dbPTM

PPHLN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPHLN_HUMAN
UniProt AC	Q8NEY8
Protein Name	Periphilin-1 {ECO:0000303\|PubMed:12853457}
Gene Name	PPHLN1 {ECO:0000312\|HGNC:HGNC:19369}
Organism	Homo sapiens (Human).
Sequence Length	458
Subcellular Localization	Nucleus . Cytoplasm . Chromosome . In undifferentiated keratinocytes expressed in speckle-type nuclear granules and at the nuclear membrane, but in the differentiated keratinocytes colocalized with periplakin at the cell periphery and at cell-cell ju
Protein Description	Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin. [PubMed: 26022416 Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex]
Protein Sequence	MWSEGRYEYERIPRERAPPRSHPSDGYNRLVNIVPKKPPLLDRPGEGSYNRYYSHVDYRDYDEGRSFSHDRRSGPPHRGDESGYRWTRDDHSASRQPEYRDMRDGFRRKSFYSSHYARERSPYKRDNTFFRESPVGRKDSPHSRSGSSVSSRSYSPERSKSYSFHQSQHRKSVRPGASYKRQNEGNPERDKERPVQSLKTSRDTSPSSGSAVSSSKVLDKPSRLTEKELAEAASKWAAEKLEKSDESNLPEISEYEAGSTAPLFTDQPEEPESNTTHGIELFEDSQLTTRSKAIASKTKEIEQVYRQDCETFGMVVKMLIEKDPSLEKSIQFALRQNLHEIESAGQTWQQVPPVRNTEMDHDGTPENEGEETAQSAPQPPQAPQPLQPRKKRVRRTTQLRRTTGAPDITWGMLKKTTQEAERILLRTQTPFTPENLFLAMLSVVHCNSRKDVKPENKQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MWSEGRYEYE -----CCCCCCCCCC	28.95	29083192
3 (in isoform 7)	Phosphorylation	-	28.95	25072903
4 (in isoform 7)	Phosphorylation	-	31.98	25072903
7	Phosphorylation	-MWSEGRYEYERIPR -CCCCCCCCCCCCCH	33.45	26714015
9	Phosphorylation	WSEGRYEYERIPRER CCCCCCCCCCCCHHH	11.11	29083192
13 (in isoform 7)	Phosphorylation	-	38.00	25072903
21	Phosphorylation	RERAPPRSHPSDGYN HHHCCCCCCCCCCCH	45.59	30576142
21 (in isoform 3)	Phosphorylation	-	45.59	-
24	Phosphorylation	APPRSHPSDGYNRLV CCCCCCCCCCCHHHE	37.94	30576142
24 (in isoform 3)	Phosphorylation	-	37.94	-
27	Phosphorylation	RSHPSDGYNRLVNIV CCCCCCCCHHHEEEC	11.33	-
28 (in isoform 5)	Phosphorylation	-	36.02	-
28 (in isoform 6)	Phosphorylation	-	36.02	-
31 (in isoform 5)	Phosphorylation	-	4.08	-
31 (in isoform 6)	Phosphorylation	-	4.08	-
32	Phosphorylation	DGYNRLVNIVPKKPP CCCHHHEEECCCCCC	33.85	32142685
37	Ubiquitination	LVNIVPKKPPLLDRP HEEECCCCCCCCCCC	45.88	-
37	Sumoylation	LVNIVPKKPPLLDRP HEEECCCCCCCCCCC	45.88	-
37	Acetylation	LVNIVPKKPPLLDRP HEEECCCCCCCCCCC	45.88	26051181
37	Sumoylation	LVNIVPKKPPLLDRP HEEECCCCCCCCCCC	45.88	-
37	Ubiquitination	LVNIVPKKPPLLDRP HEEECCCCCCCCCCC	45.88	-
37 (in isoform 3)	Phosphorylation	-	45.88	25849741
39 (in isoform 3)	Phosphorylation	-	55.20	29116813
43	Methylation	KKPPLLDRPGEGSYN CCCCCCCCCCCCCCC	40.88	115488277
44 (in isoform 5)	Phosphorylation	-	44.87	25849741
44 (in isoform 6)	Phosphorylation	-	44.87	25849741
46 (in isoform 5)	Phosphorylation	-	47.88	29116813
46 (in isoform 6)	Phosphorylation	-	47.88	29116813
48	Phosphorylation	LDRPGEGSYNRYYSH CCCCCCCCCCCCCCC	18.22	25159151
49	Phosphorylation	DRPGEGSYNRYYSHV CCCCCCCCCCCCCCC	17.95	-
52	Phosphorylation	GEGSYNRYYSHVDYR CCCCCCCCCCCCCCC	12.99	28796482
53	Phosphorylation	EGSYNRYYSHVDYRD CCCCCCCCCCCCCCC	6.78	28796482
54	Phosphorylation	GSYNRYYSHVDYRDY CCCCCCCCCCCCCCC	14.22	28796482
55	Phosphorylation	SYNRYYSHVDYRDYD CCCCCCCCCCCCCCC	10.59	32142685
58	Phosphorylation	RYYSHVDYRDYDEGR CCCCCCCCCCCCCCC	12.33	28796482
61	Phosphorylation	SHVDYRDYDEGRSFS CCCCCCCCCCCCCCC	13.59	28796482
62	Phosphorylation	HVDYRDYDEGRSFSH CCCCCCCCCCCCCCC	57.05	32142685
66	Phosphorylation	RDYDEGRSFSHDRRS CCCCCCCCCCCCCCC	41.79	24719451
68	Phosphorylation	YDEGRSFSHDRRSGP CCCCCCCCCCCCCCC	26.23	23312004
73	Phosphorylation	SFSHDRRSGPPHRGD CCCCCCCCCCCCCCC	57.45	29496963
78	Methylation	RRSGPPHRGDESGYR CCCCCCCCCCCCCCC	61.09	81026725
78	Phosphorylation	RRSGPPHRGDESGYR CCCCCCCCCCCCCCC	61.09	32142685
82	Phosphorylation	PPHRGDESGYRWTRD CCCCCCCCCCCCCCC	45.95	28555341
85	Phosphorylation	RGDESGYRWTRDDHS CCCCCCCCCCCCCCC	31.64	32645325
92	Phosphorylation	RWTRDDHSASRQPEY CCCCCCCCCCCCCCH	34.63	23401153
94	Phosphorylation	TRDDHSASRQPEYRD CCCCCCCCCCCCHHH	34.17	30183078
99	Phosphorylation	SASRQPEYRDMRDGF CCCCCCCHHHHHHHH	20.70	23403867
100	Phosphorylation	ASRQPEYRDMRDGFR CCCCCCHHHHHHHHH	29.59	33259812
105	Ubiquitination	EYRDMRDGFRRKSFY CHHHHHHHHHHHHHH	13.95	29967540
107	Phosphorylation	RDMRDGFRRKSFYSS HHHHHHHHHHHHHHH	51.12	33259812
107	Ubiquitination	RDMRDGFRRKSFYSS HHHHHHHHHHHHHHH	51.12	33845483
109	Sumoylation	MRDGFRRKSFYSSHY HHHHHHHHHHHHHHC	40.43	-
109	Sumoylation	MRDGFRRKSFYSSHY HHHHHHHHHHHHHHC	40.43	28112733
110	Phosphorylation	RDGFRRKSFYSSHYA HHHHHHHHHHHHHCH	27.83	25159151
112	Phosphorylation	GFRRKSFYSSHYARE HHHHHHHHHHHCHHH	19.16	21945579
112	Ubiquitination	GFRRKSFYSSHYARE HHHHHHHHHHHCHHH	19.16	29967540
113	Phosphorylation	FRRKSFYSSHYARER HHHHHHHHHHCHHHC	14.50	21945579
114	Phosphorylation	RRKSFYSSHYARERS HHHHHHHHHCHHHCC	14.78	21945579
115	Ubiquitination	RKSFYSSHYARERSP HHHHHHHHCHHHCCC	17.84	32015554
116	Phosphorylation	KSFYSSHYARERSPY HHHHHHHCHHHCCCC	14.86	21945579
117	Phosphorylation	SFYSSHYARERSPYK HHHHHHCHHHCCCCC	11.05	32142685
121	Phosphorylation	SHYARERSPYKRDNT HHCHHHCCCCCCCCC	28.03	30266825
123	Phosphorylation	YARERSPYKRDNTFF CHHHCCCCCCCCCCC	21.65	30266825
128	Phosphorylation	SPYKRDNTFFRESPV CCCCCCCCCCCCCCC	28.56	29255136
131	Phosphorylation	KRDNTFFRESPVGRK CCCCCCCCCCCCCCC	39.01	32645325
133	Phosphorylation	DNTFFRESPVGRKDS CCCCCCCCCCCCCCC	22.19	29255136
138	Phosphorylation	RESPVGRKDSPHSRS CCCCCCCCCCCCCCC	57.54	32645325
140	Phosphorylation	SPVGRKDSPHSRSGS CCCCCCCCCCCCCCC	27.78	30278072
143	Phosphorylation	GRKDSPHSRSGSSVS CCCCCCCCCCCCCCC	31.37	29743597
144	Ubiquitination	RKDSPHSRSGSSVSS CCCCCCCCCCCCCCC	41.84	24816145
145	Phosphorylation	KDSPHSRSGSSVSSR CCCCCCCCCCCCCCC	46.14	28450419
146	Ubiquitination	DSPHSRSGSSVSSRS CCCCCCCCCCCCCCC	23.88	29967540
147	Phosphorylation	SPHSRSGSSVSSRSY CCCCCCCCCCCCCCC	28.90	28450419
148	Phosphorylation	PHSRSGSSVSSRSYS CCCCCCCCCCCCCCC	29.55	28450419
150	Phosphorylation	SRSGSSVSSRSYSPE CCCCCCCCCCCCCCC	23.21	25159151
151	Phosphorylation	RSGSSVSSRSYSPER CCCCCCCCCCCCCCC	24.08	30576142
151	Ubiquitination	RSGSSVSSRSYSPER CCCCCCCCCCCCCCC	24.08	24816145
153	Phosphorylation	GSSVSSRSYSPERSK CCCCCCCCCCCCCCC	31.73	23927012
153	Ubiquitination	GSSVSSRSYSPERSK CCCCCCCCCCCCCCC	31.73	32015554
154	Phosphorylation	SSVSSRSYSPERSKS CCCCCCCCCCCCCCC	27.43	30576142
155	Phosphorylation	SVSSRSYSPERSKSY CCCCCCCCCCCCCCC	22.87	28355574
157	Phosphorylation	SSRSYSPERSKSYSF CCCCCCCCCCCCCCC	64.74	32645325
159	Phosphorylation	RSYSPERSKSYSFHQ CCCCCCCCCCCCCCH	25.04	17287340
160	Sumoylation	SYSPERSKSYSFHQS CCCCCCCCCCCCCHH	60.68	28112733
160	Ubiquitination	SYSPERSKSYSFHQS CCCCCCCCCCCCCHH	60.68	32015554
161	Phosphorylation	YSPERSKSYSFHQSQ CCCCCCCCCCCCHHH	27.53	23401153
161	Ubiquitination	YSPERSKSYSFHQSQ CCCCCCCCCCCCHHH	27.53	32015554
162	Phosphorylation	SPERSKSYSFHQSQH CCCCCCCCCCCHHHH	21.06	27794612
163	Phosphorylation	PERSKSYSFHQSQHR CCCCCCCCCCHHHHH	24.28	23401153
165	Ubiquitination	RSKSYSFHQSQHRKS CCCCCCCCHHHHHCC	22.05	29967540
166	Ubiquitination	SKSYSFHQSQHRKSV CCCCCCCHHHHHCCC	42.66	27667366
167	Phosphorylation	KSYSFHQSQHRKSVR CCCCCCHHHHHCCCC	21.27	23401153
167	Ubiquitination	KSYSFHQSQHRKSVR CCCCCCHHHHHCCCC	21.27	29967540
168	Ubiquitination	SYSFHQSQHRKSVRP CCCCCHHHHHCCCCC	33.56	32015554
171	Sumoylation	FHQSQHRKSVRPGAS CCHHHHHCCCCCCHH	51.70	-
171	Sumoylation	FHQSQHRKSVRPGAS CCHHHHHCCCCCCHH	51.70	-
172	Phosphorylation	HQSQHRKSVRPGASY CHHHHHCCCCCCHHH	24.26	23401153
172	Ubiquitination	HQSQHRKSVRPGASY CHHHHHCCCCCCHHH	24.26	32015554
173	Ubiquitination	QSQHRKSVRPGASYK HHHHHCCCCCCHHHC	10.84	27667366
178	Phosphorylation	KSVRPGASYKRQNEG CCCCCCHHHCCCCCC	36.78	23401153
178 (in isoform 9)	Phosphorylation	-	36.78	24719451
179	Phosphorylation	SVRPGASYKRQNEGN CCCCCHHHCCCCCCC	15.06	26074081
179	Ubiquitination	SVRPGASYKRQNEGN CCCCCHHHCCCCCCC	15.06	32015554
180	Acetylation	VRPGASYKRQNEGNP CCCCHHHCCCCCCCC	45.04	25953088
180	Sumoylation	VRPGASYKRQNEGNP CCCCHHHCCCCCCCC	45.04	28112733
180	Ubiquitination	VRPGASYKRQNEGNP CCCCHHHCCCCCCCC	45.04	32015554
185	Acetylation	SYKRQNEGNPERDKE HHCCCCCCCCCCCCC	63.64	19608861
185	Ubiquitination	SYKRQNEGNPERDKE HHCCCCCCCCCCCCC	63.64	27667366
186	Phosphorylation	YKRQNEGNPERDKER HCCCCCCCCCCCCCC	29.13	32645325
186 (in isoform 9)	Phosphorylation	-	29.13	29666759
187	Acetylation	KRQNEGNPERDKERP CCCCCCCCCCCCCCC	49.18	19608861
187	Ubiquitination	KRQNEGNPERDKERP CCCCCCCCCCCCCCC	49.18	32015554
188 (in isoform 9)	Phosphorylation	-	76.99	24719451
191	2-Hydroxyisobutyrylation	EGNPERDKERPVQSL CCCCCCCCCCCCCCC	62.94	-
192	Acetylation	GNPERDKERPVQSLK CCCCCCCCCCCCCCC	67.51	19608861
192	Ubiquitination	GNPERDKERPVQSLK CCCCCCCCCCCCCCC	67.51	27667366
193	Phosphorylation	NPERDKERPVQSLKT CCCCCCCCCCCCCCC	42.29	32645325
197	Phosphorylation	DKERPVQSLKTSRDT CCCCCCCCCCCCCCC	31.87	30266825
199	Sumoylation	ERPVQSLKTSRDTSP CCCCCCCCCCCCCCC	50.10	28112733
199	Ubiquitination	ERPVQSLKTSRDTSP CCCCCCCCCCCCCCC	50.10	24816145
200	Phosphorylation	RPVQSLKTSRDTSPS CCCCCCCCCCCCCCC	34.00	23927012
201	Phosphorylation	PVQSLKTSRDTSPSS CCCCCCCCCCCCCCC	26.94	23927012
201	Ubiquitination	PVQSLKTSRDTSPSS CCCCCCCCCCCCCCC	26.94	29967540
204	Phosphorylation	SLKTSRDTSPSSGSA CCCCCCCCCCCCCCC	41.23	22167270
205	Phosphorylation	LKTSRDTSPSSGSAV CCCCCCCCCCCCCCC	27.37	29255136
206	Ubiquitination	KTSRDTSPSSGSAVS CCCCCCCCCCCCCCC	34.31	24816145
207	Phosphorylation	TSRDTSPSSGSAVSS CCCCCCCCCCCCCCC	47.28	22167270
208	Phosphorylation	SRDTSPSSGSAVSSS CCCCCCCCCCCCCCH	39.90	23401153
208	Ubiquitination	SRDTSPSSGSAVSSS CCCCCCCCCCCCCCH	39.90	32015554
210	Phosphorylation	DTSPSSGSAVSSSKV CCCCCCCCCCCCHHC	27.69	23401153
212	Phosphorylation	SPSSGSAVSSSKVLD CCCCCCCCCCHHCCC	6.46	32645325
213	Phosphorylation	PSSGSAVSSSKVLDK CCCCCCCCCHHCCCC	28.72	23401153
214	Phosphorylation	SSGSAVSSSKVLDKP CCCCCCCCHHCCCCC	27.81	23401153
215	Phosphorylation	SGSAVSSSKVLDKPS CCCCCCCHHCCCCCC	21.19	23927012
215	Ubiquitination	SGSAVSSSKVLDKPS CCCCCCCHHCCCCCC	21.19	33845483
216	Acetylation	GSAVSSSKVLDKPSR CCCCCCHHCCCCCCC	49.08	25953088
216	Ubiquitination	GSAVSSSKVLDKPSR CCCCCCHHCCCCCCC	49.08	32015554
220	Acetylation	SSSKVLDKPSRLTEK CCHHCCCCCCCCCHH	40.51	25953088
220	Ubiquitination	SSSKVLDKPSRLTEK CCHHCCCCCCCCCHH	40.51	29967540
221	Acetylation	SSKVLDKPSRLTEKE CHHCCCCCCCCCHHH	25.09	19608861
221	Ubiquitination	SSKVLDKPSRLTEKE CHHCCCCCCCCCHHH	25.09	27667366
222	Phosphorylation	SKVLDKPSRLTEKEL HHCCCCCCCCCHHHH	45.74	20068231
223	Ubiquitination	KVLDKPSRLTEKELA HCCCCCCCCCHHHHH	54.90	32015554
225	Phosphorylation	LDKPSRLTEKELAEA CCCCCCCCHHHHHHH	43.85	26074081
225	Ubiquitination	LDKPSRLTEKELAEA CCCCCCCCHHHHHHH	43.85	33845483
227	Acetylation	KPSRLTEKELAEAAS CCCCCCHHHHHHHHH	53.44	23954790
227	Sumoylation	KPSRLTEKELAEAAS CCCCCCHHHHHHHHH	53.44	28112733
227	Ubiquitination	KPSRLTEKELAEAAS CCCCCCHHHHHHHHH	53.44	32015554
228	Ubiquitination	PSRLTEKELAEAASK CCCCCHHHHHHHHHH	47.16	27667366
232	Ubiquitination	TEKELAEAASKWAAE CHHHHHHHHHHHHHH	16.07	33845483
234	Ubiquitination	KELAEAASKWAAEKL HHHHHHHHHHHHHHH	35.46	32015554
235	Sumoylation	ELAEAASKWAAEKLE HHHHHHHHHHHHHHH	35.80	-
235	Acetylation	ELAEAASKWAAEKLE HHHHHHHHHHHHHHH	35.80	19608861
235	Sumoylation	ELAEAASKWAAEKLE HHHHHHHHHHHHHHH	35.80	28112733
235	Ubiquitination	ELAEAASKWAAEKLE HHHHHHHHHHHHHHH	35.80	32015554
240	Sumoylation	ASKWAAEKLEKSDES HHHHHHHHHHHCCHH	58.16	-
240	Acetylation	ASKWAAEKLEKSDES HHHHHHHHHHHCCHH	58.16	19608861
240	Sumoylation	ASKWAAEKLEKSDES HHHHHHHHHHHCCHH	58.16	28112733
240	Ubiquitination	ASKWAAEKLEKSDES HHHHHHHHHHHCCHH	58.16	19608861
242	Acetylation	KWAAEKLEKSDESNL HHHHHHHHHCCHHCC	62.68	19608861
242	Ubiquitination	KWAAEKLEKSDESNL HHHHHHHHHCCHHCC	62.68	32015554
244	Phosphorylation	AAEKLEKSDESNLPE HHHHHHHCCHHCCCC	36.92	26074081
244	Ubiquitination	AAEKLEKSDESNLPE HHHHHHHCCHHCCCC	36.92	33845483
247	Acetylation	KLEKSDESNLPEISE HHHHCCHHCCCCCCC	48.97	19608861
247	Phosphorylation	KLEKSDESNLPEISE HHHHCCHHCCCCCCC	48.97	26074081
247	Ubiquitination	KLEKSDESNLPEISE HHHHCCHHCCCCCCC	48.97	27667366
248	Ubiquitination	LEKSDESNLPEISEY HHHCCHHCCCCCCCC	58.53	23000965
251	Ubiquitination	SDESNLPEISEYEAG CCHHCCCCCCCCCCC	63.41	33845483
254	Ubiquitination	SNLPEISEYEAGSTA HCCCCCCCCCCCCCC	53.72	21890473
255	Phosphorylation	NLPEISEYEAGSTAP CCCCCCCCCCCCCCC	12.32	-
255	Ubiquitination	NLPEISEYEAGSTAP CCCCCCCCCCCCCCC	12.32	23000965
261	Ubiquitination	EYEAGSTAPLFTDQP CCCCCCCCCCCCCCC	10.65	21890473
267	Ubiquitination	TAPLFTDQPEEPESN CCCCCCCCCCCCCCC	44.22	23000965
273	Ubiquitination	DQPEEPESNTTHGIE CCCCCCCCCCCCCEE	50.63	23000965
273 (in isoform 3)	Ubiquitination	-	50.63	21890473
274	Ubiquitination	QPEEPESNTTHGIEL CCCCCCCCCCCCEEE	47.54	23000965
280	Ubiquitination	SNTTHGIELFEDSQL CCCCCCEEEECCCCC	52.58	23000965
280 (in isoform 6)	Ubiquitination	-	52.58	21890473
287	Ubiquitination	ELFEDSQLTTRSKAI EEECCCCCCHHHHHH	6.47	33845483
298	Phosphorylation	SKAIASKTKEIEQVY HHHHHHHHHHHHHHH	31.26	20068231
299	2-Hydroxyisobutyrylation	KAIASKTKEIEQVYR HHHHHHHHHHHHHHH	61.50	-
299	Ubiquitination	KAIASKTKEIEQVYR HHHHHHHHHHHHHHH	61.50	33845483
303	Ubiquitination	SKTKEIEQVYRQDCE HHHHHHHHHHHHHHH	43.11	23000965
305	Phosphorylation	TKEIEQVYRQDCETF HHHHHHHHHHHHHHH	11.40	22817900
306	Ubiquitination	KEIEQVYRQDCETFG HHHHHHHHHHHHHHH	27.31	33845483
309	Ubiquitination	EQVYRQDCETFGMVV HHHHHHHHHHHHHHH	3.92	21890473
310	Ubiquitination	QVYRQDCETFGMVVK HHHHHHHHHHHHHHH	56.30	23000965
311 (in isoform 6)	Phosphorylation	-	31.64	-
312 (in isoform 6)	Phosphorylation	-	2.51	27067055
316	Ubiquitination	CETFGMVVKMLIEKD HHHHHHHHHHHHHCC	1.93	21890473
322	Acetylation	VVKMLIEKDPSLEKS HHHHHHHCCCCHHHH	68.87	26051181
322	Ubiquitination	VVKMLIEKDPSLEKS HHHHHHHCCCCHHHH	68.87	23000965
325	Phosphorylation	MLIEKDPSLEKSIQF HHHHCCCCHHHHHHH	60.33	25218447
328	Sumoylation	EKDPSLEKSIQFALR HCCCCHHHHHHHHHH	59.14	-
328	Sumoylation	EKDPSLEKSIQFALR HCCCCHHHHHHHHHH	59.14	28112733
328	Ubiquitination	EKDPSLEKSIQFALR HCCCCHHHHHHHHHH	59.14	23000965
328 (in isoform 1)	Ubiquitination	-	59.14	21890473
328 (in isoform 8)	Ubiquitination	-	59.14	21890473
329	Phosphorylation	KDPSLEKSIQFALRQ CCCCHHHHHHHHHHH	16.55	26074081
329	Ubiquitination	KDPSLEKSIQFALRQ CCCCHHHHHHHHHHH	16.55	23000965
335	Ubiquitination	KSIQFALRQNLHEIE HHHHHHHHHCHHHHH	21.66	21890473
335 (in isoform 2)	Ubiquitination	-	21.66	21890473
340 (in isoform 9)	Phosphorylation	-	52.17	-
341 (in isoform 9)	Phosphorylation	-	3.36	27067055
359 (in isoform 8)	Phosphorylation	-	5.36	-
360 (in isoform 8)	Phosphorylation	-	30.41	27067055
366 (in isoform 2)	Phosphorylation	-	68.69	-
367 (in isoform 2)	Phosphorylation	-	64.87	27067055
396	Phosphorylation	RKKRVRRTTQLRRTT CCHHHHHHHHHHHHH	14.34	29496963
397	Phosphorylation	KKRVRRTTQLRRTTG CHHHHHHHHHHHHHC	24.64	29496963
403	Phosphorylation	TTQLRRTTGAPDITW HHHHHHHHCCCCCCH	29.54	28555341
453	Sumoylation	CNSRKDVKPENKQ-- CCCCCCCCCCCCC--	57.66	-
453	Sumoylation	CNSRKDVKPENKQ-- CCCCCCCCCCCCC--	57.66	25218447

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
110	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASPP2_HUMAN	TP53BP2	physical	21900206
SNCAP_HUMAN	SNCAIP	physical	19730898
A4_HUMAN	APP	physical	21832049
TSG10_HUMAN	TSGA10	physical	25416956
CCD57_HUMAN	CCDC57	physical	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 PPHLN_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-235 AND LYS-240, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-201; THR-204 ANDSER-205, 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-133; SER-197 ANDSER-205, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-205, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-121; SER-145;SER-155; THR-200; SER-201; THR-204; SER-205; SER-207 AND SER-208, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND MASSSPECTROMETRY.	16964243 [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 SER-121; SER-133; SER-140;THR-200 AND SER-201, AND MASS SPECTROMETRY.	17081983 [Abstract]