PKHO1_HUMAN - dbPTM
PKHO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKHO1_HUMAN
UniProt AC Q53GL0
Protein Name Pleckstrin homology domain-containing family O member 1
Gene Name PLEKHO1
Organism Homo sapiens (Human).
Sequence Length 409
Subcellular Localization Cell membrane
Peripheral membrane protein . Nucleus . Cytoplasm . Predominantly localized to the plasma membrane through the binding to phosphatidylinositol 3-phosphate (PubMed:14729969). In C2C12 cells, with the absence of growth factor, it is fou
Protein Description Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). May function to target CK2 to the plasma membrane thereby serving as an adapter to facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears to target ATM to the plasma membrane. Appears to also inhibit tumor cell growth by inhibiting AKT-mediated cell-survival. Also implicated in PI3K-regulated muscle differentiation, the regulation of AP-1 activity (plasma membrane bound AP-1 regulator that translocates to the nucleus) and the promotion of apoptosis induced by tumor necrosis factor TNF. When bound to PKB, it inhibits it probably by decreasing PKB level of phosphorylation..
Protein Sequence MMKKNNSAKRGPQDGNQQPAPPEKVGWVRKFCGKGIFREIWKNRYVVLKGDQLYISEKEVKDEKNIQEVFDLSDYEKCEELRKSKSRSKKNHSKFTLAHSKQPGNTAPNLIFLAVSPEEKESWINALNSAITRAKNRILDEVTVEEDSYLAHPTRDRAKIQHSRRPPTRGHLMAVASTSTSDGMLTLDLIQEEDPSPEEPTSCAESFRVDLDKSVAQLAGSRRRADSDRIQPSADRASSLSRPWEKTDKGATYTPQAPKKLTPTEKGRCASLEEILSQRDAASARTLQLRAEEPPTPALPNPGQLSRIQDLVARKLEETQELLAEVQGLGDGKRKAKDPPRSPPDSESEQLLLETERLLGEASSNWSQAKRVLQEVRELRDLYRQMDLQTPDSHLRQTTPHSQYRKSLM
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
7Phosphorylation-MMKKNNSAKRGPQD
-CCCCCCCCCCCCCC
44.5629978859
143 (in isoform 2)Phosphorylation-21.8322210691
143PhosphorylationNRILDEVTVEEDSYL
CCCCCEEEECCCCCC
21.8329978859
144 (in isoform 2)Phosphorylation-10.2822210691
148PhosphorylationEVTVEEDSYLAHPTR
EEEECCCCCCCCCCC
25.8929978859
149PhosphorylationVTVEEDSYLAHPTRD
EEECCCCCCCCCCCC
21.8929978859
154PhosphorylationDSYLAHPTRDRAKIQ
CCCCCCCCCCCHHHC
35.0229978859
172 (in isoform 2)Phosphorylation-2.3422210691
214PhosphorylationFRVDLDKSVAQLAGS
HCCCCCHHHHHHHHH
23.5024117733
221PhosphorylationSVAQLAGSRRRADSD
HHHHHHHHHCCCCCC
19.6020164059
227PhosphorylationGSRRRADSDRIQPSA
HHHCCCCCCCCCCCH
28.0123401153
233PhosphorylationDSDRIQPSADRASSL
CCCCCCCCHHHHHHC
26.8223403867
238PhosphorylationQPSADRASSLSRPWE
CCCHHHHHHCCCCCC
32.4828102081
239PhosphorylationPSADRASSLSRPWEK
CCHHHHHHCCCCCCC
29.4023401153
241PhosphorylationADRASSLSRPWEKTD
HHHHHHCCCCCCCCC
37.9429978859
247PhosphorylationLSRPWEKTDKGATYT
CCCCCCCCCCCCCCC
31.2826074081
252PhosphorylationEKTDKGATYTPQAPK
CCCCCCCCCCCCCCC
36.2723403867
253PhosphorylationKTDKGATYTPQAPKK
CCCCCCCCCCCCCCC
18.8525884760
254PhosphorylationTDKGATYTPQAPKKL
CCCCCCCCCCCCCCC
12.4523403867
262PhosphorylationPQAPKKLTPTEKGRC
CCCCCCCCCCCCCCC
36.7226657352
264PhosphorylationAPKKLTPTEKGRCAS
CCCCCCCCCCCCCCC
45.1326074081
271PhosphorylationTEKGRCASLEEILSQ
CCCCCCCCHHHHHCC
39.6819664994
277PhosphorylationASLEEILSQRDAASA
CCHHHHHCCHHHHHH
28.9123403867
342PhosphorylationKAKDPPRSPPDSESE
CCCCCCCCCCCCHHH
46.7030576142
346PhosphorylationPPRSPPDSESEQLLL
CCCCCCCCHHHHHHH
49.1230108239
348PhosphorylationRSPPDSESEQLLLET
CCCCCCHHHHHHHHH
34.3030108239
363PhosphorylationERLLGEASSNWSQAK
HHHHHHHCCCHHHHH
21.65-
364PhosphorylationRLLGEASSNWSQAKR
HHHHHHCCCHHHHHH
49.74-
367PhosphorylationGEASSNWSQAKRVLQ
HHHCCCHHHHHHHHH
25.22-
383PhosphorylationVRELRDLYRQMDLQT
HHHHHHHHHHHCCCC
11.7729978859
399PhosphorylationDSHLRQTTPHSQYRK
CHHHCCCCCCHHHHH
15.6324719451

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 PKHO1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKHO1_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 PKHO1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMUF1_HUMANSMURF1physical
18641638
SMAD5_HUMANSMAD5physical
18641638
SMUF1_HUMANSMURF1physical
20580715
SMUF1_HUMANSMURF1physical
20484049
PKHO1_HUMANPLEKHO1physical
18624398
DNJB1_HUMANDNAJB1physical
18624398
CJ088_HUMANC10orf88physical
18624398
FLNB_HUMANFLNBphysical
18624398
RS20_HUMANRPS20physical
18624398
IN35_HUMANIFI35physical
18624398
PRS8_HUMANPSMC5physical
23032291
SMUF1_HUMANSMURF1physical
23032291
CHIP_MOUSEStub1physical
20368287
ARC1A_MOUSEArpc1aphysical
20368287
RS3A_MOUSERps3a1physical
20368287
AKT1_HUMANAKT1physical
17942896
AKT2_HUMANAKT2physical
17942896
PKHO1_HUMANPLEKHO1physical
17942896
SC24D_HUMANSEC24Dphysical
28514442
CENPV_HUMANCENPVphysical
28514442
CAZA1_HUMANCAPZA1physical
28514442
CAPZB_HUMANCAPZBphysical
28514442
RL26L_HUMANRPL26L1physical
28514442
RRP5_HUMANPDCD11physical
28514442
UBA6_HUMANUBA6physical
28514442
FLNC_HUMANFLNCphysical
28514442
SPT2_HUMANSPTY2D1physical
28514442
TRM1L_HUMANTRMT1Lphysical
28514442
NMNA1_HUMANNMNAT1physical
28514442
WIPI3_HUMANWDR45Bphysical
28514442
NVL_HUMANNVLphysical
28514442
FXR1_HUMANFXR1physical
28514442
NOC2L_HUMANNOC2Lphysical
28514442
GTPBA_HUMANGTPBP10physical
28514442
NPA1P_HUMANURB1physical
28514442
DDX31_HUMANDDX31physical
28514442
RL3_HUMANRPL3physical
28514442
UBP7_HUMANUSP7physical
28514442
DDX51_HUMANDDX51physical
28514442
GTPB2_HUMANGTPBP2physical
28514442
NOC3L_HUMANNOC3Lphysical
28514442
SPT5H_HUMANSUPT5Hphysical
28514442
DOK2_HUMANDOK2physical
28514442
MBB1A_HUMANMYBBP1Aphysical
28514442
STAU1_HUMANSTAU1physical
28514442
SDA1_HUMANSDAD1physical
28514442
SPB1_HUMANFTSJ3physical
28514442
GLYR1_HUMANGLYR1physical
28514442
NLE1_HUMANNLE1physical
28514442
KBTB7_HUMANKBTBD7physical
28514442
RL5_HUMANRPL5physical
28514442

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 PKHO1_HUMAN

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Related Literatures of Post-Translational Modification

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