PHTF2_HUMAN - dbPTM
PHTF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHTF2_HUMAN
UniProt AC Q8N3S3
Protein Name Putative homeodomain transcription factor 2
Gene Name PHTF2
Organism Homo sapiens (Human).
Sequence Length 785
Subcellular Localization Nucleus .
Protein Description May play a role in transcription regulation..
Protein Sequence MASKVTDAIVWYQKKEFLSVATTAPGPQQVLPGYCQCSLKDQGLFIQCLIGAYDQQIWEKSVEQREIKFIKLGLRNKPKKTAHVKPDLIDVDLVRGSAFAKAKPESPWTSLTRKGIVRVVFFPFFFRWWLQVTSKVIFFWLLVLYLLQVAAIVLFCSTSSPHSIPLTEVIGPIWLMLLLGTVHCQIVSTRTPKPPLSTGGKRRRKLRKAAHLEVHREGDGSSTTDNTQEGAVQNHGTSTSHSVGTVFRDLWHAAFFLSGSKKAKNSIDKSTETDNGYVSLDGKKTVKSGEDGIQNHEPQCETIRPEETAWNTGTLRNGPSKDTQRTITNVSDEVSSEEGPETGYSLRRHVDRTSEGVLRNRKSHHYKKHYPNEDAPKSGTSCSSRCSSSRQDSESARPESETEDVLWEDLLHCAECHSSCTSETDVENHQINPCVKKEYRDDPFHQSHLPWLHSSHPGLEKISAIVWEGNDCKKADMSVLEISGMIMNRVNSHIPGIGYQIFGNAVSLILGLTPFVFRLSQATDLEQLTAHSASELYVIAFGSNEDVIVLSMVIISFVVRVSLVWIFFFLLCVAERTYKQRLLFAKLFGHLTSARRARKSEVPHFRLKKVQNIKMWLSLRSYLKRRGPQRSVDVIVSSAFLLTISVVFICCAQLLHVHEIFLDCHYNWELVIWCISLTLFLLRFVTLGSETSKKYSNTSILLTEQINLYLKMEKKPNKKEELTLVNNVLKLATKLLKELDSPFRLYGLTMNPLLYNITQVVILSAVSGVISDLLGFNLKLWKIKS
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
26 (in isoform 4)Ubiquitination-30.1321906983
26UbiquitinationSVATTAPGPQQVLPG
EEECCCCCCCCCCCC
30.13-
26UbiquitinationSVATTAPGPQQVLPG
EEECCCCCCCCCCCC
30.1329967540
26 (in isoform 2)Ubiquitination-30.1321906983
26 (in isoform 3)Ubiquitination-30.1321906983
47UbiquitinationKDQGLFIQCLIGAYD
CCCCHHHHHHHHHHH
14.5029967540
60UbiquitinationYDQQIWEKSVEQREI
HHHHHHHHHHHHHHH
44.822190698
77AcetylationIKLGLRNKPKKTAHV
EEECCCCCCCCCCCC
52.3518586777
103UbiquitinationGSAFAKAKPESPWTS
CCHHHCCCCCCCCCC
48.92-
201AcetylationPPLSTGGKRRRKLRK
CCCCCCCHHHHHHHH
44.0419809995
221PhosphorylationVHREGDGSSTTDNTQ
EECCCCCCCCCCCCC
29.2917081983
222PhosphorylationHREGDGSSTTDNTQE
ECCCCCCCCCCCCCC
40.6417081983
223PhosphorylationREGDGSSTTDNTQEG
CCCCCCCCCCCCCCC
39.6117081983
224PhosphorylationEGDGSSTTDNTQEGA
CCCCCCCCCCCCCCC
29.2417081983
227PhosphorylationGSSTTDNTQEGAVQN
CCCCCCCCCCCCCCC
30.7017081983
231UbiquitinationTDNTQEGAVQNHGTS
CCCCCCCCCCCCCCC
10.0429967540
235UbiquitinationQEGAVQNHGTSTSHS
CCCCCCCCCCCCCCC
24.6629967540
237PhosphorylationGAVQNHGTSTSHSVG
CCCCCCCCCCCCCHH
22.6817081983
238PhosphorylationAVQNHGTSTSHSVGT
CCCCCCCCCCCCHHH
32.2917081983
239PhosphorylationVQNHGTSTSHSVGTV
CCCCCCCCCCCHHHH
30.2317081983
240PhosphorylationQNHGTSTSHSVGTVF
CCCCCCCCCCHHHHH
17.3317081983
245PhosphorylationSTSHSVGTVFRDLWH
CCCCCHHHHHHHHHH
17.8324719451
260PhosphorylationAAFFLSGSKKAKNSI
HHHHHHCCHHHHHCC
27.8324260401
277PhosphorylationSTETDNGYVSLDGKK
CCCCCCCEEEECCCE
7.9723312004
279PhosphorylationETDNGYVSLDGKKTV
CCCCCEEEECCCEEE
16.5625849741
314PhosphorylationETAWNTGTLRNGPSK
CCCCCCCCCCCCCCC
22.10-
326PhosphorylationPSKDTQRTITNVSDE
CCCCCCCEEEECCCC
23.4923663014
328PhosphorylationKDTQRTITNVSDEVS
CCCCCEEEECCCCCC
29.0223663014
329N-linked_GlycosylationDTQRTITNVSDEVSS
CCCCEEEECCCCCCC
27.69-
331PhosphorylationQRTITNVSDEVSSEE
CCEEEECCCCCCCCC
30.0822115753
335PhosphorylationTNVSDEVSSEEGPET
EECCCCCCCCCCCCC
29.9522115753
336PhosphorylationNVSDEVSSEEGPETG
ECCCCCCCCCCCCCC
44.8622115753
342PhosphorylationSSEEGPETGYSLRRH
CCCCCCCCCCCHHHH
44.5530108239
344PhosphorylationEEGPETGYSLRRHVD
CCCCCCCCCHHHHCC
16.3823090842
345PhosphorylationEGPETGYSLRRHVDR
CCCCCCCCHHHHCCC
19.4224719451
378PhosphorylationPNEDAPKSGTSCSSR
CCCCCCCCCCCHHHH
46.36-
478PhosphorylationDCKKADMSVLEISGM
CCCCCCCCHHHHHHH
24.8924719451
483PhosphorylationDMSVLEISGMIMNRV
CCCHHHHHHHHHHHH
16.9724719451
689PhosphorylationLRFVTLGSETSKKYS
HHHHHHCCCCCCCCC
40.5923090842
691PhosphorylationFVTLGSETSKKYSNT
HHHHCCCCCCCCCCC
47.7623090842
692PhosphorylationVTLGSETSKKYSNTS
HHHCCCCCCCCCCCE
24.0923090842
695PhosphorylationGSETSKKYSNTSILL
CCCCCCCCCCCEEEE
15.7621712546
696PhosphorylationSETSKKYSNTSILLT
CCCCCCCCCCEEEEH
42.3821712546
697N-linked_GlycosylationETSKKYSNTSILLTE
CCCCCCCCCEEEEHH
34.45-
698PhosphorylationTSKKYSNTSILLTEQ
CCCCCCCCEEEEHHH
15.94-
699PhosphorylationSKKYSNTSILLTEQI
CCCCCCCEEEEHHHH
18.5824248375
703PhosphorylationSNTSILLTEQINLYL
CCCEEEEHHHHHHHH
23.5421712546
709PhosphorylationLTEQINLYLKMEKKP
EHHHHHHHHHCCCCC
10.3724248375
7372-HydroxyisobutyrylationKLATKLLKELDSPFR
HHHHHHHHHCCCCHH
67.67-
756N-linked_GlycosylationTMNPLLYNITQVVIL
CCCHHHHHHHHHHHH
30.70-

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 PHTF2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHTF2_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 PHTF2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PHTF2_HUMAN !!

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 PHTF2_HUMAN

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Related Literatures of Post-Translational Modification

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