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Protein

General transcription factor IIH subunit 2

Gene

GTF2H2

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

Functioni

Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. The N-terminus interacts with and regulates XPD whereas an intact C-terminus is required for a successful escape of RNAP II form the promoter.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri291 – 30818C4-typeAdd
BLAST

GO - Molecular functioni

  • nucleic acid binding Source: ProtInc
  • protein N-terminus binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: ProtInc
  • translation factor activity, RNA binding Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
REACT_1470. mRNA Capping.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1845. Formation of RNA Pol II elongation complex.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_257. Formation of incision complex in GG-NER.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_311. Dual incision reaction in GG-NER.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_953. RNA Polymerase I Transcription Initiation.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
General transcription factor IIH subunit 2
Alternative name(s):
Basic transcription factor 2 44 kDa subunit
Short name:
BTF2 p44
General transcription factor IIH polypeptide 2
TFIIH basal transcription factor complex p44 subunit
Gene namesi
Name:GTF2H2
Synonyms:BTF2P44
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:4656. GTF2H2.

Subcellular locationi

GO - Cellular componenti

  • core TFIIH complex Source: InterPro
  • holo TFIIH complex Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi291 – 2911C → A: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity. 1 Publication
Mutagenesisi308 – 3081C → A: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity. 1 Publication
Mutagenesisi345 – 3451C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
Mutagenesisi360 – 3601C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
Mutagenesisi363 – 3631C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
Mutagenesisi376 – 3761H → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
Mutagenesisi380 – 3801H → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
Mutagenesisi382 – 3821C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication

Organism-specific databases

PharmGKBiPA29042.

Polymorphism and mutation databases

BioMutaiGTF2H2.
DMDMi17380326.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395General transcription factor IIH subunit 2PRO_0000119248Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei95 – 951PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13888.
PaxDbiQ13888.
PRIDEiQ13888.

PTM databases

PhosphoSiteiQ13888.

Expressioni

Tissue specificityi

Widely expressed, with higher expression in skeletal muscle.

Gene expression databases

BgeeiQ13888.
CleanExiHS_GTF2H2.
ExpressionAtlasiQ13888. baseline.
GenevisibleiQ13888. HS.

Interactioni

Subunit structurei

One of the 6 subunits forming the core-TFIIH basal transcription factor which associates with the CAK complex composed of CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal transcription factor. Interacts with XPB, XPD, GTF2H1 and GTF2H3. Interacts with varicella-zoster virus IE63 protein.2 Publications

Protein-protein interaction databases

BioGridi109221. 19 interactions.
608768. 1 interaction.
DIPiDIP-786N.
IntActiQ13888. 4 interactions.
MINTiMINT-3028823.
STRINGi9606.ENSP00000274400.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi333 – 3353Combined sources
Helixi336 – 3394Combined sources
Turni346 – 3494Combined sources
Beta strandi355 – 3584Combined sources
Turni361 – 3644Combined sources
Helixi369 – 3735Combined sources
Turni374 – 3785Combined sources
Beta strandi381 – 3833Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z60NMR-A328-386[»]
ProteinModelPortaliQ13888.
SMRiQ13888. Positions 328-386.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13888.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 236177VWFAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the GTF2H2 family.Curated
Contains 1 VWFA domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri291 – 30818C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5151.
GeneTreeiENSGT00490000043395.
HOGENOMiHOG000159415.
HOVERGENiHBG059468.
InParanoidiQ13888.
KOiK03142.
OMAiECKVCGL.
PhylomeDBiQ13888.
TreeFamiTF314037.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR007198. Ssl1-like.
IPR004595. TFIIH_C1-like_dom.
IPR012170. TFIIH_SSL1/p44.
IPR002035. VWF_A.
IPR007087. Znf_C2H2.
[Graphical view]
PANTHERiPTHR12695:SF2. PTHR12695:SF2. 1 hit.
PfamiPF07975. C1_4. 1 hit.
PF04056. Ssl1. 1 hit.
[Graphical view]
PIRSFiPIRSF015919. TFIIH_SSL1. 1 hit.
SMARTiSM01047. C1_4. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
TIGRFAMsiTIGR00622. ssl1. 1 hit.
PROSITEiPS50234. VWFA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms may be produced. The isoforms may be also produced by incomplete gene duplication.

Isoform 1 (identifier: Q13888-1) [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
MDEEPERTKR WEGGYERTWE ILKEDESGSL KATIEDILFK AKRKRVFEHH
60 70 80 90 100
GQVRLGMMRH LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP
110 120 130 140 150
ISQIGIIVTK SKRAEKLTEL SGNPRKHITS LKKAVDMTCH GEPSLYNSLS
160 170 180 190 200
IAMQTLKHMP GHTSREVLII FSSLTTCDPS NIYDLIKTLK AAKIRVSVIG
210 220 230 240 250
LSAEVRVCTV LARETGGTYH VILDESHYKE LLTHHVSPPP ASSSSECSLI
260 270 280 290 300
RMGFPQHTIA SLSDQDAKPS FSMAHLDGNT EPGLTLGGYF CPQCRAKYCE
310 320 330 340 350
LPVECKICGL TLVSAPHLAR SYHHLFPLDA FQEIPLEEYN GERFCYGCQG
360 370 380 390
ELKDQHVYVC AVCQNVFCVD CDVFVHDSLH CCPGCIHKIP APSGV
Length:395
Mass (Da):44,419
Last modified:November 1, 1996 - v1
Checksum:i56D1BD8841288739
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291T → S (PubMed:7552146).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti151 – 1511I → M.1 Publication
VAR_011664
Natural varianti236 – 2361V → L.1 Publication
VAR_011665

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30094 mRNA. Translation: CAA82910.1.
AF078847 mRNA. Translation: AAD44479.1.
U21911 mRNA. Translation: AAA64502.1.
U21910 mRNA. Translation: AAA64503.1.
BC005345 mRNA. Translation: AAH05345.1.
U80017 Genomic DNA. Translation: AAC52046.1.
CCDSiCCDS34183.1. [Q13888-1]
PIRiS44454.
RefSeqiNP_001506.1. NM_001515.3. [Q13888-1]
XP_005276841.1. XM_005276784.2. [Q13888-1]
XP_005276843.1. XM_005276786.3. [Q13888-1]
XP_006726280.1. XM_006726217.2. [Q13888-1]
XP_011545263.1. XM_011546961.1. [Q13888-1]
UniGeneiHs.191356.
Hs.422901.
Hs.607501.

Genome annotation databases

EnsembliENST00000274400; ENSP00000274400; ENSG00000145736.
ENST00000330280; ENSP00000328901; ENSG00000145736.
ENST00000612581; ENSP00000480548; ENSG00000276910.
ENST00000617228; ENSP00000479262; ENSG00000275045.
ENST00000619997; ENSP00000477954; ENSG00000275045.
ENST00000628423; ENSP00000486014; ENSG00000276910.
GeneIDi2966.
728340.
KEGGihsa:2966.
UCSCiuc003kau.4. human. [Q13888-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30094 mRNA. Translation: CAA82910.1.
AF078847 mRNA. Translation: AAD44479.1.
U21911 mRNA. Translation: AAA64502.1.
U21910 mRNA. Translation: AAA64503.1.
BC005345 mRNA. Translation: AAH05345.1.
U80017 Genomic DNA. Translation: AAC52046.1.
CCDSiCCDS34183.1. [Q13888-1]
PIRiS44454.
RefSeqiNP_001506.1. NM_001515.3. [Q13888-1]
XP_005276841.1. XM_005276784.2. [Q13888-1]
XP_005276843.1. XM_005276786.3. [Q13888-1]
XP_006726280.1. XM_006726217.2. [Q13888-1]
XP_011545263.1. XM_011546961.1. [Q13888-1]
UniGeneiHs.191356.
Hs.422901.
Hs.607501.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z60NMR-A328-386[»]
ProteinModelPortaliQ13888.
SMRiQ13888. Positions 328-386.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109221. 19 interactions.
608768. 1 interaction.
DIPiDIP-786N.
IntActiQ13888. 4 interactions.
MINTiMINT-3028823.
STRINGi9606.ENSP00000274400.

PTM databases

PhosphoSiteiQ13888.

Polymorphism and mutation databases

BioMutaiGTF2H2.
DMDMi17380326.

Proteomic databases

MaxQBiQ13888.
PaxDbiQ13888.
PRIDEiQ13888.

Protocols and materials databases

DNASUi2966.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274400; ENSP00000274400; ENSG00000145736.
ENST00000330280; ENSP00000328901; ENSG00000145736.
ENST00000612581; ENSP00000480548; ENSG00000276910.
ENST00000617228; ENSP00000479262; ENSG00000275045.
ENST00000619997; ENSP00000477954; ENSG00000275045.
ENST00000628423; ENSP00000486014; ENSG00000276910.
GeneIDi2966.
728340.
KEGGihsa:2966.
UCSCiuc003kau.4. human. [Q13888-1]

Organism-specific databases

CTDi2966.
728340.
GeneCardsiGC05M070330.
HGNCiHGNC:4656. GTF2H2.
MIMi601748. gene.
neXtProtiNX_Q13888.
PharmGKBiPA29042.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5151.
GeneTreeiENSGT00490000043395.
HOGENOMiHOG000159415.
HOVERGENiHBG059468.
InParanoidiQ13888.
KOiK03142.
OMAiECKVCGL.
PhylomeDBiQ13888.
TreeFamiTF314037.

Enzyme and pathway databases

ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
REACT_1470. mRNA Capping.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1845. Formation of RNA Pol II elongation complex.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_257. Formation of incision complex in GG-NER.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_311. Dual incision reaction in GG-NER.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_953. RNA Polymerase I Transcription Initiation.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

EvolutionaryTraceiQ13888.
GeneWikiiGTF2H2.
NextBioi11756.
PROiQ13888.
SOURCEiSearch...

Gene expression databases

BgeeiQ13888.
CleanExiHS_GTF2H2.
ExpressionAtlasiQ13888. baseline.
GenevisibleiQ13888. HS.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR007198. Ssl1-like.
IPR004595. TFIIH_C1-like_dom.
IPR012170. TFIIH_SSL1/p44.
IPR002035. VWF_A.
IPR007087. Znf_C2H2.
[Graphical view]
PANTHERiPTHR12695:SF2. PTHR12695:SF2. 1 hit.
PfamiPF07975. C1_4. 1 hit.
PF04056. Ssl1. 1 hit.
[Graphical view]
PIRSFiPIRSF015919. TFIIH_SSL1. 1 hit.
SMARTiSM01047. C1_4. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
TIGRFAMsiTIGR00622. ssl1. 1 hit.
PROSITEiPS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "p44 and p34 subunits of the BTF2/TFIIH transcription factor have homologies with SSL1, a yeast protein involved in DNA repair."
    Humbert S., van Vuuren H.A., Lutz Y., Hoeijmakers J.H.J., Egly J.-M., Moncollin V.
    EMBO J. 13:2393-2398(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-40; 46-54; 60-68; 117-125 AND 214-229.
  2. Zhang Q., Huang Q., Song H., Peng J., Fu G., Mao M., Dai M., Mao Y., Zhou J., Chen Z., Chen J.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pituitary tumor.
  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].
    Tissue: Skin.
  4. "A provisional transcript map of the spinal muscular atrophy (SMA) critical region."
    van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C., van Ommen G.J.B., Buys C.H.C.M.
    Eur. J. Hum. Genet. 3:87-95(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-130 AND 327-395.
    Tissue: Pre-B cell.
  5. "Sequence of a 131-kb region of 5q13.1 containing the spinal muscular atrophy candidate genes SMN and NAIP."
    Chen Q., Baird S.D., Mahadevan M., Besner-Johnston A., Farahani R., Xuan J.-Y., Kang X., Lefebvre C., Ikeda J.-E., Korneluk R.G., MacKenzie A.E.
    Genomics 48:121-127(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-395.
    Tissue: Brain.
  6. "Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
    Kershnar E., Wu S.-Y., Chiang C.-M.
    J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
  7. "A role of the C-terminal part of p44 in the promoter escape activity of transcription factor IIH."
    Tremeau-Bravard A., Perez C., Egly J.-M.
    J. Biol. Chem. 276:27693-27697(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-291; CYS-308; CYS-345; CYS-360; CYS-363; HIS-376; HIS-380 AND CYS-382.
  8. "Varicella-zoster virus IE63 protein represses the basal transcription machinery by disorganizing the pre-initiation complex."
    Di Valentin E., Bontems S., Habran L., Jolois O., Markine-Goriaynoff N., Vanderplasschen A., Sadzot-Delvaux C., Piette J.
    Biol. Chem. 386:255-267(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VARICELLA-ZOSTER VIRUS IE63 PROTEIN.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A multicopy transcription-repair gene, BTF2p44, maps to the SMA region and demonstrates SMA associated deletions."
    Carter T.A., Bonnemann C.G., Wang C.H., Obici S., Parano E., Bonaldo M.F., Ross B.M., Penchaszadeh G.K., Mackenzie A.E., Soares M.B., Kunkel L.M., Gilliam T.C.
    Hum. Mol. Genet. 6:229-236(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MET-151 AND LEU-236.

Entry informationi

Entry nameiTF2H2_HUMAN
AccessioniPrimary (citable) accession number: Q13888
Secondary accession number(s): Q15570, Q15571, Q9BS41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 165 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

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.