q9BR39-1]
UniGeneiHs.441737.

Genome annotation databases

EnsembliENST00000342272; ENSP00000344590; ENSG00000149596. [Q9BR39-2]
ENST00000372980; ENSP00000362071; ENSG00000149596. [Q9BR39-1]
GeneIDi57158.
KEGGihsa:57158.
UCSCiuc002xli.1. human. [Q9BR39-1]
uc002xlj.3. human. [Q9BR39-2]

Polymorphism databases

DMDMi27805486.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132999 mRNA. Translation: CAB61347.1.
AL035447, AL034419 Genomic DNA. Translation: CAI19380.1.
AL034419, AL035447 Genomic DNA. Translation: CAI42199.1.
AL035447 Genomic DNA. Translation: CAC18785.1.
CH471077 Genomic DNA. Translation: EAW75940.1.
CH471077 Genomic DNA. Translation: EAW75943.1.
CCDSiCCDS13325.1. [Q9BR39-1]
CCDS13326.1. [Q9BR39-2]
RefSeqiNP_065166.2. NM_020433.4. [Q9BR39-1]
NP_787109.2. NM_175913.3. [Q9BR39-2]
XP_006723895.1. XM_006723832.1. [Q9BR39-1]
UniGeneiHs.441737.

3D structure databases

ProteinModelPortaliQ9BR39.
SMRiQ9BR39. Positions 8-45, 53-144, 318-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121414. 1 interaction.
STRINGi9606.ENSP00000362071.

PTM databases

PhosphoSiteiQ9BR39.

Polymorphism databases

DMDMi27805486.

Proteomic databases

MaxQBiQ9BR39.
PaxDbiQ9BR39.
PRIDEiQ9BR39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342272; ENSP00000344590; ENSG00000149596. [Q9BR39-2]
ENST00000372980; ENSP00000362071; ENSG00000149596. [Q9BR39-1]
GeneIDi57158.
KEGGihsa:57158.
UCSCiuc002xli.1. human. [Q9BR39-1]
uc002xlj.3. human. [Q9BR39-2]

Organism-specific databases

CTDi57158.
GeneCardsiGC20M042740.
H-InvDBHIX0015833.
HGNCiHGNC:14202. JPH2.
HPAiHPA052646.
MIMi605267. gene.
613873. phenotype.
neXtProtiNX_Q9BR39.
Orphaneti155. Familial isolated hypertrophic cardiomyopathy.
PharmGKBiPA29999.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG324165.
GeneTreeiENSGT00730000110639.
HOGENOMiHOG000264244.
HOVERGENiHBG031648.
InParanoidiQ9BR39.
OMAiHERETPR.
OrthoDBiEOG7J4463.
PhylomeDBiQ9BR39.
TreeFamiTF317210.

Miscellaneous databases

ChiTaRSiJPH2. human.
GeneWikiiJPH2.
GenomeRNAii57158.
NextBioi63151.
PROiQ9BR39.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BR39.
CleanExiHS_JPH2.
ExpressionAtlasiQ9BR39. baseline and differential.
GenevestigatoriQ9BR39.

Family and domain databases

InterProiIPR017191. Junctophilin.
IPR003409. MORN.
[Graphical view]
PfamiPF02493. MORN. 8 hits.
[Graphical view]
PIRSFiPIRSF037387. Junctophilin. 1 hit.
SMARTiSM00698. MORN. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Stavrides G.S., Huckle E.J., Deloukas P.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: IDENTIFICATION (ISOFORM 1), TISSUE SPECIFICITY.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484; SER-486 AND THR-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletal muscle."
    Woo J.S., Hwang J.H., Ko J.K., Weisleder N., Kim do H., Ma J., Lee E.H.
    Biochem. J. 427:125-134(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-165, INTERACTION WITH TRPC3, FUNCTION, CHARACTERIZATION OF VARIANT PHE-165.
  8. "Human junctophilin-2 undergoes a structural rearrangement upon binding PtdIns(3,4,5)P3 and the S101R mutation identified in hypertrophic cardiomyopathy obviates this response."
    Bennett H.J., Davenport J.B., Collins R.F., Trafford A.W., Pinali C., Kitmitto A.
    Biochem. J. 456:205-217(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: MEMBRANE LIPID-BINDING, CHARACTERIZATION OF VARIANT CMH17 ARG-101, DOMAIN.
  9. Cited for: VARIANTS CYS-436 AND SER-505, CHARACTERIZATION OF VARIANT SER-505.
  10. Cited for: VARIANTS CMH17 ARG-101; HIS-141 AND PHE-165, CHARACTERIZATION OF VARIANTS CMH17 ARG-101; HIS-141 AND PHE-165.

Entry informationi

Entry nameiJPH2_HUMAN
AccessioniPrimary (citable) accession number: Q9BR39
Secondary accession number(s): E1P5X1
, O95913, Q5JY74, Q9UJN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: January 17, 2003
Last modified: February 4, 2015
This is version 124 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 20
    Human chromosome 20: 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.