INT6_HUMAN - dbPTM
INT6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INT6_HUMAN
UniProt AC Q9UL03
Protein Name Integrator complex subunit 6
Gene Name INTS6
Organism Homo sapiens (Human).
Sequence Length 887
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). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. [PubMed: 23904267 May have a tumor suppressor role; an ectopic expression suppressing tumor cell growth]
Protein Sequence MPILLFLIDTSASMNQRSHLGTTYLDTAKGAVETFMKLRARDPASRGDRYMLVTFEEPPYAIKAGWKENHATFMNELKNLQAEGLTTLGQSLRTAFDLLNLNRLVTGIDNYGQGRNPFFLEPAIIITITDGSKLTTTSGVQDELHLPLNSPLPGSELTKEPFRWDQRLFALVLRLPGTMSVESEQLTGVPLDDSAITPMCEVTGGRSYSVCSPRMLNQCLESLVQKVQSGVVINFEKAGPDPSPVEDGQPDISRPFGSQPWHSCHKLIYVRPNPKTGVPIGHWPVPESFWPDQNSPTLPPRTSHPVVKFSCTDCEPMVIDKLPFDKYELEPSPLTQFILERKSPQTCWQVYVSNSAKYSELGHPFGYLKASTALNCVNLFVMPYNYPVLLPLLDDLFKVHKAKPTLKWRQSFESYLKTMPPYYLGPLKKAVRMMGAPNLIADSMEYGLSYSVISYLKKLSQQAKIESDRVIGSVGKKVVQETGIKVRSRSHGLSMAYRKDFQQLLQGISEDVPHRLLDLNMKEYTGFQVALLNKDLKPQTFRNAYDIPRRNLLDHLTRMRSNLLKSTRRFLKGQDEDQVHSVPIAQMGNYQEYLKQVPSPLRELDPDQPRRLHTFGNPFKLDKKGMMIDEADEFVAGPQNKHKRPGEPNMQGIPKRRRCMSPLLRGRQQNPVVNNHIGGKGPPAPTTQAQPDLIKPLPLHKISETTNDSIIHDVVENHVADQLSSDITPNAMDTEFSASSPASLLERPTNHMEALGHDHLGTNDLTVGGFLENHEEPRDKEQCAEENIPASSLNKGKKLMHCRSHEEVNTELKAQIMKEIRKPGRKYERIFTLLKHVQGSLQTRLIFLQNVIKEASRFKKRMLIEQLENFLDEIHRRANQINHINSN
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
27PhosphorylationLGTTYLDTAKGAVET
CCCCHHHHHHHHHHH		27.8924719451
37UbiquitinationGAVETFMKLRARDPA
HHHHHHHHHHCCCCC		30.54-
72PhosphorylationGWKENHATFMNELKN
CCCHHHHHHHHHHHH		18.8324247654
135PhosphorylationITDGSKLTTTSGVQD
EECCCCEECCCCCCC		31.5927251275
136PhosphorylationTDGSKLTTTSGVQDE
ECCCCEECCCCCCCE		29.4227732954
137PhosphorylationDGSKLTTTSGVQDEL
CCCCEECCCCCCCEE		20.4627732954
138PhosphorylationGSKLTTTSGVQDELH
CCCEECCCCCCCEEE		34.5727732954
150PhosphorylationELHLPLNSPLPGSEL
EEECCCCCCCCCCHH		35.1830266825
155PhosphorylationLNSPLPGSELTKEPF
CCCCCCCCHHCCCCC		27.7430576142
158PhosphorylationPLPGSELTKEPFRWD
CCCCCHHCCCCCCHH		29.3428450419
159 (in isoform 1)Ubiquitination-75.8321906983
159UbiquitinationLPGSELTKEPFRWDQ
CCCCHHCCCCCCHHH		75.832190698
243PhosphorylationEKAGPDPSPVEDGQP
EECCCCCCCCCCCCC		49.2928348404
297PhosphorylationWPDQNSPTLPPRTSH
CCCCCCCCCCCCCCC		52.28-
326UbiquitinationIDKLPFDKYELEPSP
EEECCCCCCCCCCCC		40.79-
351PhosphorylationPQTCWQVYVSNSAKY
CCCEEEEEECCCHHH		5.3122817900
443PhosphorylationAPNLIADSMEYGLSY
CCCCHHHHHHHCHHH		12.4224043423
446PhosphorylationLIADSMEYGLSYSVI
CHHHHHHHCHHHHHH		18.0924043423
449PhosphorylationDSMEYGLSYSVISYL
HHHHHCHHHHHHHHH		15.8224043423
450PhosphorylationSMEYGLSYSVISYLK
HHHHCHHHHHHHHHH		16.4024043423
451PhosphorylationMEYGLSYSVISYLKK
HHHCHHHHHHHHHHH		15.0324043423
454PhosphorylationGLSYSVISYLKKLSQ
CHHHHHHHHHHHHHH		23.4324043423
455PhosphorylationLSYSVISYLKKLSQQ
HHHHHHHHHHHHHHH		16.0624043423
458UbiquitinationSVISYLKKLSQQAKI
HHHHHHHHHHHHHCC		51.26-
460PhosphorylationISYLKKLSQQAKIES
HHHHHHHHHHHCCCC		29.1724702127
476AcetylationRVIGSVGKKVVQETG
CCCHHHCHHHHHHHC		39.9925953088
477UbiquitinationVIGSVGKKVVQETGI
CCHHHCHHHHHHHCC		41.53-
482PhosphorylationGKKVVQETGIKVRSR
CHHHHHHHCCEEEEE		27.4129496963
485UbiquitinationVVQETGIKVRSRSHG
HHHHHCCEEEEECCC		32.70-
490PhosphorylationGIKVRSRSHGLSMAY
CCEEEEECCCCCHHH		24.1328555341
497PhosphorylationSHGLSMAYRKDFQQL
CCCCCHHHHHHHHHH		15.0024362263
499UbiquitinationGLSMAYRKDFQQLLQ
CCCHHHHHHHHHHHH		50.66-
545PhosphorylationPQTFRNAYDIPRRNL
CHHHHCHHHCCHHHH		20.2522817900
572UbiquitinationKSTRRFLKGQDEDQV
HHHHHHHCCCCHHCC		52.38-
581PhosphorylationQDEDQVHSVPIAQMG
CCHHCCCCCCHHHHC		30.6326074081
590PhosphorylationPIAQMGNYQEYLKQV
CHHHHCCHHHHHHCC		9.2926074081
593PhosphorylationQMGNYQEYLKQVPSP
HHCCHHHHHHCCCCC		12.0426074081
595UbiquitinationGNYQEYLKQVPSPLR
CCHHHHHHCCCCCHH		48.63-
599PhosphorylationEYLKQVPSPLRELDP
HHHHCCCCCHHHCCC		37.4026074081
614PhosphorylationDQPRRLHTFGNPFKL
CCCCCCCCCCCCCCC		37.5220068231
661PhosphorylationPKRRRCMSPLLRGRQ
CCHHHCCCHHHCCCC		18.9328857561
680AcetylationVNNHIGGKGPPAPTT
CCCCCCCCCCCCCCC		64.1326051181
695AcetylationQAQPDLIKPLPLHKI
CCCCCCCCCCCCCCC		48.0426051181
695UbiquitinationQAQPDLIKPLPLHKI
CCCCCCCCCCCCCCC		48.04-
791PhosphorylationAEENIPASSLNKGKK
HHHCCCHHHCCCCCC		29.9718669648
792PhosphorylationEENIPASSLNKGKKL
HHCCCHHHCCCCCCC		37.7625627689
795UbiquitinationIPASSLNKGKKLMHC
CCHHHCCCCCCCEEC		76.91-
804PhosphorylationKKLMHCRSHEEVNTE
CCCEECCCHHHHCHH		40.4223927012
810PhosphorylationRSHEEVNTELKAQIM
CCHHHHCHHHHHHHH		48.1228634120
886PhosphorylationNQINHINSN------
HHHHCCCCC------		43.2327251275
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 INT6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INT6_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 INT6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INT1_HUMANINTS1physical
20133760
INT2_HUMANINTS2physical
20133760
INT3_HUMANINTS3physical
20133760
INT4_HUMANINTS4physical
20133760
INT5_HUMANINTS5physical
20133760
INT6L_HUMANDDX26Bphysical
20133760
INT7_HUMANINTS7physical
20133760
INT8_HUMANINTS8physical
20133760
INT9_HUMANINTS9physical
20133760
INT10_HUMANINTS10physical
20133760
INT11_HUMANCPSF3Lphysical
20133760
INT12_HUMANINTS12physical
20133760
RPB1_HUMANPOLR2Aphysical
20133760
RPB2_HUMANPOLR2Bphysical
20133760
RPB3_HUMANPOLR2Cphysical
20133760
RPB4_HUMANPOLR2Dphysical
20133760
RPAB1_HUMANPOLR2Ephysical
20133760
RPB7_HUMANPOLR2Gphysical
20133760
RPAB3_HUMANPOLR2Hphysical
20133760
RPB11_HUMANPOLR2Jphysical
20133760
RPAB5_HUMANPOLR2Lphysical
20133760
2AAA_HUMANPPP2R1Aphysical
20133760
2AAB_HUMANPPP2R1Bphysical
20133760
PP1B_HUMANPPP1CBphysical
20133760
PP2AA_HUMANPPP2CAphysical
20133760
PP2AB_HUMANPPP2CBphysical
20133760
INT13_HUMANASUNphysical
20133760
INT14_HUMANVWA9physical
20133760
CG026_HUMANC7orf26physical
20133760
NAIF1_HUMANNAIF1physical
20133760
SOSB1_HUMANNABP2physical
20133760
PKCB1_HUMANZMYND8physical
20133760
ZN592_HUMANZNF592physical
20133760
ZN687_HUMANZNF687physical
20133760
MCM7_HUMANMCM7physical
17310990
LRP1_HUMANLRP1physical
28514442
INT3_HUMANINTS3physical
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 INT6_HUMAN

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Related Literatures of Post-Translational Modification
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-804, AND MASSSPECTROMETRY.

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