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Protein

Stonin-2

Gene

STON2

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

Functioni

Adapter protein involved in endocytic machinery. Involved in the synaptic vesicle recycling. May facilitate clathrin-coated vesicle uncoating.3 Publications

GO - Biological processi

  • hematopoietic progenitor cell differentiation Source: Ensembl
  • regulation of endocytosis Source: UniProtKB
  • synaptic vesicle endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Enzyme and pathway databases

SignaLinkiQ8WXE9.

Names & Taxonomyi

Protein namesi
Recommended name:
Stonin-2
Alternative name(s):
Stoned B
Gene namesi
Name:STON2
Synonyms:STN2, STNB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:30652. STON2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi738 – 7381W → A: Reduces interaction with SYT1. 1 Publication
Mutagenesisi740 – 7401K → A: Reduces interaction with SYT1. 1 Publication

Organism-specific databases

PharmGKBiPA143485624.

Polymorphism and mutation databases

BioMutaiSTON2.
DMDMi34098614.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 905905Stonin-2PRO_0000185732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei255 – 2551PhosphothreonineBy similarity
Modified residuei281 – 2811PhosphoserineCombined sources
Modified residuei287 – 2871PhosphoserineCombined sources
Modified residuei302 – 3021PhosphoserineCombined sources
Modified residuei762 – 7621PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated in vitro by PKD.1 Publication
Neddylated; deneddylated via its interaction with the COP9 signalosome (CSN) complex through TOR1A and COPS4.1 Publication
Ubiquitinated; leading to its degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8WXE9.
MaxQBiQ8WXE9.
PaxDbiQ8WXE9.
PeptideAtlasiQ8WXE9.
PRIDEiQ8WXE9.

PTM databases

iPTMnetiQ8WXE9.
PhosphoSiteiQ8WXE9.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8WXE9.
CleanExiHS_STON2.
ExpressionAtlasiQ8WXE9. baseline and differential.
GenevisibleiQ8WXE9. HS.

Organism-specific databases

HPAiHPA003086.

Interactioni

Subunit structurei

Interacts with the second C2 domain of synaptotagmins SYT1 and SYT2. Interacts with EPS15, EPS15R and ITSN1. Interacts indirectly with the AP-2 adapter complex. Interacts with TOR1A and COPS4; the interaction controls STON2 protein stability.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EPS15P4256617EBI-539742,EBI-396684
NEDD8Q158432EBI-539742,EBI-716247
Syt1P217072EBI-539742,EBI-458098From a different organism.

Protein-protein interaction databases

BioGridi124526. 44 interactions.
IntActiQ8WXE9. 39 interactions.
MINTiMINT-6179820.
STRINGi9606.ENSP00000267540.

Structurei

Secondary structure

1
905
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi314 – 3174Combined sources
Turni318 – 3203Combined sources
Helixi334 – 3374Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JXCNMR-B301-340[»]
ProteinModelPortaliQ8WXE9.
SMRiQ8WXE9. Positions 301-340, 563-864.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WXE9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini427 – 560134SHDPROSITE-ProRule annotationAdd
BLAST
Domaini568 – 878311MHDPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi313 – 3153NPF 1
Motifi329 – 3313NPF 2

Domaini

The Asn-Pro-Phe (NPF) motifs, which are found in proteins involved in the endocytic pathway, mediate the interaction with the EH domain of SYT1, SYT2, EPS15, EPS15R and ITSN1.

Sequence similaritiesi

Belongs to the Stoned B family.Curated
Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation
Contains 1 SHD (stonin homology) domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2677. Eukaryota.
ENOG410XQHF. LUCA.
GeneTreeiENSGT00830000128302.
HOGENOMiHOG000236337.
HOVERGENiHBG097637.
InParanoidiQ8WXE9.
KOiK20067.
OMAiFNPLDAC.
OrthoDBiEOG7R2BHW.
PhylomeDBiQ8WXE9.
TreeFamiTF300393.

Family and domain databases

InterProiIPR028565. MHD.
IPR012320. SHD.
IPR031228. STON2.
IPR017110. Stonin.
IPR022699. Stonin2_N.
[Graphical view]
PANTHERiPTHR10529:SF246. PTHR10529:SF246. 2 hits.
PfamiPF00928. Adap_comp_sub. 1 hit.
PF12016. Stonin2_N. 1 hit.
[Graphical view]
PIRSFiPIRSF037099. Stonin. 1 hit.
SUPFAMiSSF49447. SSF49447. 2 hits.
PROSITEiPS51072. MHD. 1 hit.
PS51070. SHD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q8WXE9-1) [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
MTTLDHVIAT HQSEWVSFNE EPPFPAHSQG GTEEHLPGLS SSPDQSESSS
60 70 80 90 100
GENHVVDGGS QDHSHSEQDD SSEKMGLISE AASPPGSPEQ PPPDLASAIS
110 120 130 140 150
NWVQFEDDTP WASTSPPHQE TAETALPLTM PCWTCPSFDS LGRCPLTSES
160 170 180 190 200
SWTTHSEDTS SPSFGCSYTD LQLINAEEQT SGQASGADST DNSSSLQEDE
210 220 230 240 250
EVEMEAISWQ ASSPAMNGHP APPVTSARFP SWVTFDDNEV SCPLPPVTSP
260 270 280 290 300
LKPNTPPSAS VIPDVPYNSM GSFKKRDRPK STLMNFSKVQ KLDISSLNRT
310 320 330 340 350
PSVTEASPWR ATNPFLNETL QDVQPSPINP FSAFFEEQER RSQNSSISST
360 370 380 390 400
TGKSQRDSLI VIYQDAISFD DSSKTQSHSD AVEKLKQLQI DDPDHFGSAT
410 420 430 440 450
LPDDDPVAWI ELDAHPPGSA RSQPRDGWPM MLRIPEKKNI MSSRHWGPIF
460 470 480 490 500
VKLTDTGYLQ LYYEQGLEKP FREFKLEICH EISEPRLQNY DENGRIHSLR
510 520 530 540 550
IDRVTYKEKK KYQPKPAVAH TAEREQVIKL GTTNYDDFLS FIHAVQDRLM
560 570 580 590 600
DLPVLSMDLS TVGLNYLEEE ITVDVRDEFS GIVSKGDNQI LQHHVLTRIH
610 620 630 640 650
ILSFLSGLAE CRLGLNDILV KGNEIVLRQD IMPTTTTKWI KLHECRFHGC
660 670 680 690 700
VDEDVFHNSR VILFNPLDAC RFELMRFRTV FAEKTLPFTL RTATSVNGAE
710 720 730 740 750
VEVQSWLRMS TGFSANRDPL TQVPCENVMI RYPVPSEWVK NFRRESVLGE
760 770 780 790 800
KSLKAKVNRG ASFGSTSVSG SEPVMRVTLG TAKYEHAFNS IVWRINRLPD
810 820 830 840 850
KNSASGHPHC FFCHLELGSD REVPSRFANH VNVEFSMPTT SASKASVRSI
860 870 880 890 900
SVEDKTDVRK WVNYSAHYSY QVALGSIWLM LPTPFVHPTT LPLLFLLAML

TMFAW
Length:905
Mass (Da):101,165
Last modified:March 1, 2002 - v1
Checksum:i59F5810DEC540CA3
GO
Isoform 2 (identifier: Q8WXE9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     872-905: VALGSIWLMLPTPFVHPTTLPLLFLLAMLTMFAW → TTETDNLPNP...PLASSIRTMV

Note: No experimental confirmation available.Curated
Show »
Length:920
Mass (Da):102,835
Checksum:i85140C1E96940A27
GO

Sequence cautioni

The sequence AAK57558.1 differs from that shown.Intron retention.Curated
The sequence AAK57558.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAK76362.1 differs from that shown. Reason: Frameshift at position 122. Curated
The sequence BAD92185.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1222TA → NS in AAK76362 (PubMed:11454741).Curated
Isoform 2 (identifier: Q8WXE9-3)
Sequence conflicti899 – 8991V → L in BAD92185 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti307 – 3071S → P.3 Publications
Corresponds to variant rs3813535 [ dbSNP | Ensembl ].
VAR_020182
Natural varianti646 – 6461R → H.
Corresponds to variant rs34323725 [ dbSNP | Ensembl ].
VAR_046643
Natural varianti694 – 6941T → A.
Corresponds to variant rs35689202 [ dbSNP | Ensembl ].
VAR_046644
Natural varianti851 – 8511S → A.
Corresponds to variant rs2241621 [ dbSNP | Ensembl ].
VAR_021912

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei872 – 90534VALGS…TMFAW → TTETDNLPNPLYCSCLPHTD LKRGSKRVVKIRWNASLEVP LASSIRTMV in isoform 2. 1 PublicationVSP_044863Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF380833 mRNA. Translation: AAK76362.1. Frameshift.
AF449430 mRNA. Translation: AAL47008.1.
AB208948 mRNA. Translation: BAD92185.1. Different initiation.
AL121769 Genomic DNA. No translation available.
AL136040 Genomic DNA. No translation available.
BC069389 mRNA. Translation: AAH69389.1.
BC117493 mRNA. Translation: AAI17494.1.
AF255309 mRNA. Translation: AAK57558.1. Sequence problems.
CCDSiCCDS58332.1. [Q8WXE9-3]
CCDS9875.1. [Q8WXE9-1]
RefSeqiNP_001243359.1. NM_001256430.1. [Q8WXE9-3]
NP_149095.2. NM_033104.3. [Q8WXE9-1]
UniGeneiHs.14248.

Genome annotation databases

EnsembliENST00000267540; ENSP00000267540; ENSG00000140022. [Q8WXE9-1]
ENST00000555447; ENSP00000450857; ENSG00000140022. [Q8WXE9-3]
ENST00000614646; ENSP00000477736; ENSG00000140022. [Q8WXE9-3]
GeneIDi85439.
KEGGihsa:85439.
UCSCiuc001xvk.3. human. [Q8WXE9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF380833 mRNA. Translation: AAK76362.1. Frameshift.
AF449430 mRNA. Translation: AAL47008.1.
AB208948 mRNA. Translation: BAD92185.1. Different initiation.
AL121769 Genomic DNA. No translation available.
AL136040 Genomic DNA. No translation available.
BC069389 mRNA. Translation: AAH69389.1.
BC117493 mRNA. Translation: AAI17494.1.
AF255309 mRNA. Translation: AAK57558.1. Sequence problems.
CCDSiCCDS58332.1. [Q8WXE9-3]
CCDS9875.1. [Q8WXE9-1]
RefSeqiNP_001243359.1. NM_001256430.1. [Q8WXE9-3]
NP_149095.2. NM_033104.3. [Q8WXE9-1]
UniGeneiHs.14248.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JXCNMR-B301-340[»]
ProteinModelPortaliQ8WXE9.
SMRiQ8WXE9. Positions 301-340, 563-864.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124526. 44 interactions.
IntActiQ8WXE9. 39 interactions.
MINTiMINT-6179820.
STRINGi9606.ENSP00000267540.

PTM databases

iPTMnetiQ8WXE9.
PhosphoSiteiQ8WXE9.

Polymorphism and mutation databases

BioMutaiSTON2.
DMDMi34098614.

Proteomic databases

EPDiQ8WXE9.
MaxQBiQ8WXE9.
PaxDbiQ8WXE9.
PeptideAtlasiQ8WXE9.
PRIDEiQ8WXE9.

Protocols and materials databases

DNASUi85439.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267540; ENSP00000267540; ENSG00000140022. [Q8WXE9-1]
ENST00000555447; ENSP00000450857; ENSG00000140022. [Q8WXE9-3]
ENST00000614646; ENSP00000477736; ENSG00000140022. [Q8WXE9-3]
GeneIDi85439.
KEGGihsa:85439.
UCSCiuc001xvk.3. human. [Q8WXE9-1]

Organism-specific databases

CTDi85439.
GeneCardsiSTON2.
HGNCiHGNC:30652. STON2.
HPAiHPA003086.
MIMi608467. gene.
neXtProtiNX_Q8WXE9.
PharmGKBiPA143485624.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2677. Eukaryota.
ENOG410XQHF. LUCA.
GeneTreeiENSGT00830000128302.
HOGENOMiHOG000236337.
HOVERGENiHBG097637.
InParanoidiQ8WXE9.
KOiK20067.
OMAiFNPLDAC.
OrthoDBiEOG7R2BHW.
PhylomeDBiQ8WXE9.
TreeFamiTF300393.

Enzyme and pathway databases

SignaLinkiQ8WXE9.

Miscellaneous databases

ChiTaRSiSTON2. human.
EvolutionaryTraceiQ8WXE9.
GenomeRNAii85439.
PROiQ8WXE9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WXE9.
CleanExiHS_STON2.
ExpressionAtlasiQ8WXE9. baseline and differential.
GenevisibleiQ8WXE9. HS.

Family and domain databases

InterProiIPR028565. MHD.
IPR012320. SHD.
IPR031228. STON2.
IPR017110. Stonin.
IPR022699. Stonin2_N.
[Graphical view]
PANTHERiPTHR10529:SF246. PTHR10529:SF246. 2 hits.
PfamiPF00928. Adap_comp_sub. 1 hit.
PF12016. Stonin2_N. 1 hit.
[Graphical view]
PIRSFiPIRSF037099. Stonin. 1 hit.
SUPFAMiSSF49447. SSF49447. 2 hits.
PROSITEiPS51072. MHD. 1 hit.
PS51070. SHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human stoned B interacts with AP-2 and synaptotagmin and facilitates clathrin-coated vesicle uncoating."
    Walther K., Krauss M., Diril M.K., Lemke S., Ricotta D., Hoening S., Kaiser S., Haucke V.
    EMBO Rep. 2:634-640(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SYT1 AND WITH THE AP-2 COMPLEX, MUTAGENESIS OF TRP-738 AND LYS-740, VARIANT PRO-307.
    Tissue: Brain.
  2. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PRO-307.
    Tissue: Spleen.
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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-307.
    Tissue: Brain.
  5. "Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery."
    Martina J.A., Bonangelino C.J., Aguilar R.C., Bonifacino J.S.
    J. Cell Biol. 153:1111-1120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 191-905 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH EPS15; EPS15R; ITSN1; SYT1 AND SYT2.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process."
    Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.
    EMBO J. 30:181-193(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SYNAPTIC VESICLE RECYCLING, INTERACTION WITH TOR1A AND COPS4, PHOSPHORYLATION, NEDDYLATION, UBIQUITINATION.
  8. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281; SER-287; SER-302 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  9. "Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity."
    Rumpf J., Simon B., Jung N., Maritzen T., Haucke V., Sattler M., Groemping Y.
    EMBO J. 27:558-569(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH EPS15.

Entry informationi

Entry nameiSTON2_HUMAN
AccessioniPrimary (citable) accession number: Q8WXE9
Secondary accession number(s): G3V2T7
, Q17R24, Q59H11, Q6NT47, Q96RI7, Q96RU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 132 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 14
    Human chromosome 14: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.