HEXI1_HUMAN - dbPTM
HEXI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HEXI1_HUMAN
UniProt AC O94992
Protein Name Protein HEXIM1
Gene Name HEXIM1
Organism Homo sapiens (Human).
Sequence Length 359
Subcellular Localization Nucleus . Cytoplasm . Binds alpha-importin and is mostly nuclear (PubMed:16362050).
Protein Description Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. [PubMed: 14580347]
Protein Sequence MAEPFLSEYQHQPQTSNCTGAAAVQEELNPERPPGAEERVPEEDSRWQSRAFPQLGGRPGPEGEGSLESQPPPLQTQACPESSCLREGEKGQNGDDSSAGGDFPPPAEVEPTPEAELLAQPCHDSEASKLGAPAAGGEEEWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRIRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYSKRAAAKSDDTSDDDFMEEGGEEDGGSDGMGGDGSEFLQRDFSETYERYHTESLQNMSKQELIKEYLELEKCLSRMEDENNRLRLESKRLGGDDARVRELELELDRLRAENLQLLTENELHRQQERAPLSKFGD
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
66PhosphorylationPGPEGEGSLESQPPP
CCCCCCCCCCCCCCC		25.3529507054
69PhosphorylationEGEGSLESQPPPLQT
CCCCCCCCCCCCCCC		53.9625850435
76PhosphorylationSQPPPLQTQACPESS
CCCCCCCCCCCCCHH		26.3022210691
97PhosphorylationKGQNGDDSSAGGDFP
CCCCCCCCCCCCCCC		27.1626503892
98PhosphorylationGQNGDDSSAGGDFPP
CCCCCCCCCCCCCCC		37.6226503892
112PhosphorylationPPAEVEPTPEAELLA
CCCCCCCCCHHHHHC		21.9130576142
125PhosphorylationLAQPCHDSEASKLGA
HCCCCCCHHHHHCCC		16.0522777824
128PhosphorylationPCHDSEASKLGAPAA
CCCCHHHHHCCCCCC		25.1022777824
146MethylationEEWGQQQRQLGKKKH
HHHHHHHHHHCHHHC		29.3856117457
150UbiquitinationQQQRQLGKKKHRRRP
HHHHHHCHHHCCCCC		68.2129967540
158PhosphorylationKKHRRRPSKKKRHWK
HHCCCCCCCCCCCCC		56.1226657352
165AcetylationSKKKRHWKPYYKLTW
CCCCCCCCCCCCCCH		19.6023749302
167PhosphorylationKKRHWKPYYKLTWEE
CCCCCCCCCCCCHHH		14.9826657352
168PhosphorylationKRHWKPYYKLTWEEK
CCCCCCCCCCCHHHH		14.1926657352
169UbiquitinationRHWKPYYKLTWEEKK
CCCCCCCCCCHHHHH		33.3329967540
175UbiquitinationYKLTWEEKKKFDEKQ
CCCCHHHHHCCCHHH		50.1529967540
181UbiquitinationEKKKFDEKQSLRASR
HHHCCCHHHHHHHHH		47.2133845483
183PhosphorylationKKFDEKQSLRASRIR
HCCCHHHHHHHHHHH		30.7821857030
196UbiquitinationIRAEMFAKGQPVAPY
HHHHHHHCCCCCCCC		46.9821906983
206PhosphorylationPVAPYNTTQFLMDDH
CCCCCCCCCCCCCCC		17.43-
221UbiquitinationDQEEPDLKTGLYSKR
CCCCCCHHHCCCCHH		48.1824816145
226PhosphorylationDLKTGLYSKRAAAKS
CHHHCCCCHHHHHCC		22.2524719451
227UbiquitinationLKTGLYSKRAAAKSD
HHHCCCCHHHHHCCC		32.2829967540
227AcetylationLKTGLYSKRAAAKSD
HHHCCCCHHHHHCCC		32.2825953088
233PhosphorylationSKRAAAKSDDTSDDD
CHHHHHCCCCCCCHH		35.6726055452
236PhosphorylationAAAKSDDTSDDDFME
HHHCCCCCCCHHHHH		38.7626055452
237PhosphorylationAAKSDDTSDDDFMEE
HHCCCCCCCHHHHHH		46.1421955146
252PhosphorylationGGEEDGGSDGMGGDG
CCCCCCCCCCCCCCH		36.2021955146
260PhosphorylationDGMGGDGSEFLQRDF
CCCCCCHHHHHHHHH		29.8923663014
268PhosphorylationEFLQRDFSETYERYH
HHHHHHHHHHHHHHH		33.0628985074
270PhosphorylationLQRDFSETYERYHTE
HHHHHHHHHHHHHHH		29.5028796482
271PhosphorylationQRDFSETYERYHTES
HHHHHHHHHHHHHHH		8.3828796482
273MethylationDFSETYERYHTESLQ
HHHHHHHHHHHHHHH		20.3756117467
274PhosphorylationFSETYERYHTESLQN
HHHHHHHHHHHHHHH		10.93-
276PhosphorylationETYERYHTESLQNMS
HHHHHHHHHHHHHCC		20.5228555341
278PhosphorylationYERYHTESLQNMSKQ
HHHHHHHHHHHCCHH		36.0928555341
283PhosphorylationTESLQNMSKQELIKE
HHHHHHCCHHHHHHH		38.4420068231
284UbiquitinationESLQNMSKQELIKEY
HHHHHCCHHHHHHHH		36.7023000965
284AcetylationESLQNMSKQELIKEY
HHHHHCCHHHHHHHH		36.7020167786
289UbiquitinationMSKQELIKEYLELEK
CCHHHHHHHHHHHHH		53.5923000965
289AcetylationMSKQELIKEYLELEK
CCHHHHHHHHHHHHH		53.5956117465
291PhosphorylationKQELIKEYLELEKCL
HHHHHHHHHHHHHHH		10.65-
296UbiquitinationKEYLELEKCLSRMED
HHHHHHHHHHHHCCH		53.771961771
296MethylationKEYLELEKCLSRMED
HHHHHHHHHHHHCCH		53.77-
296AcetylationKEYLELEKCLSRMED
HHHHHHHHHHHHCCH		53.7720167786
331MethylationELELELDRLRAENLQ
HHHHHHHHHHHHHHH		38.40115478465
341PhosphorylationAENLQLLTENELHRQ
HHHHHHHHHHHHHHH		45.41-
347MethylationLTENELHRQQERAPL
HHHHHHHHHHHHCCH		53.1356117463
355PhosphorylationQQERAPLSKFGD---
HHHHCCHHHCCC---		25.5329083192
355O-linked_GlycosylationQQERAPLSKFGD---
HHHHCCHHHCCC---		25.5323301498
356UbiquitinationQERAPLSKFGD----
HHHCCHHHCCC----		62.1333845483
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
158SPhosphorylationKinasePKACAP17612
PSP
158SPhosphorylationKinasePRKCAP17252
GPS
158SPhosphorylationKinasePKCTQ04759
PSP
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:19617712
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HEXI1_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 HEXI1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNT1_HUMANCCNT1physical
12832472
CCNT2_HUMANCCNT2physical
12832472
CDK9_HUMANCDK9physical
12832472
TF65_HUMANRELAphysical
12581153
AFF1_HUMANAFF1physical
21030982
CDK9_HUMANCDK9physical
14580347
CCNT1_HUMANCCNT1physical
14580347
DHX9_HUMANDHX9physical
17531811
P53_HUMANTP53physical
22948151
CDK9_HUMANCDK9physical
22948151
CDK9_HUMANCDK9physical
15713661
ESR1_HUMANESR1physical
15940264
CCNT1_HUMANCCNT1physical
15940264
CCNT1_HUMANCCNT1physical
16109377
CDK9_HUMANCDK9physical
16109377
CDK9_HUMANCDK9physical
15169877
CCNT1_HUMANCCNT1physical
15169877
CDK9_HUMANCDK9physical
15201869
CCNT1_HUMANCCNT1physical
15201869
LARP7_HUMANLARP7physical
18483487
CCNT1_HUMANCCNT1physical
18483487
CDK9_HUMANCDK9physical
18483487
EGLN3_HUMANEGLN3physical
24015760
HDAC1_HUMANHDAC1physical
24015760
AP1M1_HUMANAP1M1physical
22863883
FHL2_HUMANFHL2physical
22863883
CDK9_HUMANCDK9physical
24367103
CCNT1_HUMANCCNT1physical
24367103
AFF1_HUMANAFF1physical
24367103
LARP7_HUMANLARP7physical
24367103
LARP7_HUMANLARP7physical
26186194
CDK9_HUMANCDK9physical
26186194
OSBL1_HUMANOSBPL1Aphysical
26186194
UBE2O_HUMANUBE2Ophysical
26186194
MEPCE_HUMANMEPCEphysical
26186194
CSK22_HUMANCSNK2A2physical
26186194
CSK21_HUMANCSNK2A1physical
26186194
EF1A2_HUMANEEF1A2physical
26186194
HEXI2_HUMANHEXIM2physical
26186194
CSK2B_HUMANCSNK2Bphysical
26186194
CCNT2_HUMANCCNT2physical
26186194
CCNT1_HUMANCCNT1physical
26186194
FAN_HUMANNSMAFphysical
26186194
PEO1_HUMANC10orf2physical
26186194
HEXI2_HUMANHEXIM2physical
28514442
CCNT2_HUMANCCNT2physical
28514442
CDK9_HUMANCDK9physical
28514442
CCNT1_HUMANCCNT1physical
28514442
OSBL1_HUMANOSBPL1Aphysical
28514442
MEPCE_HUMANMEPCEphysical
28514442
FAN_HUMANNSMAFphysical
28514442
CSK22_HUMANCSNK2A2physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
LARP7_HUMANLARP7physical
28514442
PEO1_HUMANC10orf2physical
28514442
EF1A2_HUMANEEF1A2physical
28514442
CCNT1_HUMANCCNT1physical
15855166
HEXI1_HUMANHEXIM1physical
15855166
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 HEXI1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; THR-236; SER-237AND SER-252, 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-97; SER-98; SER-233;THR-236; SER-237 AND SER-252, 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-97 AND SER-98, AND MASSSPECTROMETRY.

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