dbPTM

VIGLN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VIGLN_HUMAN
UniProt AC	Q00341
Protein Name	Vigilin
Gene Name	HDLBP
Organism	Homo sapiens (Human).
Sequence Length	1268
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol..
Protein Sequence	MSSVAVLTQESFAEHRSGLVPQQIKVATLNSEEESDPPTYKDAFPPLPEKAACLESAQEPSGAWGNKIRPIKASVITQVFHVPLEERKYKDMNQFGEGEQAKICLEIMQRTGAHLELSLAKDQGLSIMVSGKLDAVMKARKDIVARLQTQASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAEQDKRAVERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTEIVFTGEKEQLAQAVARIKKIYEEKKKKTTTIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEVYAKANSFTVSSVAAPSWLHRFIIGKKGQNLAKITQQMPKVHIEFTEGEDKITLEGPTEDVNVAQEQIEGMVKDLINRMDYVEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELASRMENERTKDLIIEQRFHRTIIGQKGERIREIRDKFPEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKMVADLVENSYSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRILSIQKDLANIAEVEVSIPAKLHNSLIGTKGRLIRSIMEECGGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEEKQTKSFTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQDLITIIGKEDAVREAQKELEALIQNLDNVVEDSMLVDPKHHRHFVIRRGQVLREIAEEYGGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEIIEDLEAQVTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAVHSTEPVVQENGDEAGEGREAKDCDPGSPRRCDIIIISGRKEKCEAAKEALEALVPVTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKAGLLERVKELQAEQEDRALRSFKLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNQPQDQITITGYEKNTEAARDAILRIVGELEQMVSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNCVTVTGLPENVEEAIDHILNLEEEYLADVVDSEALQVYMKPPAHEEAKAPSRGFVVRDAPWTASSSEKAPDMSSSEEFPSFGAQVAPKTLPWGPKR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSVAVLTQ ------CCCEEEEEH	44.84	22223895
2	Phosphorylation	------MSSVAVLTQ ------CCCEEEEEH	44.84	28857561
3	Phosphorylation	-----MSSVAVLTQE -----CCCEEEEEHH	26.42	28857561
8	Phosphorylation	MSSVAVLTQESFAEH CCCEEEEEHHHHHHH	24.56	29083192
11	Phosphorylation	VAVLTQESFAEHRSG EEEEEHHHHHHHCCC	21.68	29514088
17	Phosphorylation	ESFAEHRSGLVPQQI HHHHHHCCCCCCCEE	38.08	29514088
25	Ubiquitination	GLVPQQIKVATLNSE CCCCCEEEEEECCCC	22.83	-
28	Phosphorylation	PQQIKVATLNSEEES CCEEEEEECCCCCCC	29.47	30266825
31	Phosphorylation	IKVATLNSEEESDPP EEEEECCCCCCCCCC	49.88	19664994
35	Phosphorylation	TLNSEEESDPPTYKD ECCCCCCCCCCCCHH	59.71	22167270
39	Phosphorylation	EEESDPPTYKDAFPP CCCCCCCCCHHCCCC	48.90	22167270
40	Phosphorylation	EESDPPTYKDAFPPL CCCCCCCCHHCCCCC	16.79	22167270
41	Ubiquitination	ESDPPTYKDAFPPLP CCCCCCCHHCCCCCC	45.09	-
50	Acetylation	AFPPLPEKAACLESA CCCCCCHHHHHHHHC	39.07	26051181
74	Phosphorylation	KIRPIKASVITQVFH CCCCCCCHHEEEEEE	14.73	30087585
77	Phosphorylation	PIKASVITQVFHVPL CCCCHHEEEEEECCH	19.27	24719451
88	Ubiquitination	HVPLEERKYKDMNQF ECCHHHHCCCCHHHC	60.99	-
90	Ubiquitination	PLEERKYKDMNQFGE CHHHHCCCCHHHCCC	54.24	-
90	Malonylation	PLEERKYKDMNQFGE CHHHHCCCCHHHCCC	54.24	26320211
92	Sulfoxidation	EERKYKDMNQFGEGE HHHCCCCHHHCCCHH	3.57	21406390
104	Glutathionylation	EGEQAKICLEIMQRT CHHHHHHHHHHHHHH	2.48	22555962
108	Sulfoxidation	AKICLEIMQRTGAHL HHHHHHHHHHHCCEE	1.29	21406390
111	Phosphorylation	CLEIMQRTGAHLELS HHHHHHHHCCEEEEE	23.10	26074081
118	Phosphorylation	TGAHLELSLAKDQGL HCCEEEEEEHHHCCC	19.53	26074081
126	Phosphorylation	LAKDQGLSIMVSGKL EHHHCCCEEEEECCH	18.57	28258704
130	Phosphorylation	QGLSIMVSGKLDAVM CCCEEEEECCHHHHH	16.90	28258704
138	Ubiquitination	GKLDAVMKARKDIVA CCHHHHHHHHHHHHH	38.14	-
138	2-Hydroxyisobutyrylation	GKLDAVMKARKDIVA CCHHHHHHHHHHHHH	38.14	-
138	Malonylation	GKLDAVMKARKDIVA CCHHHHHHHHHHHHH	38.14	26320211
138	Acetylation	GKLDAVMKARKDIVA CCHHHHHHHHHHHHH	38.14	25953088
149	Phosphorylation	DIVARLQTQASATVA HHHHHHHHHCCCEEE	30.60	28857561
152	Phosphorylation	ARLQTQASATVAIPK HHHHHHCCCEEEECH	18.04	27251275
154	Phosphorylation	LQTQASATVAIPKEH HHHHCCCEEEECHHH	14.15	28857561
159	Ubiquitination	SATVAIPKEHHRFVI CCEEEECHHHCEEEE	64.66	-
172	Ubiquitination	VIGKNGEKLQDLELK EECCCCCEEECCCCC	53.50	-
179	Ubiquitination	KLQDLELKTATKIQI EEECCCCCCCCEEEC	27.09	-
180	Phosphorylation	LQDLELKTATKIQIP EECCCCCCCCEEECC	52.78	28857561
182	Phosphorylation	DLELKTATKIQIPRP CCCCCCCCEEECCCC	33.63	30631047
197	Ubiquitination	DDPSNQIKITGTKEG CCCCCCEEEECCHHH	25.17	-
197	Malonylation	DDPSNQIKITGTKEG CCCCCCEEEECCHHH	25.17	26320211
202	Ubiquitination	QIKITGTKEGIEKAR CEEEECCHHHHHHHH	56.11	-
202	Acetylation	QIKITGTKEGIEKAR CEEEECCHHHHHHHH	56.11	23236377
216	Phosphorylation	RHEVLLISAEQDKRA HEEEEEEEHHHHHHH	26.23	20068231
221	Ubiquitination	LISAEQDKRAVERLE EEEHHHHHHHHHHHH	41.78	-
221	Acetylation	LISAEQDKRAVERLE EEEHHHHHHHHHHHH	41.78	26051181
231	Ubiquitination	VERLEVEKAFHPFIA HHHHHHHHHHCHHHC	62.62	21890473
231	Acetylation	VERLEVEKAFHPFIA HHHHHHHHHHCHHHC	62.62	26051181
241	Phosphorylation	HPFIAGPYNRLVGEI CHHHCCHHHHHHHHH	16.40	28152594
249	Sulfoxidation	NRLVGEIMQETGTRI HHHHHHHHHHHCCCC	2.28	21406390
252	Phosphorylation	VGEIMQETGTRINIP HHHHHHHHCCCCCCC	27.28	28857561
262	Phosphorylation	RINIPPPSVNRTEIV CCCCCCCCCCCEEEE	37.49	20873877
267	Ubiquitination	PPSVNRTEIVFTGEK CCCCCCEEEEEECCH	33.64	21890473
271	Phosphorylation	NRTEIVFTGEKEQLA CCEEEEEECCHHHHH	33.27	27251275
274	Ubiquitination	EIVFTGEKEQLAQAV EEEEECCHHHHHHHH	52.70	-
274	2-Hydroxyisobutyrylation	EIVFTGEKEQLAQAV EEEEECCHHHHHHHH	52.70	-
274	Acetylation	EIVFTGEKEQLAQAV EEEEECCHHHHHHHH	52.70	26051181
294	Ubiquitination	IYEEKKKKTTTIAVE HHHHHCCCCCEEEEE	61.04	-
295	Phosphorylation	YEEKKKKTTTIAVEV HHHHCCCCCEEEEEE	37.74	21082442
296	Phosphorylation	EEKKKKTTTIAVEVK HHHCCCCCEEEEEEE	25.69	22817900
297	Phosphorylation	EKKKKTTTIAVEVKK HHCCCCCEEEEEEEC	16.51	22817900
303	2-Hydroxyisobutyrylation	TTIAVEVKKSQHKYV CEEEEEEECCCCCEE	32.95	-
308	Acetylation	EVKKSQHKYVIGPKG EEECCCCCEEECCCC	33.31	18604469
308	Ubiquitination	EVKKSQHKYVIGPKG EEECCCCCEEECCCC	33.31	-
314	Ubiquitination	HKYVIGPKGNSLQEI CCEEECCCCCCHHHH	66.56	-
317	Phosphorylation	VIGPKGNSLQEILER EECCCCCCHHHHHHH	39.85	22617229
349	Ubiquitination	ILRGEPEKLGQALTE EECCCHHHHHHHHHH	69.50	-
358	Phosphorylation	GQALTEVYAKANSFT HHHHHHHHHHHCCCC	8.99	21945579
360	Ubiquitination	ALTEVYAKANSFTVS HHHHHHHHHCCCCHH	30.34	-
363	Phosphorylation	EVYAKANSFTVSSVA HHHHHHCCCCHHCCC	27.44	20873877
365	Phosphorylation	YAKANSFTVSSVAAP HHHHCCCCHHCCCCC	21.21	20873877
367	Phosphorylation	KANSFTVSSVAAPSW HHCCCCHHCCCCCHH	18.94	20873877
368	Phosphorylation	ANSFTVSSVAAPSWL HCCCCHHCCCCCHHH	16.07	20873877
373	Phosphorylation	VSSVAAPSWLHRFII HHCCCCCHHHHHHHH	37.23	20873877
383	Ubiquitination	HRFIIGKKGQNLAKI HHHHHCCCCCCHHHH	61.59	-
389	Ubiquitination	KKGQNLAKITQQMPK CCCCCHHHHHHCCCC	49.83	-
402	Phosphorylation	PKVHIEFTEGEDKIT CCEEEEEECCCCCEE	30.23	-
437	Phosphorylation	DLINRMDYVEINIDH HHHHHCCEEEEECCC	7.22	22115753
445	Acetylation	VEINIDHKFHRHLIG EEEECCCHHHHHHCC	38.83	26051181
453	Ubiquitination	FHRHLIGKSGANINR HHHHHCCCCCCCHHH	38.43	-
453	2-Hydroxyisobutyrylation	FHRHLIGKSGANINR HHHHHCCCCCCCHHH	38.43	-
453	Malonylation	FHRHLIGKSGANINR HHHHHCCCCCCCHHH	38.43	32601280
454	Phosphorylation	HRHLIGKSGANINRI HHHHCCCCCCCHHHC	37.61	29214152
465	Phosphorylation	INRIKDQYKVSVRIP HHHCCCEEEEEEECC	24.40	23312004
466	Ubiquitination	NRIKDQYKVSVRIPP HHCCCEEEEEEECCC	23.54	-
466	Malonylation	NRIKDQYKVSVRIPP HHCCCEEEEEEECCC	23.54	32601280
468	Phosphorylation	IKDQYKVSVRIPPDS CCCEEEEEEECCCCC	11.09	30108239
477	Ubiquitination	RIPPDSEKSNLIRIE ECCCCCCCCCCEEEE	48.90	-
477	Malonylation	RIPPDSEKSNLIRIE ECCCCCCCCCCEEEE	48.90	26320211
494	Ubiquitination	PQGVQQAKRELLELA HHHHHHHHHHHHHHH	41.91	-
494	2-Hydroxyisobutyrylation	PQGVQQAKRELLELA HHHHHHHHHHHHHHH	41.91	-
494	Acetylation	PQGVQQAKRELLELA HHHHHHHHHHHHHHH	41.91	26051181
510	Ubiquitination	RMENERTKDLIIEQR HHCCHHHHHHHHHHH	57.68	-
510	Malonylation	RMENERTKDLIIEQR HHCCHHHHHHHHHHH	57.68	26320211
521	Phosphorylation	IEQRFHRTIIGQKGE HHHHHHHHHCCCCCH	14.37	28857561
526	Ubiquitination	HRTIIGQKGERIREI HHHHCCCCCHHHHHH	58.49	-
526	2-Hydroxyisobutyrylation	HRTIIGQKGERIREI HHHHCCCCCHHHHHH	58.49	-
526	Malonylation	HRTIIGQKGERIREI HHHHCCCCCHHHHHH	58.49	26320211
536	Acetylation	RIREIRDKFPEVIIN HHHHHHHHCCCEEEC	53.63	26051181
536	Ubiquitination	RIREIRDKFPEVIIN HHHHHHHHCCCEEEC	53.63	-
550	Ubiquitination	NFPDPAQKSDIVQLR CCCCHHHCCCCEEEC	52.80	-
551	Phosphorylation	FPDPAQKSDIVQLRG CCCHHHCCCCEEECC	22.08	20873877
565	Acetylation	GPKNEVEKCTKYMQK CCHHHHHHHHHHHHH	52.99	26051181
569	Phosphorylation	EVEKCTKYMQKMVAD HHHHHHHHHHHHHHH	6.14	28348404
581	Phosphorylation	VADLVENSYSISVPI HHHHHHCCCCCCHHH	13.52	21945579
582	Phosphorylation	ADLVENSYSISVPIF HHHHHCCCCCCHHHH	22.93	21945579
583	Phosphorylation	DLVENSYSISVPIFK HHHHCCCCCCHHHHH	14.28	21945579
585	Phosphorylation	VENSYSISVPIFKQF HHCCCCCCHHHHHHH	18.85	21945579
594	Ubiquitination	PIFKQFHKNIIGKGG HHHHHHHHHCCCCCC	51.64	-
599	Ubiquitination	FHKNIIGKGGANIKK HHHHCCCCCCCCHHH	43.70	-
599	Malonylation	FHKNIIGKGGANIKK HHHHCCCCCCCCHHH	43.70	26320211
605	Ubiquitination	GKGGANIKKIREESN CCCCCCHHHHHHHCC	41.79	-
611	Phosphorylation	IKKIREESNTKIDLP HHHHHHHCCCCEECC	45.08	-
613	Phosphorylation	KIREESNTKIDLPAE HHHHHCCCCEECCCC	38.36	-
614	Ubiquitination	IREESNTKIDLPAEN HHHHCCCCEECCCCC	38.17	-
622	Phosphorylation	IDLPAENSNSETIII EECCCCCCCCCEEEE	32.98	20873877
624	Phosphorylation	LPAENSNSETIIITG CCCCCCCCCEEEEEC	35.62	20873877
626	Phosphorylation	AENSNSETIIITGKR CCCCCCCEEEEECCC	19.80	20873877
630	Phosphorylation	NSETIIITGKRANCE CCCEEEEECCCCCHH	26.66	20873877
632	Methylation	ETIIITGKRANCEAA CEEEEECCCCCHHHH	39.42	115978801
632	Ubiquitination	ETIIITGKRANCEAA CEEEEECCCCCHHHH	39.42	-
632	2-Hydroxyisobutyrylation	ETIIITGKRANCEAA CEEEEECCCCCHHHH	39.42	-
632	Malonylation	ETIIITGKRANCEAA CEEEEECCCCCHHHH	39.42	26320211
632	Acetylation	ETIIITGKRANCEAA CEEEEECCCCCHHHH	39.42	25953088
645	Phosphorylation	AARSRILSIQKDLAN HHHHHHHHHHHHHHC	22.17	25159151
659	Phosphorylation	NIAEVEVSIPAKLHN CCCEEEEECCHHHHC	14.89	27251275
663	Ubiquitination	VEVSIPAKLHNSLIG EEEECCHHHHCCCCC	44.95	-
663	Acetylation	VEVSIPAKLHNSLIG EEEECCHHHHCCCCC	44.95	26051181
667	Phosphorylation	IPAKLHNSLIGTKGR CCHHHHCCCCCCHHH	15.60	30108239
671	Phosphorylation	LHNSLIGTKGRLIRS HHCCCCCCHHHHHHH	24.27	20873877
672	Ubiquitination	HNSLIGTKGRLIRSI HCCCCCCHHHHHHHH	36.50	-
672	2-Hydroxyisobutyrylation	HNSLIGTKGRLIRSI HCCCCCCHHHHHHHH	36.50	-
672	Malonylation	HNSLIGTKGRLIRSI HCCCCCCHHHHHHHH	36.50	26320211
678	Phosphorylation	TKGRLIRSIMEECGG CHHHHHHHHHHHHCC	21.20	26126808
706	Phosphorylation	TVVIRGPSSDVEKAK EEEEECCCCHHHHHH	41.83	30576142
711	Ubiquitination	GPSSDVEKAKKQLLH CCCCHHHHHHHHHHH	66.41	-
713	Ubiquitination	SSDVEKAKKQLLHLA CCHHHHHHHHHHHHH	52.71	-
714	Ubiquitination	SDVEKAKKQLLHLAE CHHHHHHHHHHHHHH	51.54	-
714	Malonylation	SDVEKAKKQLLHLAE CHHHHHHHHHHHHHH	51.54	26320211
723	Ubiquitination	LLHLAEEKQTKSFTV HHHHHHHHCCCCEEE	55.56	-
723	Malonylation	LLHLAEEKQTKSFTV HHHHHHHHCCCCEEE	55.56	26320211
727	Phosphorylation	AEEKQTKSFTVDIRA HHHHCCCCEEEEEEC	29.54	28857561
729	Phosphorylation	EKQTKSFTVDIRAKP HHCCCCEEEEEECCH	25.10	28857561
745	Acetylation	YHKFLIGKGGGKIRK HHCEEECCCCCCEEE	47.60	25953088
749	Ubiquitination	LIGKGGGKIRKVRDS EECCCCCCEEEEECC	42.48	-
756	Phosphorylation	KIRKVRDSTGARVIF CEEEEECCCCCEEEE	20.41	20068231
757	Phosphorylation	IRKVRDSTGARVIFP EEEEECCCCCEEEEE	38.87	26699800
769	Ubiquitination	IFPAAEDKDQDLITI EEECCCCCCCCEEEE	49.12	-
769	2-Hydroxyisobutyrylation	IFPAAEDKDQDLITI EEECCCCCCCCEEEE	49.12	-
769	Acetylation	IFPAAEDKDQDLITI EEECCCCCCCCEEEE	49.12	26051181
775	Phosphorylation	DKDQDLITIIGKEDA CCCCCEEEEECHHHH	17.53	27499020
779	Ubiquitination	DLITIIGKEDAVREA CEEEEECHHHHHHHH	41.85	-
779	2-Hydroxyisobutyrylation	DLITIIGKEDAVREA CEEEEECHHHHHHHH	41.85	-
804	Phosphorylation	LDNVVEDSMLVDPKH HHHHHHHCCCCCCCC	10.66	27499020
810	Ubiquitination	DSMLVDPKHHRHFVI HCCCCCCCCCCCEEE	47.80	-
840	Phosphorylation	VMVSFPRSGTQSDKV EEEECCCCCCCCCCE	46.56	23403867
842	O-linked_Glycosylation	VSFPRSGTQSDKVTL EECCCCCCCCCCEEE	26.58	23301498
842	Phosphorylation	VSFPRSGTQSDKVTL EECCCCCCCCCCEEE	26.58	23403867
844	Phosphorylation	FPRSGTQSDKVTLKG CCCCCCCCCCEEECC	38.96	23403867
846	Ubiquitination	RSGTQSDKVTLKGAK CCCCCCCCEEECCHH	42.22	-
846	2-Hydroxyisobutyrylation	RSGTQSDKVTLKGAK CCCCCCCCEEECCHH	42.22	-
848	Phosphorylation	GTQSDKVTLKGAKDC CCCCCCEEECCHHHH	28.61	21601212
883	Ubiquitination	LECAIPQKFHRSVMG EEEECCHHHHHHHCC	37.47	-
887	Phosphorylation	IPQKFHRSVMGPKGS CCHHHHHHHCCCCCC	14.11	29514088
892	Methylation	HRSVMGPKGSRIQQI HHHHCCCCCCCCCCC	64.88	23644510
894	Phosphorylation	SVMGPKGSRIQQITR HHCCCCCCCCCCCCC	32.13	21406692
900	Phosphorylation	GSRIQQITRDFSVQI CCCCCCCCCCEEEEE	21.61	29514088
904	Phosphorylation	QQITRDFSVQIKFPD CCCCCCEEEEEECCC	19.87	23401153
908	Acetylation	RDFSVQIKFPDREEN CCEEEEEECCCCCCC	33.48	26051181
944	Phosphorylation	AKDCDPGSPRRCDII CCCCCCCCCCCCEEE	22.18	29255136
948	Glutathionylation	DPGSPRRCDIIIISG CCCCCCCCEEEEEEC	4.68	22555962
954	Phosphorylation	RCDIIIISGRKEKCE CCEEEEEECCHHHHH	23.33	26074081
959	Acetylation	IISGRKEKCEAAKEA EEECCHHHHHHHHHH	40.17	21466224
991	Acetylation	HRYVIGQKGSGIRKM HHHHHCCCCCHHHHH	50.24	-
991	Ubiquitination	HRYVIGQKGSGIRKM HHHHHCCCCCHHHHH	50.24	-
991	2-Hydroxyisobutyrylation	HRYVIGQKGSGIRKM HHHHHCCCCCHHHHH	50.24	-
991	Malonylation	HRYVIGQKGSGIRKM HHHHHCCCCCHHHHH	50.24	26320211
993	Phosphorylation	YVIGQKGSGIRKMMD HHHCCCCCHHHHHHH	37.77	24719451
1031	Ubiquitination	AANLDRAKAGLLERV HHHHHHHHHHHHHHH	43.83	-
1031	2-Hydroxyisobutyrylation	AANLDRAKAGLLERV HHHHHHHHHHHHHHH	43.83	-
1039	Ubiquitination	AGLLERVKELQAEQE HHHHHHHHHHHHHHH	59.95	-
1048	Methylation	LQAEQEDRALRSFKL HHHHHHHHHHHHCEE	34.47	115919801
1054	Ubiquitination	DRALRSFKLSVTVDP HHHHHHCEEEEEECC	40.89	-
1056	Phosphorylation	ALRSFKLSVTVDPKY HHHHCEEEEEECCCC	19.14	20068231
1058	Phosphorylation	RSFKLSVTVDPKYHP HHCEEEEEECCCCCC	18.80	20068231
1062	Ubiquitination	LSVTVDPKYHPKIIG EEEEECCCCCCCCCC	52.29	-
1062	2-Hydroxyisobutyrylation	LSVTVDPKYHPKIIG EEEEECCCCCCCCCC	52.29	-
1062	Malonylation	LSVTVDPKYHPKIIG EEEEECCCCCCCCCC	52.29	32601280
1062	Acetylation	LSVTVDPKYHPKIIG EEEEECCCCCCCCCC	52.29	23236377
1066	Ubiquitination	VDPKYHPKIIGRKGA ECCCCCCCCCCCCCE	33.37	-
1071	Malonylation	HPKIIGRKGAVITQI CCCCCCCCCEEEEEE	46.11	26320211
1076	Phosphorylation	GRKGAVITQIRLEHD CCCCEEEEEEEEECE	16.02	-
1108	Ubiquitination	ITITGYEKNTEAARD EEEECCCCCHHHHHH	61.76	-
1127	Sulfoxidation	IVGELEQMVSEDVPL HHHHHHHHHCCCCCC	2.33	30846556
1152	Malonylation	ARGKAIRKIMDEFKV CHHHHHHHHHHHHCC	35.95	26320211
1210	Phosphorylation	DSEALQVYMKPPAHE CHHHHHHHCCCCCCC	6.10	22817900
1223	Phosphorylation	HEEAKAPSRGFVVRD CCCCCCCCCCEEEEE	50.31	20068231
1224	Methylation	EEAKAPSRGFVVRDA CCCCCCCCCEEEEEC	41.32	54429977
1234	Phosphorylation	VVRDAPWTASSSEKA EEEECCCCCCCCCCC	18.66	30576142
1236	Phosphorylation	RDAPWTASSSEKAPD EECCCCCCCCCCCCC	27.33	25159151
1237	Phosphorylation	DAPWTASSSEKAPDM ECCCCCCCCCCCCCC	39.80	25159151
1238	Phosphorylation	APWTASSSEKAPDMS CCCCCCCCCCCCCCC	40.39	22199227
1240	Ubiquitination	WTASSSEKAPDMSSS CCCCCCCCCCCCCCC	68.14	21890473
1245	Phosphorylation	SEKAPDMSSSEEFPS CCCCCCCCCCCCCCC	37.78	20873877
1246	Phosphorylation	EKAPDMSSSEEFPSF CCCCCCCCCCCCCCC	34.82	25159151
1247	Phosphorylation	KAPDMSSSEEFPSFG CCCCCCCCCCCCCCC	33.56	25159151
1252	Phosphorylation	SSSEEFPSFGAQVAP CCCCCCCCCCCCCCC	41.45	25072903
1261	Phosphorylation	GAQVAPKTLPWGPKR CCCCCCCCCCCCCCC	36.67	18212344

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
8	T	Phosphorylation	Kinase	CHEK1	O14757	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XPOT_HUMAN	XPOT	physical	10657246
XRCC5_HUMAN	XRCC5	physical	15723802
PRKDC_HUMAN	PRKDC	physical	15723802
DSRAD_HUMAN	ADAR	physical	15723802
DHX9_HUMAN	DHX9	physical	15723802
VPS35_HUMAN	VPS35	physical	22939629
VPS29_HUMAN	VPS29	physical	22939629
VP26A_HUMAN	VPS26A	physical	22939629
VPS36_HUMAN	VPS36	physical	22939629
VPS25_HUMAN	VPS25	physical	22939629
ZW10_HUMAN	ZW10	physical	22939629
ZN598_HUMAN	ZNF598	physical	22939629
DYL1_HUMAN	DYNLL1	physical	22863883
EIF2A_HUMAN	EIF2A	physical	22863883
UBIM_HUMAN	FAU	physical	22863883
NEMO_HUMAN	IKBKG	physical	22863883
CLU_HUMAN	CLUH	physical	26344197
DDX43_HUMAN	DDX43	physical	26344197
GLMN_HUMAN	GLMN	physical	26344197

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 VIGLN_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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-31 AND SER-944, AND MASSSPECTROMETRY.	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-31, AND MASSSPECTROMETRY.	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 SER-944 AND SER-1223, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-944, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-437, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-437, AND MASSSPECTROMETRY.	15592455 [Abstract]