THOC1_HUMAN - dbPTM
THOC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THOC1_HUMAN
UniProt AC Q96FV9
Protein Name THO complex subunit 1
Gene Name THOC1
Organism Homo sapiens (Human).
Sequence Length 657
Subcellular Localization Isoform 1: Nucleus speckle. Nucleus, nucleoplasm. Nucleus matrix. Cytoplasm. Can shuttle between the nucleus and cytoplasm. Nuclear localization is required for induction of apoptotic cell death. Translocates to the cytoplasm during the early phase o
Protein Description Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation.; Participates in an apoptotic pathway which is characterized by activation of caspase-6, increases in the expression of BAK1 and BCL2L1 and activation of NF-kappa-B. This pathway does not require p53/TP53, nor does the presence of p53/TP53 affect the efficiency of cell killing. Activates a G2/M cell cycle checkpoint prior to the onset of apoptosis. Apoptosis is inhibited by association with RB1..
Protein Sequence MSPTPPLFSLPEARTRFTKSTREALNNKNIKPLLSTFSQVPGSENEKKCTLDQAFRGILEEEIINHSSCENVLAIISLAIGGVTEGICTASTPFVLLGDVLDCLPLDQCDTIFTFVEKNVATWKSNTFYSAGKNYLLRMCNDLLRRLSKSQNTVFCGRIQLFLARLFPLSEKSGLNLQSQFNLENVTVFNTNEQESTLGQKHTEDREEGMDVEEGEMGDEEAPTTCSIPIDYNLYRKFWSLQDYFRNPVQCYEKISWKTFLKYSEEVLAVFKSYKLDDTQASRKKMEELKTGGEHVYFAKFLTSEKLMDLQLSDSNFRRHILLQYLILFQYLKGQVKFKSSNYVLTDEQSLWIEDTTKSVYQLLSENPPDGERFSKMVEHILNTEENWNSWKNEGCPSFVKERTSDTKPTRIIRKRTAPEDFLGKGPTKKILMGNEELTRLWNLCPDNMEACKSETREHMPTLEEFFEEAIEQADPENMVENEYKAVNNSNYGWRALRLLARRSPHFFQPTNQQFKSLPEYLENMVIKLAKELPPPSEEIKTGEDEDEEDNDALLKENESPDVRRDKPVTGEQIEVFANKLGEQWKILAPYLEMKDSEIRQIECDSEDMKMRAKQLLVAWQDQEGVHATPENLINALNKSGLSDLAESLTNDNETNS
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
1Acetylation-------MSPTPPLF
-------CCCCCCCC		11.0520068231
2Phosphorylation------MSPTPPLFS
------CCCCCCCCC		37.1629255136
4Phosphorylation----MSPTPPLFSLP
----CCCCCCCCCCH		30.1730266825
9PhosphorylationSPTPPLFSLPEARTR
CCCCCCCCCHHHHHH		51.1823663014
15PhosphorylationFSLPEARTRFTKSTR
CCCHHHHHHCCHHHH		36.8624719451
18PhosphorylationPEARTRFTKSTREAL
HHHHHHCCHHHHHHH		22.3124719451
28UbiquitinationTREALNNKNIKPLLS
HHHHHHCCCCHHHHH		60.0022817900
31SumoylationALNNKNIKPLLSTFS
HHHCCCCHHHHHHHH		38.7228112733
31 (in isoform 1)Ubiquitination-38.7221890473
31 (in isoform 2)Ubiquitination-38.7221890473
31SumoylationALNNKNIKPLLSTFS
HHHCCCCHHHHHHHH		38.72-
31UbiquitinationALNNKNIKPLLSTFS
HHHCCCCHHHHHHHH		38.7222817900
47AcetylationVPGSENEKKCTLDQA
CCCCCCCCCCCHHHH		65.8125953088
99UbiquitinationTPFVLLGDVLDCLPL
CCEEEECCHHHCCCH		37.4621890473
122PhosphorylationFVEKNVATWKSNTFY
EEHHCCCCCCCCCHH		29.1928348404
125PhosphorylationKNVATWKSNTFYSAG
HCCCCCCCCCHHHCC		32.4428348404
127PhosphorylationVATWKSNTFYSAGKN
CCCCCCCCHHHCCHH		30.9228348404
129PhosphorylationTWKSNTFYSAGKNYL
CCCCCCHHHCCHHHH		8.7924719451
130PhosphorylationWKSNTFYSAGKNYLL
CCCCCHHHCCHHHHH		26.7628348404
133MalonylationNTFYSAGKNYLLRMC
CCHHHCCHHHHHHHH		41.9826320211
133AcetylationNTFYSAGKNYLLRMC
CCHHHCCHHHHHHHH		41.9819608861
173PhosphorylationLFPLSEKSGLNLQSQ
HCCCCCCCCCCCCCC		44.4522468782
191PhosphorylationENVTVFNTNEQESTL
CCEEEEECCHHCCCC		28.7722468782
203PhosphorylationSTLGQKHTEDREEGM
CCCCCCCCCCHHCCC		46.7627251275
224PhosphorylationMGDEEAPTTCSIPID
CCCCCCCCCCCCEEC		47.7027251275
225PhosphorylationGDEEAPTTCSIPIDY
CCCCCCCCCCCEECH		11.8227251275
227PhosphorylationEEAPTTCSIPIDYNL
CCCCCCCCCEECHHH		29.3427251275
232PhosphorylationTCSIPIDYNLYRKFW
CCCCEECHHHHHHHH		14.0527251275
235PhosphorylationIPIDYNLYRKFWSLQ
CEECHHHHHHHHCHH		14.2327251275
237AcetylationIDYNLYRKFWSLQDY
ECHHHHHHHHCHHHH		37.3126051181
237 (in isoform 1)Ubiquitination-37.3121890473
237 (in isoform 2)Ubiquitination-37.3121890473
237UbiquitinationIDYNLYRKFWSLQDY
ECHHHHHHHHCHHHH		37.3122817900
240PhosphorylationNLYRKFWSLQDYFRN
HHHHHHHCHHHHHCC		21.2027251275
254AcetylationNPVQCYEKISWKTFL
CHHHHHHHCCHHHHH		18.6326051181
258AcetylationCYEKISWKTFLKYSE
HHHHCCHHHHHHCCH		23.7026051181
258UbiquitinationCYEKISWKTFLKYSE
HHHHCCHHHHHHCCH		23.70-
263PhosphorylationSWKTFLKYSEEVLAV
CHHHHHHCCHHHHHH		24.38-
264PhosphorylationWKTFLKYSEEVLAVF
HHHHHHCCHHHHHHH		26.20-
272AcetylationEEVLAVFKSYKLDDT
HHHHHHHHHCCCCCH		46.4019821611
273PhosphorylationEVLAVFKSYKLDDTQ
HHHHHHHHCCCCCHH		18.9420860994
274PhosphorylationVLAVFKSYKLDDTQA
HHHHHHHCCCCCHHH		19.0322817900
290UbiquitinationRKKMEELKTGGEHVY
HHHHHHHHCCCCEEE		48.6929967540
290AcetylationRKKMEELKTGGEHVY
HHHHHHHHCCCCEEE		48.6925953088
300AcetylationGEHVYFAKFLTSEKL
CCEEEEEEHHHCHHH		30.8919608861
306AcetylationAKFLTSEKLMDLQLS
EEHHHCHHHHHCCCC		49.2126051181
310UbiquitinationTSEKLMDLQLSDSNF
HCHHHHHCCCCCCHH		3.2524816145
313PhosphorylationKLMDLQLSDSNFRRH
HHHHCCCCCCHHHHH		26.4920363803
315PhosphorylationMDLQLSDSNFRRHIL
HHCCCCCCHHHHHHH		34.2020363803
359PhosphorylationWIEDTTKSVYQLLSE
EEEHHHHHHHHHHHH		24.7820068231
376UbiquitinationPDGERFSKMVEHILN
CCCHHHHHHHHHHHC		44.2329967540
392UbiquitinationEENWNSWKNEGCPSF
HHHHHHHCCCCCCHH		44.9629967540
401AcetylationEGCPSFVKERTSDTK
CCCCHHHHHCCCCCC		39.1926051181
401UbiquitinationEGCPSFVKERTSDTK
CCCCHHHHHCCCCCC		39.19-
408SumoylationKERTSDTKPTRIIRK
HHCCCCCCCCEEEEC		49.7525218447
408SumoylationKERTSDTKPTRIIRK
HHCCCCCCCCEEEEC		49.75-
417PhosphorylationTRIIRKRTAPEDFLG
CEEEECCCCCHHHCC		49.9928555341
425MethylationAPEDFLGKGPTKKIL
CCHHHCCCCCCCEEE		64.96115979957
425AcetylationAPEDFLGKGPTKKIL
CCHHHCCCCCCCEEE		64.9625953088
425UbiquitinationAPEDFLGKGPTKKIL
CCHHHCCCCCCCEEE		64.9629967540
428PhosphorylationDFLGKGPTKKILMGN
HHCCCCCCCEEECCC		54.35-
430UbiquitinationLGKGPTKKILMGNEE
CCCCCCCEEECCCHH		43.4829967540
433SulfoxidationGPTKKILMGNEELTR
CCCCEEECCCHHHHH		6.5321406390
439PhosphorylationLMGNEELTRLWNLCP
ECCCHHHHHHHHHCC		27.3120068231
453UbiquitinationPDNMEACKSETREHM
CCCHHHHHHHHHHHC		59.3729967540
479UbiquitinationEQADPENMVENEYKA
HHCCHHHHCCCCHHH		3.6924816145
484PhosphorylationENMVENEYKAVNNSN
HHHCCCCHHHHHCCC		18.8121406692
490PhosphorylationEYKAVNNSNYGWRAL
CHHHHHCCCHHHHHH		26.6521406692
492PhosphorylationKAVNNSNYGWRALRL
HHHHCCCHHHHHHHH		20.2021406692
504PhosphorylationLRLLARRSPHFFQPT
HHHHHHCCCCCCCCC		19.7120873877
521PhosphorylationQFKSLPEYLENMVIK
HHHCHHHHHHHHHHH		19.85-
531UbiquitinationNMVIKLAKELPPPSE
HHHHHHHHCCCCCHH		70.94-
537PhosphorylationAKELPPPSEEIKTGE
HHCCCCCHHHCCCCC		54.3521815630
542PhosphorylationPPSEEIKTGEDEDEE
CCHHHCCCCCCCCHH		52.0125159151
560PhosphorylationALLKENESPDVRRDK
HHHHCCCCCCCCCCC		37.6729255136
567AcetylationSPDVRRDKPVTGEQI
CCCCCCCCCCCHHHH		39.3126051181
570PhosphorylationVRRDKPVTGEQIEVF
CCCCCCCCHHHHHHH		43.4526074081
580UbiquitinationQIEVFANKLGEQWKI
HHHHHHHHHHHHHHH		55.2129967540
580AcetylationQIEVFANKLGEQWKI
HHHHHHHHHHHHHHH		55.2126051181
580SumoylationQIEVFANKLGEQWKI
HHHHHHHHHHHHHHH		55.2128112733
595UbiquitinationLAPYLEMKDSEIRQI
HHHHHHCCHHHHEEE		49.0432015554
595SumoylationLAPYLEMKDSEIRQI
HHHHHHCCHHHHEEE		49.0425114211
595SumoylationLAPYLEMKDSEIRQI
HHHHHHCCHHHHEEE		49.04-
610UbiquitinationECDSEDMKMRAKQLL
ECCHHHHHHHHHHHH		37.2424816145
617UbiquitinationKMRAKQLLVAWQDQE
HHHHHHHHHHHHCCC		1.9824816145
640PhosphorylationLINALNKSGLSDLAE
HHHHHHHCCHHHHHH		43.8420873877
643PhosphorylationALNKSGLSDLAESLT
HHHHCCHHHHHHHHH		33.8220873877
648PhosphorylationGLSDLAESLTNDNET
CHHHHHHHHHCCCCC		34.5830108239
650PhosphorylationSDLAESLTNDNETNS
HHHHHHHHCCCCCCC		50.2130108239
655PhosphorylationSLTNDNETNS-----
HHHCCCCCCC-----		47.1930576142
657PhosphorylationTNDNETNS-------
HCCCCCCC-------		49.3625262027
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
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:23460917
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THOC1_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 THOC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_HUMANRB1physical
7525595
THOC2_HUMANTHOC2physical
22939629
THOC3_HUMANTHOC3physical
22939629
DX39B_HUMANDDX39Bphysical
22939629
THOC5_HUMANTHOC5physical
22939629
THOC7_HUMANTHOC7physical
22939629
THOC6_HUMANTHOC6physical
22939629
ZCHC8_HUMANZCCHC8physical
22939629
UTRO_HUMANUTRNphysical
22939629
ZC3HF_HUMANZC3H15physical
22939629
UBR7_HUMANUBR7physical
22939629
U3IP2_HUMANRRP9physical
22939629
XPO4_HUMANXPO4physical
22939629
VPS53_HUMANVPS53physical
22939629
TR112_HUMANTRMT112physical
22939629
TPM3_HUMANTPM3physical
22939629
TPM1_HUMANTPM1physical
22939629
UBP13_HUMANUSP13physical
22939629
ZN830_HUMANZNF830physical
22939629
SF3B2_HUMANSF3B2physical
22365833
RED_HUMANIKphysical
22365833
DHX8_HUMANDHX8physical
22365833
THOC1_HUMANTHOC1physical
22365833
F10C1_HUMANFRA10AC1physical
22365833
THOC5_HUMANTHOC5physical
22365833
S30BP_HUMANSAP30BPphysical
22365833
MEP50_HUMANWDR77physical
22365833
RABX5_HUMANRABGEF1physical
25416956
TRI54_HUMANTRIM54physical
25416956
MOAP1_HUMANMOAP1physical
25416956
USBP1_HUMANUSHBP1physical
25416956
THOC5_HUMANTHOC5physical
26344197
DSRAD_HUMANADARphysical
26496610
DHX9_HUMANDHX9physical
26496610
FMR1_HUMANFMR1physical
26496610
GELS_HUMANGSNphysical
26496610
ANM1_HUMANPRMT1physical
26496610
SP110_HUMANSP110physical
26496610
IKBL1_HUMANNFKBIL1physical
26496610
DX39B_HUMANDDX39Bphysical
26496610
FXR1_HUMANFXR1physical
26496610
DUS11_HUMANDUSP11physical
26496610
THOC5_HUMANTHOC5physical
26496610
TOP3B_HUMANTOP3Bphysical
26496610
BCLF1_HUMANBCLAF1physical
26496610
IF4A3_HUMANEIF4A3physical
26496610
ZC11A_HUMANZC3H11Aphysical
26496610
TR150_HUMANTHRAP3physical
26496610
THOC4_HUMANALYREFphysical
26496610
DX39A_HUMANDDX39Aphysical
26496610
KIF1C_HUMANKIF1Cphysical
26496610
B4GT7_HUMANB4GALT7physical
26496610
ZC3HD_HUMANZC3H13physical
26496610
ZZEF1_HUMANZZEF1physical
26496610
ZC3H3_HUMANZC3H3physical
26496610
CHTOP_HUMANCHTOPphysical
26496610
RB15B_HUMANRBM15Bphysical
26496610
RT17_HUMANMRPS17physical
26496610
GTSE1_HUMANGTSE1physical
26496610
CN166_HUMANC14orf166physical
26496610
RBM27_HUMANRBM27physical
26496610
NCBP3_HUMANC17orf85physical
26496610
BCCIP_HUMANBCCIPphysical
26496610
THOC2_HUMANTHOC2physical
26496610
SFR19_HUMANSCAF1physical
26496610
THOC6_HUMANTHOC6physical
26496610
ZC3HE_HUMANZC3H14physical
26496610
CAAP1_HUMANCAAP1physical
26496610
THOC7_HUMANTHOC7physical
26496610
TDRD3_HUMANTDRD3physical
26496610
UIF_HUMANFYTTD1physical
26496610
PDIP3_HUMANPOLDIP3physical
26496610
THOC3_HUMANTHOC3physical
26496610
SARNP_HUMANSARNPphysical
26496610
PWP2A_HUMANPWWP2Aphysical
26496610
ATG4A_HUMANATG4Aphysical
26496610
SYTC2_HUMANTARSL2physical
26496610
CS047_HUMANC19orf47physical
26496610
RBM33_HUMANRBM33physical
26496610
ZC3H1_HUMANZFC3H1physical
26496610
CO052_HUMANC15orf52physical
26496610
NEDD4_HUMANNEDD4physical
23460917
THOC7_HUMANTHOC7physical
28514442
THOC5_HUMANTHOC5physical
28514442
THOC2_HUMANTHOC2physical
28514442
THOC6_HUMANTHOC6physical
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 THOC1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133 AND LYS-300, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND MASSSPECTROMETRY.

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