INT3_HUMAN - dbPTM
INT3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INT3_HUMAN
UniProt AC Q68E01
Protein Name Integrator complex subunit 3
Gene Name INTS3
Organism Homo sapiens (Human).
Sequence Length 1043
Subcellular Localization Nucleus . Cytoplasm . Localizes to nuclear foci following DNA damage.
Protein Description Component of the Integrator (INT) complex. The Integrator complex is 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; Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. The SOSS complex is required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. In the SOSS complex, it is required for the assembly of the complex and for stabilization of the complex at DNA damage sites.]
Protein Sequence MELQKGKGAAAAAAASGAAGGGGGGAGAGAPGGGRLLLSTSLDAKDELEERLERCMSIVTSMTAGVSEREANDALNAYVCKGLPQHEEICLGLFTLILTEPAQAQKCYRDLALVSRDGMNIVLNKINQILMEKYLKLQDTCRTQLVWLVRELVKSGVLGADGVCMTFMKQIAGGGDVTAKNIWLAESVLDILTEQREWVLKSSILIAMAVYTYLRLIVDHHGTAQLQALRQKEVDFCISLLRERFMECLMIGRDLVRLLQNVARIPEFELLWKDIIHNPQALSPQFTGILQLLQSRTSRKFLACRLTPDMETKLLFMTSRVRFGQQKRYQDWFQRQYLSTPDSQSLRCDLIRYICGVVHPSNEVLSSDILPRWAIIGWLLTTCTSNVAASNAKLALFYDWLFFSPDKDSIMNIEPAILVMHHSMKPHPAITATLLDFMCRIIPNFYPPLEGHVRQGVFSSLNHIVEKRVLAHLAPLFDNPKLDKELRAMLREKFPEFCSSPSPPVEVKIEEPVSMEMDNHMSDKDESCYDNAEAAFSDDEEDLNSKGKKREFRFHPIKETVVEEPVDITPYLDQLDESLRDKVLQLQKGSDTEAQCEVMQEIVDQVLEEDFDSEQLSVLASCLQELFKAHFRGEVLPEEITEESLEESVGKPLYLIFRNLCQMQEDNSSFSLLLDLLSELYQKQPKIGYHLLYYLRASKAAAGKMNLYESFAQATQLGDLHTCLMMDMKACQEDDVRLLCHLTPSIYTEFPDETLRSGELLNMIVAVIDSAQLQELVCHVMMGNLVMFRKDSVLNILIQSLDWETFEQYCAWQLFLAHNIPLETIIPILQHLKYKEHPEALSCLLLQLRREKPSEEMVKMVLSRPCHPDDQFTTSILRHWCMKHDELLAEHIKSLLIKNNSLPRKRQSLRSSSSKLAQLTLEQILEHLDNLRLNLTNTKQNFFSQTPILQALQHVQASCDEAHKMKFSDLFSLAEEYEDSSTKPPKSRRKAALSSPRSRKNATQPPNAEEESGSSSASEEEDTKPKPTKRKRKGSSAVGSDSD
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-------MELQKGKG
-------CCCCCCHH		47.9322814378
5Acetylation---MELQKGKGAAAA
---CCCCCCHHHHHH		75.1925953088
5Ubiquitination---MELQKGKGAAAA
---CCCCCCHHHHHH		75.1922817900
7Acetylation-MELQKGKGAAAAAA
-CCCCCCHHHHHHHH		53.0326051181
7Ubiquitination-MELQKGKGAAAAAA
-CCCCCCHHHHHHHH		53.0321906983
7 (in isoform 1)Ubiquitination-53.0321890473
7 (in isoform 2)Ubiquitination-53.0321890473
12 (in isoform 4)Phosphorylation-7.9129116813
14 (in isoform 4)Phosphorylation-9.4629507054
16PhosphorylationAAAAAAASGAAGGGG
HHHHHHHCCCCCCCC		25.0020068231
16 (in isoform 2)Phosphorylation-25.00-
45AcetylationLSTSLDAKDELEERL
EECCCCCHHHHHHHH		51.9426051181
133AcetylationINQILMEKYLKLQDT
HHHHHHHHHHHHHHH		41.7526051181
134PhosphorylationNQILMEKYLKLQDTC
HHHHHHHHHHHHHHH		8.8620860994
1362-HydroxyisobutyrylationILMEKYLKLQDTCRT
HHHHHHHHHHHHHHH		40.80-
155PhosphorylationLVRELVKSGVLGADG
HHHHHHHCCCCCCCC		27.0120068231
166PhosphorylationGADGVCMTFMKQIAG
CCCCCHHHHHHHHHC		18.5620068231
166 (in isoform 2)Phosphorylation-18.56-
211PhosphorylationILIAMAVYTYLRLIV
HHHHHHHHHHHHHHH		4.7125072903
212PhosphorylationLIAMAVYTYLRLIVD
HHHHHHHHHHHHHHC		14.9625072903
213PhosphorylationIAMAVYTYLRLIVDH
HHHHHHHHHHHHHCC		3.3825072903
283PhosphorylationIHNPQALSPQFTGIL
HCCHHHCCHHHHHHH		21.48-
337PhosphorylationQDWFQRQYLSTPDSQ
HHHHHHHHCCCCCHH		12.57-
353PhosphorylationLRCDLIRYICGVVHP
HHHHHHHHHHCCCCC		8.12-
371UbiquitinationVLSSDILPRWAIIGW
HHCCCCHHHHHHHHH		30.0521890473
371 (in isoform 4)Ubiquitination-30.0521890473
410UbiquitinationFSPDKDSIMNIEPAI
CCCCHHHCCCCCCHH		3.3421890473
410 (in isoform 4)Ubiquitination-3.3421890473
427UbiquitinationMHHSMKPHPAITATL
HCCCCCCCHHHHHHH		20.9322817900
446PhosphorylationCRIIPNFYPPLEGHV
HHHCCCCCCCCCCHH		15.58-
451UbiquitinationNFYPPLEGHVRQGVF
CCCCCCCCHHHCCHH		32.0721963094
467AcetylationSLNHIVEKRVLAHLA
HCHHHHHHHHHHHHH		36.5925953088
492UbiquitinationELRAMLREKFPEFCS
HHHHHHHHHCHHHHC		55.9029967540
498 (in isoform 2)Phosphorylation-3.6227251275
499PhosphorylationEKFPEFCSSPSPPVE
HHCHHHHCCCCCCCE		51.0830266825
500PhosphorylationKFPEFCSSPSPPVEV
HCHHHHCCCCCCCEE		30.4930266825
501PhosphorylationFPEFCSSPSPPVEVK
CHHHHCCCCCCCEEE		34.2619413330
501 (in isoform 2)Phosphorylation-34.2624719451
502PhosphorylationPEFCSSPSPPVEVKI
HHHHCCCCCCCEEEE		43.7329255136
514PhosphorylationVKIEEPVSMEMDNHM
EEECCCCCCCCCCCC		21.5330576142
521PhosphorylationSMEMDNHMSDKDESC
CCCCCCCCCCCCCCH		7.5018669648
521 (in isoform 2)Phosphorylation-7.50-
522PhosphorylationMEMDNHMSDKDESCY
CCCCCCCCCCCCCHH		33.6818669648
527PhosphorylationHMSDKDESCYDNAEA
CCCCCCCCHHHCHHH		28.2730576142
529PhosphorylationSDKDESCYDNAEAAF
CCCCCCHHHCHHHHC		22.8530576142
536PhosphorylationYDNAEAAFSDDEEDL
HHCHHHHCCCCHHHH		12.1019413330
536 (in isoform 2)Phosphorylation-12.1024719451
537PhosphorylationDNAEAAFSDDEEDLN
HCHHHHCCCCHHHHH		39.1522167270
545PhosphorylationDDEEDLNSKGKKREF
CCHHHHHHCCCCCCC		50.5123663014
557UbiquitinationREFRFHPIKETVVEE
CCCCCCCCCCCEEEC		4.7729967540
558AcetylationEFRFHPIKETVVEEP
CCCCCCCCCCEEECC		52.3526051181
578PhosphorylationYLDQLDESLRDKVLQ
HHHHHCHHHHHHHHH		28.5025159151
581UbiquitinationQLDESLRDKVLQLQK
HHCHHHHHHHHHHHC		51.1929967540
652 (in isoform 3)Ubiquitination-21.9521890473
681PhosphorylationLDLLSELYQKQPKIG
HHHHHHHHHHCCCHH		15.04-
691 (in isoform 3)Ubiquitination-2.1821890473
710PhosphorylationGKMNLYESFAQATQL
CCCCHHHHHHHHHHH		16.6020860994
715PhosphorylationYESFAQATQLGDLHT
HHHHHHHHHHCCHHH		16.5520860994
722PhosphorylationTQLGDLHTCLMMDMK
HHHCCHHHHHHCCHH		18.0320860994
803UbiquitinationILIQSLDWETFEQYC
HHHHCCCHHHHHHHH		16.3021890473
842UbiquitinationKEHPEALSCLLLQLR
CCCHHHHHHHHHHHH		15.1221890473
858UbiquitinationEKPSEEMVKMVLSRP
CCCCHHHHHHHHCCC		4.0121890473
858 (in isoform 2)Ubiquitination-4.0121890473
859UbiquitinationKPSEEMVKMVLSRPC
CCCHHHHHHHHCCCC		23.2121890473
859 (in isoform 1)Ubiquitination-23.2121890473
875PhosphorylationPDDQFTTSILRHWCM
CCCHHHHHHHHHHHH		19.3024719451
892UbiquitinationDELLAEHIKSLLIKN
HHHHHHHHHHHHHHC		2.1429967540
893AcetylationELLAEHIKSLLIKNN
HHHHHHHHHHHHHCC		36.6425953088
897UbiquitinationEHIKSLLIKNNSLPR
HHHHHHHHHCCCCCH		5.6421890473
897 (in isoform 2)Ubiquitination-5.6421890473
898UbiquitinationHIKSLLIKNNSLPRK
HHHHHHHHCCCCCHH		50.4721890473
898 (in isoform 1)Ubiquitination-50.4721890473
908PhosphorylationSLPRKRQSLRSSSSK
CCCHHHHHHHCCHHH		29.7730576142
912PhosphorylationKRQSLRSSSSKLAQL
HHHHHHCCHHHHHHH		32.0030576142
914UbiquitinationQSLRSSSSKLAQLTL
HHHHCCHHHHHHHHH		33.3733845483
914 (in isoform 2)Ubiquitination-33.3721890473
915UbiquitinationSLRSSSSKLAQLTLE
HHHCCHHHHHHHHHH		50.192190698
915 (in isoform 1)Ubiquitination-50.1921890473
938UbiquitinationLRLNLTNTKQNFFSQ
CCCCCCCCCCCCCCC		28.8621963094
939UbiquitinationRLNLTNTKQNFFSQT
CCCCCCCCCCCCCCC		45.36-
946PhosphorylationKQNFFSQTPILQALQ
CCCCCCCCHHHHHHH		15.8825159151
965UbiquitinationSCDEAHKMKFSDLFS
CCHHHHHCCHHHHHH		3.6829967540
968PhosphorylationEAHKMKFSDLFSLAE
HHHHCCHHHHHHHHH		28.0823312004
972PhosphorylationMKFSDLFSLAEEYED
CCHHHHHHHHHHHCC		33.6923312004
977PhosphorylationLFSLAEEYEDSSTKP
HHHHHHHHCCCCCCC		19.2823312004
980PhosphorylationLAEEYEDSSTKPPKS
HHHHHCCCCCCCCHH		28.1523312004
981PhosphorylationAEEYEDSSTKPPKSR
HHHHCCCCCCCCHHH		53.4223312004
982PhosphorylationEEYEDSSTKPPKSRR
HHHCCCCCCCCHHHH		52.0723312004
982UbiquitinationEEYEDSSTKPPKSRR
HHHCCCCCCCCHHHH		52.0729967540
983AcetylationEYEDSSTKPPKSRRK
HHCCCCCCCCHHHHH		62.3626051181
985UbiquitinationEDSSTKPPKSRRKAA
CCCCCCCCHHHHHHH		49.1329967540
993 (in isoform 2)Phosphorylation-6.6021406692
994PhosphorylationSRRKAALSSPRSRKN
HHHHHHHCCCCHHCC		33.3030266825
994 (in isoform 2)Phosphorylation-33.3024719451
995PhosphorylationRRKAALSSPRSRKNA
HHHHHHCCCCHHCCC		25.7830266825
998PhosphorylationAALSSPRSRKNATQP
HHHCCCCHHCCCCCC		51.4929514088
1003PhosphorylationPRSRKNATQPPNAEE
CCHHCCCCCCCCCCC		51.5121406692
1011 (in isoform 2)Phosphorylation-52.4821406692
1012PhosphorylationPPNAEEESGSSSASE
CCCCCCCCCCCCCCC		47.4520363803
1013 (in isoform 2)Phosphorylation-34.5221406692
1014PhosphorylationNAEEESGSSSASEEE
CCCCCCCCCCCCCCC		30.3320363803
1014 (in isoform 2)Phosphorylation-30.3321406692
1015PhosphorylationAEEESGSSSASEEED
CCCCCCCCCCCCCCC		33.1920363803
1015 (in isoform 2)Phosphorylation-33.1921406692
1016PhosphorylationEEESGSSSASEEEDT
CCCCCCCCCCCCCCC		37.2020363803
1017 (in isoform 2)Phosphorylation-23.9421406692
1018PhosphorylationESGSSSASEEEDTKP
CCCCCCCCCCCCCCC		47.7020363803
1023PhosphorylationSASEEEDTKPKPTKR
CCCCCCCCCCCCCCC		53.1521406692
1028PhosphorylationEDTKPKPTKRKRKGS
CCCCCCCCCCCCCCC		50.0021406692
1034PhosphorylationPTKRKRKGSSAVGSD
CCCCCCCCCCCCCCC		30.7619651622
1034 (in isoform 2)Phosphorylation-30.76-
1035PhosphorylationTKRKRKGSSAVGSDS
CCCCCCCCCCCCCCC		20.4033259812
1035 (in isoform 2)Phosphorylation-20.40-
1036PhosphorylationKRKRKGSSAVGSDSD
CCCCCCCCCCCCCCC		35.3320068231
1039PhosphorylationRKGSSAVGSDSD---
CCCCCCCCCCCC---		26.0019651622
1039 (in isoform 2)Phosphorylation-26.0021406692
1040PhosphorylationKGSSAVGSDSD----
CCCCCCCCCCC----		27.6128176443
1041PhosphorylationGSSAVGSDSD-----
CCCCCCCCCC-----		51.3919651622
1041 (in isoform 2)Phosphorylation-51.3924719451
1042PhosphorylationSSAVGSDSD------
CCCCCCCCC------		47.0928176443
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 INT3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INT3_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 INT3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INT1_HUMANINTS1physical
20133760
INT2_HUMANINTS2physical
20133760
INT4_HUMANINTS4physical
20133760
INT5_HUMANINTS5physical
20133760
INT6_HUMANINTS6physical
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
2AAA_HUMANPPP2R1Aphysical
20133760
2AAB_HUMANPPP2R1Bphysical
20133760
PP2AB_HUMANPPP2CBphysical
20133760
INT13_HUMANASUNphysical
20133760
INT14_HUMANVWA9physical
20133760
CG026_HUMANC7orf26physical
20133760
NAIF1_HUMANNAIF1physical
20133760
SOSB1_HUMANNABP2physical
20133760
SOSB2_HUMANNABP1physical
20133760
PKCB1_HUMANZMYND8physical
20133760
ZN592_HUMANZNF592physical
20133760
ZN687_HUMANZNF687physical
20133760
SOSB1_HUMANNABP2physical
19683501
SOSB2_HUMANNABP1physical
19683501
SOSSC_HUMANINIPphysical
19683501
A4_HUMANAPPphysical
21832049
SOSSC_HUMANINIPphysical
22939629
SOSSC_HUMANINIPphysical
26344197
INT1_HUMANINTS1physical
26344197
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 INT3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-537, ANDMASS SPECTROMETRY.
"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-502 AND SER-537, ANDMASS SPECTROMETRY.
"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-502, AND MASSSPECTROMETRY.

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