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Protein

Ras-related GTP-binding protein C

Gene

RRAGC

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

Functioni

Guanine nucleotide-binding protein forming heterodimeric Rag complexes required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi68 – 758GTPBy similarity
Nucleotide bindingi116 – 1205GTPBy similarity
Nucleotide bindingi178 – 1814GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: HGNC
  4. magnesium ion binding Source: UniProtKB
  5. protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cell growth Source: UniProtKB
  3. cellular protein localization Source: UniProtKB
  4. cellular response to amino acid stimulus Source: UniProtKB
  5. cellular response to starvation Source: GO_Central
  6. positive regulation of TOR signaling Source: GO_Central
  7. regulation of autophagy Source: GO_Central
  8. RNA splicing Source: UniProtKB
  9. small GTPase mediated signal transduction Source: UniProtKB
  10. transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related GTP-binding protein C
Short name:
Rag C
Short name:
RagC
Alternative name(s):
GTPase-interacting protein 2
TIB929
Gene namesi
Name:RRAGCImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:19902. RRAGC.

Subcellular locationi

Cytoplasm. Nucleus. Lysosome
Note: Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state of associated RRAGA.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. EGO complex Source: GO_Central
  3. Gtr1-Gtr2 GTPase complex Source: GO_Central
  4. intracellular membrane-bounded organelle Source: HPA
  5. lysosome Source: UniProtKB
  6. nucleoplasm Source: HPA
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lysosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi75 – 751S → L: Increased RPTOR-binding. 1 Publication
Mutagenesisi120 – 1201Q → L: Decreased RPTOR-binding. 1 Publication

Organism-specific databases

PharmGKBiPA134862062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 399398Ras-related GTP-binding protein CPRO_0000239951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei96 – 961PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9HB90.
PaxDbiQ9HB90.
PeptideAtlasiQ9HB90.
PRIDEiQ9HB90.

PTM databases

PhosphoSiteiQ9HB90.

Expressioni

Gene expression databases

BgeeiQ9HB90.
CleanExiHS_RRAGC.
ExpressionAtlasiQ9HB90. baseline and differential.
GenevestigatoriQ9HB90.

Organism-specific databases

HPAiHPA018247.
HPA055489.

Interactioni

Subunit structurei

Forms a heterodimer with RRAGA, in a sequence-independent manner, and RRAGB. Heterodimerization stabilizes proteins of the heterodimer. In complex with RRAGA or RRAGB, interacts with RPTOR; this interaction is particularly efficient with GTP-loaded RRAGB and GDP-loaded RRAGC. Interacts with NOL8. Interacts with SH3BP4; the interaction with this negative regulator is most probably direct, preferentially occurs with the inactive GDP-bound form of RRAGB, is negatively regulated by amino acids and prevents interaction with RPTOR (PubMed:11073942, PubMed:14660641, PubMed:18497260, PubMed:22575674). The Rag heterodimer interacts with SLC38A9; the probable amino acid sensor (PubMed:25561175, PubMed:25567906).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RRAGAQ7L52318EBI-752390,EBI-752376
RRAGBQ5VZM25EBI-752390,EBI-993049
SLC38A9Q8NBW49EBI-752390,EBI-9978316

Protein-protein interaction databases

BioGridi122074. 19 interactions.
IntActiQ9HB90. 15 interactions.
MINTiMINT-1451634.
STRINGi9606.ENSP00000362092.

Structurei

Secondary structure

1
399
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi63 – 697Combined sources
Helixi74 – 829Combined sources
Helixi87 – 926Combined sources
Beta strandi100 – 1045Combined sources
Beta strandi112 – 1165Combined sources
Helixi130 – 1356Combined sources
Beta strandi138 – 1458Combined sources
Helixi151 – 16717Combined sources
Beta strandi172 – 1787Combined sources
Helixi180 – 1823Combined sources
Helixi185 – 20521Combined sources
Beta strandi213 – 2186Combined sources
Helixi224 – 23512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LLUX-ray1.40A60-237[»]
ProteinModelPortaliQ9HB90.
SMRiQ9HB90. Positions 57-367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HB90.

Family & Domainsi

Sequence similaritiesi

Belongs to the GTR/RAG GTP-binding protein family.Curated

Phylogenomic databases

eggNOGiNOG250062.
GeneTreeiENSGT00550000074708.
HOGENOMiHOG000203695.
HOVERGENiHBG059482.
InParanoidiQ9HB90.
KOiK16186.
OMAiVFQKMSP.
OrthoDBiEOG7FXZZ8.
PhylomeDBiQ9HB90.
TreeFamiTF300659.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006762. Gtr1_RagA.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11259. PTHR11259. 1 hit.
PfamiPF04670. Gtr1_RagA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9HB90-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLQYGAEET PLAGSYGAAD SFPKDFGYGV EEEEEEAAAA GGGVGAGAGG
60 70 80 90 100
GCGPGGADSS KPRILLMGLR RSGKSSIQKV VFHKMSPNET LFLESTNKIY
110 120 130 140 150
KDDISNSSFV NFQIWDFPGQ MDFFDPTFDY EMIFRGTGAL IYVIDAQDDY
160 170 180 190 200
MEALTRLHIT VSKAYKVNPD MNFEVFIHKV DGLSDDHKIE TQRDIHQRAN
210 220 230 240 250
DDLADAGLEK LHLSFYLTSI YDHSIFEAFS KVVQKLIPQL PTLENLLNIF
260 270 280 290 300
ISNSGIEKAF LFDVVSKIYI ATDSSPVDMQ SYELCCDMID VVIDVSCIYG
310 320 330 340 350
LKEDGSGSAY DKESMAIIKL NNTTVLYLKE VTKFLALVCI LREESFERKG
360 370 380 390
LIDYNFHCFR KAIHEVFEVG VTSHRSCGHQ TSASSLKALT HNGTPRNAI
Length:399
Mass (Da):44,224
Last modified:March 1, 2001 - v1
Checksum:i35B3171253CC69CF
GO

Sequence cautioni

The sequence BAB14548.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061A → S in AAG45221 (PubMed:11145883).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323609 mRNA. Translation: AAG45221.1.
AF272035 mRNA. Translation: AAG32662.1.
AL139260 Genomic DNA. Translation: CAI23049.1.
BC016668 mRNA. Translation: AAH16668.1.
AK023373 mRNA. Translation: BAB14548.1. Different initiation.
CCDSiCCDS430.1.
RefSeqiNP_001258780.1. NM_001271851.1.
NP_071440.1. NM_022157.3.
UniGeneiHs.532461.

Genome annotation databases

EnsembliENST00000373001; ENSP00000362092; ENSG00000116954.
GeneIDi64121.
KEGGihsa:64121.
UCSCiuc001ccq.3. human.

Polymorphism databases

DMDMi74752776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323609 mRNA. Translation: AAG45221.1.
AF272035 mRNA. Translation: AAG32662.1.
AL139260 Genomic DNA. Translation: CAI23049.1.
BC016668 mRNA. Translation: AAH16668.1.
AK023373 mRNA. Translation: BAB14548.1. Different initiation.
CCDSiCCDS430.1.
RefSeqiNP_001258780.1. NM_001271851.1.
NP_071440.1. NM_022157.3.
UniGeneiHs.532461.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LLUX-ray1.40A60-237[»]
ProteinModelPortaliQ9HB90.
SMRiQ9HB90. Positions 57-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122074. 19 interactions.
IntActiQ9HB90. 15 interactions.
MINTiMINT-1451634.
STRINGi9606.ENSP00000362092.

PTM databases

PhosphoSiteiQ9HB90.

Polymorphism databases

DMDMi74752776.

Proteomic databases

MaxQBiQ9HB90.
PaxDbiQ9HB90.
PeptideAtlasiQ9HB90.
PRIDEiQ9HB90.

Protocols and materials databases

DNASUi64121.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373001; ENSP00000362092; ENSG00000116954.
GeneIDi64121.
KEGGihsa:64121.
UCSCiuc001ccq.3. human.

Organism-specific databases

CTDi64121.
GeneCardsiGC01M039303.
HGNCiHGNC:19902. RRAGC.
HPAiHPA018247.
HPA055489.
MIMi608267. gene.
neXtProtiNX_Q9HB90.
PharmGKBiPA134862062.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG250062.
GeneTreeiENSGT00550000074708.
HOGENOMiHOG000203695.
HOVERGENiHBG059482.
InParanoidiQ9HB90.
KOiK16186.
OMAiVFQKMSP.
OrthoDBiEOG7FXZZ8.
PhylomeDBiQ9HB90.
TreeFamiTF300659.

Miscellaneous databases

ChiTaRSiRRAGC. human.
EvolutionaryTraceiQ9HB90.
GeneWikiiRRAGC.
GenomeRNAii64121.
NextBioi65996.
PROiQ9HB90.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HB90.
CleanExiHS_RRAGC.
ExpressionAtlasiQ9HB90. baseline and differential.
GenevestigatoriQ9HB90.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006762. Gtr1_RagA.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11259. PTHR11259. 1 hit.
PfamiPF04670. Gtr1_RagA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Adenovirus immunoregulatory genes and their cellular targets."
    Horwitz M.S.
    Virology 279:1-8(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B."
    Sekiguchi T., Hirose E., Nakashima N., Ii M., Nishimoto T.
    J. Biol. Chem. 276:7246-7257(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RRAGA AND RRAGB, SUBCELLULAR LOCATION, GTP-BINDING.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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].
    Tissue: LymphImported.
  5. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 266-399.
    Tissue: OvaryImported.
  6. "A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D."
    Sekiguchi T., Todaka Y., Wang Y., Hirose E., Nakashima N., Nishimoto T.
    J. Biol. Chem. 279:8343-8350(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOL8 AND RRAGA.
  7. "The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1."
    Sancak Y., Peterson T.R., Shaul Y.D., Lindquist R.A., Thoreen C.C., Bar-Peled L., Sabatini D.M.
    Science 320:1496-1501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPTOR, MUTAGENESIS OF SER-75 AND GLN-120.
  8. "Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids."
    Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.
    Cell 141:290-303(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1 signaling."
    Kim Y.M., Stone M., Hwang T.H., Kim Y.G., Dunlevy J.R., Griffin T.J., Kim D.H.
    Mol. Cell 46:833-846(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH3BP4.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. Cited for: INTERACTION WITH SLC38A9.
  13. Cited for: INTERACTION WITH SLC38A9.

Entry informationi

Entry nameiRRAGC_HUMAN
AccessioniPrimary (citable) accession number: Q9HB90
Secondary accession number(s): Q9H202, Q9H8Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 1, 2001
Last modified: March 4, 2015
This is version 109 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 1
    Human chromosome 1: 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.