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Protein

Rab3 GTPase-activating protein catalytic subunit

Gene

RAB3GAP1

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

Functioni

Probable catalytic subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters.2 Publications

Kineticsi

  1. KM=75 µM for GTP-loaded RAB3A1 Publication

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB
  2. Rab GTPase binding Source: UniProtKB

GO - Biological processi

  1. brain development Source: BHF-UCL
  2. camera-type eye development Source: BHF-UCL
  3. establishment of protein localization to endoplasmic reticulum membrane Source: UniProtKB
  4. face morphogenesis Source: BHF-UCL
  5. hypothalamus development Source: BHF-UCL
  6. lipid particle organization Source: MGI
  7. positive regulation of endoplasmic reticulum tubular network organization Source: UniProtKB
  8. positive regulation of glutamate neurotransmitter secretion in response to membrane depolarization Source: ParkinsonsUK-UCL
  9. positive regulation of GTPase activity Source: UniProtKB
  10. regulation of calcium ion-dependent exocytosis of neurotransmitter Source: ParkinsonsUK-UCL
  11. regulation of excitatory postsynaptic membrane potential Source: ParkinsonsUK-UCL
  12. regulation of GTPase activity Source: UniProtKB
  13. regulation of short-term neuronal synaptic plasticity Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Rab3 GTPase-activating protein catalytic subunit
Alternative name(s):
RAB3 GTPase-activating protein 130 kDa subunit
Rab3-GAP p130
Short name:
Rab3-GAP
Gene namesi
Name:RAB3GAP1
Synonyms:KIAA0066, RAB3GAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:17063. RAB3GAP1.

Subcellular locationi

  1. Cytoplasm 1 Publication

  2. Note: In neurons, it is enriched in the synaptic soluble fraction.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. endoplasmic reticulum tubular network Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Warburg micro syndrome 1 (WARBM1)1 Publication

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

Disease descriptionA rare syndrome characterized by microcephaly, microphthalmia, microcornia, congenital cataracts, optic atrophy, cortical dysplasia, in particular corpus callosum hypoplasia, severe mental retardation, spastic diplegia, and hypogonadism.

See also OMIM:600118

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi619 – 6191R → A: No effect. 1 Publication
Mutagenesisi700 – 7001R → A: No effect. 1 Publication
Mutagenesisi728 – 7281R → A: Loss of function. 1 Publication
Mutagenesisi753 – 7531R → A: No effect. 1 Publication

Organism-specific databases

MIMi600118. phenotype.
Orphaneti1387. Cataract - intellectual disability - hypogonadism.
2510. Micro syndrome.
PharmGKBiPA134969639.

Polymorphism and mutation databases

BioMutaiRAB3GAP1.
DMDMi62511099.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 981980Rab3 GTPase-activating protein catalytic subunitPRO_0000191655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei590 – 5901Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15042.
PaxDbiQ15042.
PRIDEiQ15042.

PTM databases

PhosphoSiteiQ15042.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ15042.
CleanExiHS_RAB3GAP1.
ExpressionAtlasiQ15042. baseline and differential.
GenevestigatoriQ15042.

Organism-specific databases

HPAiHPA034494.
HPA034495.

Interactioni

Subunit structurei

The Rab3 GTPase-activating complex is a heterodimer composed of RAB3GAP and RAB3-GAP150. The Rab3 GTPase-activating complex interacts with DMXL2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi116590. 24 interactions.
IntActiQ15042. 2 interactions.
STRINGi9606.ENSP00000264158.

Structurei

3D structure databases

ProteinModelPortaliQ15042.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab3-GAP catalytic subunit family.Curated

Phylogenomic databases

eggNOGiNOG307494.
GeneTreeiENSGT00390000006705.
HOGENOMiHOG000253924.
HOVERGENiHBG079116.
InParanoidiQ15042.
KOiK18270.
OMAiPIQAPHW.
OrthoDBiEOG783MTK.
PhylomeDBiQ15042.
TreeFamiTF314500.

Family and domain databases

InterProiIPR026147. Rab3-GAP_cat_su.
[Graphical view]
PANTHERiPTHR21422. PTHR21422. 1 hit.
PfamiPF13890. Rab3-GTPase_cat. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15042-1) [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
MAADSEPESE VFEITDFTTA SEWERFISKV EEVLNDWKLI GNSLGKPLEK
60 70 80 90 100
GIFTSGTWEE KSDEISFADF KFSVTHHYLV QESTDKEGKD ELLEDVVPQS
110 120 130 140 150
MQDLLGMNND FPPRAHCLVR WYGLREFVVI APAAHSDAVL SESKCNLLLS
160 170 180 190 200
SVSIALGNTG CQVPLFVQIH HKWRRMYVGE CQGPGVRTDF EMVHLRKVPN
210 220 230 240 250
QYTHLSGLLD IFKSKIGCPL TPLPPVSIAI RFTYVLQDWQ QYFWPQQPPD
260 270 280 290 300
IDALVGGEVG GLEFGKLPFG ACEDPISELH LATTWPHLTE GIIVDNDVYS
310 320 330 340 350
DLDPIQAPHW SVRVRKAENP QCLLGDFVTE FFKICRRKES TDEILGRSAF
360 370 380 390 400
EEEGKETADI THALSKLTEP ASVPIHKLSV SNMVHTAKKK IRKHRGVEES
410 420 430 440 450
PLNNDVLNTI LLFLFPDAVS EKPLDGTTST DNNNPPSESE DYNLYNQFKS
460 470 480 490 500
APSDSLTYKL ALCLCMINFY HGGLKGVAHL WQEFVLEMRF RWENNFLIPG
510 520 530 540 550
LASGPPDLRC CLLHQKLQML NCCIERKKAR DEGKKTSASD VTNIYPGDAG
560 570 580 590 600
KAGDQLVPDN LKETDKEKGE VGKSWDSWSD SEEEFFECLS DTEELKGNGQ
610 620 630 640 650
ESGKKGGPKE MANLRPEGRL YQHGKLTLLH NGEPLYIPVT QEPAPMTEDL
660 670 680 690 700
LEEQSEVLAK LGTSAEGAHL RARMQSACLL SDMESFKAAN PGCSLEDFVR
710 720 730 740 750
WYSPRDYIEE EVIDEKGNVV LKGELSARMK IPSNMWVEAW ETAKPIPARR
760 770 780 790 800
QRRLFDDTRE AEKVLHYLAI QKPADLARHL LPCVIHAAVL KVKEEESLEN
810 820 830 840 850
ISSVKKIIKQ IISHSSKVLH FPNPEDKKLE EIIHQITNVE ALIARARSLK
860 870 880 890 900
AKFGTEKCEQ EEEKEDLERF VSCLLEQPEV LVTGAGRGHA GRIIHKLFVN
910 920 930 940 950
AQRAAAMTPP EEELKRMGSP EERRQNSVSD FPPPAGREFI LRTTVPRPAP
960 970 980
YSKALPQRMY SVLTKEDFRL AGAFSSDTSF F
Length:981
Mass (Da):110,524
Last modified:January 23, 2007 - v3
Checksum:i0673611C5C49641C
GO
Isoform 2 (identifier: Q15042-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     903-903: R → RLTESSDE

Note: No experimental confirmation available.

Show »
Length:988
Mass (Da):111,285
Checksum:i53B04747CCD4B2D8
GO
Isoform 3 (identifier: Q15042-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: MAADSEPESEVFEITDFTTASEWERFISKVEEVLNDWKLIGNSLGKPLEK → MFSLIS
     972-981: GAFSSDTSFF → VKIIDGDV

Note: No experimental confirmation available.

Show »
Length:935
Mass (Da):105,296
Checksum:i15466F1985DFFB72
GO

Sequence cautioni

The sequence BC071602 differs from that shown. Reason: Frameshift at position 211. Curated
The sequence CAH56411.1 differs from that shown.Probable cloning artifact.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti598 – 5981N → S.1 Publication
Corresponds to variant rs10445686 [ dbSNP | Ensembl ].
VAR_051716

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5050MAADS…KPLEK → MFSLIS in isoform 3. 1 PublicationVSP_054475Add
BLAST
Alternative sequencei903 – 9031R → RLTESSDE in isoform 2. 1 PublicationVSP_054068
Alternative sequencei972 – 98110GAFSSDTSFF → VKIIDGDV in isoform 3. 1 PublicationVSP_054476

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31886 mRNA. Translation: BAA06684.1.
AC017031 Genomic DNA. No translation available.
AC020602 Genomic DNA. No translation available.
BC022977 mRNA. Translation: AAH22977.1.
BC071602 mRNA. No translation available.
BC146809 mRNA. Translation: AAI46810.1.
AL096752 mRNA. Translation: CAH56411.1. Sequence problems.
CCDSiCCDS33294.1. [Q15042-1]
CCDS54402.1. [Q15042-3]
RefSeqiNP_001165906.1. NM_001172435.1. [Q15042-3]
NP_036365.1. NM_012233.2. [Q15042-1]
UniGeneiHs.306327.

Genome annotation databases

EnsembliENST00000264158; ENSP00000264158; ENSG00000115839. [Q15042-1]
ENST00000442034; ENSP00000411418; ENSG00000115839. [Q15042-3]
ENST00000539493; ENSP00000444306; ENSG00000115839. [Q15042-4]
GeneIDi22930.
KEGGihsa:22930.
UCSCiuc002tuj.3. human. [Q15042-1]

Polymorphism and mutation databases

BioMutaiRAB3GAP1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31886 mRNA. Translation: BAA06684.1.
AC017031 Genomic DNA. No translation available.
AC020602 Genomic DNA. No translation available.
BC022977 mRNA. Translation: AAH22977.1.
BC071602 mRNA. No translation available.
BC146809 mRNA. Translation: AAI46810.1.
AL096752 mRNA. Translation: CAH56411.1. Sequence problems.
CCDSiCCDS33294.1. [Q15042-1]
CCDS54402.1. [Q15042-3]
RefSeqiNP_001165906.1. NM_001172435.1. [Q15042-3]
NP_036365.1. NM_012233.2. [Q15042-1]
UniGeneiHs.306327.

3D structure databases

ProteinModelPortaliQ15042.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116590. 24 interactions.
IntActiQ15042. 2 interactions.
STRINGi9606.ENSP00000264158.

PTM databases

PhosphoSiteiQ15042.

Polymorphism and mutation databases

BioMutaiRAB3GAP1.
DMDMi62511099.

Proteomic databases

MaxQBiQ15042.
PaxDbiQ15042.
PRIDEiQ15042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264158; ENSP00000264158; ENSG00000115839. [Q15042-1]
ENST00000442034; ENSP00000411418; ENSG00000115839. [Q15042-3]
ENST00000539493; ENSP00000444306; ENSG00000115839. [Q15042-4]
GeneIDi22930.
KEGGihsa:22930.
UCSCiuc002tuj.3. human. [Q15042-1]

Organism-specific databases

CTDi22930.
GeneCardsiGC02P135809.
HGNCiHGNC:17063. RAB3GAP1.
HPAiHPA034494.
HPA034495.
MIMi600118. phenotype.
602536. gene.
neXtProtiNX_Q15042.
Orphaneti1387. Cataract - intellectual disability - hypogonadism.
2510. Micro syndrome.
PharmGKBiPA134969639.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG307494.
GeneTreeiENSGT00390000006705.
HOGENOMiHOG000253924.
HOVERGENiHBG079116.
InParanoidiQ15042.
KOiK18270.
OMAiPIQAPHW.
OrthoDBiEOG783MTK.
PhylomeDBiQ15042.
TreeFamiTF314500.

Miscellaneous databases

ChiTaRSiRAB3GAP1. human.
GeneWikiiRAB3GAP1.
GenomeRNAii22930.
NextBioi35462401.
PROiQ15042.
SOURCEiSearch...

Gene expression databases

BgeeiQ15042.
CleanExiHS_RAB3GAP1.
ExpressionAtlasiQ15042. baseline and differential.
GenevestigatoriQ15042.

Family and domain databases

InterProiIPR026147. Rab3-GAP_cat_su.
[Graphical view]
PANTHERiPTHR21422. PTHR21422. 1 hit.
PfamiPF13890. Rab3-GTPase_cat. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 439-981 (ISOFORM 1), VARIANT SER-598.
    Tissue: Placenta.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 764-981.
    Tissue: Testis.
  5. "Isolation and characterization of a GTPase activating protein specific for the Rab3 subfamily of small G proteins."
    Fukui K., Sasaki T., Imazumi K., Matsuura Y., Nakanishi H., Takai Y.
    J. Biol. Chem. 272:4655-4658(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. "Localization of the Rab3 small G protein regulators in nerve terminals and their involvement in Ca2+-dependent exocytosis."
    Oishi H., Sasaki T., Nagano F., Ikeda W., Ohya T., Wada M., Ide N., Nakanishi H., Takai Y.
    J. Biol. Chem. 273:34580-34585(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP."
    Clabecq A., Henry J.-P., Darchen F.
    J. Biol. Chem. 275:31786-31791(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-619; ARG-700; ARG-728 AND ARG-753.
  8. Cited for: INVOLVEMENT IN WARBM1.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRB3GP_HUMAN
AccessioniPrimary (citable) accession number: Q15042
Secondary accession number(s): A6H8Z3
, C9J837, Q659F5, Q8TBB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 107 of the entry and version 3 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 2
    Human chromosome 2: 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.