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Protein

Transcription factor IIIB 50 kDa subunit

Gene

BRF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites.3 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi7 – 71ZincBy similarity
Metal bindingi10 – 101ZincBy similarity
Metal bindingi28 – 281ZincBy similarity
Metal bindingi31 – 311ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2 – 3635TFIIB-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor IIIB 50 kDa subunit
Short name:
TFIIIB50
Short name:
hTFIIIB50
Alternative name(s):
B-related factor 2
Short name:
BRF-2
hBRFU
Gene namesi
Name:BRF2
Synonyms:BRFU
ORF Names:PRO1470
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:17298. BRF2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164741329.

Polymorphism and mutation databases

BioMutaiBRF2.
DMDMi74734246.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419Transcription factor IIIB 50 kDa subunitPRO_0000337187Add
BLAST

Proteomic databases

MaxQBiQ9HAW0.
PaxDbiQ9HAW0.
PRIDEiQ9HAW0.

PTM databases

iPTMnetiQ9HAW0.
PhosphoSiteiQ9HAW0.

Expressioni

Inductioni

Down-regulated by epigallocatechin gallate (EGCG) treatment.1 Publication

Gene expression databases

BgeeiQ9HAW0.
CleanExiHS_BRF2.
ExpressionAtlasiQ9HAW0. baseline and differential.
GenevisibleiQ9HAW0. HS.

Organism-specific databases

HPAiCAB019269.
HPA023378.

Interactioni

Subunit structurei

Component of TFIIIB complex. The TFIIIB complex has two activities, alpha and beta. The TFIIIB-alpha activity complex is composed of TBP, BDP1, and a complex containing both BRF2 and at least four stably associated proteins; this complex inhibits the transcription by pol III via its phosphorylation by CK2; YY1 facilitates the TFIIIB-alpha complex formation. BRF2 recruitment to the TATA box containing small nuclear RNA (snRNA) gene templates is TBP-dependent. Interacts with TBP; this interaction with TBP mediates its TATA-box recruitment of these promoters. Interacts with TBP and the BURE sequence (GC-rich sequence downstream from the TATA box) to form a strong ternary complex which is joined by BDP1; this ternary complex stimulates pol III transcription. Forms a trimeric complex composed of TBP, BRF2 and mini-SNAPc complex (SNAP43, SNAP50, and the N-terminal third of SNAP190) on the promoter. Assembly of the TBP-BRF2 complex is stimulated by SNAP190. Interacts with MAF1 and SNAPC4.8 Publications

Protein-protein interaction databases

BioGridi120578. 30 interactions.
STRINGi9606.ENSP00000220659.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi67 – 8216Combined sources
Helixi87 – 10115Combined sources
Helixi104 – 1074Combined sources
Helixi111 – 12818Combined sources
Helixi135 – 1428Combined sources
Helixi146 – 15914Combined sources
Helixi169 – 17810Combined sources
Helixi191 – 1933Combined sources
Helixi197 – 21317Combined sources
Helixi223 – 23715Combined sources
Helixi239 – 2424Combined sources
Helixi247 – 2537Combined sources
Helixi262 – 27716Combined sources
Helixi281 – 2844Combined sources
Turni285 – 2873Combined sources
Turni290 – 2934Combined sources
Helixi294 – 2963Combined sources
Helixi297 – 3026Combined sources
Helixi304 – 31310Combined sources
Turni360 – 3623Combined sources
Helixi386 – 3905Combined sources
Helixi396 – 40611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ROCX-ray1.90A62-419[»]
4RODX-ray2.70A62-419[»]
4ROEX-ray2.20A62-419[»]
ProteinModelPortaliQ9HAW0.
SMRiQ9HAW0. Positions 66-236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati72 – 157861Add
BLAST
Repeati173 – 249772Add
BLAST

Sequence similaritiesi

Belongs to the TFIIB family.Curated
Contains 1 TFIIB-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2 – 3635TFIIB-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1598. Eukaryota.
COG1405. LUCA.
GeneTreeiENSGT00390000002288.
HOGENOMiHOG000095260.
HOVERGENiHBG107537.
InParanoidiQ9HAW0.
KOiK15197.
OMAiCMLKPPK.
OrthoDBiEOG773XGF.
PhylomeDBiQ9HAW0.
TreeFamiTF331596.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR013763. Cyclin-like.
IPR000812. TFIIB.
IPR013137. Znf_TFIIB.
[Graphical view]
PANTHERiPTHR11618. PTHR11618. 1 hit.
PfamiPF08271. TF_Zn_Ribbon. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 1 hit.
PROSITEiPS51134. ZF_TFIIB. 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: Q9HAW0-1) [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
MPGRGRCPDC GSTELVEDSH YSQSQLVCSD CGCVVTEGVL TTTFSDEGNL
60 70 80 90 100
REVTYSRSTG ENEQVSRSQQ RGLRRVRDLC RVLQLPPTFE DTAVAYYQQA
110 120 130 140 150
YRHSGIRAAR LQKKEVLVGC CVLITCRQHN WPLTMGAICT LLYADLDVFS
160 170 180 190 200
STYMQIVKLL GLDVPSLCLA ELVKTYCSSF KLFQASPSVP AKYVEDKEKM
210 220 230 240 250
LSRTMQLVEL ANETWLVTGR HPLPVITAAT FLAWQSLQPA DRLSCSLARF
260 270 280 290 300
CKLANVDLPY PASSRLQELL AVLLRMAEQL AWLRVLRLDK RSVVKHIGDL
310 320 330 340 350
LQHRQSLVRS AFRDGTAEVE TREKEPPGWG QGQGEGEVGN NSLGLPQGKR
360 370 380 390 400
PASPALLLPP CMLKSPKRIC PVPPVSTVTG DENISDSEIE QYLRTPQEVR
410
DFQRAQAARQ AATSVPNPP
Length:419
Mass (Da):46,533
Last modified:March 1, 2001 - v1
Checksum:i90A39F72DBA14888
GO
Isoform 2 (identifier: Q9HAW0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     10-32: Missing.

Note: No experimental confirmation available.
Show »
Length:396
Mass (Da):44,104
Checksum:iBBD3AA1989495531
GO

Sequence cautioni

The sequence AAG35486.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531Y → C in BAA91975 (PubMed:14702039).Curated
Sequence conflicti376 – 3761S → F in AAG35669 (PubMed:11121026).Curated
Sequence conflicti379 – 3791T → I in BAG57607 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei10 – 3223Missing in isoform 2. 1 PublicationVSP_056834Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF298153 mRNA. Translation: AAG30222.1.
AF206673 mRNA. Translation: AAG35669.2.
AK001914 mRNA. Translation: BAA91975.1.
AK294337 mRNA. Translation: BAG57607.1.
AK315420 mRNA. Translation: BAG37809.1.
CH471080 Genomic DNA. Translation: EAW63351.1.
CH471080 Genomic DNA. Translation: EAW63352.1.
CH471080 Genomic DNA. Translation: EAW63353.1.
BC010648 mRNA. Translation: AAH10648.1.
AF130058 mRNA. Translation: AAG35486.1. Different initiation.
CCDSiCCDS6098.1. [Q9HAW0-1]
RefSeqiNP_060780.2. NM_018310.3. [Q9HAW0-1]
UniGeneiHs.709301.

Genome annotation databases

EnsembliENST00000220659; ENSP00000220659; ENSG00000104221. [Q9HAW0-1]
GeneIDi55290.
KEGGihsa:55290.
UCSCiuc003xkk.4. human. [Q9HAW0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF298153 mRNA. Translation: AAG30222.1.
AF206673 mRNA. Translation: AAG35669.2.
AK001914 mRNA. Translation: BAA91975.1.
AK294337 mRNA. Translation: BAG57607.1.
AK315420 mRNA. Translation: BAG37809.1.
CH471080 Genomic DNA. Translation: EAW63351.1.
CH471080 Genomic DNA. Translation: EAW63352.1.
CH471080 Genomic DNA. Translation: EAW63353.1.
BC010648 mRNA. Translation: AAH10648.1.
AF130058 mRNA. Translation: AAG35486.1. Different initiation.
CCDSiCCDS6098.1. [Q9HAW0-1]
RefSeqiNP_060780.2. NM_018310.3. [Q9HAW0-1]
UniGeneiHs.709301.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ROCX-ray1.90A62-419[»]
4RODX-ray2.70A62-419[»]
4ROEX-ray2.20A62-419[»]
ProteinModelPortaliQ9HAW0.
SMRiQ9HAW0. Positions 66-236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120578. 30 interactions.
STRINGi9606.ENSP00000220659.

PTM databases

iPTMnetiQ9HAW0.
PhosphoSiteiQ9HAW0.

Polymorphism and mutation databases

BioMutaiBRF2.
DMDMi74734246.

Proteomic databases

MaxQBiQ9HAW0.
PaxDbiQ9HAW0.
PRIDEiQ9HAW0.

Protocols and materials databases

DNASUi55290.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000220659; ENSP00000220659; ENSG00000104221. [Q9HAW0-1]
GeneIDi55290.
KEGGihsa:55290.
UCSCiuc003xkk.4. human. [Q9HAW0-1]

Organism-specific databases

CTDi55290.
GeneCardsiBRF2.
HGNCiHGNC:17298. BRF2.
HPAiCAB019269.
HPA023378.
MIMi607013. gene.
neXtProtiNX_Q9HAW0.
PharmGKBiPA164741329.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1598. Eukaryota.
COG1405. LUCA.
GeneTreeiENSGT00390000002288.
HOGENOMiHOG000095260.
HOVERGENiHBG107537.
InParanoidiQ9HAW0.
KOiK15197.
OMAiCMLKPPK.
OrthoDBiEOG773XGF.
PhylomeDBiQ9HAW0.
TreeFamiTF331596.

Enzyme and pathway databases

ReactomeiR-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Miscellaneous databases

ChiTaRSiBRF2. human.
GeneWikiiBRF2_(gene).
GenomeRNAii55290.
PROiQ9HAW0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HAW0.
CleanExiHS_BRF2.
ExpressionAtlasiQ9HAW0. baseline and differential.
GenevisibleiQ9HAW0. HS.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR013763. Cyclin-like.
IPR000812. TFIIB.
IPR013137. Znf_TFIIB.
[Graphical view]
PANTHERiPTHR11618. PTHR11618. 1 hit.
PfamiPF08271. TF_Zn_Ribbon. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 1 hit.
PROSITEiPS51134. ZF_TFIIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Different human TFIIIB activities direct RNA polymerase III transcription from TATA-containing and TATA-less promoters."
    Schramm L., Pendergrast P.S., Sun Y., Hernandez N.
    Genes Dev. 14:2650-2663(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  2. "A stable complex of a novel transcription factor IIB- related factor, human TFIIIB50, and associated proteins mediate selective transcription by RNA polymerase III of genes with upstream promoter elements."
    Teichmann M., Wang Z., Roeder R.G.
    Proc. Natl. Acad. Sci. U.S.A. 97:14200-14205(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Amygdala, Placenta and Umbilical cord blood.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Eye.
  6. "Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs."
    Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.
    Genome Res. 11:1392-1403(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-419 (ISOFORM 1).
    Tissue: Fetal liver.
  7. "BRFU, a TFIIB-like factor, is directly recruited to the TATA-box of polymerase III small nuclear RNA gene promoters through its interaction with TATA-binding protein."
    Cabart P., Murphy S.
    J. Biol. Chem. 276:43056-43064(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TBP.
  8. "Assembly of human small nuclear RNA gene-specific transcription factor IIIB complex de novo on and off promoter."
    Cabart P., Murphy S.
    J. Biol. Chem. 277:26831-26838(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TFIIIB-ALPHA COMPLEX.
  9. "Redundant cooperative interactions for assembly of a human U6 transcription initiation complex."
    Ma B., Hernandez N.
    Mol. Cell. Biol. 22:8067-8078(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "The small nuclear RNA-activating protein 190 Myb DNA binding domain stimulates TATA box-binding protein-TATA box recognition."
    Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.
    J. Biol. Chem. 278:18649-18657(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAPC4, SUBUNIT.
  11. "A minimal RNA polymerase III transcription system from human cells reveals positive and negative regulatory roles for CK2."
    Hu P., Wu S., Hernandez N.
    Mol. Cell 12:699-709(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  12. "Structure-function analysis of the human TFIIB-related factor II protein reveals an essential role for the C-terminal domain in RNA polymerase III transcription."
    Saxena A., Ma B., Schramm L., Hernandez N.
    Mol. Cell. Biol. 25:9406-9418(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  13. "A role for Yin Yang-1 (YY1) in the assembly of snRNA transcription complexes."
    Emran F., Florens L., Ma B., Swanson S.K., Washburn M.P., Hernandez N.
    Gene 377:96-108(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  14. "Human Maf1 negatively regulates RNA polymerase III transcription via the TFIIB family members Brf1 and Brf2."
    Rollins J., Veras I., Cabarcas S., Willis I., Schramm L.
    Int. J. Biol. Sci. 3:292-302(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAF1, SUBCELLULAR LOCATION.
  15. "The green tea component EGCG inhibits RNA polymerase III transcription."
    Jacob J., Cabarcas S., Veras I., Zaveri N., Schramm L.
    Biochem. Biophys. Res. Commun. 360:778-783(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiBRF2_HUMAN
AccessioniPrimary (citable) accession number: Q9HAW0
Secondary accession number(s): B2RD62
, B4DFZ6, D3DSW6, Q9H2Y3, Q9H3B3, Q9NUY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 134 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 8
    Human chromosome 8: 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

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.