dbPTM

PALM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PALM_HUMAN
UniProt AC	O75781
Protein Name	Paralemmin-1
Gene Name	PALM
Organism	Homo sapiens (Human).
Sequence Length	387
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side . Cell projection, filopodium membrane Lipid-anchor . Cell projection, axon. Cell projection, dendrite. Cell projection, dendritic spine. Basolateral cell membrane Lipid-anchor. Apicolateral cell membrane
Protein Description	Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner..
Protein Sequence	MEVLAAETTSQQERLQAIAEKRKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVLERGDSAPATAKENAAAPSPVRAPAPSPAKEERKTEVVMNSQQTPVGTPKDKRVSNTPLRTVDGSPMMKAAMYSVEITVEKDKVTGETRVLSSTTLLPRQPLPLGIKVYEDETKVVHAVDGTAENGIHPLSSSEVDELIHKADEVTLSEAGSTAGAAETRGAVEGAARTTPSRREITGVQAQPGEATSGPPGIQPGQEPPVTMIFMGYQNVEDEAETKKVLGLQDTITAELVVIEDAAEPKEPAPPNGSAAEPPTEAASREENQAGPEATTSDPQDLDMKKHRCKCCSIM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEVLAAET -------CCCCCCCC	7.88	22223895
8	Phosphorylation	MEVLAAETTSQQERL CCCCCCCCCCHHHHH	27.33	28857561
9	Phosphorylation	EVLAAETTSQQERLQ CCCCCCCCCHHHHHH	18.95	28857561
10	Phosphorylation	VLAAETTSQQERLQA CCCCCCCCHHHHHHH	36.97	28857561
59	Phosphorylation	ERWLLEGTPSSASEG HHHHHCCCCCCCCCC	15.60	18669648
61	Phosphorylation	WLLEGTPSSASEGDE HHHCCCCCCCCCCCH	38.07	28555341
62	Phosphorylation	LLEGTPSSASEGDED HHCCCCCCCCCCCHH	36.70	30576142
64	Phosphorylation	EGTPSSASEGDEDLR CCCCCCCCCCCHHHH	44.02	27251275
93	Ubiquitination	DSVSRLEKEIEVLER HHHHHHHHHHHHHHC	69.45	-
103	Phosphorylation	EVLERGDSAPATAKE HHHHCCCCCCCHHHH	38.69	24732914
107	Phosphorylation	RGDSAPATAKENAAA CCCCCCCHHHHHCCC	36.88	24732914
116	Phosphorylation	KENAAAPSPVRAPAP HHHCCCCCCCCCCCC	31.16	29255136
124	Phosphorylation	PVRAPAPSPAKEERK CCCCCCCCCCCHHHC	39.33	25159151
132	Phosphorylation	PAKEERKTEVVMNSQ CCCHHHCCEEEECCC	39.99	24732914
138	Phosphorylation	KTEVVMNSQQTPVGT CCEEEECCCCCCCCC	12.93	21955146
141	Phosphorylation	VVMNSQQTPVGTPKD EEECCCCCCCCCCCC	16.59	22167270
145	Phosphorylation	SQQTPVGTPKDKRVS CCCCCCCCCCCCCCC	27.65	22167270
152	Phosphorylation	TPKDKRVSNTPLRTV CCCCCCCCCCCCEEE	38.73	30266825
154	Phosphorylation	KDKRVSNTPLRTVDG CCCCCCCCCCEEECC	19.05	30266825
158	Phosphorylation	VSNTPLRTVDGSPMM CCCCCCEEECCCHHH	30.54	23403867
162	Phosphorylation	PLRTVDGSPMMKAAM CCEEECCCHHHHHEE	12.73	19664994
162 (in isoform 2)	Phosphorylation	-	12.73	19664994
170	Phosphorylation	PMMKAAMYSVEITVE HHHHHEEEEEEEEEE	12.58	27642862
171	Phosphorylation	MMKAAMYSVEITVEK HHHHEEEEEEEEEEE	10.53	28348404
189	Phosphorylation	TGETRVLSSTTLLPR CCCEEEEEECCCCCC	23.84	28857561
190	Phosphorylation	GETRVLSSTTLLPRQ CCEEEEEECCCCCCC	22.65	28857561
191	Phosphorylation	ETRVLSSTTLLPRQP CEEEEEECCCCCCCC	20.35	28857561
192	Phosphorylation	TRVLSSTTLLPRQPL EEEEEECCCCCCCCC	28.39	28509920
201 (in isoform 2)	Phosphorylation	-	17.03	25921289
205 (in isoform 2)	Phosphorylation	-	6.30	25921289
206	Phosphorylation	LPLGIKVYEDETKVV CCCCEEEEECCCEEE	16.80	23532336
243	Phosphorylation	IHKADEVTLSEAGST HHHCCEEEHHHCCCC	23.63	-
245	Phosphorylation	KADEVTLSEAGSTAG HCCEEEHHHCCCCCC	18.94	30266825
249	Phosphorylation	VTLSEAGSTAGAAET EEHHHCCCCCCHHHH	23.33	30266825
250	Phosphorylation	TLSEAGSTAGAAETR EHHHCCCCCCHHHHH	28.35	28857561
256	Phosphorylation	STAGAAETRGAVEGA CCCCHHHHHHCCCCC	29.67	30266825
305	Phosphorylation	VTMIFMGYQNVEDEA EEEEEECCCCCCCHH	5.78	25884760
333 (in isoform 2)	Ubiquitination	-	39.70	21906983
346	Phosphorylation	EPAPPNGSAAEPPTE CCCCCCCCCCCCCCH	30.83	15345747
352	Phosphorylation	GSAAEPPTEAASREE CCCCCCCCHHHCHHH	49.31	30266825
356	Phosphorylation	EPPTEAASREENQAG CCCCHHHCHHHHCCC	47.47	30266825
367	Phosphorylation	NQAGPEATTSDPQDL HCCCCCCCCCCHHHH	25.77	15345747
368	Phosphorylation	QAGPEATTSDPQDLD CCCCCCCCCCHHHHC	37.87	27732954
369	Phosphorylation	AGPEATTSDPQDLDM CCCCCCCCCHHHHCH	42.83	15345747
377	Ubiquitination	DPQDLDMKKHRCKCC CHHHHCHHHHCCCCC	45.13	2190698
377 (in isoform 1)	Ubiquitination	-	45.13	21906983
381	S-palmitoylation	LDMKKHRCKCCSIM- HCHHHHCCCCCCCC-	3.85	-
383	S-palmitoylation	MKKHRCKCCSIM--- HHHHCCCCCCCC---	2.23	-
384	Methylation	KKHRCKCCSIM---- HHHCCCCCCCC----	1.56	-
384	Farnesylation	KKHRCKCCSIM---- HHHCCCCCCCC----	1.56	-

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 PALM_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PALM_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 PALM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PALM_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 PALM_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-124; THR-141 ANDTHR-145, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-116; SER-124; THR-141;THR-145; THR-154 AND SER-162, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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 THR-141 AND THR-145, ANDMASS SPECTROMETRY.	17081983 [Abstract]