PHLP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PHLP_HUMAN
• UniProt AC: Q13371
• Protein Name: Phosducin-like protein
• Gene Name: PDCL
• Organism: Homo sapiens (Human).
• Sequence Length: 301
• Subcellular Localization: Cell projection, cilium .
• Protein Description: Acts as a positive regulator of hedgehog signaling and regulates ciliary function.; Isoform 1: Functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitates the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers.; Isoform 2: Acts as a negative regulator of heterotrimeric G proteins assembly by trapping the preloaded G beta subunits inside the CCT chaperonin..
• Protein Sequence: MTTLDDKLLGEKLQYYYSSSEDEDSDHEDKDRGRCAPASSSVPAEAELAGEGISVNTGPKGVINDWRRFKQLETEQREEQCREMERLIKKLSMTCRSHLDEEEEQQKQKDLQEKISGKMTLKEFAIMNEDQDDEEFLQQYRKQRMEEMRQQLHKGPQFKQVFEISSGEGFLDMIDKEQKSIVIMVHIYEDGIPGTEAMNGCMICLAAEYPAVKFCKVKSSVIGASSQFTRNALPALLIYKGGELIGNFVRVTDQLGDDFFAVDLEAFLQEFGLLPEKEVLVLTSVRNSATCHSEDSDLEID

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
2	Acetylation	------MTTLDDKLL ------CCCHHHHHH	35.75	17322306
2	Phosphorylation	------MTTLDDKLL ------CCCHHHHHH	35.75	21406692
3	Phosphorylation	-----MTTLDDKLLG -----CCCHHHHHHH	27.22	21406692
15	Phosphorylation	LLGEKLQYYYSSSED HHHHHHHHCCCCCCC	18.14	20873877
16	Phosphorylation	LGEKLQYYYSSSEDE HHHHHHHCCCCCCCC	5.50	20873877
17	Phosphorylation	GEKLQYYYSSSEDED HHHHHHCCCCCCCCC	9.35	25849741
18	Phosphorylation	EKLQYYYSSSEDEDS HHHHHCCCCCCCCCC	15.97	17081983
19	Phosphorylation	KLQYYYSSSEDEDSD HHHHCCCCCCCCCCC	22.94	17081983
20	Phosphorylation	LQYYYSSSEDEDSDH HHHCCCCCCCCCCCC	43.03	17081983
25	Phosphorylation	SSSEDEDSDHEDKDR CCCCCCCCCCCCCCC	38.53	25072903
41	Phosphorylation	RCAPASSSVPAEAEL CCCCCCCCCCCHHHH	29.62	24719451
54	Phosphorylation	ELAGEGISVNTGPKG HHCCCCCCCCCCCCC	21.85	28555341
70	Ubiquitination	INDWRRFKQLETEQR HHCHHHHHHHHHHHH	52.76	29967540
89	Ubiquitination	REMERLIKKLSMTCR HHHHHHHHHHHHHHH	52.86	29967540
90	Ubiquitination	EMERLIKKLSMTCRS HHHHHHHHHHHHHHH	38.51	29967540
92	Phosphorylation	ERLIKKLSMTCRSHL HHHHHHHHHHHHHCC	22.41	24719451
94	Phosphorylation	LIKKLSMTCRSHLDE HHHHHHHHHHHCCCH	11.03	-
97	Phosphorylation	KLSMTCRSHLDEEEE HHHHHHHHCCCHHHH	30.46	-
114	Ubiquitination	KQKDLQEKISGKMTL HHHHHHHHHCCCCCH	29.25	33845483
118	Ubiquitination	LQEKISGKMTLKEFA HHHHHCCCCCHHHHH	23.17	29967540
120	Phosphorylation	EKISGKMTLKEFAIM HHHCCCCCHHHHHCC	37.86	29759185
122	Ubiquitination	ISGKMTLKEFAIMNE HCCCCCHHHHHCCCC	41.44	32015554
140	Phosphorylation	DEEFLQQYRKQRMEE HHHHHHHHHHHHHHH	13.55	29759185
142	Ubiquitination	EFLQQYRKQRMEEMR HHHHHHHHHHHHHHH	37.00	29967540
154	Ubiquitination	EMRQQLHKGPQFKQV HHHHHHHCCHHHHEE	79.48	29967540
225	Phosphorylation	KSSVIGASSQFTRNA CCCCCCCCCHHHCCC	21.32	23186163
226	Phosphorylation	SSVIGASSQFTRNAL CCCCCCCCHHHCCCC	28.87	23186163
239	Phosphorylation	ALPALLIYKGGELIG CCCEEEEEECCEEEE	11.98	-
288	Phosphorylation	VLTSVRNSATCHSED EEEEECCCCCCCCCC	17.87	29209046
290	Phosphorylation	TSVRNSATCHSEDSD EEECCCCCCCCCCCC	15.57	29209046
293	Phosphorylation	RNSATCHSEDSDLEI CCCCCCCCCCCCCCC	45.29	22167270
296	Phosphorylation	ATCHSEDSDLEID-- CCCCCCCCCCCCC--	39.79	22167270

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
18	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
19	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
20	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
25	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
296	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PHLP_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PHLP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GBB1_HUMAN	GNB1	physical	15889144
TCPE_HUMAN	CCT5	physical	15889144
PRS8_HUMAN	PSMC5	physical	25416956
PRS8_HUMAN	PSMC5	physical	15604093
PRS8_HUMAN	PSMC5	physical	21516116
GBB1_HUMAN	GNB1	physical	25675501
TCPA_DROME	T-cp1	physical	25675501
TCPG_DROME	Cctgamma	physical	25675501

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-290; SER-293 ANDSER-296, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-293 AND SER-296, ANDMASS SPECTROMETRY.
PubMed: 18669648

"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-18; SER-19; SER-20 ANDSER-25, AND MASS SPECTROMETRY.
PubMed: 17081983

"Identification of phosphorylation sites on phosducin-like protein byQTOF mass spectrometry.";
Carter M.D., Southwick K., Lukov G., Willardson B.M., Thulin C.D.;
J. Biomol. Tech. 15:257-264(2004).
Cited for: PHOSPHORYLATION AT SER-296.
PubMed: 15585822