INT10_HUMAN - dbPTM
INT10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INT10_HUMAN
UniProt AC Q9NVR2
Protein Name Integrator complex subunit 10
Gene Name INTS10
Organism Homo sapiens (Human).
Sequence Length 710
Subcellular Localization Nucleus .
Protein Description Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). May be not involved in the recruitment of cytoplasmic dynein to the nuclear envelope by different components of the INT complex. [PubMed: 23904267]
Protein Sequence MSAQGDCEFLVQRARELVPQDLWAAKAWLITARSLYPADFNIQYEMYTIERNAERTATAGRLLYDMFVNFPDQPVVWREISIITSALRNDSQDKQTQFLRSLFETLPGRVQCEMLLKVTEQCFNTLERSEMLLLLLRRFPETVVQHGVGLGEALLEAETIEEQESPVNCFRKLFVCDVLPLIINNHDVRLPANLLYKYLNKAAEFYINYVTRSTQIENQHQGAQDTSDLMSPSKRSSQKYIIEGLTEKSSQIVDPWERLFKILNVVGMRCEWQMDKGRRSYGDILHRMKDLCRYMNNFDSEAHAKYKNQVVYSTMLVFFKNAFQYVNSIQPSLFQGPNAPSQVPLVLLEDVSNVYGDVEIDRNKHIHKKRKLAEGREKTMSSDDEDCSAKGRNRHIVVNKAELANSTEVLESFKLARESWELLYSLEFLDKEFTRICLAWKTDTWLWLRIFLTDMIIYQGQYKKAIASLHHLAALQGSISQPQITGQGTLEHQRALIQLATCHFALGEYRMTCEKVLDLMCYMVLPIQDGGKSQEEPSKVKPKFRKGSDLKLLPCTSKAIMPYCLHLMLACFKLRAFTDNRDDMALGHVIVLLQQEWPRGENLFLKAVNKICQQGNFQYENFFNYVTNIDMLEEFAYLRTQEGGKIHLELLPNQGMLIKHHTVTRGITKGVKEDFRLAMERQVSRCGENLMVVLHRFCINEKILLLQTLT
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
2Phosphorylation------MSAQGDCEF
------CCCCCHHHH		29.3325159151
26UbiquitinationPQDLWAAKAWLITAR
CHHHHHHHHHHHHHH		32.14-
35UbiquitinationWLITARSLYPADFNI
HHHHHHHHCCCCCCE		5.0422817900
81PhosphorylationPVVWREISIITSALR
CCCHHHHHHHHHHHH		11.82-
84PhosphorylationWREISIITSALRNDS
HHHHHHHHHHHHCCC		13.28-
94UbiquitinationLRNDSQDKQTQFLRS
HHCCCHHHHHHHHHH		47.8321906983
94AcetylationLRNDSQDKQTQFLRS
HHCCCHHHHHHHHHH		47.8326051181
118PhosphorylationQCEMLLKVTEQCFNT
HHHHHHHHHHHHHHH		7.8032142685
121UbiquitinationMLLKVTEQCFNTLER
HHHHHHHHHHHHHHH		27.9522817900
126UbiquitinationTEQCFNTLERSEMLL
HHHHHHHHHHHHHHH		5.5922817900
132PhosphorylationTLERSEMLLLLLRRF
HHHHHHHHHHHHHHC		2.4032645325
135UbiquitinationRSEMLLLLLRRFPET
HHHHHHHHHHHCCHH		3.3622817900
153PhosphorylationHGVGLGEALLEAETI
CCCCHHHHHHHCCCC		18.6932645325
172UbiquitinationSPVNCFRKLFVCDVL
CCCCHHHHHHHHCHH		26.48-
186PhosphorylationLPLIINNHDVRLPAN
HHHHHCCCCCCCCHH		30.3832142685
197AcetylationLPANLLYKYLNKAAE
CCHHHHHHHHHHHHH		43.1426051181
213PhosphorylationYINYVTRSTQIENQH
HHHHHHHCHHCHHCC		18.4624732914
214PhosphorylationINYVTRSTQIENQHQ
HHHHHHCHHCHHCCC		30.2124732914
226PhosphorylationQHQGAQDTSDLMSPS
CCCCCCCHHHHCCCC		16.4430266825
227PhosphorylationHQGAQDTSDLMSPSK
CCCCCCHHHHCCCCH		36.7230266825
231PhosphorylationQDTSDLMSPSKRSSQ
CCHHHHCCCCHHHCC		33.0629255136
233PhosphorylationTSDLMSPSKRSSQKY
HHHHCCCCHHHCCCC		33.1330266825
234UbiquitinationSDLMSPSKRSSQKYI
HHHCCCCHHHCCCCE		60.7322817900
236PhosphorylationLMSPSKRSSQKYIIE
HCCCCHHHCCCCEEE		40.6426074081
237PhosphorylationMSPSKRSSQKYIIEG
CCCCHHHCCCCEEEH		34.4226074081
239UbiquitinationPSKRSSQKYIIEGLT
CCHHHCCCCEEEHHC		40.1222817900
239AcetylationPSKRSSQKYIIEGLT
CCHHHCCCCEEEHHC		40.1226051181
240PhosphorylationSKRSSQKYIIEGLTE
CHHHCCCCEEEHHCH		10.2526074081
248UbiquitinationIIEGLTEKSSQIVDP
EEEHHCHHHHHCCCH		50.6121906983
261UbiquitinationDPWERLFKILNVVGM
CHHHHHHHHHHHHCC		51.37-
269PhosphorylationILNVVGMRCEWQMDK
HHHHHCCCEEEECCC		14.8532645325
280PhosphorylationQMDKGRRSYGDILHR
ECCCCCCCHHHHHHH		31.9127134283
281PhosphorylationMDKGRRSYGDILHRM
CCCCCCCHHHHHHHH		19.6021712546
300PhosphorylationRYMNNFDSEAHAKYK
HHHHCCCHHHHHHHH		32.33-
302UbiquitinationMNNFDSEAHAKYKNQ
HHCCCHHHHHHHHCH		16.3422817900
306PhosphorylationDSEAHAKYKNQVVYS
CHHHHHHHHCHHHHE		18.89-
312PhosphorylationKYKNQVVYSTMLVFF
HHHCHHHHEEHHHHH		10.28-
314PhosphorylationKNQVVYSTMLVFFKN
HCHHHHEEHHHHHHH		9.24-
319UbiquitinationYSTMLVFFKNAFQYV
HEEHHHHHHHHHHHH		4.6824816145
337PhosphorylationQPSLFQGPNAPSQVP
CHHHHCCCCCCCCCC		24.0332645325
361PhosphorylationVYGDVEIDRNKHIHK
HHCCEEECCCCCHHH		34.3032645325
379PhosphorylationLAEGREKTMSSDDED
HHHCCCCCCCCCCHH		19.9628985074
381PhosphorylationEGREKTMSSDDEDCS
HCCCCCCCCCCHHHH		35.5325159151
382PhosphorylationGREKTMSSDDEDCSA
CCCCCCCCCCHHHHH		37.9523401153
388PhosphorylationSSDDEDCSAKGRNRH
CCCCHHHHHCCCCCE		45.3928985074
414UbiquitinationTEVLESFKLARESWE
HHHHHHHHHHHHHHH		50.9822817900
415UbiquitinationEVLESFKLARESWEL
HHHHHHHHHHHHHHH		5.2422817900
424PhosphorylationRESWELLYSLEFLDK
HHHHHHHHHHHHHCH		24.67-
453PhosphorylationLWLRIFLTDMIIYQG
HHHHHHHHHHHHHCC		16.8725072903
458PhosphorylationFLTDMIIYQGQYKKA
HHHHHHHHCCHHHHH		8.8225072903
462PhosphorylationMIIYQGQYKKAIASL
HHHHCCHHHHHHHHH		22.6825072903
464SumoylationIYQGQYKKAIASLHH
HHCCHHHHHHHHHHH		39.8428112733
578PhosphorylationCFKLRAFTDNRDDMA
HHHHHHHCCCCHHHH		31.2322617229
586UbiquitinationDNRDDMALGHVIVLL
CCCHHHHHHHHHEEE		3.8024816145
672UbiquitinationRGITKGVKEDFRLAM
CCCCCCHHHHHHHHH		61.3024816145
672AcetylationRGITKGVKEDFRLAM
CCCCCCHHHHHHHHH		61.3023749302
673UbiquitinationGITKGVKEDFRLAME
CCCCCHHHHHHHHHH		61.0324816145
698UbiquitinationMVVLHRFCINEKILL
HHHHHHHHHCHHHHH		3.0924816145
699UbiquitinationVVLHRFCINEKILLL
HHHHHHHHCHHHHHH		7.3924816145
702UbiquitinationHRFCINEKILLLQTL
HHHHHCHHHHHHHHC		33.88-
708PhosphorylationEKILLLQTLT-----
HHHHHHHHCC-----		32.1320068231
710PhosphorylationILLLQTLT-------
HHHHHHCC-------		39.7020068231
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 INT10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INT10_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 INT10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB1_HUMANPOLR2Aphysical
16239144
RPB2_HUMANPOLR2Bphysical
16239144
RPB4_HUMANPOLR2Dphysical
16239144
RPAB1_HUMANPOLR2Ephysical
16239144
RPAB3_HUMANPOLR2Hphysical
16239144
INT1_HUMANINTS1physical
16239144
INT2_HUMANINTS2physical
16239144
INT3_HUMANINTS3physical
16239144
INT4_HUMANINTS4physical
16239144
INT5_HUMANINTS5physical
16239144
INT6_HUMANINTS6physical
16239144
INT7_HUMANINTS7physical
16239144
INT8_HUMANINTS8physical
16239144
INT9_HUMANINTS9physical
16239144
INT11_HUMANCPSF3Lphysical
16239144
INT12_HUMANINTS12physical
16239144
INT2_HUMANINTS2physical
26344197
INT13_HUMANASUNphysical
28514442
INT14_HUMANVWA9physical
28514442
PGK2_HUMANPGK2physical
28514442
ACTBL_HUMANACTBL2physical
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 INT10_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY.
"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-231, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY.

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