INT5_HUMAN - dbPTM
INT5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INT5_HUMAN
UniProt AC Q6P9B9
Protein Name Integrator complex subunit 5
Gene Name INTS5
Organism Homo sapiens (Human).
Sequence Length 1019
Subcellular Localization Nucleus membrane
Multi-pass membrane protein . Nucleus . Cytoplasm .
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 MSALCDPPGAPGPPGPAPATHGPAPLSAQELSQEIKAFLTGVDPILGHQLSAREHARCGLLLLRSLPPARAAVLDHLRGVFDESVRAHLAALDETPVAGPPHLRPPPPSHVPAGGPGLEDVVQEVQQVLSEFIRANPKAWAPVISAWSIDLMGQLSSTYSGQHQRVPHATGALNELLQLWMGCRATRTLMDIYVQCLSALIGSCPDACVDALLDTSVQHSPHFDWVVAHIGSSFPGTIISRVLSCGLKDFCVHGGAGGGAGSSGGSSSQTPSTDPFPGSPAIPAEKRVPKIASVVGILGHLASRHGDSIRRELLRMFHDSLAGGSGGRSGDPSLQATVPFLLQLAVMSPALLGTVSGELVDCLKPPAVLSQLQQHLQGFPREELDNMLNLAVHLVSQASGAGAYRLLQFLVDTAMPASVITTQGLAVPDTVREACDRLIQLLLLHLQKLVHHRGGSPGEGVLGPPPPPRLVPFLDALKNHVGELCGETLRLERKRFLWQHQLLGLLSVYTRPSCGPEALGHLLSRARSPEELSLATQLYAGLVVSLSGLLPLAFRSCLARVHAGTLQPPFTARFLRNLALLVGWEQQGGEGPAALGAHFGESASAHLSDLAPLLLHPEEEVAEAAASLLAICPFPSEALSPSQLLGLVRAGVHRFFASLRLHGPPGVASACQLLTRLSQTSPAGLKAVLQLLVEGALHRGNTELFGGQVDGDNETLSVVSASLASASLLDTNRRHTAAVPGPGGIWSVFHAGVIGRGLKPPKFVQSRNQQEVIYNTQSLLSLLVHCCSAPGGTECGECWGAPILSPEAAKAVAVTLVESVCPDAAGAELAWPPEEHARATVERDLRIGRRFREQPLLFELLKLVAAAPPALCYCSVLLRGLLAALLGHWEASRHPDTTHSPWHLEASCTLVAVMAEGSLLPPALGNMHEVFSQLAPFEVRLLLLSVWGFLREHGPLPQKFIFQSERGRFIRDFSREGGGEGGPHLAVLHSVLHRNIDRLGLFSGRFQAPSPSTLLRQGT
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------MSALCDPPG
------CCCCCCCCC		41.0519413330
244PhosphorylationTIISRVLSCGLKDFC
HHHHHHHHCCCCCEE		11.8623312004
262PhosphorylationGAGGGAGSSGGSSSQ
CCCCCCCCCCCCCCC		25.8527080861
263PhosphorylationAGGGAGSSGGSSSQT
CCCCCCCCCCCCCCC		46.3727080861
266PhosphorylationGAGSSGGSSSQTPST
CCCCCCCCCCCCCCC		30.2730108239
267PhosphorylationAGSSGGSSSQTPSTD
CCCCCCCCCCCCCCC		29.7330108239
268PhosphorylationGSSGGSSSQTPSTDP
CCCCCCCCCCCCCCC		39.5130108239
270PhosphorylationSGGSSSQTPSTDPFP
CCCCCCCCCCCCCCC		22.5830108239
272PhosphorylationGSSSQTPSTDPFPGS
CCCCCCCCCCCCCCC		49.1628450419
273PhosphorylationSSSQTPSTDPFPGSP
CCCCCCCCCCCCCCC		49.2328450419
279PhosphorylationSTDPFPGSPAIPAEK
CCCCCCCCCCCCHHH		16.0525159151
286UbiquitinationSPAIPAEKRVPKIAS
CCCCCHHHCCHHHHH		61.88-
430PhosphorylationQGLAVPDTVREACDR
CCCCCCHHHHHHHHH		18.52-
456PhosphorylationLVHHRGGSPGEGVLG
HHHCCCCCCCCCCCC		32.3428555341
528PhosphorylationHLLSRARSPEELSLA
HHHHHCCCHHHHHHH		35.3625072903
533PhosphorylationARSPEELSLATQLYA
CCCHHHHHHHHHHHH		21.1625072903
536PhosphorylationPEELSLATQLYAGLV
HHHHHHHHHHHHHHH		25.1325072903
539PhosphorylationLSLATQLYAGLVVSL
HHHHHHHHHHHHHCH		6.7125072903
545PhosphorylationLYAGLVVSLSGLLPL
HHHHHHHCHHCHHHH		14.8825072903
547PhosphorylationAGLVVSLSGLLPLAF
HHHHHCHHCHHHHHH		21.6425072903
571PhosphorylationGTLQPPFTARFLRNL
CCCCCCHHHHHHHHH		23.7724719451
680PhosphorylationLLTRLSQTSPAGLKA
HHHHHHCCCHHHHHH		33.05-
686UbiquitinationQTSPAGLKAVLQLLV
CCCHHHHHHHHHHHH		35.22-
1003PhosphorylationIDRLGLFSGRFQAPS
CCCCCCCCCCCCCCC		33.8224719451
1010PhosphorylationSGRFQAPSPSTLLRQ
CCCCCCCCHHHHHCC		34.2030266825
1012PhosphorylationRFQAPSPSTLLRQGT
CCCCCCHHHHHCCCC		35.7030266825
1013PhosphorylationFQAPSPSTLLRQGT-
CCCCCHHHHHCCCC-		32.9430266825
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 INT5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INT5_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 INT5_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
INT6_HUMANINTS6physical
20133760
INT6L_HUMANDDX26Bphysical
20133760
INT7_HUMANINTS7physical
20133760
INT8_HUMANINTS8physical
20133760
INT9_HUMANINTS9physical
20133760
INT11_HUMANCPSF3Lphysical
20133760
INT12_HUMANINTS12physical
20133760
RPB1_HUMANPOLR2Aphysical
20133760
RPB2_HUMANPOLR2Bphysical
20133760
RPB3_HUMANPOLR2Cphysical
20133760
INT10_HUMANINTS10physical
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
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
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 INT5_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-279, AND MASSSPECTROMETRY.
"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-1010, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory