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Protein

Transcription termination factor 1

Gene

TTF1

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

Functioni

Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity.1 Publication

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. chromatin remodeling Source: Ensembl
  2. DNA-templated transcription, termination Source: UniProtKB
  3. gene expression Source: Reactome
  4. negative regulation of DNA replication Source: UniProtKB-KW
  5. negative regulation of gene expression, epigenetic Source: Reactome
  6. regulation of gene expression, epigenetic Source: Reactome
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  8. termination of RNA polymerase I transcription Source: Reactome
  9. transcription from RNA polymerase I promoter Source: Reactome
  10. transcription initiation from RNA polymerase I promoter Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

DNA replication inhibitor

Keywords - Biological processi

Transcription, Transcription regulation, Transcription termination

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_953. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription termination factor 1
Short name:
TTF-1
Alternative name(s):
RNA polymerase I termination factor
Transcription termination factor I
Short name:
TTF-I
Gene namesi
Name:TTF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:12397. TTF1.

Subcellular locationi

Nucleus. Nucleusnucleolus By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleolus Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 905905Transcription termination factor 1PRO_0000250472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine2 Publications
Modified residuei240 – 2401Phosphoserine1 Publication
Modified residuei403 – 4031Phosphoserine1 Publication
Modified residuei476 – 4761Phosphotyrosine1 Publication
Modified residuei478 – 4781Phosphoserine1 Publication
Modified residuei481 – 4811Phosphoserine3 Publications
Modified residuei487 – 4871Phosphoserine5 Publications
Modified residuei872 – 8721Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15361.
PaxDbiQ15361.
PRIDEiQ15361.

PTM databases

PhosphoSiteiQ15361.

Expressioni

Gene expression databases

BgeeiQ15361.
CleanExiHS_TTF1.
ExpressionAtlasiQ15361. baseline and differential.
GenevestigatoriQ15361.

Organism-specific databases

HPAiHPA051105.
HPA054837.

Interactioni

Subunit structurei

Oligomer. The oligomeric structure enables to interact simultaneously with two separate DNA fragments. Interacts with BAZ2A/TIP5.

Protein-protein interaction databases

BioGridi113121. 12 interactions.
IntActiQ15361. 2 interactions.
MINTiMINT-1181965.
STRINGi9606.ENSP00000333920.

Structurei

3D structure databases

ProteinModelPortaliQ15361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini612 – 66150Myb-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini661 – 74585Myb-like 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 223223N-terminal region (NRD)By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 215Poly-Lys
Compositional biasi216 – 22510Poly-Lys
Compositional biasi272 – 28211Poly-LysAdd
BLAST
Compositional biasi329 – 33810Poly-Lys

Domaini

The N-terminal region (NRD) inhibits DNA-binding via its interaction with the C-terminal region.By similarity

Sequence similaritiesi

Contains 2 Myb-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG262979.
GeneTreeiENSGT00530000063659.
HOGENOMiHOG000231811.
HOVERGENiHBG104803.
InParanoidiQ15361.
KOiK15225.
OMAiDYLYETT.
OrthoDBiEOG7ZKS9N.
PhylomeDBiQ15361.
TreeFamiTF333537.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
InterProiIPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR001005. SANT/Myb.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
[Graphical view]
PROSITEiPS50090. MYB_LIKE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15361-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGESSRFEI HTPVSDKKKK KCSIHKERPQ KHSHEIFRDS SLVNEQSQIT
60 70 80 90 100
RRKKRKKDFQ HLISSPLKKS RICDETANAT STLKKRKKRR YSALEVDEEA
110 120 130 140 150
GVTVVLVDKE NINNTPKHFR KDVDVVCVDM SIEQKLPRKP KTDKFQVLAK
160 170 180 190 200
SHAHKSEALH SKVREKKNKK HQRKAASWES QRARDTLPQS ESHQEESWLS
210 220 230 240 250
VGPGGEITEL PASAHKNKSK KKKKKSSNRE YETLAMPEGS QAGREAGTDM
260 270 280 290 300
QESQPTVGLD DETPQLLGPT HKKKSKKKKK KKSNHQEFEA LAMPEGSQVG
310 320 330 340 350
SEVGADMQES RPAVGLHGET AGIPAPAYKN KSKKKKKKSN HQEFEAVAMP
360 370 380 390 400
ESLESAYPEG SQVGSEVGTV EGSTALKGFK ESNSTKKKSK KRKLTSVKRA
410 420 430 440 450
RVSGDDFSVP SKNSESTLFD SVEGDGAMME EGVKSRPRQK KTQACLASKH
460 470 480 490 500
VQEAPRLEPA NEEHNVETAE DSEIRYLSAD SGDADDSDAD LGSAVKQLQE
510 520 530 540 550
FIPNIKDRAT STIKRMYRDD LERFKEFKAQ GVAIKFGKFS VKENKQLEKN
560 570 580 590 600
VEDFLALTGI ESADKLLYTD RYPEEKSVIT NLKRRYSFRL HIGRNIARPW
610 620 630 640 650
KLIYYRAKKM FDVNNYKGRY SEGDTEKLKM YHSLLGNDWK TIGEMVARSS
660 670 680 690 700
LSVALKFSQI SSQRNRGAWS KSETRKLIKA VEEVILKKMS PQELKEVDSK
710 720 730 740 750
LQENPESCLS IVREKLYKGI SWVEVEAKVQ TRNWMQCKSK WTEILTKRMT
760 770 780 790 800
NGRRIYYGMN ALRAKVSLIE RLYEINVEDT NEIDWEDLAS AIGDVPPSYV
810 820 830 840 850
QTKFSRLKAV YVPFWQKKTF PEIIDYLYET TLPLLKEKLE KMMEKKGTKI
860 870 880 890 900
QTPAAPKQVF PFRDIFYYED DSEGEDIEKE SEGQAPCMAH ACNSSTLGGQ

GRWII
Length:905
Mass (Da):103,051
Last modified:September 11, 2007 - v3
Checksum:i12F829CEFDDF96E8
GO

Sequence cautioni

The sequence AAH62692.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI04640.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI27670.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence AAI27671.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence AAI43049.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence AAI43050.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence CAA58807.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence CAA58807.1 differs from that shown. Reason: Frameshift at position 875. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 2811K → T in AAH50734 (PubMed:15489334).Curated
Sequence conflicti649 – 6491S → R in CAA58807 (PubMed:7597036).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351E → K.1 Publication
Corresponds to variant rs11550314 [ dbSNP | Ensembl ].
VAR_027563
Natural varianti290 – 2901A → S.
Corresponds to variant rs8999 [ dbSNP | Ensembl ].
VAR_027564
Natural varianti303 – 3031V → A.
Corresponds to variant rs3739914 [ dbSNP | Ensembl ].
VAR_027565
Natural varianti360 – 3601G → V.
Corresponds to variant rs3739915 [ dbSNP | Ensembl ].
VAR_027566
Natural varianti401 – 4011R → Q.
Corresponds to variant rs3739916 [ dbSNP | Ensembl ].
VAR_027567
Natural varianti473 – 4731E → K.
Corresponds to variant rs12336746 [ dbSNP | Ensembl ].
VAR_050201
Natural varianti885 – 8851A → V.
Corresponds to variant rs1752676 [ dbSNP | Ensembl ].
VAR_061363

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83973 mRNA. Translation: CAA58807.1. Sequence problems.
AL353701 Genomic DNA. Translation: CAI94997.2.
BC050734 mRNA. Translation: AAH50734.1.
BC062692 mRNA. Translation: AAH62692.1. Sequence problems.
BC104639 mRNA. Translation: AAI04640.1. Sequence problems.
BC127669 mRNA. Translation: AAI27670.1. Sequence problems.
BC127670 mRNA. Translation: AAI27671.1. Sequence problems.
BC143048 mRNA. Translation: AAI43049.1. Sequence problems.
BC143049 mRNA. Translation: AAI43050.1. Sequence problems.
CCDSiCCDS6948.1.
PIRiI38182.
RefSeqiNP_001192225.1. NM_001205296.1.
NP_031370.2. NM_007344.3.
UniGeneiHs.54780.
Hs.732733.

Genome annotation databases

EnsembliENST00000334270; ENSP00000333920; ENSG00000125482.
GeneIDi7270.
KEGGihsa:7270.
UCSCiuc004cbl.3. human.

Polymorphism databases

DMDMi158518534.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83973 mRNA. Translation: CAA58807.1. Sequence problems.
AL353701 Genomic DNA. Translation: CAI94997.2.
BC050734 mRNA. Translation: AAH50734.1.
BC062692 mRNA. Translation: AAH62692.1. Sequence problems.
BC104639 mRNA. Translation: AAI04640.1. Sequence problems.
BC127669 mRNA. Translation: AAI27670.1. Sequence problems.
BC127670 mRNA. Translation: AAI27671.1. Sequence problems.
BC143048 mRNA. Translation: AAI43049.1. Sequence problems.
BC143049 mRNA. Translation: AAI43050.1. Sequence problems.
CCDSiCCDS6948.1.
PIRiI38182.
RefSeqiNP_001192225.1. NM_001205296.1.
NP_031370.2. NM_007344.3.
UniGeneiHs.54780.
Hs.732733.

3D structure databases

ProteinModelPortaliQ15361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113121. 12 interactions.
IntActiQ15361. 2 interactions.
MINTiMINT-1181965.
STRINGi9606.ENSP00000333920.

PTM databases

PhosphoSiteiQ15361.

Polymorphism databases

DMDMi158518534.

Proteomic databases

MaxQBiQ15361.
PaxDbiQ15361.
PRIDEiQ15361.

Protocols and materials databases

DNASUi7270.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334270; ENSP00000333920; ENSG00000125482.
GeneIDi7270.
KEGGihsa:7270.
UCSCiuc004cbl.3. human.

Organism-specific databases

CTDi7270.
GeneCardsiGC09M135250.
H-InvDBHIX0201412.
HGNCiHGNC:12397. TTF1.
HPAiHPA051105.
HPA054837.
MIMi600777. gene.
neXtProtiNX_Q15361.
PharmGKBiPA37062.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG262979.
GeneTreeiENSGT00530000063659.
HOGENOMiHOG000231811.
HOVERGENiHBG104803.
InParanoidiQ15361.
KOiK15225.
OMAiDYLYETT.
OrthoDBiEOG7ZKS9N.
PhylomeDBiQ15361.
TreeFamiTF333537.

Enzyme and pathway databases

ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSiTTF1. human.
GeneWikiiTranscription_termination_factor,_RNA_polymerase_I.
GenomeRNAii7270.
NextBioi28421.
PROiQ15361.
SOURCEiSearch...

Gene expression databases

BgeeiQ15361.
CleanExiHS_TTF1.
ExpressionAtlasiQ15361. baseline and differential.
GenevestigatoriQ15361.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
InterProiIPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR001005. SANT/Myb.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
[Graphical view]
PROSITEiPS50090. MYB_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular evolution of mammalian ribosomal gene terminator sequences and the transcription termination factor TTF-1."
    Evers R., Grummt I.
    Proc. Natl. Acad. Sci. U.S.A. 92:5827-5831(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2003) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-338 AND 457-905, VARIANT LYS-35.
    Tissue: Uterus.
  4. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-403; SER-481 AND SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-476; SER-481 AND SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-487 AND SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-481; SER-487 AND SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487 AND SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTTF1_HUMAN
AccessioniPrimary (citable) accession number: Q15361
Secondary accession number(s): A1L160
, Q4VXF3, Q58EY2, Q6P5T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: September 11, 2007
Last modified: April 1, 2015
This is version 125 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 9
    Human chromosome 9: 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.