PKHF2_HUMAN - dbPTM
PKHF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKHF2_HUMAN
UniProt AC Q9H8W4
Protein Name Pleckstrin homology domain-containing family F member 2
Gene Name PLEKHF2
Organism Homo sapiens (Human).
Sequence Length 249
Subcellular Localization Early endosome membrane
Peripheral membrane protein . Endoplasmic reticulum . Colocalizes with EEA1 and RAB5 at endosomal membrane fusion hot spots (PubMed:19995552). May translocate to the endoplasmic reticulum in the early phase of apoptosis (Pub
Protein Description May play a role in early endosome fusion upstream of RAB5, hence regulating receptor trafficking and fluid-phase transport. Enhances cellular sensitivity to TNF-induced apoptosis. [PubMed: 18288467]
Protein Sequence MVDRLANSEANTRRISIVENCFGAAGQPLTIPGRVLIGEGVLTKLCRKKPKARQFFLFNDILVYGNIVIQKKKYNKQHIIPLENVTIDSIKDEGDLRNGWLIKTPTKSFAVYAATATEKSEWMNHINKCVTDLLSKSGKTPSNEHAAVWVPDSEATVCMRCQKAKFTPVNRRHHCRKCGFVVCGPCSEKRFLLPSQSSKPVRICDFCYDLLSAGDMATCQPARSDSYSQSLKSPLNDMSDDDDDDDSSD
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
12PhosphorylationLANSEANTRRISIVE
HCCCCCCCCCEEEEE		28.5126074081
16PhosphorylationEANTRRISIVENCFG
CCCCCCEEEEECCCC		20.8323401153
44AcetylationIGEGVLTKLCRKKPK
ECCCHHHHHHCCCCC		41.2419608861
44UbiquitinationIGEGVLTKLCRKKPK
ECCCHHHHHHCCCCC		41.2433845483
86PhosphorylationIIPLENVTIDSIKDE
EEECCCEEECCCCCC		30.5628348404
89PhosphorylationLENVTIDSIKDEGDL
CCCEEECCCCCCCCC		27.9024719451
91UbiquitinationNVTIDSIKDEGDLRN
CEEECCCCCCCCCCC		54.3929967540
104PhosphorylationRNGWLIKTPTKSFAV
CCCEEEECCCCEEEE		29.2425159151
112PhosphorylationPTKSFAVYAATATEK
CCCEEEEEEEECCCH		6.2627642862
137PhosphorylationVTDLLSKSGKTPSNE
HHHHHHHCCCCCCCC		41.9928348404
140PhosphorylationLLSKSGKTPSNEHAA
HHHHCCCCCCCCCCE		35.1622468782
142PhosphorylationSKSGKTPSNEHAAVW
HHCCCCCCCCCCEEE		61.1422468782
153PhosphorylationAAVWVPDSEATVCMR
CEEECCCCCCEEEEC		24.0622468782
163UbiquitinationTVCMRCQKAKFTPVN
EEEECCCCCCCCCCC		58.1123000965
165UbiquitinationCMRCQKAKFTPVNRR
EECCCCCCCCCCCCC		57.7323000965
167PhosphorylationRCQKAKFTPVNRRHH
CCCCCCCCCCCCCCC		26.1423532336
195PhosphorylationEKRFLLPSQSSKPVR
CCEECCCCCCCCCEE		42.5428857561
197PhosphorylationRFLLPSQSSKPVRIC
EECCCCCCCCCEEHH		44.6728857561
198PhosphorylationFLLPSQSSKPVRICD
ECCCCCCCCCEEHHH		33.0828857561
199UbiquitinationLLPSQSSKPVRICDF
CCCCCCCCCEEHHHH		53.4227667366
208PhosphorylationVRICDFCYDLLSAGD
EEHHHHHHHHHHCCC		15.0422210691
212PhosphorylationDFCYDLLSAGDMATC
HHHHHHHHCCCCCCC		37.1922210691
218PhosphorylationLSAGDMATCQPARSD
HHCCCCCCCCCCCCC		12.6828102081
224PhosphorylationATCQPARSDSYSQSL
CCCCCCCCCCCHHHC		32.7728176443
226PhosphorylationCQPARSDSYSQSLKS
CCCCCCCCCHHHCCC		28.1223401153
227PhosphorylationQPARSDSYSQSLKSP
CCCCCCCCHHHCCCC		18.7328176443
228PhosphorylationPARSDSYSQSLKSPL
CCCCCCCHHHCCCCH		19.7628176443
230PhosphorylationRSDSYSQSLKSPLND
CCCCCHHHCCCCHHC		31.6524702127
233PhosphorylationSYSQSLKSPLNDMSD
CCHHHCCCCHHCCCC		39.6530576142
239PhosphorylationKSPLNDMSDDDDDDD
CCCHHCCCCCCCCCC		40.5330278072
247PhosphorylationDDDDDDDSSD-----
CCCCCCCCCC-----		43.3230278072
248PhosphorylationDDDDDDSSD------
CCCCCCCCC------		55.1025159151
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 PKHF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKHF2_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 PKHF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
MBIP1_HUMANMBIPphysical
19060904
CHIC2_HUMANCHIC2physical
19060904
KAP0_HUMANPRKAR1Aphysical
19060904
PRAF1_HUMANRABAC1physical
19060904
DUT_HUMANDUTphysical
19060904
EAF6_HUMANMEAF6physical
19060904
BEND7_HUMANBEND7physical
19060904
DP13A_HUMANAPPL1physical
19060904
LDOC1_HUMANLDOC1physical
19060904
CEP44_HUMANCEP44physical
25416956
FRMD8_HUMANFRMD8physical
25416956
LMBL3_HUMANL3MBTL3physical
25416956
ACY3_HUMANACY3physical
25416956
DTX2_HUMANDTX2physical
25416956
RSPO2_HUMANRSPO2physical
25416956
CGBP1_HUMANCGGBP1physical
21516116
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 PKHF2_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.
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-239 AND SER-248, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASSSPECTROMETRY.

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