HSF2_HUMAN - dbPTM
HSF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSF2_HUMAN
UniProt AC Q03933
Protein Name Heat shock factor protein 2
Gene Name HSF2
Organism Homo sapiens (Human).
Sequence Length 536
Subcellular Localization Cytoplasm . Nucleus . Cytoplasmic during normal growth and moves to the nucleus upon activation.
Protein Description DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked..
Protein Sequence MKQSSNVPAFLSKLWTLVEETHTNEFITWSQNGQSFLVLDEQRFAKEILPKYFKHNNMASFVRQLNMYGFRKVVHIDSGIVKQERDGPVEFQHPYFKQGQDDLLENIKRKVSSSKPEENKIRQEDLTKIISSAQKVQIKQETIESRLSELKSENESLWKEVSELRAKHAQQQQVIRKIVQFIVTLVQNNQLVSLKRKRPLLLNTNGAQKKNLFQHIVKEPTDNHHHKVPHSRTEGLKPRERISDDIIIYDVTDDNADEENIPVIPETNEDVISDPSNCSQYPDIVIVEDDNEDEYAPVIQSGEQNEPARESLSSGSDGSSPLMSSAVQLNGSSSLTSEDPVTMMDSILNDNINLLGKVELLDYLDSIDCSLEDFQAMLSGRQFSIDPDLLVDLFTSSVQMNPTDYINNTKSENKGLETTKNNVVQPVSEEGRKSKSKPDKQLIQYTAFPLLAFLDGNPASSVEQASTTASSEVLSSVDKPIEVDELLDSSLDPEPTQSKLVRLEPLTEAEASEATLFYLCELAPAPLDSDMPLLDS
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
2Sumoylation------MKQSSNVPA
------CCCCCCHHH		59.9128112733
51UbiquitinationFAKEILPKYFKHNNM
HHHHHHHHHHCCCCH		60.9321890473
51UbiquitinationFAKEILPKYFKHNNM
HHHHHHHHHHCCCCH		60.9321890473
51UbiquitinationFAKEILPKYFKHNNM
HHHHHHHHHHCCCCH		60.9321890473
54UbiquitinationEILPKYFKHNNMASF
HHHHHHHCCCCHHHH		42.1921890473
54UbiquitinationEILPKYFKHNNMASF
HHHHHHHCCCCHHHH		42.1921890473
54UbiquitinationEILPKYFKHNNMASF
HHHHHHHCCCCHHHH		42.1921890473
54MalonylationEILPKYFKHNNMASF
HHHHHHHCCCCHHHH		42.1926320211
82SumoylationHIDSGIVKQERDGPV
EECCCCCCCCCCCCC		44.51-
82UbiquitinationHIDSGIVKQERDGPV
EECCCCCCCCCCCCC		44.51-
82SumoylationHIDSGIVKQERDGPV
EECCCCCCCCCCCCC		44.5116428449
97UbiquitinationEFQHPYFKQGQDDLL
CCCCCHHHCCCHHHH		47.91-
108UbiquitinationDDLLENIKRKVSSSK
HHHHHHHHHHHHCCC		58.72-
110UbiquitinationLLENIKRKVSSSKPE
HHHHHHHHHHCCCCC		41.28-
128UbiquitinationIRQEDLTKIISSAQK
CCHHHHHHHHHHHHH		45.39-
135UbiquitinationKIISSAQKVQIKQET
HHHHHHHHHHHCHHH		35.50-
135SumoylationKIISSAQKVQIKQET
HHHHHHHHHHHCHHH		35.5028112733
135AcetylationKIISSAQKVQIKQET
HHHHHHHHHHHCHHH		35.5025953088
135SumoylationKIISSAQKVQIKQET
HHHHHHHHHHHCHHH		35.50-
139SumoylationSAQKVQIKQETIESR
HHHHHHHCHHHHHHH		25.6216428449
139SumoylationSAQKVQIKQETIESR
HHHHHHHCHHHHHHH		25.62-
139UbiquitinationSAQKVQIKQETIESR
HHHHHHHCHHHHHHH		25.62-
142PhosphorylationKVQIKQETIESRLSE
HHHHCHHHHHHHHHH		27.79-
151SumoylationESRLSELKSENESLW
HHHHHHHHHHCHHHH		52.2328112733
151SumoylationESRLSELKSENESLW
HHHHHHHHHHCHHHH		52.23-
151UbiquitinationESRLSELKSENESLW
HHHHHHHHHHCHHHH		52.2321906983
159UbiquitinationSENESLWKEVSELRA
HHCHHHHHHHHHHHH		54.23-
167UbiquitinationEVSELRAKHAQQQQV
HHHHHHHHHHHHHHH		32.79-
197UbiquitinationQLVSLKRKRPLLLNT
CEECEECCCCEEECC		57.70-
210UbiquitinationNTNGAQKKNLFQHIV
CCCCHHHCCHHHHHH		46.9621890473
210UbiquitinationNTNGAQKKNLFQHIV
CCCCHHHCCHHHHHH		46.9621890473
210SumoylationNTNGAQKKNLFQHIV
CCCCHHHCCHHHHHH		46.9628112733
210UbiquitinationNTNGAQKKNLFQHIV
CCCCHHHCCHHHHHH		46.9621890473
218SumoylationNLFQHIVKEPTDNHH
CHHHHHHCCCCCCCC		58.3228112733
237SumoylationHSRTEGLKPRERISD
CCCCCCCCCHHHCCC		53.5428112733
237AcetylationHSRTEGLKPRERISD
CCCCCCCCCHHHCCC		53.5425953088
384 (in isoform 2)Phosphorylation-20.1128634120
384PhosphorylationMLSGRQFSIDPDLLV
HHHCCCEECCHHHHH		20.1127251275
420UbiquitinationNKGLETTKNNVVQPV
CCCCCCCCCCEEECC		54.682190698
489PhosphorylationEVDELLDSSLDPEPT
EHHHHHHCCCCCCCC		32.5426074081
490PhosphorylationVDELLDSSLDPEPTQ
HHHHHHCCCCCCCCC		36.1426074081
496PhosphorylationSSLDPEPTQSKLVRL
CCCCCCCCCHHHEEE		43.7626074081
498PhosphorylationLDPEPTQSKLVRLEP
CCCCCCCHHHEEEEE		30.3626074081
507PhosphorylationLVRLEPLTEAEASEA
HEEEEECCHHHCCHH		43.8126074081
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 HSF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSF2_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 HSF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC9_HUMANUBE2Iphysical
11278381
CUL3_HUMANCUL3physical
19768582
PCGF2_HUMANPCGF2physical
18211895
TPM3_HUMANTPM3physical
25416956
WDR5_HUMANWDR5physical
25416956
MTUS2_HUMANMTUS2physical
25416956
NUP62_HUMANNUP62physical
25416956
IMPA2_HUMANIMPA2physical
26186194
SAP3_HUMANGM2Aphysical
26186194
DR9C7_HUMANSDR9C7physical
26186194
ASAH1_HUMANASAH1physical
26186194
HSF1_HUMANHSF1physical
26186194
ANM1_HUMANPRMT1physical
26496610
HSF1_HUMANHSF1physical
26496610
NCBP1_HUMANNCBP1physical
26496610
PRCC_HUMANPRCCphysical
26496610
RBBP6_HUMANRBBP6physical
26496610
SRSF7_HUMANSRSF7physical
26496610
TYB4_HUMANTMSB4Xphysical
26496610
THOC5_HUMANTHOC5physical
26496610
RAD50_HUMANRAD50physical
26496610
RBM7_HUMANRBM7physical
26496610
INADL_HUMANINADLphysical
26496610
ECI2_HUMANECI2physical
26496610
ANKL2_HUMANANKLE2physical
26496610
CHTOP_HUMANCHTOPphysical
26496610
OTUD4_HUMANOTUD4physical
26496610
PLXA3_HUMANPLXNA3physical
26496610
ZNFX1_HUMANZNFX1physical
26496610
ZC3HE_HUMANZC3H14physical
26496610
OBSCN_HUMANOBSCNphysical
26496610
HSF1_HUMANHSF1physical
28514442
HSP7C_HUMANHSPA8physical
28514442
DR9C7_HUMANSDR9C7physical
28514442
IMPA2_HUMANIMPA2physical
28514442
PPAP_HUMANACPPphysical
28514442
ASAH1_HUMANASAH1physical
28514442
SAP3_HUMANGM2Aphysical
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 HSF2_HUMAN

loading...

Related Literatures of Post-Translational Modification

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