TF2H1_HUMAN - dbPTM
TF2H1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TF2H1_HUMAN
UniProt AC P32780
Protein Name General transcription factor IIH subunit 1
Gene Name GTF2H1
Organism Homo sapiens (Human).
Sequence Length 548
Subcellular Localization Nucleus.
Protein Description Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription..
Protein Sequence MATSSEEVLLIVKKVRQKKQDGALYLMAERIAWAPEGKDRFTISHMYADIKCQKISPEGKAKIQLQLVLHAGDTTNFHFSNESTAVKERDAVKDLLQQLLPKFKRKANKELEEKNRMLQEDPVLFQLYKDLVVSQVISAEEFWANRLNVNATDSSSTSNHKQDVGISAAFLADVRPQTDGCNGLRYNLTSDIIESIFRTYPAVKMKYAENVPHNMTEKEFWTRFFQSHYFHRDRLNTGSKDLFAECAKIDEKGLKTMVSLGVKNPLLDLTALEDKPLDEGYGISSVPSASNSKSIKENSNAAIIKRFNHHSAMVLAAGLRKQEAQNEQTSEPSNMDGNSGDADCFQPAVKRAKLQESIEYEDLGKNNSVKTIALNLKKSDRYYHGPTPIQSLQYATSQDIINSFQSIRQEMEAYTPKLTQVLSSSAASSTITALSPGGALMQGGTQQAINQMVPNDIQSELKHLYVAVGELLRHFWSCFPVNTPFLEEKVVKMKSNLERFQVTKLCPFQEKIRRQYLSTNLVSHIEEMLQTAYNKLHTWQSRRLMKKT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MATSSEEVL
------CCCCHHHHH		19.05-
25PhosphorylationKKQDGALYLMAERIA
CCCCCCEEEEEEEEE		8.22-
38UbiquitinationIAWAPEGKDRFTISH
EECCCCCCCCEEEEE		44.03-
54AcetylationYADIKCQKISPEGKA
EEEEEEEECCCCCCE		55.4025953088
74PhosphorylationLVLHAGDTTNFHFSN
EEEECCCCCCEECCC		23.79-
93UbiquitinationVKERDAVKDLLQQLL
HHHHHHHHHHHHHHH		44.3621890473
93UbiquitinationVKERDAVKDLLQQLL
HHHHHHHHHHHHHHH		44.3621890473
102UbiquitinationLLQQLLPKFKRKANK
HHHHHHHHHHHHHHH		64.58-
102UbiquitinationLLQQLLPKFKRKANK
HHHHHHHHHHHHHHH		64.58-
124UbiquitinationMLQEDPVLFQLYKDL
HHHHCHHHHHHHHHH		2.49-
124AcetylationMLQEDPVLFQLYKDL
HHHHCHHHHHHHHHH		2.49-
158PhosphorylationATDSSSTSNHKQDVG
CCCCCCCCCCCCCCC		38.5925159151
207PhosphorylationYPAVKMKYAENVPHN
CCHHHHHHCCCCCCC		18.69-
218UbiquitinationVPHNMTEKEFWTRFF
CCCCCCHHHHHHHHH		49.3921890473
218AcetylationVPHNMTEKEFWTRFF
CCCCCCHHHHHHHHH		49.3925953088
218UbiquitinationVPHNMTEKEFWTRFF
CCCCCCHHHHHHHHH		49.3921890473
237PhosphorylationFHRDRLNTGSKDLFA
CCHHHCCCCCHHHHH		47.6421406692
239PhosphorylationRDRLNTGSKDLFAEC
HHHCCCCCHHHHHHH		22.4321406692
240UbiquitinationDRLNTGSKDLFAECA
HHCCCCCHHHHHHHH		60.85-
240AcetylationDRLNTGSKDLFAECA
HHCCCCCHHHHHHHH		60.8523954790
254UbiquitinationAKIDEKGLKTMVSLG
HHCCHHHHHHHHHCC		6.55-
256PhosphorylationIDEKGLKTMVSLGVK
CCHHHHHHHHHCCCC		28.0421406692
259PhosphorylationKGLKTMVSLGVKNPL
HHHHHHHHCCCCCCC		14.4821406692
261UbiquitinationLKTMVSLGVKNPLLD
HHHHHHCCCCCCCCC		22.35-
275UbiquitinationDLTALEDKPLDEGYG
CCEECCCCCCCCCCC		37.80-
288PhosphorylationYGISSVPSASNSKSI
CCCCCCCCCCCCCCH		42.0226074081
290PhosphorylationISSVPSASNSKSIKE
CCCCCCCCCCCCHHH		46.0726074081
292PhosphorylationSVPSASNSKSIKENS
CCCCCCCCCCHHHCC		25.8626074081
293UbiquitinationVPSASNSKSIKENSN
CCCCCCCCCHHHCCC		61.52-
294PhosphorylationPSASNSKSIKENSNA
CCCCCCCCHHHCCCC		38.4226074081
296UbiquitinationASNSKSIKENSNAAI
CCCCCCHHHCCCCCH		58.91-
299PhosphorylationSKSIKENSNAAIIKR
CCCHHHCCCCCHHHH		29.0123532336
305AcetylationNSNAAIIKRFNHHSA
CCCCCHHHHCCHHHH		44.8425953088
329PhosphorylationQEAQNEQTSEPSNMD
HHHHHCCCCCCCCCC		28.9530108239
330PhosphorylationEAQNEQTSEPSNMDG
HHHHCCCCCCCCCCC		47.4030108239
333PhosphorylationNEQTSEPSNMDGNSG
HCCCCCCCCCCCCCC		40.5128450419
339PhosphorylationPSNMDGNSGDADCFQ
CCCCCCCCCCCHHHH		43.5119413330
350AcetylationDCFQPAVKRAKLQES
HHHHHHHHHHHHHHH		49.0626051181
353AcetylationQPAVKRAKLQESIEY
HHHHHHHHHHHHCCC		55.5326051181
353UbiquitinationQPAVKRAKLQESIEY
HHHHHHHHHHHHCCC		55.53-
357PhosphorylationKRAKLQESIEYEDLG
HHHHHHHHCCCHHCC		14.0425159151
360PhosphorylationKLQESIEYEDLGKNN
HHHHHCCCHHCCCCC		17.0528796482
365AcetylationIEYEDLGKNNSVKTI
CCCHHCCCCCCEEEE		61.3226051181
365UbiquitinationIEYEDLGKNNSVKTI
CCCHHCCCCCCEEEE		61.32-
368PhosphorylationEDLGKNNSVKTIALN
HHCCCCCCEEEEEEE		34.0919664995
370UbiquitinationLGKNNSVKTIALNLK
CCCCCCEEEEEEECC		33.75-
377UbiquitinationKTIALNLKKSDRYYH
EEEEEECCCCCCCCC		49.51-
388UbiquitinationRYYHGPTPIQSLQYA
CCCCCCCCCCCHHHH		26.25-
406PhosphorylationDIINSFQSIRQEMEA
HHHHHHHHHHHHHHH		20.0924719451
415PhosphorylationRQEMEAYTPKLTQVL
HHHHHHHCHHHHHHH		22.46-
504UbiquitinationLERFQVTKLCPFQEK
HHHHHHHHHCHHHHH		49.59-
504AcetylationLERFQVTKLCPFQEK
HHHHHHHHHCHHHHH		49.5926051181
516PhosphorylationQEKIRRQYLSTNLVS
HHHHHHHHHHHHHHH		10.7822817900
533PhosphorylationEEMLQTAYNKLHTWQ
HHHHHHHHHHHHHHH		19.0622817900
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TF2H1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TF2H1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TF2H1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCSE2_HUMANCCSER2physical
16169070
ESR1_HUMANESR1physical
10949034
ERCC3_HUMANERCC3physical
9130708
ERCC2_HUMANERCC2physical
9130708
E2F1_HUMANE2F1physical
10428966
CDK7_HUMANCDK7physical
7533895
CCNH_HUMANCCNHphysical
7533895
HXC11_HUMANHOXC11physical
20211142
OBF1_HUMANPOU2AF1physical
20211142
BRPF1_HUMANBRPF1physical
20211142
JDP2_HUMANJDP2physical
20211142
ZSCA1_HUMANZSCAN1physical
20211142
TRXR2_HUMANTXNRD2physical
15625236
CDK7_HUMANCDK7physical
9852112
CCNH_HUMANCCNHphysical
9852112
MAT1_HUMANMNAT1physical
9852112
ERCC1_HUMANERCC1physical
11259578
XPF_HUMANERCC4physical
11259578
ERCC5_HUMANERCC5physical
11259578
RFA1_HUMANRPA1physical
11259578
RFA2_HUMANRPA2physical
11259578
RD23B_HUMANRAD23Bphysical
11259578
XPC_HUMANXPCphysical
11259578
XPA_HUMANXPAphysical
11259578
CCNH_HUMANCCNHphysical
11259578
ERCC3_HUMANERCC3physical
11259578
TF2H2_HUMANGTF2H2physical
8194529
TF2H3_HUMANGTF2H3physical
8194529
RPB1_HUMANPOLR2Aphysical
15282296
TF2H3_HUMANGTF2H3physical
22939629
TF2H4_HUMANGTF2H4physical
22939629
T2EA_HUMANGTF2E1physical
18160537
T2EA_HUMANGTF2E1physical
18354501
ERCC5_HUMANERCC5physical
15195146
IMA4_HUMANKPNA3physical
21988832
TARA_HUMANTRIOBPphysical
21988832
TF2H2_HUMANGTF2H2physical
21988832
REEP5_HUMANREEP5physical
21988832
TNIP1_HUMANTNIP1physical
21988832
USBP1_HUMANUSHBP1physical
21988832
T2H2L_HUMANGTF2H2Cphysical
26344197
TF2H2_HUMANGTF2H2physical
26344197
TF2H4_HUMANGTF2H4physical
26344197
RPB1_HUMANPOLR2Aphysical
8934526
NUDC_HUMANNUDCphysical
27173435
ERCC2_HUMANERCC2physical
26340423
TF2H2_HUMANGTF2H2physical
26340423
TF2H3_HUMANGTF2H3physical
26340423
ERCC3_HUMANERCC3physical
26340423
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TF2H1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-339, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-339, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory