TRIP4_HUMAN - dbPTM
TRIP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIP4_HUMAN
UniProt AC Q15650
Protein Name Activating signal cointegrator 1 {ECO:0000303|PubMed:10454579}
Gene Name TRIP4 {ECO:0000312|EMBL:AAC41738.1, ECO:0000312|HGNC:HGNC:12310}
Organism Homo sapiens (Human).
Sequence Length 581
Subcellular Localization Nucleus . Cytoplasm, cytosol . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasmic under conditions of serum deprivation (PubMed:10454579). Colocalizes with NEK6 in the centrosome (PubMed:20873783).
Protein Description Transcription coactivator which associates with nuclear receptors, transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription. May thereby play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a role in thyroid hormone receptor and estrogen receptor transactivation. [PubMed: 10454579]
Protein Sequence MAVAGAVSGEPLVHWCTQQLRKTFGLDVSEEIIQYVLSIESAEEIREYVTDLLQGNEGKKGQFIEELITKWQKNDQELISDPLQQCFKKDEILDGQKSGDHLKRGRKKGRNRQEVPAFTEPDTTAEVKTPFDLAKAQENSNSVKKKTKFVNLYTREGQDRLAVLLPGRHPCDCLGQKHKLINNCLICGRIVCEQEGSGPCLFCGTLVCTHEEQDILQRDSNKSQKLLKKLMSGVENSGKVDISTKDLLPHQELRIKSGLEKAIKHKDKLLEFDRTSIRRTQVIDDESDYFASDSNQWLSKLERETLQKREEELRELRHASRLSKKVTIDFAGRKILEEENSLAEYHSRLDETIQAIANGTLNQPLTKLDRSSEEPLGVLVNPNMYQSPPQWVDHTGAASQKKAFRSSGFGLEFNSFQHQLRIQDQEFQEGFDGGWCLSVHQPWASLLVRGIKRVEGRSWYTPHRGRLWIAATAKKPSPQEVSELQATYRLLRGKDVEFPNDYPSGCLLGCVDLIDCLSQKQFKEQFPDISQESDSPFVFICKNPQEMVVKFPIKGNPKIWKLDSKIHQGAKKGLMKQNKAV
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------MAVAGAVSG
------CCCCCCCCC		10.4019413330
8PhosphorylationMAVAGAVSGEPLVHW
CCCCCCCCCCCHHHH		36.5824043423
15UbiquitinationSGEPLVHWCTQQLRK
CCCCHHHHHHHHHHH		4.5621890473
17PhosphorylationEPLVHWCTQQLRKTF
CCHHHHHHHHHHHHH		17.7324043423
26UbiquitinationQLRKTFGLDVSEEII
HHHHHHCCCCCHHHH		5.2627667366
31UbiquitinationFGLDVSEEIIQYVLS
HCCCCCHHHHHHHHC		37.5729967540
38UbiquitinationEIIQYVLSIESAEEI
HHHHHHHCCCCHHHH		17.7929967540
69PhosphorylationQFIEELITKWQKNDQ
HHHHHHHHHHHHCCH		38.56-
70UbiquitinationFIEELITKWQKNDQE
HHHHHHHHHHHCCHH		40.4022817900
73UbiquitinationELITKWQKNDQELIS
HHHHHHHHCCHHHCC		62.4729967540
88UbiquitinationDPLQQCFKKDEILDG
HHHHHHHCCCHHHCC		67.9329967540
89UbiquitinationPLQQCFKKDEILDGQ
HHHHHHCCCHHHCCC		40.1029967540
95UbiquitinationKKDEILDGQKSGDHL
CCCHHHCCCCCCHHH		33.1133845483
98PhosphorylationEILDGQKSGDHLKRG
HHHCCCCCCHHHHHH		41.3829214152
104UbiquitinationKSGDHLKRGRKKGRN
CCCHHHHHHHHCCCC		57.4133845483
123PhosphorylationPAFTEPDTTAEVKTP
CCCCCCCCCCEECCH		38.3228555341
128UbiquitinationPDTTAEVKTPFDLAK
CCCCCEECCHHHHHH		41.8229967540
129PhosphorylationDTTAEVKTPFDLAKA
CCCCEECCHHHHHHH		34.0721815630
135UbiquitinationKTPFDLAKAQENSNS
CCHHHHHHHHHCCCH		58.8821906983
137UbiquitinationPFDLAKAQENSNSVK
HHHHHHHHHCCCHHH		50.0932015554
140PhosphorylationLAKAQENSNSVKKKT
HHHHHHCCCHHHHHH		29.7229978859
142PhosphorylationKAQENSNSVKKKTKF
HHHHCCCHHHHHHEE		34.8229978859
147PhosphorylationSNSVKKKTKFVNLYT
CCHHHHHHEEEECEE		38.3029083192
153PhosphorylationKTKFVNLYTREGQDR
HHEEEECEECCCCCE		9.8825394399
154PhosphorylationTKFVNLYTREGQDRL
HEEEECEECCCCCEE		25.9729083192
177UbiquitinationPCDCLGQKHKLINNC
CCCCCCCHHCHHCCC		40.6929967540
205PhosphorylationGPCLFCGTLVCTHEE
CCCEECCEEEECHHH		19.7319690332
209PhosphorylationFCGTLVCTHEEQDIL
ECCEEEECHHHHHHH		25.5022817900
232PhosphorylationKLLKKLMSGVENSGK
HHHHHHHHCCCCCCC		50.5624173317
237PhosphorylationLMSGVENSGKVDIST
HHHCCCCCCCCCCCH		26.87-
239UbiquitinationSGVENSGKVDISTKD
HCCCCCCCCCCCHHH		36.2333845483
245UbiquitinationGKVDISTKDLLPHQE
CCCCCCHHHCCCCCH		39.3222817900
256UbiquitinationPHQELRIKSGLEKAI
CCCHHHHHHHHHHHH		31.8527667366
261UbiquitinationRIKSGLEKAIKHKDK
HHHHHHHHHHHCCHH		61.5329967540
268UbiquitinationKAIKHKDKLLEFDRT
HHHHCCHHHHHCCCC		60.8329967540
274MethylationDKLLEFDRTSIRRTQ
HHHHHCCCCCCCEEE		35.38115918981
275PhosphorylationKLLEFDRTSIRRTQV
HHHHCCCCCCCEEEE		30.2824117733
276PhosphorylationLLEFDRTSIRRTQVI
HHHCCCCCCCEEEEE		18.2624117733
280PhosphorylationDRTSIRRTQVIDDES
CCCCCCEEEEECCCC		19.8327642862
287PhosphorylationTQVIDDESDYFASDS
EEEECCCCCCCCCCH		44.6029978859
289PhosphorylationVIDDESDYFASDSNQ
EECCCCCCCCCCHHH		15.4319605366
292PhosphorylationDESDYFASDSNQWLS
CCCCCCCCCHHHHHH		31.5029978859
293UbiquitinationESDYFASDSNQWLSK
CCCCCCCCHHHHHHH		48.4529967540
294PhosphorylationSDYFASDSNQWLSKL
CCCCCCCHHHHHHHH		28.5529978859
300UbiquitinationDSNQWLSKLERETLQ
CHHHHHHHHHHHHHH		52.8021906983
323PhosphorylationLRHASRLSKKVTIDF
HHHHHHHCCCEEEEC		29.3524719451
324UbiquitinationRHASRLSKKVTIDFA
HHHHHHCCCEEEECC		56.7232142685
325UbiquitinationHASRLSKKVTIDFAG
HHHHHCCCEEEECCC		41.0333845483
327PhosphorylationSRLSKKVTIDFAGRK
HHHCCCEEEECCCHH		24.5728857561
334UbiquitinationTIDFAGRKILEEENS
EEECCCHHHHHHHCC		51.2133845483
335UbiquitinationIDFAGRKILEEENSL
EECCCHHHHHHHCCH		5.8829967540
341PhosphorylationKILEEENSLAEYHSR
HHHHHHCCHHHHHHH		32.0329978859
345PhosphorylationEENSLAEYHSRLDET
HHCCHHHHHHHHHHH		10.2525394399
347PhosphorylationNSLAEYHSRLDETIQ
CCHHHHHHHHHHHHH		33.3723186163
367UbiquitinationTLNQPLTKLDRSSEE
CCCCCCCCCCCCCCC		56.9522817900
371PhosphorylationPLTKLDRSSEEPLGV
CCCCCCCCCCCCCEE		41.59-
385PhosphorylationVLVNPNMYQSPPQWV
EEECCCCCCCCCHHC		16.6918669648
387PhosphorylationVNPNMYQSPPQWVDH
ECCCCCCCCCHHCCC		22.5125159151
395PhosphorylationPPQWVDHTGAASQKK
CCHHCCCCCHHHHHH		24.8527174698
399PhosphorylationVDHTGAASQKKAFRS
CCCCCHHHHHHHHHH		41.8327174698
406PhosphorylationSQKKAFRSSGFGLEF
HHHHHHHHCCCCCEE		28.4928450419
407PhosphorylationQKKAFRSSGFGLEFN
HHHHHHHCCCCCEEC		33.6128450419
415PhosphorylationGFGLEFNSFQHQLRI
CCCCEECCCEEEEEE		31.4428857561
477PhosphorylationAATAKKPSPQEVSEL
EEECCCCCHHHHHHH		48.36-
482PhosphorylationKPSPQEVSELQATYR
CCCHHHHHHHHHHHH		31.66-
523UbiquitinationCLSQKQFKEQFPDIS
HHCCHHHHHHCCCCC		48.3829967540
554UbiquitinationMVVKFPIKGNPKIWK
EEEEEECCCCCCEEE		53.5332142685
5542-HydroxyisobutyrylationMVVKFPIKGNPKIWK
EEEEEECCCCCCEEE		53.53-
565UbiquitinationKIWKLDSKIHQGAKK
CEEECCHHHHHHHHH		43.8229967540
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 TRIP4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIP4_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 TRIP4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBP_HUMANCREBBPphysical
10454579
NCOA1_HUMANNCOA1physical
10454579
MED12_HUMANMED12physical
20133760
MED13_HUMANMED13physical
20133760
MED25_HUMANMED25physical
20133760
MED17_HUMANMED17physical
20133760
MED1_HUMANMED1physical
20133760
MED28_HUMANMED28physical
20133760
MED24_HUMANMED24physical
20133760
MED23_HUMANMED23physical
20133760
MED4_HUMANMED4physical
20133760
MED8_HUMANMED8physical
20133760
MED15_HUMANMED15physical
20133760
MED10_HUMANMED10physical
20133760
RPB1_HUMANPOLR2Aphysical
20133760
RCOR1_HUMANRCOR1physical
20133760
MED27_HUMANMED27physical
20133760
MED11_HUMANMED11physical
20133760
RXRA_HUMANRXRAphysical
10454579
THB_HUMANTHRBphysical
10454579
NFKB1_HUMANNFKB1physical
12077347
TF65_HUMANRELAphysical
12077347
JUN_HUMANJUNphysical
12077347
SRF_HUMANSRFphysical
12077347
CSRP1_HUMANCSRP1physical
26924529
ASCC1_HUMANASCC1physical
26924529
ASCC2_HUMANASCC2physical
26924529
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 TRIP4_HUMAN

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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, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-289, AND MASSSPECTROMETRY.

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