HIC1_HUMAN - dbPTM
HIC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HIC1_HUMAN
UniProt AC Q14526
Protein Name Hypermethylated in cancer 1 protein
Gene Name HIC1
Organism Homo sapiens (Human).
Sequence Length 733
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor. Recognizes and binds to the consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. May act as a tumor suppressor. May be involved in development of head, face, limbs and ventral body wall. Involved in down-regulation of SIRT1 and thereby is involved in regulation of p53/TP53-dependent apoptotic DNA-damage responses. The specific target gene promoter association seems to be depend on corepressors, such as CTBP1 or CTBP2 and MTA1. The regulation of SIRT1 transcription in response to nutrient deprivation seems to involve CTBP1. In cooperation with MTA1 (indicative for an association with the NuRD complex) represses transcription from CCND1/cyclin-D1 and CDKN1C/p57Kip2 specifically in quiescent cells. Involved in regulation of the Wnt signaling pathway probably by association with TCF7L2 and preventing TCF7L2 and CTNNB1 association with promoters of TCF-responsive genes. Seems to repress transcription from E2F1 and ATOH1 which involves ARID1A, indicative for the participation of a distinct SWI/SNF-type chromatin-remodeling complex. Probably represses transcription from ACKR3, FGFBP1 and EFNA1..
Protein Sequence MTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLNNQRTKGFLCDVIIVVQNALFRAHKNVLAASSAYLKSLVVHDNLLNLDHDMVSPAVFRLVLDFIYTGRLADGAEAAAAAAVAPGAEPSLGAVLAAASYLQIPDLVALCKKRLKRHGKYCHLRGGGGGGGGYAPYGRPGRGLRAATPVIQACYPSPVGPPPPPAAEPPSGPEAAVNTHCAELYASGPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPGAGGDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPESFGDNLYVCIPCGKGFPSSEQLNAHVEAHVEEEEALYGRAEAAEVAAGAAGLGPPFGGGGDKVAGAPGGLGELLRPYRCASCDKSYKDPATLRQHEKTHWLTRPYPCTICGKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLGGLPGVPGPDGKGKLDFPEGVFAVARLTAEQLSLKQQDKAAAAELLAQTTHFLHDPKVALESLYPLAKFTAELGLSPDKAAEVLSQGAHLAAGPDGRTIDRFSPT
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
12PhosphorylationEADILLKSGECAGQT
HHHEEECCCCCCCCC		39.53-
19PhosphorylationSGECAGQTMLDTMEA
CCCCCCCCHHHCCCC		20.84-
30PhosphorylationTMEAPGHSRQLLLQL
CCCCCCCHHHHHHHH		27.86-
41MethylationLLQLNNQRTKGFLCD
HHHHCCCCCCCCCCH		40.29115478487
155PhosphorylationRLKRHGKYCHLRGGG
HHHHHCCCCCCCCCC		6.95-
159MethylationHGKYCHLRGGGGGGG
HCCCCCCCCCCCCCC		20.32-
168PhosphorylationGGGGGGGYAPYGRPG
CCCCCCCCCCCCCCC		14.00-
171PhosphorylationGGGGYAPYGRPGRGL
CCCCCCCCCCCCCCC		20.00-
182PhosphorylationGRGLRAATPVIQACY
CCCCCCCCCCCHHCC		19.6627251275
191PhosphorylationVIQACYPSPVGPPPP
CCHHCCCCCCCCCCC		13.0227251275
232PhosphorylationPAAALCASERRCSPL
HHHHHHHHCCCCCCC		30.55-
237PhosphorylationCASERRCSPLCGLDL
HHHCCCCCCCCCCCC		21.0628348404
245PhosphorylationPLCGLDLSKKSPPGS
CCCCCCCCCCCCCCC		37.3923684312
248PhosphorylationGLDLSKKSPPGSAAP
CCCCCCCCCCCCCCC		39.8126657352
252PhosphorylationSKKSPPGSAAPERPL
CCCCCCCCCCCCCCC		27.3423403867
270PhosphorylationELPPRPDSPPSAGPA
CCCCCCCCCCCCCCC		41.2026657352
273PhosphorylationPRPDSPPSAGPAAYK
CCCCCCCCCCCCCCC		49.6026657352
279PhosphorylationPSAGPAAYKEPPLAL
CCCCCCCCCCCCCCC		20.2823312004
304PhosphorylationLEEAAPPSDPFRGGS
HHHCCCCCCCCCCCC		57.7827251275
311PhosphorylationSDPFRGGSGSPGPEP
CCCCCCCCCCCCCCC		38.6330108239
313PhosphorylationPFRGGSGSPGPEPPG
CCCCCCCCCCCCCCC		28.5130108239
314 (in isoform 2)Sumoylation-66.92-
329PhosphorylationPDGPSLLYRWMKHEP
CCCCHHHHHHHHCCC		13.9227642862
333SumoylationSLLYRWMKHEPGLGS
HHHHHHHHCCCCCCC		37.55-
333SumoylationSLLYRWMKHEPGLGS
HHHHHHHHCCCCCCC		37.5517283066
333AcetylationSLLYRWMKHEPGLGS
HHHHHHHHCCCCCCC		37.5517283066
340PhosphorylationKHEPGLGSYGDELGR
HCCCCCCCCHHHHHH		30.8723312004
341PhosphorylationHEPGLGSYGDELGRE
CCCCCCCCHHHHHHC		27.1423312004
351PhosphorylationELGRERGSPSERCEE
HHHHCCCCHHHHHHH		31.3227251275
366PhosphorylationRGGDAAVSPGGPPLG
HCCCCCCCCCCCCCC		17.0729978859
535PhosphorylationTHWLTRPYPCTICGK
HCCCCCCCCCEECCC		13.9826503892
538PhosphorylationLTRPYPCTICGKKFT
CCCCCCCEECCCEEE		18.1326503892
608PhosphorylationAQQRNLISHMKMHAV
HHHHHHHHHHHHHHH		22.2424719451
656PhosphorylationVFAVARLTAEQLSLK
HHHHHHHCHHHHCCH		23.6929396449
698PhosphorylationLYPLAKFTAELGLSP
HHHHHHHHHHCCCCH		20.6527080861
704PhosphorylationFTAELGLSPDKAAEV
HHHHCCCCHHHHHHH		29.2926657352
713PhosphorylationDKAAEVLSQGAHLAA
HHHHHHHHCCCEECC		31.5727080861
726PhosphorylationAAGPDGRTIDRFSPT
CCCCCCCCCCCCCCC		32.5329514088
731PhosphorylationGRTIDRFSPT-----
CCCCCCCCCC-----		28.6428355574
733PhosphorylationTIDRFSPT-------
CCCCCCCC-------		50.4729691806
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 HIC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
333KAcetylation

17283066
333KAcetylation

17283066
333KSumoylation

17283066
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 HIC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIC1_HUMANHIC1physical
10611298
CTBP1_MOUSECtbp1physical
12052894
CTBP1_HUMANCTBP1physical
19486893
CTBP2_HUMANCTBP2physical
19486893
ARI1A_HUMANARID1Aphysical
19486893
SIR1_HUMANSIRT1physical
17283066
HDAC4_HUMANHDAC4physical
17283066
MTA1_HUMANMTA1physical
20547755
MBD3_HUMANMBD3physical
20547755
CHD3_HUMANCHD3physical
20547755
CTBP2_HUMANCTBP2physical
20547755
RBBP4_HUMANRBBP4physical
20547755
PHF19_HUMANPHF19physical
22315224
PHF1_HUMANPHF1physical
22315224
EZH2_HUMANEZH2physical
22315224
SUZ12_HUMANSUZ12physical
22315224
EED_HUMANEEDphysical
22315224
SIR1_HUMANSIRT1physical
22510409
CTBP1_HUMANCTBP1physical
16762039
CTBP2_HUMANCTBP2physical
16762039
SIR1_HUMANSIRT1physical
16269335
HIC2_HUMANHIC2physical
11554746
MTA1_HUMANMTA1physical
23417673
SIR1_HUMANSIRT1physical
23417673
UBC9_HUMANUBE2Iphysical
23417673
STAT3_HUMANSTAT3physical
24067369
TF7L2_HUMANTCF7L2physical
16724116
EVI1_HUMANMECOMphysical
24907396
STAT3_HUMANSTAT3physical
27085461
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 HIC1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"An acetylation/deacetylation-SUMOylation switch through aphylogenetically conserved psiKXEP motif in the tumor suppressor HIC1regulates transcriptional repression activity.";
Stankovic-Valentin N., Deltour S., Seeler J., Pinte S., Vergoten G.,Guerardel C., Dejean A., Leprince D.;
Mol. Cell. Biol. 27:2661-2675(2007).
Cited for: SUMOYLATION AT LYS-333, ACETYLATION AT LYS-333, AND MUTAGENESIS OFLYS-333; GLU-335 AND PRO-336.
Sumoylation
ReferencePubMed
"An acetylation/deacetylation-SUMOylation switch through aphylogenetically conserved psiKXEP motif in the tumor suppressor HIC1regulates transcriptional repression activity.";
Stankovic-Valentin N., Deltour S., Seeler J., Pinte S., Vergoten G.,Guerardel C., Dejean A., Leprince D.;
Mol. Cell. Biol. 27:2661-2675(2007).
Cited for: SUMOYLATION AT LYS-333, ACETYLATION AT LYS-333, AND MUTAGENESIS OFLYS-333; GLU-335 AND PRO-336.

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