THAP7_HUMAN - dbPTM
THAP7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THAP7_HUMAN
UniProt AC Q9BT49
Protein Name THAP domain-containing protein 7
Gene Name THAP7
Organism Homo sapiens (Human).
Sequence Length 309
Subcellular Localization Nucleus. Chromosome.
Protein Description Chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressors..
Protein Sequence MPRHCSAAGCCTRDTRETRNRGISFHRLPKKDNPRRGLWLANCQRLDPSGQGLWDPASEYIYFCSKHFEEDCFELVGISGYHRLKEGAVPTIFESFSKLRRTTKTKGHSYPPGPAEVSRLRRCRKRCSEGRGPTTPFSPPPPADVTCFPVEEASAPATLPASPAGRLEPGLSSPFSDLLGPLGAQADEAGCSAQPSPERQPSPLEPRPVSPSAYMLRLPPPAGAYIQNEHSYQVGSALLWKRRAEAALDALDKAQRQLQACKRREQRLRLRLTKLQQERAREKRAQADARQTLKEHVQDFAMQLSSSMA
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
91PhosphorylationLKEGAVPTIFESFSK
HHCCCCCHHHHHHHH
31.53-
95PhosphorylationAVPTIFESFSKLRRT
CCCHHHHHHHHHHCC
24.8724719451
97PhosphorylationPTIFESFSKLRRTTK
CHHHHHHHHHHCCCC
39.81-
146PhosphorylationPPPPADVTCFPVEEA
CCCCCCCEEEECHHC
14.6926074081
154PhosphorylationCFPVEEASAPATLPA
EEECHHCCCCCCCCC
37.7626074081
158PhosphorylationEEASAPATLPASPAG
HHCCCCCCCCCCCCC
32.0126074081
162PhosphorylationAPATLPASPAGRLEP
CCCCCCCCCCCCCCC
17.2229255136
192PhosphorylationQADEAGCSAQPSPER
CCCCCCCCCCCCCCC
29.0828348404
196PhosphorylationAGCSAQPSPERQPSP
CCCCCCCCCCCCCCC
27.5828348404
202PhosphorylationPSPERQPSPLEPRPV
CCCCCCCCCCCCCCC
33.5023312004
210PhosphorylationPLEPRPVSPSAYMLR
CCCCCCCCCCCEEEE
18.8028348404
212PhosphorylationEPRPVSPSAYMLRLP
CCCCCCCCCEEEECC
25.2423312004
253UbiquitinationAALDALDKAQRQLQA
HHHHHHHHHHHHHHH
47.4729967540
274AcetylationRLRLRLTKLQQERAR
HHHHHHHHHHHHHHH
49.2269507

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 THAP7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THAP7_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 THAP7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LURA1_HUMANLURAP1physical
16189514
KR412_HUMANKRTAP4-12physical
16189514
TAF1B_HUMANTAF1Bphysical
16195249
H31_HUMANHIST1H3Aphysical
15561719
HDAC3_HUMANHDAC3physical
15561719
HINFP_HUMANHINFPphysical
17577209
A4_HUMANAPPphysical
21832049
THAP7_HUMANTHAP7physical
25416956
LZTS2_HUMANLZTS2physical
25416956
LNX1_HUMANLNX1physical
25416956
K1C40_HUMANKRT40physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
RL26L_HUMANRPL26L1physical
26186194
RL26_HUMANRPL26physical
26186194
NIP7_HUMANNIP7physical
26186194
ASPM_HUMANASPMphysical
26186194
DDX24_HUMANDDX24physical
26186194
ZN512_HUMANZNF512physical
26186194
RL7_HUMANRPL7physical
26186194
CEBPZ_HUMANCEBPZphysical
26186194
EXOC1_HUMANEXOC1physical
26186194
RS3A_HUMANRPS3Aphysical
26186194
NOP56_HUMANNOP56physical
26186194
RL13_HUMANRPL13physical
26186194
CG050_HUMANC7orf50physical
26186194
EBP2_HUMANEBNA1BP2physical
26186194
FBX11_HUMANFBXO11physical
26186194
NOP2_HUMANNOP2physical
26186194
RS27A_HUMANRPS27Aphysical
26186194
RBM34_HUMANRBM34physical
26186194
PUM3_HUMANKIAA0020physical
26186194
RL32_HUMANRPL32physical
26186194
RL13A_HUMANRPL13Aphysical
26186194
RL18A_HUMANRPL18Aphysical
26186194
NLE1_HUMANNLE1physical
26186194
ASH1L_HUMANASH1Lphysical
26186194
TRI26_HUMANTRIM26physical
26186194
RS27A_HUMANRPS27Aphysical
28514442
RL26L_HUMANRPL26L1physical
28514442
EXOC1_HUMANEXOC1physical
28514442
NLE1_HUMANNLE1physical
28514442
TRI26_HUMANTRIM26physical
28514442
CEBPZ_HUMANCEBPZphysical
28514442
RL18A_HUMANRPL18Aphysical
28514442
FBX11_HUMANFBXO11physical
28514442
NOP2_HUMANNOP2physical
28514442
PUM3_HUMANKIAA0020physical
28514442
RL32_HUMANRPL32physical
28514442
ASH1L_HUMANASH1Lphysical
28514442

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 THAP7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASSSPECTROMETRY.

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