HPF1_HUMAN - dbPTM
HPF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HPF1_HUMAN
UniProt AC Q9NWY4
Protein Name Histone PARylation factor 1 {ECO:0000303|PubMed:27067600, ECO:0000312|HGNC:HGNC:26051}
Gene Name HPF1 {ECO:0000303|PubMed:27067600, ECO:0000312|HGNC:HGNC:26051}
Organism Homo sapiens (Human).
Sequence Length 346
Subcellular Localization
Protein Description Acts as a cofactor for serine ADP-ribosylation by conferring serine specificity on PARP1 and PARP2: interacts with PARP1 and PARP1 and is able to change amino acid specificity toward serine. [PubMed: 28190768 Promotes histone serine ADP-ribosylation in response to DNA damage, limiting DNA damage-induced PARP1 hyper-automodification, and ensuring genome stability]
Protein Sequence MVGGGGKRRPGGEGPQCEKTTDVKKSKFCEADVSSDLRKEVENHYKLSLPEDFYHFWKFCEELDPEKPSDSLSASLGLQLVGPYDILAGKHKTKKKSTGLNFNLHWRFYYDPPEFQTIIIGDNKTQYHMGYFRDSPDEFPVYVGINEAKKNCIIVPNGDNVFAAVKLFLTKKLREITDKKKINLLKNIDEKLTEAARELGYSLEQRTVKMKQRDKKVVTKTFHGAGLVVPVDKNDVGYRELPETDADLKRICKTIVEAASDEERLKAFAPIQEMMTFVQFANDECDYGMGLELGMDLFCYGSHYFHKVAGQLLPLAYNLLKRNLFAEIIEEHLANRSQENIDQLAA
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
1Acetylation-------MVGGGGKR
-------CCCCCCCC
22814378
7Acetylation-MVGGGGKRRPGGEG
-CCCCCCCCCCCCCC
25953088
19AcetylationGEGPQCEKTTDVKKS
CCCCCCCCCCCCCHH
25953088
19UbiquitinationGEGPQCEKTTDVKKS
CCCCCCCCCCCCCHH
29967540
25AcetylationEKTTDVKKSKFCEAD
CCCCCCCHHHCCCCC
25953088
27AcetylationTTDVKKSKFCEADVS
CCCCCHHHCCCCCCC
19608861
27UbiquitinationTTDVKKSKFCEADVS
CCCCCHHHCCCCCCC
19608861
39UbiquitinationDVSSDLRKEVENHYK
CCCHHHHHHHHHHHC
29967540
46UbiquitinationKEVENHYKLSLPEDF
HHHHHHHCCCCCHHH
29967540
90UbiquitinationPYDILAGKHKTKKKS
HHHHHCCCCCCCCCC
29967540
97ADP-ribosylationKHKTKKKSTGLNFNL
CCCCCCCCCCCCCEE
30257210
149UbiquitinationYVGINEAKKNCIIVP
EEECCCCCCCEEEEC
29967540
149AcetylationYVGINEAKKNCIIVP
EEECCCCCCCEEEEC
26051181
150UbiquitinationVGINEAKKNCIIVPN
EECCCCCCCEEEECC
-
186AcetylationKKKINLLKNIDEKLT
HHHHHHHHCHHHHHH
19608861
186UbiquitinationKKKINLLKNIDEKLT
HHHHHHHHCHHHHHH
19608861
191UbiquitinationLLKNIDEKLTEAARE
HHHCHHHHHHHHHHH
29967540
191AcetylationLLKNIDEKLTEAARE
HHHCHHHHHHHHHHH
25953088
193O-linked_GlycosylationKNIDEKLTEAARELG
HCHHHHHHHHHHHHC
30379171
220UbiquitinationRDKKVVTKTFHGAGL
CCCCEEEEEECCCCE
29967540
233UbiquitinationGLVVPVDKNDVGYRE
CEEEEECCCCCCCCC
32015554
233AcetylationGLVVPVDKNDVGYRE
CEEEEECCCCCCCCC
19608861
238ADP-ribosylationVDKNDVGYRELPETD
ECCCCCCCCCCCCCH
30257210
249UbiquitinationPETDADLKRICKTIV
CCCHHHHHHHHHHHH
24816145
249AcetylationPETDADLKRICKTIV
CCCHHHHHHHHHHHH
25953088
253UbiquitinationADLKRICKTIVEAAS
HHHHHHHHHHHHHCC
29967540
253AcetylationADLKRICKTIVEAAS
HHHHHHHHHHHHHCC
25953088
260PhosphorylationKTIVEAASDEERLKA
HHHHHHCCCHHHHHH
-
321AcetylationPLAYNLLKRNLFAEI
HHHHHHHHHHHHHHH
26051181
321UbiquitinationPLAYNLLKRNLFAEI
HHHHHHHHHHHHHHH
22505724
337PhosphorylationEEHLANRSQENIDQL
HHHHHHCCHHCHHHH
27690223

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 HPF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HPF1_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 HPF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GMPPB_HUMANGMPPBphysical
26344197
PFKAM_HUMANPFKMphysical
26344197
THIO_HUMANTXNphysical
26344197
PARP1_HUMANPARP1physical
27067600
H2A2C_HUMANHIST2H2ACphysical
27067600
H2B2E_HUMANHIST2H2BEphysical
27067600
H31T_HUMANHIST3H3physical
27067600
H2AY_HUMANH2AFYphysical
27067600
PARP2_HUMANPARP2physical
27067600
PARP1_HUMANPARP1physical
28190768
PARP2_HUMANPARP2physical
28190768
H10_HUMANH1F0physical
28190768
H33_HUMANH3F3Aphysical
28190768
H31_HUMANHIST1H3Aphysical
28190768
HMGN4_HUMANHMGN4physical
28190768
HMGN2_HUMANHMGN2physical
28190768
HMGN1_HUMANHMGN1physical
28190768
HMGB1_HUMANHMGB1physical
28190768
HMGA1_HUMANHMGA1physical
28190768
H15_HUMANHIST1H1Bphysical
28190768
H31T_HUMANHIST3H3physical
28190768
H15_HUMANHIST1H1Bphysical
27067600
MKLN1_HUMANMKLN1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HPF1_HUMAN

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Related Literatures of Post-Translational Modification

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