Q13888 (TF2H2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GTF2H2
Synonyms:	BTF2P44

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.6 Ref.8
Subcellular location	Nucleus.
Tissue specificity	Widely expressed, with higher expression in skeletal muscle.
Sequence similarities	Belongs to the GTF2H2 family. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Traceable author statement. Source: Reactome G-protein coupled receptor internalization Inferred from mutant phenotype PubMed 15775968. Source: UniProtKB nucleotide-excision repair, DNA damage removal Traceable author statement. Source: Reactome positive regulation of viral transcription Traceable author statement. Source: Reactome protein phosphorylation Inferred from direct assay Ref.6. Source: GOC response to UV Traceable author statement Ref.1. Source: ProtInc termination of RNA polymerase I transcription Traceable author statement. Source: Reactome transcription elongation from RNA polymerase I promoter Traceable author statement. Source: Reactome transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase I promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription-coupled nucleotide-excision repair Traceable author statement. Source: Reactome viral reproductive process Traceable author statement. Source: Reactome
Cellular_component	core TFIIH complex Inferred from electronic annotation. Source: InterPro holo TFIIH complex Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	sequence-specific DNA binding transcription factor activity Non-traceable author statement Ref.1. Source: ProtInc translation factor activity, nucleic acid binding Traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

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

Isoform 1 (identifier: Q13888-1)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 395

395

General transcription factor IIH subunit 2

PRO_0000119248

Regions

Domain

60 – 236

177

VWFA

Zinc finger

291 – 308

18

C4-type

Natural variations

Natural variant

151

1

I → M. Ref.10

VAR_011664

Natural variant

236

1

V → L. Ref.10

VAR_011665

Experimental info

Mutagenesis

291

1

C → A: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity. Ref.7

Mutagenesis

308

1

C → A: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity. Ref.7

Mutagenesis

345

1

C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7

Mutagenesis

360

1

C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7

Mutagenesis

363

1

C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7

Mutagenesis

376

1

H → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7

Mutagenesis

380

1

H → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7

Mutagenesis

382

1

C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7

Sequence conflict

129

1

T → S Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

395

Helix Strand Turn

Details...

Beta strand

333 – 335

3

Helix

336 – 339

4

Turn

346 – 349

4

Beta strand

355 – 358

4

Turn

361 – 364

4

Helix

369 – 373

5

Turn

374 – 378

5

Beta strand

381 – 383

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 56D1BD8841288739	FASTA	395	44,419
	10 20 30 40 50 60 MDEEPERTKR WEGGYERTWE ILKEDESGSL KATIEDILFK AKRKRVFEHH GQVRLGMMRH 70 80 90 100 110 120 LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP ISQIGIIVTK SKRAEKLTEL 130 140 150 160 170 180 SGNPRKHITS LKKAVDMTCH GEPSLYNSLS IAMQTLKHMP GHTSREVLII FSSLTTCDPS 190 200 210 220 230 240 NIYDLIKTLK AAKIRVSVIG LSAEVRVCTV LARETGGTYH VILDESHYKE LLTHHVSPPP 250 260 270 280 290 300 ASSSSECSLI RMGFPQHTIA SLSDQDAKPS FSMAHLDGNT EPGLTLGGYF CPQCRAKYCE 310 320 330 340 350 360 LPVECKICGL TLVSAPHLAR SYHHLFPLDA FQEIPLEEYN GERFCYGCQG ELKDQHVYVC 370 380 390 AVCQNVFCVD CDVFVHDSLH CCPGCIHKIP APSGV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00426640.

PIR

S44454.

RefSeq

NP_001506.1. NM_001515.3.

UniGene

Hs.191356.
Hs.607501.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z60	NMR	-	A	328-386	[»]

ProteinModelPortal

Q13888.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-786N.

IntAct

Q13888. 3 interactions.

MINT

MINT-3028823.

STRING

9606.ENSP00000274400.

PTM databases

PhosphoSite

Q13888.

Polymorphism databases

DMDM

17380326.

Proteomic databases

PaxDb

Q13888.

PRIDE

Q13888.

Protocols and materials databases

DNASU

2966.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000274400; ENSP00000274400; ENSG00000145736.
ENST00000330280; ENSP00000328901; ENSG00000145736.
ENST00000522323; ENSP00000429126; ENSG00000145736.
ENST00000573143; ENSP00000458297; ENSG00000262169.
ENST00000575673; ENSP00000459636; ENSG00000262169.

GeneID

2966.

KEGG

hsa:2966.

UCSC

uc003kau.4. human.

Organism-specific databases

CTD

2966.

GeneCards

GC05M070366.

HGNC

HGNC:4656. GTF2H2.

MIM

601748. gene.

neXtProt

NX_Q13888.

PharmGKB

PA29042.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5151.

HOGENOM

HOG000159415.

HOVERGEN

HBG059468.

InParanoid

Q13888.

KO

K03142.

OMA

ECKVCGL.

OrthoDB

EOG4M0F1X.

PhylomeDB

Q13888.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q13888.

Bgee

Q13888.

CleanEx

HS_GTF2H2.

Genevestigator

Q13888.

GermOnline

ENSG00000145736. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.410. 1 hit.

InterPro

IPR007198. Ssl1-like.
IPR004595. TFIIH_C1-like_dom.
IPR012170. TFIIH_SSL1/p44.
IPR002035. VWF_A.
IPR007087. Znf_C2H2.
[Graphical view]

PANTHER

PTHR12695. PTHR12695. 1 hit.

Pfam

PF07975. C1_4. 1 hit.
PF04056. Ssl1. 1 hit.
[Graphical view]

PIRSF

PIRSF015919. TFIIH_SSL1. 1 hit.

SMART

SM01047. C1_4. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00622. ssl1. 1 hit.

PROSITE

PS50234. VWFA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q13888.

GenomeRNAi

2966.

NextBio

11756.

SOURCE

Search...

Entry information

Entry name

TF2H2_HUMAN

Accession

Primary (citable) accession number: Q13888
Secondary accession number(s): Q15570, Q15571, Q9BS41

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 143 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.