PIF1_HUMAN - dbPTM
PIF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIF1_HUMAN
UniProt AC Q9H611
Protein Name ATP-dependent DNA helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176}
Gene Name PIF1 {ECO:0000255|HAMAP-Rule:MF_03176}
Organism Homo sapiens (Human).
Sequence Length 641
Subcellular Localization Nucleus .
Isoform 4: Mitochondrion .
Protein Description DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Possesses an intrinsic strand annealing activity..
Protein Sequence MLSGIEAAAGEYEDSELRCRVAVEELSPGGQPRRRQALRTAELSLGRNERRELMLRLQAPGPAGRPRCFPLRAARLFTRFAEAGRSTLRLPAHDTPGAGAVQLLLSDCPPDRLRRFLRTLRLKLAAAPGPGPASARAQLLGPRPRDFVTISPVQPEERRLRAATRVPDTTLVKRPVEPQAGAEPSTEAPRWPLPVKRLSLPSTKPQLSEEQAAVLRAVLKGQSIFFTGSAGTGKSYLLKRILGSLPPTGTVATASTGVAACHIGGTTLHAFAGIGSGQAPLAQCVALAQRPGVRQGWLNCQRLVIDEISMVEADLFDKLEAVARAVRQQNKPFGGIQLIICGDFLQLPPVTKGSQPPRFCFQSKSWKRCVPVTLELTKVWRQADQTFISLLQAVRLGRCSDEVTRQLQATASHKVGRDGIVATRLCTHQDDVALTNERRLQELPGKVHRFEAMDSNPELASTLDAQCPVSQLLQLKLGAQVMLVKNLSVSRGLVNGARGVVVGFEAEGRGLPQVRFLCGVTEVIHADRWTVQATGGQLLSRQQLPLQLAWAMSIHKSQGMTLDCVEISLGRVFASGQAYVALSRARSLQGLRVLDFDPMAVRCDPRVLHFYATLRRGRSLSLESPDDDEAASDQENMDPIL
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
27PhosphorylationRVAVEELSPGGQPRR
EEEEECCCCCCCHHH		25.4429255136
44PhosphorylationALRTAELSLGRNERR
HHHHHHHHCCHHHHH		21.9324670416
149PhosphorylationPRPRDFVTISPVQPE
CCCCCCEEECCCCHH		18.7430266825
151PhosphorylationPRDFVTISPVQPEER
CCCCEEECCCCHHHH		15.0619664994
151 (in isoform 3)Phosphorylation-15.0621406692
199PhosphorylationPLPVKRLSLPSTKPQ
CCCCCCCCCCCCCCC		42.1225159151
202PhosphorylationVKRLSLPSTKPQLSE
CCCCCCCCCCCCCCH		55.1228555341
204 (in isoform 3)Ubiquitination-34.79-
204UbiquitinationRLSLPSTKPQLSEEQ
CCCCCCCCCCCCHHH		34.79-
235PhosphorylationGSAGTGKSYLLKRIL
CCCCCCHHHHHHHHH		23.5124719451
236PhosphorylationSAGTGKSYLLKRILG
CCCCCHHHHHHHHHC		21.3824719451
244PhosphorylationLLKRILGSLPPTGTV
HHHHHHCCCCCCCCE		33.97-
363PhosphorylationPPRFCFQSKSWKRCV
CCCEECCCCCHHCEE		14.3827794612
393UbiquitinationTFISLLQAVRLGRCS
HHHHHHHHHHHCCCC		6.5929967540
423PhosphorylationGRDGIVATRLCTHQD
CCCCEEEEEECCCCC		17.18-
446UbiquitinationRLQELPGKVHRFEAM
HHHHCCCCEEEEEEC		32.6929967540
488PhosphorylationVMLVKNLSVSRGLVN
EEEEECCCCCCCCCC		27.6924719451
530PhosphorylationVIHADRWTVQATGGQ
EEECCCEEEEECCCC		12.0222210691
553PhosphorylationLQLAWAMSIHKSQGM
HHHHHHHHHHHHCCC		17.5022210691
557PhosphorylationWAMSIHKSQGMTLDC
HHHHHHHHCCCEEEE		20.1522210691
561PhosphorylationIHKSQGMTLDCVEIS
HHHHCCCEEEEEEEE		26.6930624053
568PhosphorylationTLDCVEISLGRVFAS
EEEEEEEECCEEECC		15.9730624053
575PhosphorylationSLGRVFASGQAYVAL
ECCEEECCCHHHHHH		21.7030624053
579PhosphorylationVFASGQAYVALSRAR
EECCCHHHHHHHHCH		4.3730624053
619 (in isoform 3)Phosphorylation-25.7422210691
658 (in isoform 3)Phosphorylation-30631047
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 PIF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIF1_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 PIF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PIF1_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 PIF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY.

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