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Protein

General transcription factor IIH subunit 1

Gene

GTF2H1

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.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

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 1
Alternative name(s):
Basic transcription factor 2 62 kDa subunit
Short name:
BTF2 p62
General transcription factor IIH polypeptide 1
TFIIH basal transcription factor complex p62 subunit
Gene namesi
Name:GTF2H1
Synonyms:BTF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:4655. GTF2H1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29041.

Polymorphism and mutation databases

BioMutaiGTF2H1.
DMDMi416727.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548General transcription factor IIH subunit 1PRO_0000119245Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei240 – 2401N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32780.
PaxDbiP32780.
PeptideAtlasiP32780.
PRIDEiP32780.

PTM databases

PhosphoSiteiP32780.

Expressioni

Gene expression databases

BgeeiP32780.
CleanExiHS_GTF2H1.
ExpressionAtlasiP32780. baseline and differential.
GenevisibleiP32780. HS.

Organism-specific databases

HPAiCAB004637.
HPA046660.

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 PUF60.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GTF2E1P2908317EBI-715539,EBI-5462215
TP53P046375EBI-715539,EBI-366083
XPCQ018312EBI-715539,EBI-372610

Protein-protein interaction databases

BioGridi109220. 53 interactions.
DIPiDIP-708N.
IntActiP32780. 14 interactions.
MINTiMINT-192215.
STRINGi9606.ENSP00000265963.

Structurei

Secondary structure

1
548
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi8 – 136Combined sources
Beta strandi23 – 275Combined sources
Beta strandi30 – 345Combined sources
Beta strandi36 – 405Combined sources
Beta strandi42 – 465Combined sources
Turni47 – 493Combined sources
Beta strandi53 – 553Combined sources
Beta strandi58 – 625Combined sources
Beta strandi64 – 685Combined sources
Beta strandi70 – 723Combined sources
Beta strandi74 – 785Combined sources
Turni82 – 843Combined sources
Helixi87 – 10317Combined sources
Helixi109 – 12012Combined sources
Helixi122 – 13211Combined sources
Turni133 – 1353Combined sources
Helixi139 – 1468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PFJNMR-A1-108[»]
2DIINMR-A103-150[»]
2RNRNMR-B1-108[»]
2RUKNMR-B1-108[»]
ProteinModelPortaliP32780.
SMRiP32780. Positions 1-155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32780.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 15456BSD 1PROSITE-ProRule annotationAdd
BLAST
Domaini180 – 23253BSD 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 BSD domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG315835.
GeneTreeiENSGT00390000015066.
HOGENOMiHOG000006589.
HOVERGENiHBG060375.
InParanoidiP32780.
KOiK03141.
OMAiTAYNKFH.
OrthoDBiEOG7FV3Q4.
PhylomeDBiP32780.
TreeFamiTF314689.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR005607. BSD.
IPR011993. PH_like_dom.
IPR027079. Tfb1/p62.
IPR013876. TFIIH_BTF_p62_N.
[Graphical view]
PANTHERiPTHR12856. PTHR12856. 1 hit.
PfamiPF03909. BSD. 2 hits.
PF08567. TFIIH_BTF_p62_N. 1 hit.
[Graphical view]
SMARTiSM00751. BSD. 2 hits.
[Graphical view]
PROSITEiPS50858. BSD. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P32780-1) [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
MATSSEEVLL IVKKVRQKKQ DGALYLMAER IAWAPEGKDR FTISHMYADI
60 70 80 90 100
KCQKISPEGK AKIQLQLVLH AGDTTNFHFS NESTAVKERD AVKDLLQQLL
110 120 130 140 150
PKFKRKANKE LEEKNRMLQE DPVLFQLYKD LVVSQVISAE EFWANRLNVN
160 170 180 190 200
ATDSSSTSNH KQDVGISAAF LADVRPQTDG CNGLRYNLTS DIIESIFRTY
210 220 230 240 250
PAVKMKYAEN VPHNMTEKEF WTRFFQSHYF HRDRLNTGSK DLFAECAKID
260 270 280 290 300
EKGLKTMVSL GVKNPLLDLT ALEDKPLDEG YGISSVPSAS NSKSIKENSN
310 320 330 340 350
AAIIKRFNHH SAMVLAAGLR KQEAQNEQTS EPSNMDGNSG DADCFQPAVK
360 370 380 390 400
RAKLQESIEY EDLGKNNSVK TIALNLKKSD RYYHGPTPIQ SLQYATSQDI
410 420 430 440 450
INSFQSIRQE MEAYTPKLTQ VLSSSAASST ITALSPGGAL MQGGTQQAIN
460 470 480 490 500
QMVPNDIQSE LKHLYVAVGE LLRHFWSCFP VNTPFLEEKV VKMKSNLERF
510 520 530 540
QVTKLCPFQE KIRRQYLSTN LVSHIEEMLQ TAYNKLHTWQ SRRLMKKT
Length:548
Mass (Da):62,032
Last modified:October 1, 1993 - v1
Checksum:i8F0FCEBBB1FC9C1D
GO
Isoform 2 (identifier: P32780-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-116: Missing.

Note: No experimental confirmation available.
Show »
Length:432
Mass (Da):48,738
Checksum:i894C7C56EF0407DE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti292 – 2921S → P in BAB15621 (PubMed:14702039).Curated
Sequence conflicti385 – 3851G → A in BAB15621 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti234 – 2341R → W.1 Publication
Corresponds to variant rs4150603 [ dbSNP | Ensembl ].
VAR_014345
Natural varianti285 – 2851S → F.1 Publication
Corresponds to variant rs4150636 [ dbSNP | Ensembl ].
VAR_014346
Natural varianti517 – 5171L → V.1 Publication
Corresponds to variant rs4150665 [ dbSNP | Ensembl ].
VAR_014347

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 116116Missing in isoform 2. 1 PublicationVSP_056562Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95809 mRNA. Translation: AAA58399.1.
AK027003 mRNA. Translation: BAB15621.1.
AK127204 mRNA. Translation: BAG54452.1.
AY163770 Genomic DNA. Translation: AAN46740.1.
CR457368 mRNA. Translation: CAG33649.1.
AC084117 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68399.1.
CH471064 Genomic DNA. Translation: EAW68400.1.
CH471064 Genomic DNA. Translation: EAW68401.1.
BC000365 mRNA. Translation: AAH00365.1.
BC004452 mRNA. Translation: AAH04452.1.
AJ131959 Genomic DNA. Translation: CAC00685.1.
CCDSiCCDS7838.1. [P32780-1]
PIRiS27958.
RefSeqiNP_001135779.1. NM_001142307.1. [P32780-1]
NP_005307.1. NM_005316.3. [P32780-1]
XP_006718271.1. XM_006718208.2. [P32780-1]
UniGeneiHs.577202.

Genome annotation databases

EnsembliENST00000265963; ENSP00000265963; ENSG00000110768. [P32780-1]
ENST00000453096; ENSP00000393638; ENSG00000110768. [P32780-1]
ENST00000534641; ENSP00000435375; ENSG00000110768. [P32780-2]
GeneIDi2965.
KEGGihsa:2965.
UCSCiuc001moh.2. human. [P32780-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95809 mRNA. Translation: AAA58399.1.
AK027003 mRNA. Translation: BAB15621.1.
AK127204 mRNA. Translation: BAG54452.1.
AY163770 Genomic DNA. Translation: AAN46740.1.
CR457368 mRNA. Translation: CAG33649.1.
AC084117 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68399.1.
CH471064 Genomic DNA. Translation: EAW68400.1.
CH471064 Genomic DNA. Translation: EAW68401.1.
BC000365 mRNA. Translation: AAH00365.1.
BC004452 mRNA. Translation: AAH04452.1.
AJ131959 Genomic DNA. Translation: CAC00685.1.
CCDSiCCDS7838.1. [P32780-1]
PIRiS27958.
RefSeqiNP_001135779.1. NM_001142307.1. [P32780-1]
NP_005307.1. NM_005316.3. [P32780-1]
XP_006718271.1. XM_006718208.2. [P32780-1]
UniGeneiHs.577202.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PFJNMR-A1-108[»]
2DIINMR-A103-150[»]
2RNRNMR-B1-108[»]
2RUKNMR-B1-108[»]
ProteinModelPortaliP32780.
SMRiP32780. Positions 1-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109220. 53 interactions.
DIPiDIP-708N.
IntActiP32780. 14 interactions.
MINTiMINT-192215.
STRINGi9606.ENSP00000265963.

PTM databases

PhosphoSiteiP32780.

Polymorphism and mutation databases

BioMutaiGTF2H1.
DMDMi416727.

Proteomic databases

MaxQBiP32780.
PaxDbiP32780.
PeptideAtlasiP32780.
PRIDEiP32780.

Protocols and materials databases

DNASUi2965.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265963; ENSP00000265963; ENSG00000110768. [P32780-1]
ENST00000453096; ENSP00000393638; ENSG00000110768. [P32780-1]
ENST00000534641; ENSP00000435375; ENSG00000110768. [P32780-2]
GeneIDi2965.
KEGGihsa:2965.
UCSCiuc001moh.2. human. [P32780-1]

Organism-specific databases

CTDi2965.
GeneCardsiGC11P018343.
HGNCiHGNC:4655. GTF2H1.
HPAiCAB004637.
HPA046660.
MIMi189972. gene.
neXtProtiNX_P32780.
PharmGKBiPA29041.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG315835.
GeneTreeiENSGT00390000015066.
HOGENOMiHOG000006589.
HOVERGENiHBG060375.
InParanoidiP32780.
KOiK03141.
OMAiTAYNKFH.
OrthoDBiEOG7FV3Q4.
PhylomeDBiP32780.
TreeFamiTF314689.

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

EvolutionaryTraceiP32780.
GeneWikiiGTF2H1.
GenomeRNAii2965.
NextBioi11752.
PROiP32780.
SOURCEiSearch...

Gene expression databases

BgeeiP32780.
CleanExiHS_GTF2H1.
ExpressionAtlasiP32780. baseline and differential.
GenevisibleiP32780. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR005607. BSD.
IPR011993. PH_like_dom.
IPR027079. Tfb1/p62.
IPR013876. TFIIH_BTF_p62_N.
[Graphical view]
PANTHERiPTHR12856. PTHR12856. 1 hit.
PfamiPF03909. BSD. 2 hits.
PF08567. TFIIH_BTF_p62_N. 1 hit.
[Graphical view]
SMARTiSM00751. BSD. 2 hits.
[Graphical view]
PROSITEiPS50858. BSD. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the 62-kilodalton component of basic transcription factor BTF2."
    Fischer L., Gerard M., Chalut C., Lutz Y., Humbert S., Kanno M., Chambon P., Egly J.-M.
    Science 257:1392-1395(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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: Hippocampus and Liver.
  3. NIEHS SNPs program
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-234; PHE-285 AND VAL-517.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Lung.
  8. "An aphidicolin-sensitive fragile site (FRA11C) lies within 100 kb of the putative tumour suppressor gene TSG101 on both human and mouse chromosomes."
    Critcher R., Palin A.H., Zhang J., Chin S.F., Gayther S.A., Li L., Cohen S.N., Caldas C., Farr C.J.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 521-548.
  9. "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.
  10. "The FBP interacting repressor targets TFIIH to inhibit activated transcription."
    Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D.
    Mol. Cell 5:331-341(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PUF60.
  11. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Solution structure of the BSD domain of human TFIIH basal transcription factor complex p62 subunit."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 103-155.

Entry informationi

Entry nameiTF2H1_HUMAN
AccessioniPrimary (citable) accession number: P32780
Secondary accession number(s): B3KXE0
, D3DQY2, Q6I9Y7, Q9H5K5, Q9NQD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 24, 2015
This is version 149 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 11
    Human chromosome 11: 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.