PKHF1_HUMAN - dbPTM
PKHF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKHF1_HUMAN
UniProt AC Q96S99
Protein Name Pleckstrin homology domain-containing family F member 1
Gene Name PLEKHF1
Organism Homo sapiens (Human).
Sequence Length 279
Subcellular Localization Nucleus . Cytoplasm, perinuclear region . Lysosome . Translocates to lysosome during apoptosis.
Protein Description May induce apoptosis through the lysosomal-mitochondrial pathway. Translocates to the lysosome initiating the permeabilization of lysosomal membrane (LMP) and resulting in the release of CTSD and CTSL to the cytoplasm. Triggers the caspase-independent apoptosis by altering mitochondrial membrane permeabilization (MMP) resulting in the release of PDCD8..
Protein Sequence MVDHLANTEINSQRIAAVESCFGASGQPLALPGRVLLGEGVLTKECRKKAKPRIFFLFNDILVYGSIVLNKRKYRSQHIIPLEEVTLELLPETLQAKNRWMIKTAKKSFVVSAASATERQEWISHIEECVRRQLRATGRPPSTEHAAPWIPDKATDICMRCTQTRFSALTRRHHCRKCGFVVCAECSRQRFLLPRLSPKPVRVCSLCYRELAAQQRQEEAEEQGAGSPGQPAHLARPICGASSGDDDDSDEDKEGSRDGDWPSSVEFYASGVAWSAFHS
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
8PhosphorylationMVDHLANTEINSQRI
CCCCCCCCCCHHHHH
32.4125002506
12PhosphorylationLANTEINSQRIAAVE
CCCCCCHHHHHHHHH
26.8825002506
44MalonylationLGEGVLTKECRKKAK
ECCCCCCHHHHHHCC
51.1326320211
44AcetylationLGEGVLTKECRKKAK
ECCCCCCHHHHHHCC
51.1323749302
44UbiquitinationLGEGVLTKECRKKAK
ECCCCCCHHHHHHCC
51.1319608861
97UbiquitinationLPETLQAKNRWMIKT
CHHHHHHCCCEEEHH
33.80-
108PhosphorylationMIKTAKKSFVVSAAS
EEHHCHHHEEEECCC
23.6721955146
112PhosphorylationAKKSFVVSAASATER
CHHHEEEECCCCHHH
16.8921955146
115PhosphorylationSFVVSAASATERQEW
HEEEECCCCHHHHHH
35.1321955146
137PhosphorylationVRRQLRATGRPPSTE
HHHHHHHHCCCCCCC
27.5626437602
142PhosphorylationRATGRPPSTEHAAPW
HHHCCCCCCCCCCCC
49.4628348404
143PhosphorylationATGRPPSTEHAAPWI
HHCCCCCCCCCCCCC
37.2528348404
197PhosphorylationRFLLPRLSPKPVRVC
CCCCCCCCCCCEEHH
31.9626434776
205PhosphorylationPKPVRVCSLCYRELA
CCCEEHHHHHHHHHH
20.7222617229
227PhosphorylationAEEQGAGSPGQPAHL
HHHCCCCCCCCCCCC
25.8923401153
242PhosphorylationARPICGASSGDDDDS
CCCCCCCCCCCCCCC
21.8223663014
243PhosphorylationRPICGASSGDDDDSD
CCCCCCCCCCCCCCC
45.7923663014
249PhosphorylationSSGDDDDSDEDKEGS
CCCCCCCCCCCCCCC
50.3123663014
256PhosphorylationSDEDKEGSRDGDWPS
CCCCCCCCCCCCCCC
28.4325850435

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 PKHF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKHF1_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 PKHF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LMBL3_HUMANL3MBTL3physical
25416956

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 PKHF1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, AND MASS SPECTROMETRY.

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