INT4_HUMAN - dbPTM
INT4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INT4_HUMAN
UniProt AC Q96HW7
Protein Name Integrator complex subunit 4
Gene Name INTS4
Organism Homo sapiens (Human).
Sequence Length 963
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]
Protein Sequence MAAHLKKRVYEEFTKVVQPQEEIATKKLRLTKPSKSAALHIDLCKATSPADALQYLLQFARKPVEAESVEGVVRILLEHYYKENDPSVRLKIASLLGLLSKTAGFSPDCIMDDAINILQNEKSHQVLAQLLDTLLAIGTKLPENQAIQMRLVDVACKHLTDTSHGVRNKCLQLLGNLGSLEKSVTKDAEGLAARDVQKIIGDYFSDQDPRVRTAAIKAMLQLHERGLKLHQTIYNQACKLLSDDYEQVRSAAVQLIWVVSQLYPESIVPIPSSNEEIRLVDDAFGKICHMVSDGSWVVRVQAAKLLGSMEQVSSHFLEQTLDKKLMSDLRRKRTAHERAKELYSSGEFSSGRKWGDDAPKEEVDTGAVNLIESGACGAFVHGLEDEMYEVRIAAVEALCMLAQSSPSFAEKCLDFLVDMFNDEIEEVRLQSIHTMRKISNNITLREDQLDTVLAVLEDSSRDIREALHELLCCTNVSTKEGIHLALVELLKNLTKYPTDRDSIWKCLKFLGSRHPTLVLPLVPELLSTHPFFDTAEPDMDDPAYIAVLVLIFNAAKTCPTMPALFSDHTFRHYAYLRDSLSHLVPALRLPGRKLVSSAVSPSIIPQEDPSQQFLQQSLERVYSLQHLDPQGAQELLEFTIRDLQRLGELQSELAGVADFSATYLRCQLLLIKALQEKLWNVAAPLYLKQSDLASAAAKQIMEETYKMEFMYSGVENKQVVIIHHMRLQAKALQLIVTARTTRGLDPLFGMCEKFLQEVDFFQRYFIADLPHLQDSFVDKLLDLMPRLMTSKPAEVVKILQTMLRQSAFLHLPLPEQIHKASATIIEPAGESDNPLRFTSGLVVALDVDATLEHVQDPQNTVKVQVLYPDGQAQMIHPKPADFRNPGPGRHRLITQVYLSHTAWTEACQVEVRLLLAYNSSARIPKCPWMEGGEMSPQVETSIEGTIPFSKPVKVYIMPKPARR
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
3 (in isoform 3)Phosphorylation-13.7723836654
4 (in isoform 3)Phosphorylation-28.7523836654
5 (in isoform 3)Phosphorylation-6.3223836654
10PhosphorylationAHLKKRVYEEFTKVV
HHHHHHHHHHHHHHC		17.49-
12 (in isoform 4)Phosphorylation-40.7122468782
15AcetylationRVYEEFTKVVQPQEE
HHHHHHHHHCCCHHH		45.8126051181
15UbiquitinationRVYEEFTKVVQPQEE
HHHHHHHHHCCCHHH		45.8129967540
25O-linked_GlycosylationQPQEEIATKKLRLTK
CCHHHHHCCCCCCCC		34.0830379171
26AcetylationPQEEIATKKLRLTKP
CHHHHHCCCCCCCCC		40.5723954790
26UbiquitinationPQEEIATKKLRLTKP
CHHHHHCCCCCCCCC		40.5722505724
27AcetylationQEEIATKKLRLTKPS
HHHHHCCCCCCCCCC		34.19132977
27UbiquitinationQEEIATKKLRLTKPS
HHHHHCCCCCCCCCC		34.19-
47PhosphorylationHIDLCKATSPADALQ
HHCCHHCCCHHHHHH		22.2728348404
48PhosphorylationIDLCKATSPADALQY
HCCHHCCCHHHHHHH		23.9728348404
62UbiquitinationYLLQFARKPVEAESV
HHHHHHCCCCCCCHH		50.4124816145
82AcetylationILLEHYYKENDPSVR
HHHHHHHHHCCHHHH		42.7625953088
82UbiquitinationILLEHYYKENDPSVR
HHHHHHHHHCCHHHH		42.7624816145
87PhosphorylationYYKENDPSVRLKIAS
HHHHCCHHHHHHHHH		23.8027155012
94PhosphorylationSVRLKIASLLGLLSK
HHHHHHHHHHHHHHH		27.8327155012
100PhosphorylationASLLGLLSKTAGFSP
HHHHHHHHHHCCCCC		32.7624719451
149SulfoxidationPENQAIQMRLVDVAC
CCCCHHHHHHHHHHH		2.6721406390
157UbiquitinationRLVDVACKHLTDTSH
HHHHHHHHHCCCCCH		31.73-
169UbiquitinationTSHGVRNKCLQLLGN
CCHHHHHHHHHHHHC		26.26-
182UbiquitinationGNLGSLEKSVTKDAE
HCHHHHHHHHCCCCC		56.3629967540
186AcetylationSLEKSVTKDAEGLAA
HHHHHHCCCCCHHHH		53.4326051181
186UbiquitinationSLEKSVTKDAEGLAA
HHHHHHCCCCCHHHH		53.4329967540
192 (in isoform 3)Ubiquitination-16.0021906983
198UbiquitinationLAARDVQKIIGDYFS
HHHHHHHHHHHHHCC		35.8229967540
205PhosphorylationKIIGDYFSDQDPRVR
HHHHHHCCCCCHHHH		28.29-
228UbiquitinationQLHERGLKLHQTIYN
HHHHHCHHHHHHHHH		46.9029967540
242O-linked_GlycosylationNQACKLLSDDYEQVR
HHHHHHCCCCHHHHH		38.5830379171
245PhosphorylationCKLLSDDYEQVRSAA
HHHCCCCHHHHHHHH		17.16-
292PhosphorylationGKICHMVSDGSWVVR
HHHHHHCCCCCEEEH		28.78-
304UbiquitinationVVRVQAAKLLGSMEQ
EEHHHHHHHHCCHHH		47.46-
323AcetylationFLEQTLDKKLMSDLR
HHHHHHCHHHHHHHH		51.4225953088
324UbiquitinationLEQTLDKKLMSDLRR
HHHHHCHHHHHHHHH		49.44-
340 (in isoform 1)Ubiquitination-55.2421906983
340 (in isoform 2)Ubiquitination-55.2421906983
340UbiquitinationRTAHERAKELYSSGE
HHHHHHHHHHHHCCC		55.2429967540
343PhosphorylationHERAKELYSSGEFSS
HHHHHHHHHCCCCCC		11.2430108239
344PhosphorylationERAKELYSSGEFSSG
HHHHHHHHCCCCCCC		44.4830108239
345PhosphorylationRAKELYSSGEFSSGR
HHHHHHHCCCCCCCC		28.8721815630
349PhosphorylationLYSSGEFSSGRKWGD
HHHCCCCCCCCCCCC		27.8130108239
350PhosphorylationYSSGEFSSGRKWGDD
HHCCCCCCCCCCCCC		48.1929978859
407PhosphorylationMLAQSSPSFAEKCLD
HHHHCCHHHHHHHHH		38.7524719451
443PhosphorylationRKISNNITLREDQLD
HHHHCCCCCCHHHHH		23.1422210691
495UbiquitinationELLKNLTKYPTDRDS
HHHHHHHCCCCCHHH		53.0129967540
496PhosphorylationLLKNLTKYPTDRDSI
HHHHHHCCCCCHHHH		13.2130266825
498PhosphorylationKNLTKYPTDRDSIWK
HHHHCCCCCHHHHHH		40.3430266825
502PhosphorylationKYPTDRDSIWKCLKF
CCCCCHHHHHHHHHH		31.1030266825
596PhosphorylationLPGRKLVSSAVSPSI
CCCCCCCCCCCCCCC		24.0225022875
597PhosphorylationPGRKLVSSAVSPSII
CCCCCCCCCCCCCCC		25.8025022875
600PhosphorylationKLVSSAVSPSIIPQE
CCCCCCCCCCCCCCC		16.7923401153
602PhosphorylationVSSAVSPSIIPQEDP
CCCCCCCCCCCCCCH		26.1630278072
610PhosphorylationIIPQEDPSQQFLQQS
CCCCCCHHHHHHHHH		49.2728450419
617PhosphorylationSQQFLQQSLERVYSL
HHHHHHHHHHHHHCC		21.1620068231
639PhosphorylationAQELLEFTIRDLQRL
HHHHHHHHHHHHHHH		13.0124719451
660PhosphorylationLAGVADFSATYLRCQ
HCCCCCHHHHHHHHH		21.9019690332
677UbiquitinationLIKALQEKLWNVAAP
HHHHHHHHHHHCHHC		45.93-
686PhosphorylationWNVAAPLYLKQSDLA
HHCHHCHHHCHHHHH		15.7020068231
688UbiquitinationVAAPLYLKQSDLASA
CHHCHHHCHHHHHHH		33.9129967540
698UbiquitinationDLASAAAKQIMEETY
HHHHHHHHHHHHHHH		35.3129967540
737PhosphorylationKALQLIVTARTTRGL
HHHHHHHHHHHCCCC		11.93-
740PhosphorylationQLIVTARTTRGLDPL
HHHHHHHHCCCCCHH		20.55-
741PhosphorylationLIVTARTTRGLDPLF
HHHHHHHCCCCCHHH		19.72-
791SumoylationMPRLMTSKPAEVVKI
HHHHCCCCHHHHHHH		38.8025114211
791SumoylationMPRLMTSKPAEVVKI
HHHHCCCCHHHHHHH		38.80-
801PhosphorylationEVVKILQTMLRQSAF
HHHHHHHHHHHHCCC		18.0918187866
935PhosphorylationWMEGGEMSPQVETSI
CCCCCCCCCCEEEEE		14.1028102081
940PhosphorylationEMSPQVETSIEGTIP
CCCCCEEEEEECEEC		35.8328102081
941PhosphorylationMSPQVETSIEGTIPF
CCCCEEEEEECEECC		12.7228102081
945PhosphorylationVETSIEGTIPFSKPV
EEEEEECEECCCCCE		16.8228102081
949PhosphorylationIEGTIPFSKPVKVYI
EECEECCCCCEEEEE		30.6028102081
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 INT4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INT4_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 INT4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INT9_HUMANINTS9physical
22939629
CG026_HUMANC7orf26physical
26344197
INT11_HUMANCPSF3Lphysical
26344197
FA98A_HUMANFAM98Aphysical
26344197
INT5_HUMANINTS5physical
26344197
INT9_HUMANINTS9physical
26344197
BMP2K_HUMANBMP2Kphysical
28514442
AP2A1_HUMANAP2A1physical
28514442
AP2A2_HUMANAP2A2physical
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 INT4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-801, AND MASSSPECTROMETRY.

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