HBP1_HUMAN - dbPTM
HBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HBP1_HUMAN
UniProt AC O60381
Protein Name HMG box-containing protein 1
Gene Name HBP1
Organism Homo sapiens (Human).
Sequence Length 514
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor that binds to the promoter region of target genes. Plays a role in the regulation of the cell cycle and of the Wnt pathway. Binds preferentially to the sequence 5'-TTCATTCATTCA-3'. Binding to the H1F0 promoter is enhanced by interaction with RB1. Disrupts the interaction between DNA and TCF4..
Protein Sequence MVWEVKTNQMPNAVQKLLLVMDKRASGMNDSLELLQCNENLPSSPGYNSCDEHMELDDLPELQAVQSDPTQSGMYQLSSDVSHQEYPRSSWNQNTSDIPETTYRENEVDWLTELANIATSPQSPLMQCSFYNRSSPVHIIATSKSLHSYARPPPVSSSSKSEPAFPHHHWKEETPVRHERANSESESGIFCMSSLSDDDDLGWCNSWPSTVWHCFLKGTRLCFHKGSNKEWQDVEDFARAEGCDNEEDLQMGIHKGYGSDGLKLLSHEESVSFGESVLKLTFDPGTVEDGLLTVECKLDHPFYVKNKGWSSFYPSLTVVQHGIPCCEVHIGDVCLPPGHPDAINFDDSGVFDTFKSYDFTPMDSSAVYVLSSMARQRRASLSCGGPGGQDFARSGFSKNCGSPGSSQLSSNSLYAKAVKNHSSGTVSATSPNKCKRPMNAFMLFAKKYRVEYTQMYPGKDNRAISVILGDRWKKMKNEERRMYTLEAKALAEEQKRLNPDCWKRKRTNSGSQQH
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
16 (in isoform 3)Ubiquitination-34.2121890473
16 (in isoform 2)Ubiquitination-34.2121890473
16UbiquitinationQMPNAVQKLLLVMDK
CCCHHHHHHHHHHHH		34.2121890473
23UbiquitinationKLLLVMDKRASGMND
HHHHHHHHHCCCCCH		31.59-
26UbiquitinationLVMDKRASGMNDSLE
HHHHHHCCCCCHHHH		42.4821890473
26 (in isoform 1)Ubiquitination-42.4821890473
134PhosphorylationQCSFYNRSSPVHIIA
CCCCCCCCCCEEEEE		35.0430266825
135PhosphorylationCSFYNRSSPVHIIAT
CCCCCCCCCEEEEEE		27.9225849741
142PhosphorylationSPVHIIATSKSLHSY
CCEEEEEECCCHHHC		26.6930266825
143PhosphorylationPVHIIATSKSLHSYA
CEEEEEECCCHHHCC		15.9523403867
145PhosphorylationHIIATSKSLHSYARP
EEEEECCCHHHCCCC		30.9527251275
156PhosphorylationYARPPPVSSSSKSEP
CCCCCCCCCCCCCCC		30.2121712546
156O-linked_GlycosylationYARPPPVSSSSKSEP
CCCCCCCCCCCCCCC		30.2130059200
157PhosphorylationARPPPVSSSSKSEPA
CCCCCCCCCCCCCCC		38.5721712546
158PhosphorylationRPPPVSSSSKSEPAF
CCCCCCCCCCCCCCC		33.99-
159PhosphorylationPPPVSSSSKSEPAFP
CCCCCCCCCCCCCCC		41.99-
171AcetylationAFPHHHWKEETPVRH
CCCCCCCCCCCCCCC		41.1221967847
225UbiquitinationGTRLCFHKGSNKEWQ
CCEEEEECCCCCCCC		43.72-
229UbiquitinationCFHKGSNKEWQDVED
EEECCCCCCCCCHHH		63.13-
255UbiquitinationDLQMGIHKGYGSDGL
HHHCHHCCCCCCHHH		52.48-
263UbiquitinationGYGSDGLKLLSHEES
CCCCHHHHCCCCHHH		53.57-
297UbiquitinationGLLTVECKLDHPFYV
CEEEEEEECCCCEEE		43.36-
297AcetylationGLLTVECKLDHPFYV
CEEEEEEECCCCEEE		43.3621967847
305AcetylationLDHPFYVKNKGWSSF
CCCCEEECCCCCCCC		41.3821967847
305UbiquitinationLDHPFYVKNKGWSSF
CCCCEEECCCCCCCC		41.38-
307AcetylationHPFYVKNKGWSSFYP
CCEEECCCCCCCCCC		56.9121967847
372PhosphorylationSAVYVLSSMARQRRA
HHHHHHHHHHHHHHH		16.58-
380PhosphorylationMARQRRASLSCGGPG
HHHHHHHHHCCCCCC		21.0023927012
382PhosphorylationRQRRASLSCGGPGGQ
HHHHHHHCCCCCCHH		14.2823927012
390PhosphorylationCGGPGGQDFARSGFS
CCCCCHHHHHHHCCC		42.3127251275
398UbiquitinationFARSGFSKNCGSPGS
HHHHCCCCCCCCCCC		54.73-
402PhosphorylationGFSKNCGSPGSSQLS
CCCCCCCCCCCHHCC		28.4325159151
405PhosphorylationKNCGSPGSSQLSSNS
CCCCCCCCHHCCCCC		20.4930108239
406PhosphorylationNCGSPGSSQLSSNSL
CCCCCCCHHCCCCCH		40.8430108239
409PhosphorylationSPGSSQLSSNSLYAK
CCCCHHCCCCCHHHH		21.6030108239
412PhosphorylationSSQLSSNSLYAKAVK
CHHCCCCCHHHHHHH		25.3827251275
416UbiquitinationSSNSLYAKAVKNHSS
CCCCHHHHHHHHCCC		39.91-
419UbiquitinationSLYAKAVKNHSSGTV
CHHHHHHHHCCCCCC		54.53-
419AcetylationSLYAKAVKNHSSGTV
CHHHHHHHHCCCCCC		54.5321967847
422PhosphorylationAKAVKNHSSGTVSAT
HHHHHHCCCCCCCCC		39.6021955146
423PhosphorylationKAVKNHSSGTVSATS
HHHHHCCCCCCCCCC		30.8221955146
425PhosphorylationVKNHSSGTVSATSPN
HHHCCCCCCCCCCCC		17.1521955146
427PhosphorylationNHSSGTVSATSPNKC
HCCCCCCCCCCCCCC		26.1828450419
429PhosphorylationSSGTVSATSPNKCKR
CCCCCCCCCCCCCCC		36.8925159151
430PhosphorylationSGTVSATSPNKCKRP
CCCCCCCCCCCCCCC		26.6225159151
433UbiquitinationVSATSPNKCKRPMNA
CCCCCCCCCCCCCCH		44.51-
440PhosphorylationKCKRPMNAFMLFAKK
CCCCCCCHHHHHHHH		5.7427251275
448 (in isoform 2)Phosphorylation-21.1329116813
452 (in isoform 2)Phosphorylation-10.2229116813
453PhosphorylationKKYRVEYTQMYPGKD
HHHCEEEEEECCCCC		8.05-
453 (in isoform 2)Phosphorylation-8.0529116813
484PhosphorylationNEERRMYTLEAKALA
HHHHHHHHHHHHHHH		14.58-
488UbiquitinationRMYTLEAKALAEEQK
HHHHHHHHHHHHHHH		34.26-
495UbiquitinationKALAEEQKRLNPDCW
HHHHHHHHHHCHHHH		63.23-
503UbiquitinationRLNPDCWKRKRTNSG
HHCHHHHHHHCCCCC		55.14-
509PhosphorylationWKRKRTNSGSQQH--
HHHHCCCCCCCCC--		38.93-
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
372SPhosphorylationKinasePIM1P11309
PSP
380SPhosphorylationKinasePIM1P11309
PSP
402SPhosphorylationKinaseMAPK11Q15759
GPS
402SPhosphorylationKinaseMAPK14Q16539
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HBP1_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 HBP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_HUMANRB1physical
9178770
RBL2_HUMANRBL2physical
9178770
SIN3A_HUMANSIN3Aphysical
15235594
MYC_HUMANMYCphysical
20008325
EP300_HUMANEP300physical
21967847
CBP_HUMANCREBBPphysical
21967847
EWS_HUMANEWSR1physical
16713569
KBP_HUMANKIAA1279physical
16713569
CCGL_HUMANTMEM37physical
21988832
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 HBP1_HUMAN

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Related Literatures of Post-Translational Modification

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