HEXI2_HUMAN - dbPTM
HEXI2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HEXI2_HUMAN
UniProt AC Q96MH2
Protein Name Protein HEXIM2
Gene Name HEXIM2
Organism Homo sapiens (Human).
Sequence Length 286
Subcellular Localization Nucleus .
Protein Description Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation..
Protein Sequence MMATPNQTACNAESPVALEEAKTSGAPGSPQTPPERHDSGGSLPLTPRMESHSEDEDLAGAVGGLGWNSRSPRTQSPGGCSAEAVLARKKHRRRPSKRKRHWRPYLELSWAEKQQRDERQSQRASRVREEMFAKGQPVAPYNTTQFLMNDRDPEEPNLDVPHGISHPGSSGESEAGDSDGRGRAHGEFQRKDFSETYERFHTESLQGRSKQELVRDYLELEKRLSQAEEETRRLQQLQACTGQQSCRQVEELAAEVQRLRTENQRLRQENQMWNREGCRCDEEPGT
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
4Phosphorylation----MMATPNQTACN
----CCCCCCCCCCC		12.6025159151
8PhosphorylationMMATPNQTACNAESP
CCCCCCCCCCCCCCC		39.5626074081
14PhosphorylationQTACNAESPVALEEA
CCCCCCCCCCCHHHH		23.4322199227
23PhosphorylationVALEEAKTSGAPGSP
CCHHHHHHCCCCCCC		39.1730266825
24PhosphorylationALEEAKTSGAPGSPQ
CHHHHHHCCCCCCCC		32.0523927012
29PhosphorylationKTSGAPGSPQTPPER
HHCCCCCCCCCCCCC		16.8729255136
32PhosphorylationGAPGSPQTPPERHDS
CCCCCCCCCCCCCCC		44.1629255136
36PhosphorylationSPQTPPERHDSGGSL
CCCCCCCCCCCCCCC		44.69-
39PhosphorylationTPPERHDSGGSLPLT
CCCCCCCCCCCCCCC		38.6427273156
42PhosphorylationERHDSGGSLPLTPRM
CCCCCCCCCCCCCCC		30.2727273156
45PhosphorylationDSGGSLPLTPRMESH
CCCCCCCCCCCCCCC		14.4518669648
46PhosphorylationSGGSLPLTPRMESHS
CCCCCCCCCCCCCCC		13.6027273156
51PhosphorylationPLTPRMESHSEDEDL
CCCCCCCCCCCCCCH		23.9925159151
53PhosphorylationTPRMESHSEDEDLAG
CCCCCCCCCCCCHHH		56.9025159151
54PhosphorylationPRMESHSEDEDLAGA
CCCCCCCCCCCHHHH		61.0619651622
61PhosphorylationEDEDLAGAVGGLGWN
CCCCHHHHCCCCCCC		7.38-
64PhosphorylationDLAGAVGGLGWNSRS
CHHHHCCCCCCCCCC		17.89-
68PhosphorylationAVGGLGWNSRSPRTQ
HCCCCCCCCCCCCCC		26.2518220336
69PhosphorylationVGGLGWNSRSPRTQS
CCCCCCCCCCCCCCC		27.8523927012
71PhosphorylationGLGWNSRSPRTQSPG
CCCCCCCCCCCCCCC		20.6822115753
73PhosphorylationGWNSRSPRTQSPGGC
CCCCCCCCCCCCCCC		46.7920068231
74PhosphorylationWNSRSPRTQSPGGCS
CCCCCCCCCCCCCCC		36.4629255136
75PhosphorylationNSRSPRTQSPGGCSA
CCCCCCCCCCCCCCH		49.2420068231
76PhosphorylationSRSPRTQSPGGCSAE
CCCCCCCCCCCCCHH		25.5419664994
81PhosphorylationTQSPGGCSAEAVLAR
CCCCCCCCHHHHHHH		32.2125159151
89AcetylationAEAVLARKKHRRRPS
HHHHHHHHHHHCCCC		47.5312655687
90AcetylationEAVLARKKHRRRPSK
HHHHHHHHHHCCCCC		36.4712655697
91PhosphorylationAVLARKKHRRRPSKR
HHHHHHHHHCCCCCC		31.3618669648
93PhosphorylationLARKKHRRRPSKRKR
HHHHHHHCCCCCCCC		55.3620068231
96PhosphorylationKKHRRRPSKRKRHWR
HHHHCCCCCCCCCCH		43.1920068231
98PhosphorylationHRRRPSKRKRHWRPY
HHCCCCCCCCCCHHH		45.6519664994
103PhosphorylationSKRKRHWRPYLELSW
CCCCCCCHHHHHHHH		12.1218669648
105PhosphorylationRKRHWRPYLELSWAE
CCCCCHHHHHHHHHH		12.3027642862
143PhosphorylationQPVAPYNTTQFLMND
CCCCCCCHHHHHCCC		19.0128787133
144PhosphorylationPVAPYNTTQFLMNDR
CCCCCCHHHHHCCCC		17.4328787133
165PhosphorylationLDVPHGISHPGSSGE
CCCCCCCCCCCCCCC		28.3723663014
169PhosphorylationHGISHPGSSGESEAG
CCCCCCCCCCCCCCC		39.3523663014
170PhosphorylationGISHPGSSGESEAGD
CCCCCCCCCCCCCCC		53.1223663014
173PhosphorylationHPGSSGESEAGDSDG
CCCCCCCCCCCCCCC		35.9523663014
178PhosphorylationGESEAGDSDGRGRAH
CCCCCCCCCCCCCCC		40.8423663014
187PhosphorylationGRGRAHGEFQRKDFS
CCCCCCCCHHCCCHH		28.83-
191PhosphorylationAHGEFQRKDFSETYE
CCCCHHCCCHHHHHH		52.95-
192PhosphorylationHGEFQRKDFSETYER
CCCHHCCCHHHHHHH		55.27-
194PhosphorylationEFQRKDFSETYERFH
CHHCCCHHHHHHHHH		38.8822617229
196PhosphorylationQRKDFSETYERFHTE
HCCCHHHHHHHHHHH		29.5028796482
197PhosphorylationRKDFSETYERFHTES
CCCHHHHHHHHHHHH		10.8928796482
199MethylationDFSETYERFHTESLQ
CHHHHHHHHHHHHHC		20.4556117471
202PhosphorylationETYERFHTESLQGRS
HHHHHHHHHHHCCCC		25.2627732954
204PhosphorylationYERFHTESLQGRSKQ
HHHHHHHHHCCCCHH		27.4427732954
215MethylationRSKQELVRDYLELEK
CCHHHHHHHHHHHHH		39.2156117473
215DimethylationRSKQELVRDYLELEK
CCHHHHHHHHHHHHH		39.21-
216PhosphorylationSKQELVRDYLELEKR
CHHHHHHHHHHHHHH		44.91-
221MethylationVRDYLELEKRLSQAE
HHHHHHHHHHHHHHH		27.10-
222UbiquitinationRDYLELEKRLSQAEE
HHHHHHHHHHHHHHH		71.8629967540
223MethylationDYLELEKRLSQAEEE
HHHHHHHHHHHHHHH		30.1456117469
223DimethylationDYLELEKRLSQAEEE
HHHHHHHHHHHHHHH		30.14-
225PhosphorylationLELEKRLSQAEEETR
HHHHHHHHHHHHHHH		31.2329214152
237MethylationETRRLQQLQACTGQQ
HHHHHHHHHHHHCHH		1.94-
244UbiquitinationLQACTGQQSCRQVEE
HHHHHCHHHHHHHHH		45.93-
245MethylationQACTGQQSCRQVEEL
HHHHCHHHHHHHHHH		11.90-
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 HEXI2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HEXI2_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 HEXI2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDK9_HUMANCDK9physical
15713661
HEXI1_HUMANHEXIM1physical
15713661
HEXI2_HUMANHEXIM2physical
25416956
IHO1_HUMANCCDC36physical
25416956
HEXI2_HUMANHEXIM2physical
21516116
ZN250_HUMANZNF250physical
21516116
PRD14_HUMANPRDM14physical
21516116
HTF4_HUMANTCF12physical
21516116
CCNT1_HUMANCCNT1physical
28514442
CDK9_HUMANCDK9physical
28514442
HTF4_HUMANTCF12physical
28514442
CCNT2_HUMANCCNT2physical
28514442
SURF2_HUMANSURF2physical
28514442
CSK22_HUMANCSNK2A2physical
28514442
SAHH3_HUMANAHCYL2physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
MEPCE_HUMANMEPCEphysical
28514442
BANP_HUMANBANPphysical
28514442
SAHH2_HUMANAHCYL1physical
28514442
CSK2B_HUMANCSNK2Bphysical
28514442
MYCBP_HUMANMYCBPphysical
28514442
LARP7_HUMANLARP7physical
28514442
HUTH_HUMANHALphysical
28514442
USP9X_HUMANUSP9Xphysical
28514442
RIOX2_HUMANMINAphysical
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 HEXI2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASSSPECTROMETRY.
"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-29; THR-32; THR-74;SER-76 AND SER-81, AND MASS 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-29; THR-32; THR-46;SER-51; SER-53; SER-76 AND SER-81, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-53, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46, AND MASSSPECTROMETRY.

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